3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -19.3779    4.7472  -16.8097 N   0  0
  -18.3244    5.0182  -17.6159 C   0  0
  -18.4566    4.6354  -18.8981 N   0  0
  -17.4983    4.9628  -19.7820 C   0  0
  -16.3830    5.6205  -19.4753 N   0  0
  -16.2275    5.9581  -18.1883 C   0  0
  -17.1830    5.6534  -17.1922 C   0  0
  -15.1675    6.6395  -17.6009 N   0  0
  -13.9755    7.1175  -18.3294 C   0  0
  -12.6631    6.5469  -17.7856 C   0  0
  -11.5835    7.5564  -18.1966 C   0  0
  -12.3187    8.8451  -18.6010 C   0  0
  -13.7887    8.6289  -18.2361 C   0  0
  -15.4820    6.7376  -16.2951 C   0  0
  -16.6732    6.1193  -15.9606 C   0  0
  -17.2486    5.9866  -14.5983 C   0  0
  -17.3592    7.0910  -13.7792 C   0  0
  -17.8855    6.9741  -12.4993 C   0  0
  -18.3188    5.7477  -12.0140 C   0  0
  -18.1888    4.6353  -12.8318 C   0  0
  -17.6673    4.7608  -14.1151 C   0  0
  -18.7869    5.5963  -10.7150 O   0  0
  -19.6886    6.5505  -10.2489 C   0  0
  -20.7251    7.0638  -11.0301 C   0  0
  -21.6587    7.9289  -10.4743 C   0  0
  -21.5479    8.3094   -9.1431 C   0  0
  -20.4984    7.8276   -8.3720 C   0  0
  -19.5826    6.9405   -8.9212 C   0  0
  -20.1963    4.2955  -17.1751 H   0  0
  -19.3792    4.9818  -15.8368 H   0  0
  -17.6339    4.6644  -20.8112 H   0  0
  -14.0471    6.8518  -19.3866 H   0  0
  -12.4604    5.5443  -18.1626 H   0  0
  -12.6974    6.4835  -16.6976 H   0  0
  -10.8877    7.7331  -17.3758 H   0  0
  -11.0028    7.1766  -19.0383 H   0  0
  -12.2285    8.9897  -19.6782 H   0  0
  -11.9039    9.7294  -18.1164 H   0  0
  -13.9625    8.9719  -17.2157 H   0  0
  -14.4740    9.1689  -18.8895 H   0  0
  -14.8493    7.2421  -15.5791 H   0  0
  -17.0428    8.0669  -14.1217 H   0  0
  -17.9524    7.8406  -11.8712 H   0  0
  -18.4974    3.6658  -12.4709 H   0  0
  -17.5873    3.8705  -14.7217 H   0  0
  -20.8341    6.7740  -12.0655 H   0  0
  -22.4750    8.2954  -11.0798 H   0  0
  -22.2761    8.9784   -8.7067 H   0  0
  -20.3911    8.1422   -7.3447 H   0  0
  -18.7780    6.5496   -8.3184 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372041153085456

> <LigScore1_Dreiding>
4.79

> <LigScore2_Dreiding>
7

> <-PLP1>
122.28

> <-PLP2>
117.05

> <Jain>
8.54

> <-PMF>
117.53

> <-PMF04>
46.31

> <AbsoluteEnergy>
146.471

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
9

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
0.424

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
1

> <LibDockScore>
119.456

> <HotSpots>
-12.60,6.32,-17.69,A,17,10
-21.80,7.92,-10.89,A,54,25
-19.80,7.72,-8.89,A,70,28

> <-In-Situ Starting Energy>
-11.669

> <-In-Situ Final Energy>
43.229

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
1

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
4

> <Favorable A:ALA428>
3

> <Favorable A:LYS430>
1

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
1

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
1

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
2

> <Favorable A:CYS481>
0

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
2

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
0

> <Favorable A:PHE540>
1

> <Favorable A:LEU542>
1

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
1

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
4

> <Hydrophobic A:ALA428>
3

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
1

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
2

> <Hydrophobic A:PHE540>
1

> <Hydrophobic A:LEU542>
1

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
1

> <HydrogenBond A:MET477>
2

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -19.4107    4.7151  -16.7251 N   0  0  0  1  0  0
  -18.3569    5.0394  -17.5092 C   0  0  0  1  0  0
  -18.4622    4.6935  -18.8063 N   0  0  0  1  0  0
  -17.4900    5.0633  -19.6587 C   0  0  0  1  0  0
  -16.3977    5.7412  -19.3106 N   0  0  0  1  0  0
  -16.2791    6.0623  -18.0129 C   0  0  0  1  0  0
  -17.2437    5.6969  -17.0458 C   0  0  0  1  0  0
  -15.2653    6.7843  -17.3799 N   0  0  0  1  0  0
  -14.0808    7.3737  -18.0332 C   0  0  0  1  0  0
  -13.1971    6.3324  -18.7356 C   0  0  0  1  0  0
  -13.1628    6.7449  -20.2095 C   0  0  0  1  0  0
  -13.4024    8.2505  -20.1906 C   0  0  0  1  0  0
  -14.4427    8.4276  -19.0882 C   0  0  0  1  0  0
  -15.6015    6.8141  -16.0812 C   0  0  0  1  0  0
  -16.7741    6.1465  -15.7919 C   0  0  0  1  0  0
  -17.3587    5.9772  -14.4402 C   0  0  0  1  0  0
  -17.5246    7.0792  -13.6282 C   0  0  0  1  0  0
  -18.0436    6.9453  -12.3489 C   0  0  0  1  0  0
  -18.4134    5.7023  -11.8556 C   0  0  0  1  0  0
  -18.2263    4.5925  -12.6678 C   0  0  0  1  0  0
  -17.7210    4.7349  -13.9564 C   0  0  0  1  0  0
  -18.8891    5.5390  -10.5600 O   0  0  0  1  0  0
  -19.7611    6.5148  -10.0805 C   0  0  0  1  0  0
  -20.8216    7.0193  -10.8347 C   0  0  0  1  0  0
  -21.7115    7.9255  -10.2745 C   0  0  0  1  0  0
  -21.5354    8.3545   -8.9658 C   0  0  0  1  0  0
  -20.4616    7.8816   -8.2231 C   0  0  0  1  0  0
  -19.5884    6.9544   -8.7756 C   0  0  0  1  0  0
  -20.2226    4.2818  -17.1245 H   0  0
  -19.4200    4.8888  -15.7390 H   0  0
  -17.5958    4.7877  -20.6982 H   0  0
  -13.4793    7.8559  -17.2610 H   0  0
  -13.5713    5.3196  -18.5957 H   0  0
  -12.1882    6.3592  -18.3215 H   0  0
  -12.2318    6.4779  -20.7068 H   0  0
  -13.9764    6.2530  -20.7442 H   0  0
  -13.7274    8.6284  -21.1577 H   0  0
  -12.4809    8.7664  -19.9186 H   0  0
  -14.4621    9.4287  -18.6652 H   0  0
  -15.4306    8.2375  -19.5035 H   0  0
  -14.9989    7.3113  -15.3347 H   0  0
  -17.2564    8.0676  -13.9762 H   0  0
  -18.1562    7.8128  -11.7286 H   0  0
  -18.4779    3.6101  -12.2987 H   0  0
  -17.6006    3.8482  -14.5621 H   0  0
  -20.9772    6.7006  -11.8551 H   0  0
  -22.5445    8.2860  -10.8599 H   0  0
  -22.2314    9.0548   -8.5258 H   0  0
  -20.3020    8.2354   -7.2153 H   0  0
  -18.7622    6.5760   -8.1950 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372045448052752

> <LigScore1_Dreiding>
4.73

> <LigScore2_Dreiding>
6.83

> <-PLP1>
121.72

> <-PLP2>
118.01

> <Jain>
9.15

> <-PMF>
111.29

> <-PMF04>
39.46

> <AbsoluteEnergy>
164.152

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
51

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
18.105

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
7

> <LibDockScore>
118.453

> <HotSpots>
-17.60,6.32,-19.49,A,8,4
-17.40,4.12,-13.89,A,32,21
-21.60,7.92,-9.29,A,66,26

> <-In-Situ Starting Energy>
-30.688

> <-In-Situ Final Energy>
41.659

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
2

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
3

> <Favorable A:ALA428>
3

> <Favorable A:LYS430>
1

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
1

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
1

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
2

> <Favorable A:CYS481>
0

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
2

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
0

> <Favorable A:PHE540>
1

> <Favorable A:LEU542>
1

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
2

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
3

> <Hydrophobic A:ALA428>
3

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
1

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
2

> <Hydrophobic A:PHE540>
1

> <Hydrophobic A:LEU542>
1

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
1

> <HydrogenBond A:MET477>
2

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -15.4901    6.7435  -17.4207 N   0  0  0  1  0  0
  -15.5710    6.3989  -18.7239 C   0  0  0  1  0  0
  -16.7033    5.7674  -19.0710 N   0  0  0  1  0  0
  -16.8417    5.3331  -20.3312 C   0  0  0  1  0  0
  -15.9058    5.4513  -21.2702 N   0  0  0  1  0  0
  -14.7865    6.1112  -20.9416 C   0  0  0  1  0  0
  -14.5845    6.6497  -19.6486 C   0  0  0  1  0  0
  -13.6730    6.4040  -21.7302 N   0  0  0  1  0  0
  -13.4593    6.0436  -23.1504 C   0  0  0  1  0  0
  -14.5822    5.3414  -23.9214 C   0  0  0  1  0  0
  -13.8696    4.7769  -25.1453 C   0  0  0  1  0  0
  -12.4957    4.3344  -24.6267 C   0  0  0  1  0  0
  -12.2454    5.1266  -23.3336 C   0  0  0  1  0  0
  -12.8430    7.0921  -20.9241 C   0  0  0  1  0  0
  -13.3524    7.3423  -19.6634 C   0  0  0  1  0  0
  -12.7211    8.1760  -18.6045 C   0  0  0  1  0  0
  -13.4796    9.0467  -17.8409 C   0  0  0  1  0  0
  -12.8956    9.8471  -16.8660 C   0  0  0  1  0  0
  -11.5258    9.7990  -16.6569 C   0  0  0  1  0  0
  -10.7559    8.9358  -17.4240 C   0  0  0  1  0  0
  -11.3561    8.1244  -18.3845 C   0  0  0  1  0  0
  -10.9347   10.6433  -15.7371 O   0  0  0  1  0  0
  -10.9556   10.2317  -14.4070 C   0  0  0  1  0  0
  -10.6764   11.2091  -13.4619 C   0  0  0  1  0  0
  -10.6421   10.8987  -12.1100 C   0  0  0  1  0  0
  -10.8691    9.5954  -11.6951 C   0  0  0  1  0  0
  -11.1502    8.6069  -12.6291 C   0  0  0  1  0  0
  -11.2030    8.9228  -13.9818 C   0  0  0  1  0  0
  -16.2943    6.6185  -16.8405 H   0  0
  -14.6464    7.1076  -17.0279 H   0  0
  -17.7630    4.8372  -20.5962 H   0  0
  -13.2589    6.9761  -23.6811 H   0  0
  -15.3982    6.0167  -24.1782 H   0  0
  -14.9985    4.5096  -23.3580 H   0  0
  -14.4265    3.9680  -25.6183 H   0  0
  -13.7468    5.5695  -25.8845 H   0  0
  -12.5015    3.2664  -24.4079 H   0  0
  -11.7147    4.5137  -25.3667 H   0  0
  -11.3138    5.6926  -23.3690 H   0  0
  -12.1661    4.4394  -22.4922 H   0  0
  -11.8687    7.4281  -21.2513 H   0  0
  -14.5456    9.1336  -17.9948 H   0  0
  -13.4981   10.5321  -16.2855 H   0  0
   -9.6883    8.9087  -17.2662 H   0  0
  -10.7319    7.4608  -18.9691 H   0  0
  -10.4874   12.2189  -13.7924 H   0  0
  -10.4354   11.6725  -11.3851 H   0  0
  -10.8170    9.3618  -10.6446 H   0  0
  -11.3101    7.5879  -12.3113 H   0  0
  -11.3996    8.1274  -14.6844 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372049743020048

> <LigScore1_Dreiding>
1.67

> <LigScore2_Dreiding>
4.65

> <-PLP1>
70.89

> <-PLP2>
63.18

> <Jain>
1.27

> <-PMF>
42.83

> <-PMF04>
-2.51

> <AbsoluteEnergy>
149.211

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
23

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
3.163

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
38

> <LibDockScore>
104.021

> <HotSpots>
-19.20,4.92,-17.69,A,16,4
-16.20,4.32,-22.89,A,1,11
-12.40,7.52,-12.49,A,43,28

> <-In-Situ Starting Energy>
-307.738

> <-In-Situ Final Energy>
9.608

> <In-Situ Gradient>
0.169

> <Favorable A:LEU408>
4

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
0

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
0

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
0

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
1

> <Favorable A:CYS481>
1

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
1

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
0

> <Favorable A:PHE540>
0

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
3

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
0

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
0

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
0

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
1

> <Hydrophobic A:LEU528>
1

> <Hydrophobic A:PHE540>
0

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
1

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
1

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -19.4365    4.5262  -17.3423 N   0  0  0  1  0  0
  -18.3183    4.8977  -18.0045 C   0  0  0  1  0  0
  -18.3003    4.6678  -19.3254 N   0  0  0  1  0  0
  -17.2429    5.0667  -20.0506 C   0  0  0  1  0  0
  -16.1592    5.6475  -19.5416 N   0  0  0  1  0  0
  -16.1542    5.8297  -18.2148 C   0  0  0  1  0  0
  -17.2416    5.4702  -17.3864 C   0  0  0  1  0  0
  -15.1413    6.3584  -17.4242 N   0  0  0  1  0  0
  -13.8204    6.7669  -17.9460 C   0  0  0  1  0  0
  -12.8115    7.2107  -16.8871 C   0  0  0  1  0  0
  -11.7308    7.9218  -17.6993 C   0  0  0  1  0  0
  -12.4660    8.5706  -18.8812 C   0  0  0  1  0  0
  -13.8728    7.9531  -18.9137 C   0  0  0  1  0  0
  -15.6411    6.3733  -16.1727 C   0  0  0  1  0  0
  -16.9062    5.8205  -16.0655 C   0  0  0  1  0  0
  -17.6917    5.6950  -14.8127 C   0  0  0  1  0  0
  -18.9659    6.1956  -14.7341 C   0  0  0  1  0  0
  -19.4807    6.5931  -13.5203 C   0  0  0  1  0  0
  -18.8450    6.2541  -12.3477 C   0  0  0  1  0  0
  -17.7895    5.3710  -12.4437 C   0  0  0  1  0  0
  -17.1528    5.1601  -13.6670 C   0  0  0  1  0  0
  -19.0427    6.8745  -11.1260 O   0  0  0  1  0  0
  -20.2939    6.9204  -10.5398 C   0  0  0  1  0  0
  -20.2777    6.5964   -9.1987 C   0  0  0  1  0  0
  -21.4519    6.5578   -8.4770 C   0  0  0  1  0  0
  -22.6593    6.8758   -9.0806 C   0  0  0  1  0  0
  -22.6828    7.2357  -10.4172 C   0  0  0  1  0  0
  -21.5007    7.2912  -11.1371 C   0  0  0  1  0  0
  -20.2931    4.2817  -17.8001 H   0  0
  -19.4490    4.4637  -16.3441 H   0  0
  -17.2551    4.8872  -21.1153 H   0  0
  -13.3879    5.9104  -18.4680 H   0  0
  -12.4131    6.3782  -16.3076 H   0  0
  -13.2669    7.9204  -16.1960 H   0  0
  -11.1700    8.6430  -17.1038 H   0  0
  -11.0207    7.1845  -18.0766 H   0  0
  -12.5251    9.6514  -18.7556 H   0  0
  -11.9306    8.3783  -19.8118 H   0  0
  -14.1697    7.6497  -19.9182 H   0  0
  -14.6026    8.6849  -18.5645 H   0  0
  -15.1048    6.7749  -15.3261 H   0  0
  -19.5769    6.3561  -15.6025 H   0  0
  -20.2886    7.2835  -13.5528 H   0  0
  -17.4367    4.9476  -11.5242 H   0  0
  -16.2113    4.6344  -13.7155 H   0  0
  -19.3382    6.3500   -8.7280 H   0  0
  -21.4087    6.2311   -7.4541 H   0  0
  -23.5798    6.8429   -8.5165 H   0  0
  -23.6189    7.4747  -10.9017 H   0  0
  -21.5829    7.6470  -12.1448 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372054037987344

> <LigScore1_Dreiding>
3.62

> <LigScore2_Dreiding>
5.81

> <-PLP1>
108.97

> <-PLP2>
105.52

> <Jain>
8.4

> <-PMF>
108.44

> <-PMF04>
38.63

> <AbsoluteEnergy>
150.049

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
31

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
4.002

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
39

> <LibDockScore>
102.832

> <HotSpots>
-18.00,4.72,-19.09,A,9,4
-16.20,6.52,-15.49,A,24,14
-20.80,8.12,-10.89,P,69,22

> <-In-Situ Starting Energy>
-1171.203

> <-In-Situ Final Energy>
3.909

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
1

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
2

> <Favorable A:ALA428>
3

> <Favorable A:LYS430>
1

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
1

> <Favorable A:ILE472>
1

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
1

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
2

> <Favorable A:CYS481>
0

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
2

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
0

> <Favorable A:PHE540>
1

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
1

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
2

> <Hydrophobic A:ALA428>
3

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
1

> <Hydrophobic A:ILE472>
1

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
2

> <Hydrophobic A:PHE540>
1

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
1

> <HydrogenBond A:MET477>
2

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -15.2891    8.1022  -13.4713 N   0  0  0  1  0  0
  -15.3315    7.4900  -14.6749 C   0  0  0  1  0  0
  -14.4249    7.9259  -15.5633 N   0  0  0  1  0  0
  -14.4355    7.4171  -16.8062 C   0  0  0  1  0  0
  -15.3197    6.5227  -17.2440 N   0  0  0  1  0  0
  -16.2126    6.0727  -16.3472 C   0  0  0  1  0  0
  -16.2326    6.5077  -15.0094 C   0  0  0  1  0  0
  -17.2886    5.1938  -16.5144 N   0  0  0  1  0  0
  -17.8926    4.7641  -17.7634 C   0  0  0  1  0  0
  -18.3222    6.0425  -18.4168 C   0  0  0  1  0  0
  -17.5123    6.1743  -19.6951 C   0  0  0  1  0  0
  -17.3185    4.7390  -20.1103 C   0  0  0  1  0  0
  -17.0208    4.0700  -18.7598 C   0  0  0  1  0  0
  -17.7690    4.9360  -15.3144 C   0  0  0  1  0  0
  -17.2542    5.7699  -14.3726 C   0  0  0  1  0  0
  -17.7809    5.8231  -13.0153 C   0  0  0  1  0  0
  -18.0417    4.6657  -12.3284 C   0  0  0  1  0  0
  -18.4663    4.7278  -11.0200 C   0  0  0  1  0  0
  -18.7369    5.9488  -10.4339 C   0  0  0  1  0  0
  -18.6246    7.0953  -11.1981 C   0  0  0  1  0  0
  -18.0746    7.0321  -12.4584 C   0  0  0  1  0  0
  -19.0573    6.0200   -9.1013 O   0  0  0  1  0  0
  -20.1276    6.8362   -8.8435 C   0  0  0  1  0  0
  -21.2607    6.8654   -9.6488 C   0  0  0  1  0  0
  -22.1750    7.8829   -9.4844 C   0  0  0  1  0  0
  -21.9462    8.8482   -8.5166 C   0  0  0  1  0  0
  -20.8570    8.7729   -7.6681 C   0  0  0  1  0  0
  -19.9828    7.7159   -7.7962 C   0  0  0  1  0  0
  -14.5810    8.7972  -13.3371 H   0  0
  -15.9727    7.8853  -12.7796 H   0  0
  -13.6803    7.7599  -17.4990 H   0  0
  -18.7783    4.1668  -17.5488 H   0  0
  -18.1175    6.9123  -17.8179 H   0  0
  -19.3943    5.9192  -18.4903 H   0  0
  -17.9494    6.8376  -20.4278 H   0  0
  -16.5362    6.6036  -19.4731 H   0  0
  -16.5438    4.6560  -20.8702 H   0  0
  -18.2347    4.3404  -20.5367 H   0  0
  -17.1969    2.9967  -18.7607 H   0  0
  -15.9949    4.2751  -18.4577 H   0  0
  -18.5240    4.1905  -15.1146 H   0  0
  -17.9114    3.6934  -12.7844 H   0  0
  -18.6015    3.8076  -10.4937 H   0  0
  -18.9495    8.0390  -10.8003 H   0  0
  -17.8994    7.9177  -13.0396 H   0  0
  -21.4145    6.1383  -10.4308 H   0  0
  -23.0398    7.9190  -10.1276 H   0  0
  -22.6348    9.6481   -8.3710 H   0  0
  -20.7238    9.5053   -6.8840 H   0  0
  -19.1583    7.5813   -7.1207 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372058332954640

> <LigScore1_Dreiding>
1.49

> <LigScore2_Dreiding>
3.57

> <-PLP1>
95.8

> <-PLP2>
98.5

> <Jain>
8.24

> <-PMF>
109.36

> <-PMF04>
34.06

> <AbsoluteEnergy>
157.761

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
48

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
11.714

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
40

> <LibDockScore>
100.696

> <HotSpots>
-17.20,4.12,-18.29,A,12,13
-18.80,5.32,-15.29,A,26,14
-20.00,7.52,-7.09,A,89,28

> <-In-Situ Starting Energy>
-1409.454

> <-In-Situ Final Energy>
-22.409

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
1

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
2

> <Favorable A:ALA428>
2

> <Favorable A:LYS430>
2

> <Favorable A:MET449>
1

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
1

> <Favorable A:THR474>
1

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
1

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
0

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
3

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
0

> <Favorable A:PHE540>
1

> <Favorable A:LEU542>
1

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
1

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
1

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
2

> <Hydrophobic A:ALA428>
2

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:MET449>
1

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
1

> <Hydrophobic A:TYR476>
1

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
3

> <Hydrophobic A:PHE540>
1

> <Hydrophobic A:LEU542>
1

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
1

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -17.5917    3.0908  -13.8959 N   0  0  0  1  0  0
  -18.1133    3.9297  -12.9794 C   0  0  0  1  0  0
  -18.1239    3.5013  -11.7151 N   0  0  0  1  0  0
  -18.3075    4.4193  -10.7585 C   0  0  0  1  0  0
  -18.8138    5.5942  -10.9155 N   0  0  0  1  0  0
  -19.1012    5.8951  -12.1544 C   0  0  0  1  0  0
  -18.6228    5.1591  -13.2533 C   0  0  0  1  0  0
  -19.9882    6.8420  -12.5644 N   0  0  0  1  0  0
  -20.9592    7.5386  -11.6479 C   0  0  0  1  0  0
  -20.4125    7.8878  -10.2503 C   0  0  0  1  0  0
  -21.6341    8.2584   -9.4272 C   0  0  0  1  0  0
  -22.5446    7.0876   -9.7899 C   0  0  0  1  0  0
  -22.3181    6.8823  -11.2938 C   0  0  0  1  0  0
  -19.7002    6.8950  -13.8882 C   0  0  0  1  0  0
  -18.8156    5.9427  -14.3733 C   0  0  0  1  0  0
  -18.1835    5.7582  -15.7051 C   0  0  0  1  0  0
  -16.8345    6.0283  -15.8320 C   0  0  0  1  0  0
  -16.1967    5.9687  -17.0648 C   0  0  0  1  0  0
  -16.9143    5.6586  -18.2148 C   0  0  0  1  0  0
  -18.2502    5.3095  -18.0664 C   0  0  0  1  0  0
  -18.8799    5.3473  -16.8231 C   0  0  0  1  0  0
  -16.3806    5.5872  -19.5010 O   0  0  0  1  0  0
  -15.2667    6.3331  -19.8948 C   0  0  0  1  0  0
  -14.8455    7.5358  -19.3224 C   0  0  0  1  0  0
  -13.7167    8.1886  -19.8026 C   0  0  0  1  0  0
  -13.0232    7.6751  -20.8892 C   0  0  0  1  0  0
  -13.4763    6.5206  -21.5094 C   0  0  0  1  0  0
  -14.5997    5.8668  -21.0206 C   0  0  0  1  0  0
  -17.3419    2.1681  -13.6089 H   0  0
  -17.4770    3.3837  -14.8439 H   0  0
  -18.0177    4.3213   -9.7453 H   0  0
  -21.2749    8.4548  -12.1319 H   0  0
  -19.5761    8.5606  -10.2971 H   0  0
  -20.0336    7.0404   -9.6933 H   0  0
  -21.4300    8.3208   -8.3578 H   0  0
  -22.0599    9.2047   -9.7562 H   0  0
  -23.5886    7.2430   -9.5329 H   0  0
  -22.2190    6.1963   -9.2519 H   0  0
  -22.4096    5.8360  -11.5596 H   0  0
  -23.1221    7.4129  -11.8015 H   0  0
  -20.1512    7.6294  -14.5019 H   0  0
  -16.2484    6.3016  -14.9660 H   0  0
  -15.1344    6.1561  -17.1019 H   0  0
  -18.7976    5.0262  -18.9460 H   0  0
  -19.9301    5.0973  -16.7540 H   0  0
  -15.3804    7.9886  -18.5046 H   0  0
  -13.3752    9.0940  -19.3242 H   0  0
  -12.1324    8.1671  -21.2538 H   0  0
  -12.9455    6.1224  -22.3624 H   0  0
  -14.9564    4.9743  -21.5105 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372062627921936

> <LigScore1_Dreiding>
1.97

> <LigScore2_Dreiding>
3.79

> <-PLP1>
94.08

> <-PLP2>
93

> <Jain>
7.2

> <-PMF>
64.37

> <-PMF04>
4.61

> <AbsoluteEnergy>
146.833

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
13

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
0.786

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
41

> <LibDockScore>
100.518

> <HotSpots>
-22.60,6.72,-9.09,A,69,12
-17.80,5.12,-16.89,A,19,20
-14.40,5.92,-18.29,A,15,24

> <-In-Situ Starting Energy>
-21891142

> <-In-Situ Final Energy>
-39.53

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
1

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
1

> <Favorable A:ALA428>
2

> <Favorable A:LYS430>
3

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
2

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
1

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
0

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
1

> <Favorable A:SER538>
2

> <Favorable A:ASP539>
0

> <Favorable A:PHE540>
1

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
1

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
1

> <Hydrophobic A:ALA428>
2

> <Hydrophobic A:LYS430>
2

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
2

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
1

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
1

> <Hydrophobic A:PHE540>
1

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
1

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
2

> <HydrogenBond A:ASP539>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -14.5492    8.8031  -14.0805 N   0  0  0  1  0  0
  -14.3705    8.5894  -15.4007 C   0  0  0  1  0  0
  -13.4437    9.3794  -15.9643 N   0  0  0  1  0  0
  -13.1563    9.2251  -17.2611 C   0  0  0  1  0  0
  -13.7288    8.3221  -18.0490 N   0  0  0  1  0  0
  -14.6564    7.5254  -17.4928 C   0  0  0  1  0  0
  -15.0517    7.6436  -16.1371 C   0  0  0  1  0  0
  -15.3538    6.4647  -18.0684 N   0  0  0  1  0  0
  -15.1252    5.8995  -19.4139 C   0  0  0  1  0  0
  -14.2127    6.6485  -20.3884 C   0  0  0  1  0  0
  -14.4671    5.9822  -21.7408 C   0  0  0  1  0  0
  -15.8878    5.4044  -21.6701 C   0  0  0  1  0  0
  -16.3913    5.6299  -20.2313 C   0  0  0  1  0  0
  -16.2137    6.0463  -17.1207 C   0  0  0  1  0  0
  -16.0851    6.6953  -15.9054 C   0  0  0  1  0  0
  -16.8707    6.4086  -14.6674 C   0  0  0  1  0  0
  -17.2582    5.1154  -14.3513 C   0  0  0  1  0  0
  -17.9453    4.8298  -13.1700 C   0  0  0  1  0  0
  -18.2346    5.8391  -12.2623 C   0  0  0  1  0  0
  -17.8632    7.1321  -12.5936 C   0  0  0  1  0  0
  -17.2397    7.4165  -13.7996 C   0  0  0  1  0  0
  -18.7918    5.5349  -11.0228 O   0  0  0  1  0  0
  -19.6625    6.4709  -10.4637 C   0  0  0  1  0  0
  -20.7088    7.0440  -11.1872 C   0  0  0  1  0  0
  -21.6145    7.8905  -10.5611 C   0  0  0  1  0  0
  -21.4667    8.1916   -9.2132 C   0  0  0  1  0  0
  -20.4079    7.6488   -8.4961 C   0  0  0  1  0  0
  -19.5164    6.7848   -9.1193 C   0  0  0  1  0  0
  -14.0977    9.5940  -13.6660 H   0  0
  -15.1198    8.1947  -13.5390 H   0  0
  -12.4093    9.8757  -17.6929 H   0  0
  -14.6439    4.9493  -19.2072 H   0  0
  -13.1614    6.6044  -20.1001 H   0  0
  -14.5013    7.6978  -20.4428 H   0  0
  -14.3449    6.6810  -22.5682 H   0  0
  -13.7472    5.1797  -21.8973 H   0  0
  -16.5319    5.8762  -22.4081 H   0  0
  -15.8730    4.3437  -21.9158 H   0  0
  -16.9618    4.7796  -19.8575 H   0  0
  -17.0592    6.4889  -20.1834 H   0  0
  -16.9338    5.2597  -17.2974 H   0  0
  -17.0328    4.2929  -15.0143 H   0  0
  -18.2460    3.8162  -12.9450 H   0  0
  -18.0523    7.9190  -11.8929 H   0  0
  -17.0518    8.4532  -14.0387 H   0  0
  -20.8412    6.8092  -12.2340 H   0  0
  -22.4383    8.3040  -11.1249 H   0  0
  -22.1748    8.8456   -8.7231 H   0  0
  -20.2770    7.8951   -7.4528 H   0  0
  -18.7029    6.3492   -8.5609 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372066922889232

> <LigScore1_Dreiding>
2.51

> <LigScore2_Dreiding>
5.8

> <-PLP1>
100.25

> <-PLP2>
93.13

> <Jain>
4.96

> <-PMF>
114.73

> <-PMF04>
42.33

> <AbsoluteEnergy>
149.211

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
23

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
3.163

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
42

> <LibDockScore>
99.859

> <HotSpots>
-14.40,7.72,-18.49,A,11,13
-17.20,7.52,-13.09,A,39,21
-21.60,6.52,-10.49,A,59,24

> <-In-Situ Starting Energy>
-304.276

> <-In-Situ Final Energy>
19.637

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
1

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
3

> <Favorable A:ALA428>
1

> <Favorable A:LYS430>
2

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
1

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
1

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
2

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
0

> <Favorable A:PHE540>
1

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
1

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
1

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
1

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
3

> <Hydrophobic A:ALA428>
1

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
1

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
1

> <Hydrophobic A:LEU528>
2

> <Hydrophobic A:PHE540>
1

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -14.1634    7.8379  -13.5214 N   0  0  0  1  0  0
  -14.0742    7.9824  -14.8620 C   0  0  0  1  0  0
  -13.0290    8.7068  -15.2898 N   0  0  0  1  0  0
  -12.8342    8.8444  -16.6098 C   0  0  0  1  0  0
  -13.6136    8.3049  -17.5459 N   0  0  0  1  0  0
  -14.6557    7.5751  -17.1148 C   0  0  0  1  0  0
  -14.9565    7.4113  -15.7476 C   0  0  0  1  0  0
  -15.5942    6.8684  -17.8636 N   0  0  0  1  0  0
  -15.5662    6.8110  -19.3369 C   0  0  0  1  0  0
  -16.6219    5.9078  -19.9966 C   0  0  0  1  0  0
  -16.0312    5.4855  -21.3572 C   0  0  0  1  0  0
  -14.5504    5.8752  -21.3218 C   0  0  0  1  0  0
  -14.2521    6.2653  -19.8733 C   0  0  0  1  0  0
  -16.4464    6.3257  -16.9676 C   0  0  0  1  0  0
  -16.1507    6.6590  -15.6577 C   0  0  0  1  0  0
  -16.9305    6.3229  -14.4377 C   0  0  0  1  0  0
  -17.3757    5.0408  -14.1682 C   0  0  0  1  0  0
  -18.0769    4.7581  -12.9936 C   0  0  0  1  0  0
  -18.3501    5.7644  -12.0740 C   0  0  0  1  0  0
  -17.9315    7.0501  -12.3759 C   0  0  0  1  0  0
  -17.2364    7.3248  -13.5411 C   0  0  0  1  0  0
  -18.9448    5.4673  -10.8504 O   0  0  0  1  0  0
  -19.7773    6.4415  -10.2995 C   0  0  0  1  0  0
  -20.8248    7.0156  -11.0196 C   0  0  0  1  0  0
  -21.6869    7.9150  -10.4069 C   0  0  0  1  0  0
  -21.4928    8.2685   -9.0778 C   0  0  0  1  0  0
  -20.4278    7.7285   -8.3680 C   0  0  0  1  0  0
  -19.5806    6.8114   -8.9762 C   0  0  0  1  0  0
  -13.5291    8.3881  -12.9792 H   0  0
  -14.8308    7.1961  -13.1475 H   0  0
  -11.9874    9.4324  -16.9347 H   0  0
  -15.6704    7.8364  -19.6857 H   0  0
  -17.5854    6.4070  -20.0963 H   0  0
  -16.7823    5.0117  -19.3975 H   0  0
  -16.1756    4.4243  -21.5449 H   0  0
  -16.5146    5.9815  -22.1950 H   0  0
  -13.8969    5.0918  -21.6985 H   0  0
  -14.3903    6.7426  -21.9622 H   0  0
  -13.4283    6.9760  -19.8057 H   0  0
  -13.9978    5.4049  -19.2608 H   0  0
  -17.2890    5.7053  -17.2383 H   0  0
  -17.1844    4.2352  -14.8625 H   0  0
  -18.4133    3.7509  -12.7918 H   0  0
  -18.1426    7.8448  -11.6915 H   0  0
  -16.9470    8.3494  -13.7343 H   0  0
  -20.9885    6.7474  -12.0537 H   0  0
  -22.5124    8.3285  -10.9673 H   0  0
  -22.1682    8.9627   -8.5974 H   0  0
  -20.2560    8.0203   -7.3425 H   0  0
  -18.7599    6.3821   -8.4242 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372071217856528

> <LigScore1_Dreiding>
2.59

> <LigScore2_Dreiding>
5.65

> <-PLP1>
98.55

> <-PLP2>
92.85

> <Jain>
5.83

> <-PMF>
116.02

> <-PMF04>
42.86

> <AbsoluteEnergy>
150.049

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
31

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
4.002

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
43

> <LibDockScore>
99.229

> <HotSpots>
-15.60,6.12,-19.69,A,6,13
-18.60,7.12,-11.89,A,46,20
-22.60,6.72,-9.09,A,69,26

> <-In-Situ Starting Energy>
-435.791

> <-In-Situ Final Energy>
20.08

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
1

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
3

> <Favorable A:ALA428>
1

> <Favorable A:LYS430>
2

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
1

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
0

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
1

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
0

> <Favorable A:PHE540>
1

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
1

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
1

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
3

> <Hydrophobic A:ALA428>
1

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
1

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
1

> <Hydrophobic A:PHE540>
1

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -16.7512    5.2545  -15.5537 N   0  0  0  1  0  0
  -17.2284    4.7841  -14.3828 C   0  0  0  1  0  0
  -17.3866    3.4548  -14.2671 N   0  0  0  1  0  0
  -18.0212    2.9785  -13.1818 C   0  0  0  1  0  0
  -18.3906    3.7317  -12.1494 N   0  0  0  1  0  0
  -18.2793    5.0503  -12.2907 C   0  0  0  1  0  0
  -17.5762    5.6213  -13.3649 C   0  0  0  1  0  0
  -18.7961    6.0782  -11.5056 N   0  0  0  1  0  0
  -19.7258    5.9305  -10.3578 C   0  0  0  1  0  0
  -19.1887    6.6421   -9.1050 C   0  0  0  1  0  0
  -20.0931    7.8473   -8.9874 C   0  0  0  1  0  0
  -21.4699    7.3596   -9.3588 C   0  0  0  1  0  0
  -21.1485    6.5254  -10.5893 C   0  0  0  1  0  0
  -18.2513    7.1866  -12.0200 C   0  0  0  1  0  0
  -17.3845    6.9806  -13.0786 C   0  0  0  1  0  0
  -16.4033    7.8892  -13.7398 C   0  0  0  1  0  0
  -15.0694    7.5258  -13.6844 C   0  0  0  1  0  0
  -14.0820    8.2758  -14.3105 C   0  0  0  1  0  0
  -14.4191    9.4249  -15.0130 C   0  0  0  1  0  0
  -15.7445    9.8329  -15.0208 C   0  0  0  1  0  0
  -16.7275    9.0529  -14.4133 C   0  0  0  1  0  0
  -13.4662   10.1392  -15.7227 O   0  0  0  1  0  0
  -12.7583    9.3891  -16.6561 C   0  0  0  1  0  0
  -11.3869    9.5819  -16.7553 C   0  0  0  1  0  0
  -10.6404    8.8627  -17.6809 C   0  0  0  1  0  0
  -11.2659    7.9485  -18.5194 C   0  0  0  1  0  0
  -12.6382    7.7580  -18.4328 C   0  0  0  1  0  0
  -13.3844    8.4795  -17.5091 C   0  0  0  1  0  0
  -16.6103    4.6187  -16.3099 H   0  0
  -16.5464    6.2242  -15.6823 H   0  0
  -18.2424    1.9229  -13.1252 H   0  0
  -19.8297    4.8718  -10.1799 H   0  0
  -18.1350    6.9140   -9.1707 H   0  0
  -19.3248    6.0573   -8.2026 H   0  0
  -20.0348    8.3734   -8.0341 H   0  0
  -19.8089    8.4781   -9.8149 H   0  0
  -22.1690    8.1702   -9.5684 H   0  0
  -21.8851    6.7412   -8.5616 H   0  0
  -21.9378    5.7846  -10.7065 H   0  0
  -21.1566    7.1553  -11.4804 H   0  0
  -18.5149    8.0900  -11.5343 H   0  0
  -14.7677    6.6324  -13.1567 H   0  0
  -13.0508    7.9549  -14.2745 H   0  0
  -16.0105   10.7376  -15.5489 H   0  0
  -17.7463    9.3614  -14.5519 H   0  0
  -10.9019   10.2880  -16.0978 H   0  0
   -9.5738    9.0196  -17.7472 H   0  0
  -10.6913    7.3884  -19.2455 H   0  0
  -13.1240    7.0506  -19.0894 H   0  0
  -14.4529    8.3306  -17.4670 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372075512823824

> <LigScore1_Dreiding>
1.6

> <LigScore2_Dreiding>
4.32

> <-PLP1>
88.08

> <-PLP2>
80.91

> <Jain>
5.17

> <-PMF>
102.19

> <-PMF04>
28.5

> <AbsoluteEnergy>
155.445

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
46

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
9.398

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
50

> <LibDockScore>
96.102

> <HotSpots>
-18.40,2.92,-12.29,P,54,3
-21.60,7.92,-9.29,A,66,11
-12.60,6.32,-17.69,A,17,27

> <-In-Situ Starting Energy>
-718.586

> <-In-Situ Final Energy>
-6.263

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
0

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
2

> <Favorable A:ALA428>
2

> <Favorable A:LYS430>
4

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
2

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
0

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
1

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
2

> <Favorable A:PHE540>
0

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
2

> <Charge A:ASP539>
1

> <Hydrophobic A:LEU408>
0

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
2

> <Hydrophobic A:ALA428>
1

> <Hydrophobic A:LYS430>
2

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
1

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
1

> <Hydrophobic A:PHE540>
0

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
1

> <HydrogenBond A:LYS430>
1

> <HydrogenBond A:ILE472>
1

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
1

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -14.6000    7.7023  -13.5374 N   0  0  0  1  0  0
  -14.7758    7.5938  -14.8717 C   0  0  0  1  0  0
  -13.8383    8.1687  -15.6390 N   0  0  0  1  0  0
  -13.9281    8.0339  -16.9713 C   0  0  0  1  0  0
  -14.9232    7.4096  -17.6013 N   0  0  0  1  0  0
  -15.8796    6.8586  -16.8358 C   0  0  0  1  0  0
  -15.8289    6.9168  -15.4267 C   0  0  0  1  0  0
  -17.0599    6.1904  -17.1833 N   0  0  0  1  0  0
  -17.6807    5.9939  -18.4896 C   0  0  0  1  0  0
  -17.0277    6.5606  -19.7450 C   0  0  0  1  0  0
  -16.5370    5.3856  -20.5404 C   0  0  0  1  0  0
  -17.5522    4.3154  -20.1543 C   0  0  0  1  0  0
  -17.8655    4.5055  -18.6988 C   0  0  0  1  0  0
  -17.5917    5.7501  -16.0445 C   0  0  0  1  0  0
  -16.9546    6.2262  -14.9398 C   0  0  0  1  0  0
  -17.4590    6.0516  -13.5755 C   0  0  0  1  0  0
  -17.7413    4.8056  -13.0619 C   0  0  0  1  0  0
  -18.2734    4.6841  -11.7856 C   0  0  0  1  0  0
  -18.6291    5.8182  -11.0761 C   0  0  0  1  0  0
  -18.3842    7.0603  -11.6317 C   0  0  0  1  0  0
  -17.7270    7.1741  -12.8382 C   0  0  0  1  0  0
  -19.1504    5.6882   -9.8106 O   0  0  0  1  0  0
  -20.0600    6.6511   -9.4186 C   0  0  0  1  0  0
  -21.1743    6.9615  -10.1894 C   0  0  0  1  0  0
  -22.0321    7.9669   -9.7865 C   0  0  0  1  0  0
  -21.7714    8.6741   -8.6216 C   0  0  0  1  0  0
  -20.6601    8.3633   -7.8517 C   0  0  0  1  0  0
  -19.8261    7.3250   -8.2325 C   0  0  0  1  0  0
  -13.8730    8.3175  -13.2313 H   0  0
  -15.1943    7.1635  -12.9439 H   0  0
  -13.1423    8.4654  -17.5750 H   0  0
  -18.6657    6.4372  -18.4103 H   0  0
  -16.2393    7.2862  -19.5772 H   0  0
  -17.8123    7.0542  -20.3152 H   0  0
  -16.5032    5.5730  -21.6139 H   0  0
  -15.5226    5.1880  -20.2028 H   0  0
  -17.2181    3.3164  -20.2629 H   0  0
  -18.4371    4.4088  -20.7585 H   0  0
  -18.8649    4.1650  -18.4284 H   0  0
  -17.1469    3.9312  -18.1107 H   0  0
  -18.4646    5.1118  -16.0027 H   0  0
  -17.5542    3.9105  -13.6394 H   0  0
  -18.4427    3.7087  -11.3547 H   0  0
  -18.7148    7.9435  -11.1234 H   0  0
  -17.4918    8.1503  -13.2354 H   0  0
  -21.3783    6.4379  -11.1094 H   0  0
  -22.8948    8.1814  -10.3946 H   0  0
  -22.4398    9.4543   -8.2956 H   0  0
  -20.4591    8.9148   -6.9443 H   0  0
  -18.9747    7.0539   -7.6282 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372079807791120

> <LigScore1_Dreiding>
1.86

> <LigScore2_Dreiding>
4.32

> <-PLP1>
97.68

> <-PLP2>
98.05

> <Jain>
8

> <-PMF>
114.5

> <-PMF04>
36.8

> <AbsoluteEnergy>
164.245

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
52

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
18.198

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
52

> <LibDockScore>
95.987

> <HotSpots>
-14.40,7.72,-18.49,A,11,4
-17.80,5.12,-16.89,A,19,14
-19.80,7.72,-8.89,A,70,28

> <-In-Situ Starting Energy>
-413.447

> <-In-Situ Final Energy>
-7.645

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
1

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
2

> <Favorable A:ALA428>
2

> <Favorable A:LYS430>
2

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
0

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
1

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
0

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
3

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
0

> <Favorable A:PHE540>
1

> <Favorable A:LEU542>
1

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
1

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
1

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
2

> <Hydrophobic A:ALA428>
2

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
0

> <Hydrophobic A:TYR476>
1

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
3

> <Hydrophobic A:PHE540>
1

> <Hydrophobic A:LEU542>
1

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -10.1483    7.9424  -11.7676 N   0  0  0  1  0  0
  -10.9305    8.0891  -12.8497 C   0  0  0  1  0  0
  -10.7735    7.1444  -13.7883 N   0  0  0  1  0  0
  -11.4839    7.2303  -14.9224 C   0  0  0  1  0  0
  -12.4309    8.1333  -15.1386 N   0  0  0  1  0  0
  -12.6295    9.0319  -14.1648 C   0  0  0  1  0  0
  -11.8515    9.0937  -12.9936 C   0  0  0  1  0  0
  -13.6281    9.9858  -14.0866 N   0  0  0  1  0  0
  -14.7127   10.0436  -15.0879 C   0  0  0  1  0  0
  -15.5592    8.7721  -14.9049 C   0  0  0  1  0  0
  -16.6534    9.1776  -13.9320 C   0  0  0  1  0  0
  -16.9620   10.6372  -14.2728 C   0  0  0  1  0  0
  -15.6943   11.2111  -14.9100 C   0  0  0  1  0  0
  -13.3609   10.7035  -12.9720 C   0  0  0  1  0  0
  -12.2807   10.2185  -12.2493 C   0  0  0  1  0  0
  -11.7421   10.7526  -10.9664 C   0  0  0  1  0  0
  -12.6100   11.0639   -9.9398 C   0  0  0  1  0  0
  -12.1494   11.4628   -8.6941 C   0  0  0  1  0  0
  -10.7937   11.5974   -8.4591 C   0  0  0  1  0  0
   -9.9079   11.3614   -9.5109 C   0  0  0  1  0  0
  -10.3876   10.9423  -10.7530 C   0  0  0  1  0  0
  -10.4058   11.8607   -7.1544 O   0  0  0  1  0  0
   -9.3353   12.7135   -6.9386 C   0  0  0  1  0  0
   -9.1123   13.8625   -7.6946 C   0  0  0  1  0  0
   -8.0403   14.6924   -7.3955 C   0  0  0  1  0  0
   -7.2052   14.3874   -6.3296 C   0  0  0  1  0  0
   -7.4493   13.2659   -5.5507 C   0  0  0  1  0  0
   -8.5104   12.4289   -5.8602 C   0  0  0  1  0  0
   -9.4969    7.1836  -11.7613 H   0  0
  -10.2126    8.5680  -10.9930 H   0  0
  -11.2910    6.5079  -15.7021 H   0  0
  -14.2627   10.0863  -16.0815 H   0  0
  -15.0080    7.9064  -14.5395 H   0  0
  -15.9921    8.4563  -15.8465 H   0  0
  -17.5103    8.5112  -14.0198 H   0  0
  -16.2772    9.1170  -12.9107 H   0  0
  -17.2567   11.2163  -13.3966 H   0  0
  -17.7729   10.6779  -14.9984 H   0  0
  -15.9400   11.6448  -15.8804 H   0  0
  -15.2772   12.0207  -14.3145 H   0  0
  -13.9351   11.5651  -12.6569 H   0  0
  -13.6738   10.9971  -10.0734 H   0  0
  -12.8477   11.6564   -7.8928 H   0  0
   -8.8452   11.4720   -9.3563 H   0  0
   -9.6837   10.7598  -11.5533 H   0  0
   -9.7760   14.1296   -8.5029 H   0  0
   -7.8646   15.5826   -7.9808 H   0  0
   -6.3699   15.0280   -6.0918 H   0  0
   -6.8113   13.0498   -4.7050 H   0  0
   -8.7104   11.5589   -5.2532 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372084102758416

> <LigScore1_Dreiding>
2.76

> <LigScore2_Dreiding>
5.13

> <-PLP1>
84.08

> <-PLP2>
80.06

> <Jain>
4.03

> <-PMF>
108.98

> <-PMF04>
40.86

> <AbsoluteEnergy>
152.006

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
37

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
5.959

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
53

> <LibDockScore>
95.601

> <HotSpots>
-11.40,6.12,-12.49,P,51,3
-16.80,9.32,-14.09,A,31,11
-12.00,11.32,-8.69,A,74,18

> <-In-Situ Starting Energy>
-210.905

> <-In-Situ Final Energy>
13.188

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
0

> <Favorable A:THR410>
1

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
1

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
1

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
2

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
0

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
0

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
1

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
1

> <Favorable A:PHE540>
0

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
1

> <Favorable A:TYR551>
1

> <Favorable A:LYS558>
1

> <Unfavorable A:GLY414>
1

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
2

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
0

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
1

> <Hydrophobic A:VAL416>
1

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
0

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
0

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
1

> <Hydrophobic A:PHE540>
0

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
1

> <Hydrophobic A:TYR551>
1

> <Hydrophobic A:LYS558>
1

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
1

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
1

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
   -8.6642   11.3160  -12.7936 N   0  0  0  1  0  0
   -9.0033   11.5348  -11.5027 C   0  0  0  1  0  0
   -7.9670   11.7066  -10.6537 N   0  0  0  1  0  0
   -8.2295   12.0922   -9.3924 C   0  0  0  1  0  0
   -9.4490   12.1713   -8.8699 N   0  0  0  1  0  0
  -10.4783   11.9477   -9.6997 C   0  0  0  1  0  0
  -10.3036   11.5938  -11.0599 C   0  0  0  1  0  0
  -11.8394   12.0327   -9.4318 N   0  0  0  1  0  0
  -12.4322   12.4237   -8.1362 C   0  0  0  1  0  0
  -13.2115   13.7307   -8.3128 C   0  0  0  1  0  0
  -14.6753   13.3397   -8.4770 C   0  0  0  1  0  0
  -14.8205   12.0915   -7.6117 C   0  0  0  1  0  0
  -13.4568   11.3884   -7.6367 C   0  0  0  1  0  0
  -12.4512   11.7175  -10.5849 C   0  0  0  1  0  0
  -11.5919   11.3986  -11.6179 C   0  0  0  1  0  0
  -12.0175   10.9562  -12.9753 C   0  0  0  1  0  0
  -13.1185   11.5439  -13.5733 C   0  0  0  1  0  0
  -13.5759   11.1161  -14.8145 C   0  0  0  1  0  0
  -12.9323   10.0902  -15.4931 C   0  0  0  1  0  0
  -11.8149    9.5050  -14.8969 C   0  0  0  1  0  0
  -11.3673    9.9412  -13.6533 C   0  0  0  1  0  0
  -13.4798    9.6633  -16.7000 O   0  0  0  1  0  0
  -12.6062    9.1192  -17.6298 C   0  0  0  1  0  0
  -11.4848    9.8176  -18.0684 C   0  0  0  1  0  0
  -10.6362    9.2530  -19.0127 C   0  0  0  1  0  0
  -10.9192    7.9977  -19.5349 C   0  0  0  1  0  0
  -12.0485    7.3077  -19.1134 C   0  0  0  1  0  0
  -12.8933    7.8710  -18.1661 C   0  0  0  1  0  0
   -7.7036   11.2196  -13.0482 H   0  0
   -9.3533   11.2482  -13.5161 H   0  0
   -7.3960   12.3535   -8.7533 H   0  0
  -11.6422   12.5675   -7.3965 H   0  0
  -12.8447   14.3565   -9.1268 H   0  0
  -13.1077   14.2998   -7.3978 H   0  0
  -15.3541   14.1399   -8.1787 H   0  0
  -14.8884   13.1025   -9.5192 H   0  0
  -15.6219   11.4516   -7.9737 H   0  0
  -15.0591   12.3873   -6.5900 H   0  0
  -13.1930   11.0172   -6.6455 H   0  0
  -13.4974   10.5233   -8.2959 H   0  0
  -13.5258   11.7126  -10.6878 H   0  0
  -13.6558   12.3501  -13.0879 H   0  0
  -14.4441   11.5840  -15.2584 H   0  0
  -11.2892    8.6898  -15.3744 H   0  0
  -10.5152    9.4377  -13.2181 H   0  0
  -11.2737   10.8002  -17.6730 H   0  0
   -9.7579    9.7873  -19.3448 H   0  0
  -10.2635    7.5499  -20.2709 H   0  0
  -12.2635    6.3332  -19.5280 H   0  0
  -13.7714    7.3366  -17.8364 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372088397725712

> <LigScore1_Dreiding>
2.43

> <LigScore2_Dreiding>
4.77

> <-PLP1>
65.68

> <-PLP2>
58.94

> <Jain>
0.86

> <-PMF>
72.92

> <-PMF04>
27.51

> <AbsoluteEnergy>
151.939

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
36

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
5.892

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
59

> <LibDockScore>
93.559

> <HotSpots>
-14.00,11.52,-7.09,A,94,13
-11.00,6.92,-12.09,A,44,20
-12.60,6.32,-17.69,A,17,27

> <-In-Situ Starting Energy>
-1334.716

> <-In-Situ Final Energy>
20.35

> <In-Situ Gradient>
0.397

> <Favorable A:LEU408>
0

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
1

> <Favorable A:PHE413>
2

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
0

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
0

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
0

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
1

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
0

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
1

> <Favorable A:PHE540>
0

> <Favorable A:LEU542>
1

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
1

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
0

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
2

> <Hydrophobic A:VAL416>
0

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
0

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
0

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
1

> <Hydrophobic A:LEU528>
0

> <Hydrophobic A:PHE540>
0

> <Hydrophobic A:LEU542>
1

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
1

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
1

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
1

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -14.0639    7.7496  -13.1724 N   0  0  0  1  0  0
  -14.1653    7.9284  -14.5064 C   0  0  0  1  0  0
  -13.1690    8.6119  -15.0900 N   0  0  0  1  0  0
  -13.1448    8.6994  -16.4310 C   0  0  0  1  0  0
  -14.0542    8.1559  -17.2427 N   0  0  0  1  0  0
  -15.0614    7.4964  -16.6482 C   0  0  0  1  0  0
  -15.1846    7.3911  -15.2453 C   0  0  0  1  0  0
  -16.1150    6.7898  -17.2233 N   0  0  0  1  0  0
  -16.2830    6.5213  -18.6531 C   0  0  0  1  0  0
  -15.7516    5.1325  -18.8573 C   0  0  0  1  0  0
  -16.9267    4.2042  -18.4532 C   0  0  0  1  0  0
  -18.1250    4.8803  -19.0570 C   0  0  0  1  0  0
  -17.7446    6.3499  -19.0930 C   0  0  0  1  0  0
  -16.8802    6.3802  -16.2097 C   0  0  0  1  0  0
  -16.3877    6.7031  -14.9780 C   0  0  0  1  0  0
  -17.0763    6.3660  -13.7196 C   0  0  0  1  0  0
  -17.4354    5.0620  -13.4437 C   0  0  0  1  0  0
  -18.1627    4.7539  -12.2994 C   0  0  0  1  0  0
  -18.5878    5.7628  -11.4498 C   0  0  0  1  0  0
  -18.2436    7.0695  -11.7607 C   0  0  0  1  0  0
  -17.4361    7.3623  -12.8473 C   0  0  0  1  0  0
  -19.2986    5.4308  -10.3063 O   0  0  0  1  0  0
  -20.0960    6.4333   -9.7748 C   0  0  0  1  0  0
  -21.2094    6.9002  -10.4639 C   0  0  0  1  0  0
  -21.9837    7.9125   -9.9259 C   0  0  0  1  0  0
  -21.6408    8.4807   -8.7071 C   0  0  0  1  0  0
  -20.5150    8.0328   -8.0285 C   0  0  0  1  0  0
  -19.7530    6.9992   -8.5548 C   0  0  0  1  0  0
  -13.3977    8.3260  -12.6976 H   0  0
  -14.6296    7.0379  -12.7575 H   0  0
  -12.3299    9.2472  -16.8831 H   0  0
  -15.7429    7.2592  -19.2503 H   0  0
  -14.8219    4.9274  -18.3244 H   0  0
  -15.5390    5.1274  -19.9261 H   0  0
  -16.9369    3.1732  -18.7777 H   0  0
  -17.0088    4.1376  -17.3733 H   0  0
  -18.2639    4.5194  -20.0764 H   0  0
  -19.0297    4.6899  -18.4779 H   0  0
  -18.4298    6.8675  -18.4404 H   0  0
  -17.8549    6.7423  -20.1033 H   0  0
  -17.8104    5.8447  -16.3387 H   0  0
  -17.1630    4.2581  -14.1138 H   0  0
  -18.4175    3.7273  -12.0819 H   0  0
  -18.6179    7.8727  -11.1586 H   0  0
  -17.1560    8.3884  -13.0416 H   0  0
  -21.4791    6.4908  -11.4248 H   0  0
  -22.8510    8.2421  -10.4722 H   0  0
  -22.2511    9.2656   -8.2840 H   0  0
  -20.2342    8.4863   -7.0889 H   0  0
  -18.8770    6.6493   -8.0321 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372092692693008

> <LigScore1_Dreiding>
2.08

> <LigScore2_Dreiding>
4.57

> <-PLP1>
88.98

> <-PLP2>
88.32

> <Jain>
6.71

> <-PMF>
113.51

> <-PMF04>
40.98

> <AbsoluteEnergy>
149.96

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
29

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
3.913

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
60

> <LibDockScore>
93.299

> <HotSpots>
-18.60,3.92,-18.69,A,10,11
-18.60,7.12,-11.89,A,46,20
-20.40,8.32,-7.89,A,83,27

> <-In-Situ Starting Energy>
-377.287

> <-In-Situ Final Energy>
-2.619

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
1

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
3

> <Favorable A:ALA428>
1

> <Favorable A:LYS430>
2

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
1

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
0

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
2

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
0

> <Favorable A:PHE540>
1

> <Favorable A:LEU542>
1

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
1

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
1

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
3

> <Hydrophobic A:ALA428>
1

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
1

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
2

> <Hydrophobic A:PHE540>
1

> <Hydrophobic A:LEU542>
1

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -14.5480    8.8027  -14.0813 N   0  0  0  1  0  0
  -14.3696    8.5892  -15.4016 C   0  0  0  1  0  0
  -13.4429    9.3792  -15.9653 N   0  0  0  1  0  0
  -13.1557    9.2250  -17.2621 C   0  0  0  1  0  0
  -13.7284    8.3221  -18.0500 N   0  0  0  1  0  0
  -14.6560    7.5254  -17.4937 C   0  0  0  1  0  0
  -15.0510    7.6435  -16.1380 C   0  0  0  1  0  0
  -15.3534    6.4648  -18.0692 N   0  0  0  1  0  0
  -15.1250    5.8995  -19.4148 C   0  0  0  1  0  0
  -14.2125    6.6485  -20.3894 C   0  0  0  1  0  0
  -14.4671    5.9821  -21.7417 C   0  0  0  1  0  0
  -15.8877    5.4042  -21.6708 C   0  0  0  1  0  0
  -16.3912    5.6298  -20.2320 C   0  0  0  1  0  0
  -16.2133    6.0464  -17.1215 C   0  0  0  1  0  0
  -16.0845    6.6953  -15.9062 C   0  0  0  1  0  0
  -16.8700    6.4087  -14.6681 C   0  0  0  1  0  0
  -17.2577    5.1156  -14.3521 C   0  0  0  1  0  0
  -17.9448    4.8300  -13.1708 C   0  0  0  1  0  0
  -18.2339    5.8393  -12.2630 C   0  0  0  1  0  0
  -17.8623    7.1322  -12.5942 C   0  0  0  1  0  0
  -17.2388    7.4165  -13.8002 C   0  0  0  1  0  0
  -18.7910    5.5350  -11.0235 O   0  0  0  1  0  0
  -19.6624    6.4705  -10.4645 C   0  0  0  1  0  0
  -19.5166    6.7848   -9.1202 C   0  0  0  1  0  0
  -20.4085    7.6488   -8.4975 C   0  0  0  1  0  0
  -21.4669    8.1916   -9.2150 C   0  0  0  1  0  0
  -21.6140    7.8906  -10.5631 C   0  0  0  1  0  0
  -20.7080    7.0440  -11.1887 C   0  0  0  1  0  0
  -14.0965    9.5934  -13.6668 H   0  0
  -15.1184    8.1941  -13.5398 H   0  0
  -12.4087    9.8756  -17.6940 H   0  0
  -14.6436    4.9493  -19.2080 H   0  0
  -13.1613    6.6045  -20.1011 H   0  0
  -14.5011    7.6978  -20.4438 H   0  0
  -14.3450    6.6809  -22.5692 H   0  0
  -13.7471    5.1797  -21.8982 H   0  0
  -15.8728    4.3434  -21.9164 H   0  0
  -16.5319    5.8758  -22.4089 H   0  0
  -17.0591    6.4887  -20.1841 H   0  0
  -16.9615    4.7795  -19.8581 H   0  0
  -16.9335    5.2598  -17.2982 H   0  0
  -17.0325    4.2930  -15.0152 H   0  0
  -18.2455    3.8164  -12.9458 H   0  0
  -18.0513    7.9190  -11.8935 H   0  0
  -17.0507    8.4533  -14.0392 H   0  0
  -18.7034    6.3494   -8.5614 H   0  0
  -20.2780    7.8952   -7.4541 H   0  0
  -22.1752    8.8456   -8.7253 H   0  0
  -22.4373    8.3042  -11.1273 H   0  0
  -20.8395    6.8093  -12.2356 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372096987660304

> <LigScore1_Dreiding>
2.51

> <LigScore2_Dreiding>
5.8

> <-PLP1>
100.25

> <-PLP2>
93.12

> <Jain>
4.96

> <-PMF>
114.62

> <-PMF04>
42.32

> <AbsoluteEnergy>
150.942

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
33

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
4.895

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
63

> <LibDockScore>
91.951

> <HotSpots>
-18.60,3.92,-18.69,A,10,13
-18.60,7.12,-11.89,A,46,20
-22.60,6.72,-9.09,A,69,26

> <-In-Situ Starting Energy>
-1045.633

> <-In-Situ Final Energy>
19.635

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
1

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
3

> <Favorable A:ALA428>
1

> <Favorable A:LYS430>
2

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
1

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
1

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
2

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
0

> <Favorable A:PHE540>
1

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
1

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
1

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
1

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
3

> <Hydrophobic A:ALA428>
1

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
1

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
1

> <Hydrophobic A:LEU528>
2

> <Hydrophobic A:PHE540>
1

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -15.3386    9.5249  -14.4201 N   0  0  0  1  0  0
  -14.7535    8.9767  -15.5087 C   0  0  0  1  0  0
  -13.7021    9.6693  -15.9740 N   0  0  0  1  0  0
  -13.1403    9.3071  -17.1330 C   0  0  0  1  0  0
  -13.5572    8.2894  -17.8782 N   0  0  0  1  0  0
  -14.5729    7.5566  -17.3938 C   0  0  0  1  0  0
  -15.1924    7.8343  -16.1469 C   0  0  0  1  0  0
  -15.2138    6.4639  -17.9768 N   0  0  0  1  0  0
  -14.9518    5.8770  -19.3064 C   0  0  0  1  0  0
  -14.0469    6.6377  -20.2806 C   0  0  0  1  0  0
  -14.3436    6.0270  -21.6536 C   0  0  0  1  0  0
  -15.7655    5.4528  -21.5700 C   0  0  0  1  0  0
  -16.2343    5.6608  -20.1195 C   0  0  0  1  0  0
  -16.1068    6.0521  -17.0654 C   0  0  0  1  0  0
  -16.1636    6.8207  -15.9184 C   0  0  0  1  0  0
  -17.0985    6.5958  -14.7755 C   0  0  0  1  0  0
  -16.8590    7.0503  -13.4931 C   0  0  0  1  0  0
  -17.8705    7.0641  -12.5337 C   0  0  0  1  0  0
  -19.1397    6.5781  -12.8355 C   0  0  0  1  0  0
  -19.3109    5.9730  -14.0641 C   0  0  0  1  0  0
  -18.2956    5.9440  -15.0056 C   0  0  0  1  0  0
  -20.2992    6.7180  -12.0739 O   0  0  0  1  0  0
  -20.2799    7.0790  -10.7368 C   0  0  0  1  0  0
  -21.3226    7.8868  -10.3026 C   0  0  0  1  0  0
  -21.3820    8.3121   -8.9828 C   0  0  0  1  0  0
  -20.3936    7.9192   -8.0920 C   0  0  0  1  0  0
  -19.4019    7.0392   -8.4998 C   0  0  0  1  0  0
  -19.3555    6.5995   -9.8147 C   0  0  0  1  0  0
  -14.8773   10.2769  -13.9478 H   0  0
  -16.2304    9.2237  -14.0861 H   0  0
  -12.2966    9.8828  -17.4862 H   0  0
  -14.5026    4.9108  -19.1011 H   0  0
  -12.9908    6.5724  -20.0146 H   0  0
  -14.3240    7.6920  -20.2993 H   0  0
  -14.2418    6.7611  -22.4525 H   0  0
  -13.6330    5.2293  -21.8683 H   0  0
  -15.7573    4.3963  -21.8323 H   0  0
  -16.4343    5.9280  -22.2850 H   0  0
  -16.8683    6.5436  -20.0485 H   0  0
  -16.8353    4.8278  -19.7551 H   0  0
  -16.7256    5.1835  -17.2385 H   0  0
  -15.8855    7.4205  -13.2205 H   0  0
  -17.6700    7.5086  -11.5791 H   0  0
  -20.2782    5.5737  -14.3056 H   0  0
  -18.5333    5.5017  -15.9620 H   0  0
  -22.0805    8.1923  -11.0091 H   0  0
  -22.1842    8.9583   -8.6554 H   0  0
  -20.3907    8.3002   -7.0821 H   0  0
  -18.6554    6.7155   -7.7933 H   0  0
  -18.5992    5.8920  -10.1166 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372101282627600

> <LigScore1_Dreiding>
2.15

> <LigScore2_Dreiding>
5.32

> <-PLP1>
96.49

> <-PLP2>
90.04

> <Jain>
4.26

> <-PMF>
114.88

> <-PMF04>
41.17

> <AbsoluteEnergy>
151.199

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
34

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
5.152

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
64

> <LibDockScore>
91.827

> <HotSpots>
-16.80,8.92,-13.09,P,46,1
-17.20,4.12,-18.29,A,12,13
-19.80,7.72,-8.89,A,70,24

> <-In-Situ Starting Energy>
-2477.059

> <-In-Situ Final Energy>
8.083

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
1

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
2

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
1

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
1

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
1

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
3

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
0

> <Favorable A:PHE540>
1

> <Favorable A:LEU542>
1

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
1

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
2

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
1

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
1

> <Hydrophobic A:LEU528>
3

> <Hydrophobic A:PHE540>
1

> <Hydrophobic A:LEU542>
1

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -17.5839   10.1172  -14.8992 N   0  0  0  1  0  0
  -16.2496   10.1008  -15.0456 C   0  0  0  1  0  0
  -15.7379   11.1064  -15.7666 N   0  0  0  1  0  0
  -14.4016   11.2246  -15.8525 C   0  0  0  1  0  0
  -13.5327   10.4072  -15.2613 N   0  0  0  1  0  0
  -14.0600    9.3793  -14.5843 C   0  0  0  1  0  0
  -15.4471    9.1395  -14.5042 C   0  0  0  1  0  0
  -13.4116    8.4130  -13.8281 N   0  0  0  1  0  0
  -11.9684    8.4579  -13.5133 C   0  0  0  1  0  0
  -11.8382    8.3043  -12.0005 C   0  0  0  1  0  0
  -11.5315    6.8172  -11.8022 C   0  0  0  1  0  0
  -10.5417    6.5745  -12.8981 C   0  0  0  1  0  0
  -11.1493    7.3086  -14.1096 C   0  0  0  1  0  0
  -14.3749    7.5415  -13.4580 C   0  0  0  1  0  0
  -15.6458    7.9185  -13.8305 C   0  0  0  1  0  0
  -16.9213    7.2201  -13.5294 C   0  0  0  1  0  0
  -17.3133    7.1066  -12.2278 C   0  0  0  1  0  0
  -18.5262    6.5962  -11.8519 C   0  0  0  1  0  0
  -19.5141    6.5258  -12.8067 C   0  0  0  1  0  0
  -19.0964    6.4149  -14.1304 C   0  0  0  1  0  0
  -17.7669    6.6882  -14.4744 C   0  0  0  1  0  0
  -20.8662    6.5867  -12.4954 O   0  0  0  1  0  0
  -21.3451    6.9943  -11.2470 C   0  0  0  1  0  0
  -20.7175    7.8696  -10.3559 C   0  0  0  1  0  0
  -21.3214    8.2303   -9.1647 C   0  0  0  1  0  0
  -22.5941    7.7848   -8.8964 C   0  0  0  1  0  0
  -23.2344    6.9349   -9.7732 C   0  0  0  1  0  0
  -22.5975    6.5044  -10.9146 C   0  0  0  1  0  0
  -18.0778   10.9134  -15.2403 H   0  0
  -18.1028    9.3688  -14.4802 H   0  0
  -13.9894   12.0248  -16.4466 H   0  0
  -11.5411    9.4120  -13.8302 H   0  0
  -12.7258    8.6653  -11.4894 H   0  0
  -10.9970    8.8997  -11.6421 H   0  0
  -11.1428    6.5513  -10.8239 H   0  0
  -12.3817    6.1770  -12.0095 H   0  0
   -9.6389    7.0538  -12.5474 H   0  0
  -10.3170    5.5206  -13.0426 H   0  0
  -11.7826    6.6680  -14.7151 H   0  0
  -10.4007    7.6865  -14.7973 H   0  0
  -14.2016    6.6328  -12.9061 H   0  0
  -16.7026    7.4297  -11.4337 H   0  0
  -18.7104    6.4385  -10.8015 H   0  0
  -19.8210    6.1792  -14.8949 H   0  0
  -17.4480    6.6077  -15.5039 H   0  0
  -19.7522    8.3013  -10.5528 H   0  0
  -20.8328    8.8822   -8.4578 H   0  0
  -23.1160    8.1473   -8.0348 H   0  0
  -24.2565    6.6555   -9.5982 H   0  0
  -23.1027    5.7956  -11.5479 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372105577594896

> <LigScore1_Dreiding>
1.47

> <LigScore2_Dreiding>
3.18

> <-PLP1>
88.57

> <-PLP2>
84.5

> <Jain>
7.46

> <-PMF>
81.4

> <-PMF04>
16.91

> <AbsoluteEnergy>
149.872

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
27

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
3.825

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
65

> <LibDockScore>
91.616

> <HotSpots>
-10.60,5.72,-12.49,A,42,12
-18.00,6.32,-14.09,A,30,20
-21.80,7.92,-10.89,A,54,25

> <-In-Situ Starting Energy>
-29473.715

> <-In-Situ Final Energy>
-26.225

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
0

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
2

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
3

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
1

> <Favorable A:LEU460>
1

> <Favorable A:ILE472>
0

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
1

> <Favorable A:ARG525>
1

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
2

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
2

> <Favorable A:PHE540>
0

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
1

> <Charge A:ASP539>
2

> <Hydrophobic A:LEU408>
0

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
2

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
2

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
1

> <Hydrophobic A:LEU460>
1

> <Hydrophobic A:ILE472>
0

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
2

> <Hydrophobic A:PHE540>
0

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
1

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
1

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
0

> <Other A:CYS481>
1

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -15.9356    9.9091  -13.5202 N   0  0  0  1  0  0
  -15.1374    9.5822  -14.5613 C   0  0  0  1  0  0
  -14.1858   10.4873  -14.8289 N   0  0  0  1  0  0
  -13.4343   10.3392  -15.9259 C   0  0  0  1  0  0
  -13.5217    9.3047  -16.7605 N   0  0  0  1  0  0
  -14.4273    8.3590  -16.4613 C   0  0  0  1  0  0
  -15.2697    8.4395  -15.3256 C   0  0  0  1  0  0
  -14.7381    7.1956  -17.1661 N   0  0  0  1  0  0
  -14.1282    6.7704  -18.4434 C   0  0  0  1  0  0
  -14.4224    7.7657  -19.5798 C   0  0  0  1  0  0
  -13.0789    8.3794  -19.9650 C   0  0  0  1  0  0
  -12.0865    7.2606  -19.6780 C   0  0  0  1  0  0
  -12.5984    6.6083  -18.3924 C   0  0  0  1  0  0
  -15.7022    6.5880  -16.4526 C   0  0  0  1  0  0
  -16.0730    7.2671  -15.3086 C   0  0  0  1  0  0
  -17.1150    6.8530  -14.3277 C   0  0  0  1  0  0
  -17.0177    7.1967  -13.0015 C   0  0  0  1  0  0
  -18.0992    7.0770  -12.1446 C   0  0  0  1  0  0
  -19.3194    6.5994  -12.6035 C   0  0  0  1  0  0
  -19.3418    6.0604  -13.8810 C   0  0  0  1  0  0
  -18.2369    6.1497  -14.7213 C   0  0  0  1  0  0
  -20.5327    6.6921  -11.9157 O   0  0  0  1  0  0
  -20.5744    7.1026  -10.5900 C   0  0  0  1  0  0
  -21.5473    8.0296  -10.2468 C   0  0  0  1  0  0
  -21.5908    8.5527   -8.9620 C   0  0  0  1  0  0
  -20.6535    8.1519   -8.0217 C   0  0  0  1  0  0
  -19.7589    7.1369   -8.3231 C   0  0  0  1  0  0
  -19.7422    6.5894   -9.5980 C   0  0  0  1  0  0
  -15.6675   10.6330  -12.8753 H   0  0
  -16.8139    9.4625  -13.3614 H   0  0
  -12.7120   11.1129  -16.1450 H   0  0
  -14.5694    5.8095  -18.7136 H   0  0
  -15.1620    8.5222  -19.3161 H   0  0
  -14.8088    7.2090  -20.4324 H   0  0
  -13.0488    8.7118  -21.0024 H   0  0
  -12.8603    9.2371  -19.3295 H   0  0
  -11.0563    7.6080  -19.5969 H   0  0
  -12.1363    6.5435  -20.4970 H   0  0
  -12.2948    5.5649  -18.3106 H   0  0
  -12.1748    7.1283  -17.5335 H   0  0
  -16.1498    5.6536  -16.7574 H   0  0
  -16.0970    7.5914  -12.6151 H   0  0
  -17.9789    7.4275  -11.1414 H   0  0
  -20.2528    5.6183  -14.2429 H   0  0
  -18.3354    5.7698  -15.7282 H   0  0
  -22.2504    8.3589  -10.9977 H   0  0
  -22.3360    9.2869   -8.6972 H   0  0
  -20.6292    8.6234   -7.0503 H   0  0
  -19.0663    6.7923   -7.5703 H   0  0
  -19.0481    5.7971   -9.8333 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372109872562192

> <LigScore1_Dreiding>
3.57

> <LigScore2_Dreiding>
5.75

> <-PLP1>
87.61

> <-PLP2>
80.11

> <Jain>
3.85

> <-PMF>
113.24

> <-PMF04>
38.69

> <AbsoluteEnergy>
162.605

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
49

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
16.558

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
68

> <LibDockScore>
89.909

> <HotSpots>
-12.60,6.32,-17.69,A,17,13
-19.80,7.72,-8.89,A,70,25
-21.60,6.32,-8.29,A,80,27

> <-In-Situ Starting Energy>
-577.008

> <-In-Situ Final Energy>
8.846

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
1

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
1

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
1

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
1

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
1

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
3

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
1

> <Favorable A:PHE540>
1

> <Favorable A:LEU542>
1

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
1

> <Charge A:LYS430>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
1

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
1

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
1

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
1

> <Hydrophobic A:LEU528>
3

> <Hydrophobic A:PHE540>
1

> <Hydrophobic A:LEU542>
1

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
1

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -19.4108    4.7151  -16.7249 N   0  0  0  1  0  0
  -18.3570    5.0394  -17.5090 C   0  0  0  1  0  0
  -18.4623    4.6935  -18.8061 N   0  0  0  1  0  0
  -17.4901    5.0632  -19.6585 C   0  0  0  1  0  0
  -16.3978    5.7412  -19.3104 N   0  0  0  1  0  0
  -16.2792    6.0624  -18.0127 C   0  0  0  1  0  0
  -17.2439    5.6970  -17.0455 C   0  0  0  1  0  0
  -15.2656    6.7844  -17.3797 N   0  0  0  1  0  0
  -14.0812    7.3741  -18.0330 C   0  0  0  1  0  0
  -13.1971    6.3329  -18.7353 C   0  0  0  1  0  0
  -13.1624    6.7457  -20.2092 C   0  0  0  1  0  0
  -13.4025    8.2511  -20.1902 C   0  0  0  1  0  0
  -14.4432    8.4278  -19.0881 C   0  0  0  1  0  0
  -15.6018    6.8142  -16.0810 C   0  0  0  1  0  0
  -16.7743    6.1466  -15.7917 C   0  0  0  1  0  0
  -17.3589    5.9772  -14.4400 C   0  0  0  1  0  0
  -17.5250    7.0792  -13.6280 C   0  0  0  1  0  0
  -18.0439    6.9453  -12.3487 C   0  0  0  1  0  0
  -18.4136    5.7023  -11.8554 C   0  0  0  1  0  0
  -18.2263    4.5924  -12.6676 C   0  0  0  1  0  0
  -17.7210    4.7349  -13.9561 C   0  0  0  1  0  0
  -18.8892    5.5389  -10.5598 O   0  0  0  1  0  0
  -19.7616    6.5143  -10.0800 C   0  0  0  1  0  0
  -19.5886    6.9544   -8.7754 C   0  0  0  1  0  0
  -20.4616    7.8818   -8.2231 C   0  0  0  1  0  0
  -21.5354    8.3546   -8.9658 C   0  0  0  1  0  0
  -21.7115    7.9255  -10.2745 C   0  0  0  1  0  0
  -20.8217    7.0191  -10.8345 C   0  0  0  1  0  0
  -20.2228    4.2819  -17.1243 H   0  0
  -19.4202    4.8888  -15.7388 H   0  0
  -17.5959    4.7876  -20.6979 H   0  0
  -13.4798    7.8564  -17.2608 H   0  0
  -13.5713    5.3201  -18.5957 H   0  0
  -12.1884    6.3597  -18.3208 H   0  0
  -12.2310    6.4791  -20.7060 H   0  0
  -13.9756    6.2535  -20.7442 H   0  0
  -13.7274    8.6290  -21.1574 H   0  0
  -12.4813    8.7673  -19.9179 H   0  0
  -14.4632    9.4289  -18.6651 H   0  0
  -15.4309    8.2373  -19.5037 H   0  0
  -14.9992    7.3114  -15.3345 H   0  0
  -17.2568    8.0676  -13.9760 H   0  0
  -18.1567    7.8127  -11.7284 H   0  0
  -18.4778    3.6100  -12.2984 H   0  0
  -17.6005    3.8481  -14.5619 H   0  0
  -18.7623    6.5762   -8.1948 H   0  0
  -20.3020    8.2358   -7.2153 H   0  0
  -22.2313    9.0551   -8.5259 H   0  0
  -22.5443    8.2862  -10.8601 H   0  0
  -20.9771    6.7005  -11.8550 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372114167529488

> <LigScore1_Dreiding>
4.73

> <LigScore2_Dreiding>
6.83

> <-PLP1>
121.71

> <-PLP2>
118.01

> <Jain>
9.15

> <-PMF>
111.23

> <-PMF04>
39.5

> <AbsoluteEnergy>
157.761

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
48

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
11.714

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
69

> <LibDockScore>
89.897

> <HotSpots>
-16.80,5.32,-18.29,A,13,4
-12.60,6.32,-17.69,A,17,11
-20.60,5.92,-7.09,A,88,27

> <-In-Situ Starting Energy>
-306153.469

> <-In-Situ Final Energy>
41.657

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
2

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
3

> <Favorable A:ALA428>
3

> <Favorable A:LYS430>
1

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
1

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
1

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
2

> <Favorable A:CYS481>
0

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
2

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
0

> <Favorable A:PHE540>
1

> <Favorable A:LEU542>
1

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
2

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
3

> <Hydrophobic A:ALA428>
3

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
1

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
2

> <Hydrophobic A:PHE540>
1

> <Hydrophobic A:LEU542>
1

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
1

> <HydrogenBond A:MET477>
2

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -11.4920    8.4386  -15.6215 N   0  0  0  1  0  0
  -12.7311    7.9248  -15.7973 C   0  0  0  1  0  0
  -12.9118    7.2394  -16.9367 N   0  0  0  1  0  0
  -14.1233    6.7276  -17.1946 C   0  0  0  1  0  0
  -15.1816    6.8530  -16.3939 N   0  0  0  1  0  0
  -15.0121    7.5251  -15.2439 C   0  0  0  1  0  0
  -13.7588    8.0863  -14.8970 C   0  0  0  1  0  0
  -15.9256    7.8056  -14.2120 N   0  0  0  1  0  0
  -17.3373    7.3473  -14.0795 C   0  0  0  1  0  0
  -17.7801    6.1337  -14.9242 C   0  0  0  1  0  0
  -17.4713    4.9279  -14.0470 C   0  0  0  1  0  0
  -17.9705    5.3962  -12.6854 C   0  0  0  1  0  0
  -17.6882    6.9037  -12.6406 C   0  0  0  1  0  0
  -15.2519    8.6190  -13.3744 C   0  0  0  1  0  0
  -13.8986    8.6965  -13.6343 C   0  0  0  1  0  0
  -12.8336    9.2603  -12.7648 C   0  0  0  1  0  0
  -11.7143    8.4946  -12.5088 C   0  0  0  1  0  0
  -10.6913    8.9671  -11.7040 C   0  0  0  1  0  0
  -10.7593   10.2253  -11.1249 C   0  0  0  1  0  0
  -11.8888   11.0050  -11.3843 C   0  0  0  1  0  0
  -12.9213   10.5125  -12.1858 C   0  0  0  1  0  0
   -9.6492   10.6233  -10.3812 O   0  0  0  1  0  0
   -9.7878   11.5319   -9.3345 C   0  0  0  1  0  0
  -10.8808   11.5589   -8.4675 C   0  0  0  1  0  0
  -10.9034   12.4467   -7.3983 C   0  0  0  1  0  0
   -9.8259   13.2932   -7.1732 C   0  0  0  1  0  0
   -8.7228   13.2495   -8.0144 C   0  0  0  1  0  0
   -8.7068   12.3694   -9.0886 C   0  0  0  1  0  0
  -10.7731    8.2227  -16.2799 H   0  0
  -11.2614    9.0360  -14.8534 H   0  0
  -14.2486    6.1749  -18.1149 H   0  0
  -17.9321    8.2266  -14.2967 H   0  0
  -17.3696    6.0625  -15.9259 H   0  0
  -18.8626    6.1757  -15.0579 H   0  0
  -17.9724    4.0199  -14.3851 H   0  0
  -16.3967    4.7429  -14.0251 H   0  0
  -17.5572    4.8483  -11.8433 H   0  0
  -19.0477    5.2425  -12.6549 H   0  0
  -18.5883    7.4044  -12.2879 H   0  0
  -16.9168    7.1580  -11.9225 H   0  0
  -15.7407    9.1343  -12.5599 H   0  0
  -11.6088    7.5046  -12.9327 H   0  0
   -9.8362    8.3354  -11.5296 H   0  0
  -11.9765   12.0042  -10.9833 H   0  0
  -13.7874   11.1399  -12.3593 H   0  0
  -11.7139   10.8856   -8.6008 H   0  0
  -11.7559   12.4749   -6.7345 H   0  0
   -9.8412   13.9818   -6.3402 H   0  0
   -7.8770   13.8978   -7.8301 H   0  0
   -7.8477   12.3350   -9.7405 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372118462496784

> <LigScore1_Dreiding>
2.29

> <LigScore2_Dreiding>
5.01

> <-PLP1>
82.78

> <-PLP2>
76.2

> <Jain>
2.26

> <-PMF>
136.64

> <-PMF04>
58.89

> <AbsoluteEnergy>
154.674

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
44

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
8.627

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
74

> <LibDockScore>
87.768

> <HotSpots>
-16.60,5.52,-13.89,A,33,11
-11.00,8.32,-11.89,A,47,17
-10.40,11.52,-8.49,A,77,24

> <-In-Situ Starting Energy>
-160.618

> <-In-Situ Final Energy>
12.244

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
0

> <Favorable A:THR410>
2

> <Favorable A:GLY411>
1

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
2

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
3

> <Favorable A:ALA428>
1

> <Favorable A:LYS430>
3

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
0

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
0

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
1

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
1

> <Favorable A:PHE540>
0

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
1

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
1

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
0

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
2

> <Hydrophobic A:VAL416>
3

> <Hydrophobic A:ALA428>
1

> <Hydrophobic A:LYS430>
2

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
0

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
1

> <Hydrophobic A:PHE540>
0

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
1

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
2

> <HydrogenBond A:GLY411>
1

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
1

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -14.1583   12.2033  -13.7305 N   0  0  0  1  0  0
  -15.0005   11.1776  -13.9681 C   0  0  0  1  0  0
  -16.1625   11.4903  -14.5583 N   0  0  0  1  0  0
  -17.0516   10.5308  -14.7929 C   0  0  0  1  0  0
  -16.8649    9.2482  -14.5256 N   0  0  0  1  0  0
  -15.6946    8.9228  -13.9698 C   0  0  0  1  0  0
  -14.7116    9.8787  -13.6528 C   0  0  0  1  0  0
  -15.2268    7.6622  -13.6107 N   0  0  0  1  0  0
  -16.0220    6.4215  -13.7814 C   0  0  0  1  0  0
  -16.3603    6.1316  -15.2436 C   0  0  0  1  0  0
  -17.4170    5.0275  -15.1671 C   0  0  0  1  0  0
  -18.1856    5.2867  -13.8631 C   0  0  0  1  0  0
  -17.4141    6.3887  -13.1213 C   0  0  0  1  0  0
  -13.9697    7.8678  -13.1411 C   0  0  0  1  0  0
  -13.6268    9.2114  -13.0611 C   0  0  0  1  0  0
  -12.4181    9.8555  -12.4842 C   0  0  0  1  0  0
  -11.1649    9.6714  -13.0245 C   0  0  0  1  0  0
  -10.0637   10.3342  -12.4903 C   0  0  0  1  0  0
  -10.1719   11.1392  -11.3594 C   0  0  0  1  0  0
  -11.4507   11.3643  -10.8567 C   0  0  0  1  0  0
  -12.5453   10.7075  -11.4027 C   0  0  0  1  0  0
   -8.9959   11.7086  -10.8604 O   0  0  0  1  0  0
   -8.9185   12.2525   -9.5730 C   0  0  0  1  0  0
   -9.5942   11.7623   -8.4532 C   0  0  0  1  0  0
   -9.4158   12.3428   -7.2032 C   0  0  0  1  0  0
   -8.5425   13.4094   -7.0516 C   0  0  0  1  0  0
   -7.8456   13.8870   -8.1517 C   0  0  0  1  0  0
   -8.0281   13.3052   -9.4008 C   0  0  0  1  0  0
  -14.4470   13.1169  -14.0262 H   0  0
  -13.2791   12.0901  -13.2734 H   0  0
  -17.9814   10.8298  -15.2317 H   0  0
  -15.4450    5.5822  -13.3955 H   0  0
  -15.4861    5.8868  -15.8389 H   0  0
  -16.8099    7.0025  -15.7165 H   0  0
  -18.0713    5.0192  -16.0394 H   0  0
  -16.9335    4.0533  -15.1089 H   0  0
  -18.2389    4.3735  -13.2686 H   0  0
  -19.2127    5.5981  -14.0601 H   0  0
  -17.9370    7.3304  -13.2808 H   0  0
  -17.4079    6.2252  -12.0468 H   0  0
  -13.3059    7.0691  -12.8404 H   0  0
  -11.0175    9.0250  -13.8796 H   0  0
   -9.1112   10.2305  -12.9852 H   0  0
  -11.6312   12.0595  -10.0507 H   0  0
  -13.5121   10.9212  -10.9755 H   0  0
  -10.2820   10.9393   -8.5312 H   0  0
   -9.9595   11.9688   -6.3469 H   0  0
   -8.4031   13.8655   -6.0804 H   0  0
   -7.1489   14.7039   -8.0299 H   0  0
   -7.4763   13.6756  -10.2510 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372122757464080

> <LigScore1_Dreiding>
3.12

> <LigScore2_Dreiding>
4.98

> <-PLP1>
85.06

> <-PLP2>
81.27

> <Jain>
3.15

> <-PMF>
119.95

> <-PMF04>
47.84

> <AbsoluteEnergy>
146.57

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
11

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
0.523

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
76

> <LibDockScore>
86.946

> <HotSpots>
-16.20,11.72,-14.69,P,28,3
-18.00,6.32,-14.09,A,30,12
-9.00,11.12,-7.09,A,92,25

> <-In-Situ Starting Energy>
-842.635

> <-In-Situ Final Energy>
14.231

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
0

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
2

> <Favorable A:ALA428>
1

> <Favorable A:LYS430>
3

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
0

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
0

> <Favorable A:ARG525>
1

> <Favorable A:ASN526>
2

> <Favorable A:LEU528>
2

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
2

> <Favorable A:PHE540>
0

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
1

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
1

> <Charge A:ASP539>
2

> <Hydrophobic A:LEU408>
0

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
2

> <Hydrophobic A:ALA428>
1

> <Hydrophobic A:LYS430>
2

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
0

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
2

> <Hydrophobic A:PHE540>
0

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
1

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
1

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
1

> <HydrogenBond A:ASN526>
2

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
   -8.3949   11.3977  -12.7322 N   0  0  0  1  0  0
   -8.9055   11.6821  -11.5123 C   0  0  0  1  0  0
   -7.9993   11.7923  -10.5188 N   0  0  0  1  0  0
   -8.4168   12.2382   -9.3191 C   0  0  0  1  0  0
   -9.6874   12.4735   -9.0040 N   0  0  0  1  0  0
  -10.5961   12.2965   -9.9750 C   0  0  0  1  0  0
  -10.2487   11.8644  -11.2760 C   0  0  0  1  0  0
  -11.9720   12.4994   -9.9256 N   0  0  0  1  0  0
  -12.7086   13.0094   -8.7507 C   0  0  0  1  0  0
  -13.5284   14.2660   -9.1021 C   0  0  0  1  0  0
  -14.9821   13.9464   -8.7479 C   0  0  0  1  0  0
  -14.8966   12.8218   -7.7247 C   0  0  0  1  0  0
  -13.7086   11.9877   -8.1926 C   0  0  0  1  0  0
  -12.4354   12.1516  -11.1415 C   0  0  0  1  0  0
  -11.4480   11.7444  -12.0213 C   0  0  0  1  0  0
  -11.6529   11.2960  -13.4259 C   0  0  0  1  0  0
  -12.4957   12.0051  -14.2627 C   0  0  0  1  0  0
  -12.6867   11.6160  -15.5847 C   0  0  0  1  0  0
  -12.0566   10.4876  -16.0857 C   0  0  0  1  0  0
  -11.2153    9.7660  -15.2462 C   0  0  0  1  0  0
  -11.0246   10.1692  -13.9276 C   0  0  0  1  0  0
  -12.2596   10.1258  -17.4088 O   0  0  0  1  0  0
  -12.7255    8.8327  -17.6116 C   0  0  0  1  0  0
  -13.6745    8.2355  -16.7821 C   0  0  0  1  0  0
  -14.1263    6.9495  -17.0506 C   0  0  0  1  0  0
  -13.6399    6.2564  -18.1508 C   0  0  0  1  0  0
  -12.7090    6.8553  -18.9892 C   0  0  0  1  0  0
  -12.2587    8.1412  -18.7208 C   0  0  0  1  0  0
   -7.4070   11.3102  -12.8491 H   0  0
   -8.9775   11.2720  -13.5356 H   0  0
   -7.6722   12.4161   -8.5545 H   0  0
  -12.0105   13.2692   -7.9521 H   0  0
  -13.4420   14.5597  -10.1483 H   0  0
  -13.1723   15.1059   -8.5065 H   0  0
  -15.5259   14.8137   -8.3728 H   0  0
  -15.4998   13.5774   -9.6348 H   0  0
  -15.8136   12.2407   -7.6856 H   0  0
  -14.7019   13.2358   -6.7343 H   0  0
  -13.2843   11.3792   -7.3938 H   0  0
  -14.0413   11.3087   -8.9776 H   0  0
  -13.4880   12.1946  -11.3946 H   0  0
  -13.0247   12.8813  -13.9093 H   0  0
  -13.3396   12.1871  -16.2276 H   0  0
  -10.6962    8.8937  -15.6164 H   0  0
  -10.3683    9.5742  -13.3074 H   0  0
  -14.0775    8.7656  -15.9317 H   0  0
  -14.8592    6.4899  -16.4042 H   0  0
  -13.9898    5.2551  -18.3552 H   0  0
  -12.3306    6.3268  -19.8532 H   0  0
  -11.5332    8.6061  -19.3715 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372127052431376

> <LigScore1_Dreiding>
2.58

> <LigScore2_Dreiding>
4.73

> <-PLP1>
60.35

> <-PLP2>
53.15

> <Jain>
1.82

> <-PMF>
74.59

> <-PMF04>
23.32

> <AbsoluteEnergy>
152.006

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
37

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
5.959

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
77

> <LibDockScore>
86.371

> <HotSpots>
-9.00,11.32,-8.89,A,71,4
-13.00,12.72,-7.09,A,96,10
-16.00,6.12,-17.09,A,18,26

> <-In-Situ Starting Energy>
-251.125

> <-In-Situ Final Energy>
22.018

> <In-Situ Gradient>
0.131

> <Favorable A:LEU408>
0

> <Favorable A:THR410>
1

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
1

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
1

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
0

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
0

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
1

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
0

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
1

> <Favorable A:PHE540>
0

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
1

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
0

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
1

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
0

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
0

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
0

> <Hydrophobic A:PHE540>
0

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
1

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
1

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
1

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
1

> <Other A:CYS481>
1

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
   -8.4038   11.3910  -12.8136 N   0  0  0  1  0  0
   -8.8912   11.6868  -11.5868 C   0  0  0  1  0  0
   -7.9661   11.8069  -10.6117 N   0  0  0  1  0  0
   -8.3606   12.2608   -9.4076 C   0  0  0  1  0  0
   -9.6259   12.4912   -9.0680 N   0  0  0  1  0  0
  -10.5533   12.3063  -10.0198 C   0  0  0  1  0  0
  -10.2301   11.8694  -11.3258 C   0  0  0  1  0  0
  -11.9289   12.5023   -9.9429 N   0  0  0  1  0  0
  -12.6455   13.0037   -8.7515 C   0  0  0  1  0  0
  -13.6487   11.9823   -8.1975 C   0  0  0  1  0  0
  -14.8194   12.8186   -7.6906 C   0  0  0  1  0  0
  -14.9074   13.9710   -8.6835 C   0  0  0  1  0  0
  -13.4575   14.2738   -9.0698 C   0  0  0  1  0  0
  -12.4140   12.1554  -11.1509 C   0  0  0  1  0  0
  -11.4436   11.7442  -12.0477 C   0  0  0  1  0  0
  -11.6765   11.2855  -13.4452 C   0  0  0  1  0  0
  -12.5401   11.9837  -14.2701 C   0  0  0  1  0  0
  -12.7571   11.5827  -15.5849 C   0  0  0  1  0  0
  -12.1318   10.4543  -16.0909 C   0  0  0  1  0  0
  -11.2716    9.7416  -15.2625 C   0  0  0  1  0  0
  -11.0547   10.1571  -13.9516 C   0  0  0  1  0  0
  -12.3525   10.0920  -17.4111 O   0  0  0  1  0  0
  -12.8022    8.7931  -17.6100 C   0  0  0  1  0  0
  -13.7596    8.1965  -16.7902 C   0  0  0  1  0  0
  -14.1975    6.9048  -17.0544 C   0  0  0  1  0  0
  -13.6886    6.2062  -18.1411 C   0  0  0  1  0  0
  -12.7483    6.8047  -18.9694 C   0  0  0  1  0  0
  -12.3115    8.0958  -18.7051 C   0  0  0  1  0  0
   -7.4219   11.2636  -12.9423 H   0  0
   -8.9995   11.2954  -13.6116 H   0  0
   -7.6006   12.4496   -8.6610 H   0  0
  -11.9344   13.2436   -7.9580 H   0  0
  -13.2176   11.3522   -7.4190 H   0  0
  -14.0038   11.3242   -8.9902 H   0  0
  -15.7436   12.2478   -7.6494 H   0  0
  -14.6039   13.2038   -6.6928 H   0  0
  -15.4568   13.6372   -9.5654 H   0  0
  -15.4227   14.8391   -8.2716 H   0  0
  -13.0760   15.1039   -8.4761 H   0  0
  -13.3906   14.5760  -10.1150 H   0  0
  -13.4709   12.1990  -11.3846 H   0  0
  -13.0662   12.8605  -13.9136 H   0  0
  -13.4247   12.1453  -16.2197 H   0  0
  -10.7545    8.8695  -15.6368 H   0  0
  -10.3841    9.5696  -13.3402 H   0  0
  -14.1788    8.7326  -15.9519 H   0  0
  -14.9366    6.4446  -16.4152 H   0  0
  -14.0276    5.2005  -18.3430 H   0  0
  -12.3523    6.2723  -19.8223 H   0  0
  -11.5790    8.5604  -19.3479 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372131347398672

> <LigScore1_Dreiding>
2.55

> <LigScore2_Dreiding>
4.75

> <-PLP1>
60.56

> <-PLP2>
53.32

> <Jain>
1.8

> <-PMF>
74.44

> <-PMF04>
23.58

> <AbsoluteEnergy>
146.3

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
4

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
0.253

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
79

> <LibDockScore>
85.273

> <HotSpots>
-10.20,11.32,-7.09,A,93,4
-15.40,12.12,-7.69,A,86,10
-12.60,6.32,-17.69,A,17,27

> <-In-Situ Starting Energy>
-1422.036

> <-In-Situ Final Energy>
22.151

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
0

> <Favorable A:THR410>
1

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
1

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
1

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
0

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
0

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
1

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
0

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
1

> <Favorable A:PHE540>
0

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
1

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
0

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
1

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
0

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
0

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
0

> <Hydrophobic A:PHE540>
0

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
1

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
1

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
1

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
1

> <Other A:CYS481>
1

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -14.9512    9.3335  -12.8978 N   0  0  0  1  0  0
  -14.3435    9.0375  -14.0705 C   0  0  0  1  0  0
  -13.2362    9.7631  -14.2849 N   0  0  0  1  0  0
  -12.6321    9.6943  -15.4768 C   0  0  0  1  0  0
  -13.0350    8.9139  -16.4745 N   0  0  0  1  0  0
  -14.0892    8.1173  -16.2347 C   0  0  0  1  0  0
  -14.7894    8.1178  -15.0035 C   0  0  0  1  0  0
  -14.6881    7.1983  -17.0937 N   0  0  0  1  0  0
  -14.2916    6.9573  -18.4954 C   0  0  0  1  0  0
  -14.4545    8.1880  -19.3848 C   0  0  0  1  0  0
  -13.6419    7.8539  -20.6334 C   0  0  0  1  0  0
  -12.5133    6.9319  -20.1597 C   0  0  0  1  0  0
  -12.8353    6.5354  -18.7104 C   0  0  0  1  0  0
  -15.6713    6.6217  -16.3795 C   0  0  0  1  0  0
  -15.7982    7.1169  -15.0957 C   0  0  0  1  0  0
  -16.7787    6.6635  -14.0698 C   0  0  0  1  0  0
  -17.0749    5.3268  -13.8606 C   0  0  0  1  0  0
  -17.9097    4.9306  -12.8101 C   0  0  0  1  0  0
  -18.4211    5.8683  -11.9210 C   0  0  0  1  0  0
  -18.1816    7.2045  -12.1948 C   0  0  0  1  0  0
  -17.4178    7.5885  -13.2854 C   0  0  0  1  0  0
  -19.0724    5.4562  -10.7577 O   0  0  0  1  0  0
  -19.8894    6.3944  -10.1284 C   0  0  0  1  0  0
  -21.0129    6.9250  -10.7600 C   0  0  0  1  0  0
  -21.8155    7.8465  -10.1042 C   0  0  0  1  0  0
  -21.4908    8.2622   -8.8203 C   0  0  0  1  0  0
  -20.3573    7.7562   -8.1967 C   0  0  0  1  0  0
  -19.5640    6.8205   -8.8479 C   0  0  0  1  0  0
  -14.5767   10.0615  -12.3147 H   0  0
  -15.8128    8.9454  -12.5859 H   0  0
  -11.7599   10.3124  -15.6371 H   0  0
  -14.9315    6.1694  -18.8962 H   0  0
  -14.0264    9.0675  -18.9058 H   0  0
  -15.4984    8.4067  -19.5954 H   0  0
  -14.2648    7.3067  -21.3406 H   0  0
  -13.2673    8.7441  -21.1382 H   0  0
  -11.5426    7.4262  -20.2143 H   0  0
  -12.4651    6.0602  -20.8105 H   0  0
  -12.6774    5.4776  -18.5089 H   0  0
  -12.1679    7.0803  -18.0443 H   0  0
  -16.3068    5.8436  -16.7785 H   0  0
  -16.6559    4.5638  -14.5009 H   0  0
  -18.1289    3.8843  -12.6508 H   0  0
  -18.5671    7.9490  -11.5279 H   0  0
  -17.2899    8.6328  -13.5151 H   0  0
  -21.2674    6.6274  -11.7666 H   0  0
  -22.6935    8.2309  -10.5996 H   0  0
  -22.1192    8.9784   -8.3095 H   0  0
  -20.0885    8.0930   -7.2062 H   0  0
  -18.6800    6.4307   -8.3693 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372135642365968

> <LigScore1_Dreiding>
3.81

> <LigScore2_Dreiding>
6.03

> <-PLP1>
86.01

> <-PLP2>
80.98

> <Jain>
5.2

> <-PMF>
112.47

> <-PMF04>
40.29

> <AbsoluteEnergy>
164.245

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
52

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
18.198

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
80

> <LibDockScore>
85.13

> <HotSpots>
-15.60,6.12,-19.69,A,6,13
-17.20,7.52,-13.09,A,39,21
-21.80,7.92,-10.89,A,54,25

> <-In-Situ Starting Energy>
-6890.141

> <-In-Situ Final Energy>
15.795

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
1

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
3

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
2

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
1

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
0

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
1

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
1

> <Favorable A:PHE540>
1

> <Favorable A:LEU542>
1

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
1

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
1

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
3

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
1

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
1

> <Hydrophobic A:PHE540>
1

> <Hydrophobic A:LEU542>
1

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
1

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -16.4290   10.3082  -13.7167 N   0  0  0  1  0  0
  -15.5319    9.9621  -14.6631 C   0  0  0  1  0  0
  -14.6806   10.9382  -14.9945 N   0  0  0  1  0  0
  -13.8712   10.7763  -16.0463 C   0  0  0  1  0  0
  -13.8163    9.6656  -16.7832 N   0  0  0  1  0  0
  -14.6222    8.6564  -16.4113 C   0  0  0  1  0  0
  -15.4852    8.7337  -15.2877 C   0  0  0  1  0  0
  -14.8144    7.4240  -17.0341 N   0  0  0  1  0  0
  -14.1480    6.9826  -18.2792 C   0  0  0  1  0  0
  -14.7874    5.7334  -18.9240 C   0  0  0  1  0  0
  -14.7406    5.9544  -20.4449 C   0  0  0  1  0  0
  -13.8341    7.1649  -20.6425 C   0  0  0  1  0  0
  -14.1122    8.0164  -19.4088 C   0  0  0  1  0  0
  -15.6951    6.7686  -16.2565 C   0  0  0  1  0  0
  -16.0938    7.4578  -15.1289 C   0  0  0  1  0  0
  -16.9454    6.9051  -14.0325 C   0  0  0  1  0  0
  -16.9222    7.4617  -12.7741 C   0  0  0  1  0  0
  -17.6921    6.9491  -11.7483 C   0  0  0  1  0  0
  -18.4832    5.8472  -11.9166 C   0  0  0  1  0  0
  -18.4788    5.2341  -13.1601 C   0  0  0  1  0  0
  -17.7462    5.7846  -14.2156 C   0  0  0  1  0  0
  -19.1699    5.3933  -10.8002 O   0  0  0  1  0  0
  -19.9679    6.3798  -10.2184 C   0  0  0  1  0  0
  -19.7269    6.7687   -8.9071 C   0  0  0  1  0  0
  -20.5078    7.7494   -8.3108 C   0  0  0  1  0  0
  -21.5549    8.3284   -9.0160 C   0  0  0  1  0  0
  -21.7894    7.9557  -10.3330 C   0  0  0  1  0  0
  -20.9879    6.9987  -10.9375 C   0  0  0  1  0  0
  -16.2142   11.0498  -13.0734 H   0  0
  -17.3011    9.8296  -13.6420 H   0  0
  -13.2283   11.6046  -16.3098 H   0  0
  -13.1107    6.7530  -18.0280 H   0  0
  -15.8305    5.5981  -18.6409 H   0  0
  -14.2537    4.8382  -18.6105 H   0  0
  -14.4120    5.0928  -21.0204 H   0  0
  -15.7467    6.1761  -20.7962 H   0  0
  -14.0033    7.6850  -21.5809 H   0  0
  -12.7909    6.8429  -20.6357 H   0  0
  -13.3499    8.7808  -19.2577 H   0  0
  -15.0789    8.5130  -19.4978 H   0  0
  -16.0489    5.7762  -16.4856 H   0  0
  -16.2981    8.2983  -12.5291 H   0  0
  -17.6365    7.3158  -10.7462 H   0  0
  -19.0443    4.3305  -13.3058 H   0  0
  -17.8114    5.2900  -15.1738 H   0  0
  -18.9142    6.3177   -8.3615 H   0  0
  -20.2965    8.0628   -7.2993 H   0  0
  -22.1827    9.0698   -8.5420 H   0  0
  -22.5954    8.4012  -10.8953 H   0  0
  -21.1725    6.7267  -11.9669 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372139937333264

> <LigScore1_Dreiding>
3.05

> <LigScore2_Dreiding>
5.52

> <-PLP1>
93.11

> <-PLP2>
84.23

> <Jain>
5.04

> <-PMF>
111.77

> <-PMF04>
40.17

> <AbsoluteEnergy>
155.445

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
46

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
9.398

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
85

> <LibDockScore>
83.536

> <HotSpots>
-12.60,6.32,-17.69,A,17,10
-19.80,6.72,-7.69,A,85,25
-20.40,7.32,-10.49,A,60,28

> <-In-Situ Starting Energy>
-417.618

> <-In-Situ Final Energy>
8.728

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
1

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
2

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
1

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
1

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
1

> <Favorable A:ARG525>
1

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
2

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
1

> <Favorable A:PHE540>
1

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
1

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
2

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
1

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
1

> <Hydrophobic A:LEU528>
2

> <Hydrophobic A:PHE540>
1

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
1

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
1

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -16.6541    5.8274  -20.0260 N   0  0  0  1  0  0
  -17.2198    5.6061  -18.8190 C   0  0  0  1  0  0
  -18.3700    4.9087  -18.8638 N   0  0  0  1  0  0
  -19.0655    4.7440  -17.7292 C   0  0  0  1  0  0
  -18.6822    5.1700  -16.5391 N   0  0  0  1  0  0
  -17.5286    5.8381  -16.4903 C   0  0  0  1  0  0
  -16.7175    6.0742  -17.6220 C   0  0  0  1  0  0
  -16.9686    6.4588  -15.3861 N   0  0  0  1  0  0
  -17.6520    6.5140  -14.0803 C   0  0  0  1  0  0
  -16.9606    7.3278  -12.9935 C   0  0  0  1  0  0
  -17.7611    6.9320  -11.7511 C   0  0  0  1  0  0
  -18.1574    5.4715  -11.9579 C   0  0  0  1  0  0
  -17.8817    5.1513  -13.4295 C   0  0  0  1  0  0
  -15.8009    6.9718  -15.8144 C   0  0  0  1  0  0
  -15.5780    6.7904  -17.1711 C   0  0  0  1  0  0
  -14.4000    7.2860  -17.9345 C   0  0  0  1  0  0
  -13.7860    6.5169  -18.9037 C   0  0  0  1  0  0
  -12.7252    7.0186  -19.6524 C   0  0  0  1  0  0
  -12.2301    8.2911  -19.4086 C   0  0  0  1  0  0
  -12.8186    9.0527  -18.4071 C   0  0  0  1  0  0
  -13.8921    8.5479  -17.6791 C   0  0  0  1  0  0
  -11.2433    8.8047  -20.2354 O   0  0  0  1  0  0
   -9.9615    8.9984  -19.7219 C   0  0  0  1  0  0
   -9.5993    8.9029  -18.3750 C   0  0  0  1  0  0
   -8.2877    9.1507  -17.9845 C   0  0  0  1  0  0
   -7.3217    9.4611  -18.9307 C   0  0  0  1  0  0
   -7.6712    9.5407  -20.2708 C   0  0  0  1  0  0
   -8.9855    9.3154  -20.6582 C   0  0  0  1  0  0
  -17.1643    5.5535  -20.8461 H   0  0
  -15.7655    6.2688  -20.1309 H   0  0
  -20.0065    4.2304  -17.7837 H   0  0
  -18.6318    6.9694  -14.2424 H   0  0
  -16.9824    8.4003  -13.1877 H   0  0
  -15.9194    7.0223  -12.9045 H   0  0
  -17.2487    7.0858  -10.8096 H   0  0
  -18.6684    7.5337  -11.7020 H   0  0
  -17.6485    4.7772  -11.2955 H   0  0
  -19.2057    5.3968  -11.7222 H   0  0
  -18.7025    4.6010  -13.8889 H   0  0
  -16.9837    4.5430  -13.5297 H   0  0
  -15.1096    7.4862  -15.1630 H   0  0
  -14.1260    5.5098  -19.0933 H   0  0
  -12.2779    6.4246  -20.4359 H   0  0
  -12.4480   10.0467  -18.2059 H   0  0
  -14.3354    9.1790  -16.9210 H   0  0
  -10.3124    8.6512  -17.6062 H   0  0
   -8.0160    9.1105  -16.9402 H   0  0
   -6.3000    9.6402  -18.6264 H   0  0
   -6.9224    9.7771  -21.0132 H   0  0
   -9.2575    9.3723  -21.7015 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372144232300560

> <LigScore1_Dreiding>
3.12

> <LigScore2_Dreiding>
4.9

> <-PLP1>
82.86

> <-PLP2>
78.13

> <Jain>
4.61

> <-PMF>
79.23

> <-PMF04>
19.6

> <AbsoluteEnergy>
146.3

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
4

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
0.253

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
91

> <LibDockScore>
81.76

> <HotSpots>
-19.40,4.52,-16.69,P,20,5
-18.40,4.72,-11.29,A,50,12
-12.60,6.32,-17.69,A,17,18

> <-In-Situ Starting Energy>
-206.126

> <-In-Situ Final Energy>
14.897

> <In-Situ Gradient>
0.062

> <Favorable A:LEU408>
0

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
2

> <Favorable A:ALA428>
2

> <Favorable A:LYS430>
1

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
0

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
1

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
1

> <Favorable A:CYS481>
1

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
2

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
0

> <Favorable A:PHE540>
0

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
0

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
2

> <Hydrophobic A:ALA428>
2

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
0

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
1

> <Hydrophobic A:LEU528>
2

> <Hydrophobic A:PHE540>
0

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
1

> <HydrogenBond A:MET477>
1

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -16.4232   10.3086  -13.7170 N   0  0  0  1  0  0
  -15.5271    9.9613  -14.6641 C   0  0  0  1  0  0
  -14.6746   10.9363  -14.9956 N   0  0  0  1  0  0
  -13.8660   10.7736  -16.0479 C   0  0  0  1  0  0
  -13.8131    9.6631  -16.7851 N   0  0  0  1  0  0
  -14.6202    8.6549  -16.4131 C   0  0  0  1  0  0
  -15.4825    8.7331  -15.2890 C   0  0  0  1  0  0
  -14.8141    7.4230  -17.0360 N   0  0  0  1  0  0
  -14.1485    6.9810  -18.2814 C   0  0  0  1  0  0
  -14.1122    8.0147  -19.4111 C   0  0  0  1  0  0
  -13.8346    7.1628  -20.6447 C   0  0  0  1  0  0
  -14.7416    5.9527  -20.4469 C   0  0  0  1  0  0
  -14.7891    5.7323  -18.9259 C   0  0  0  1  0  0
  -15.6953    6.7685  -16.2584 C   0  0  0  1  0  0
  -16.0928    7.4578  -15.1304 C   0  0  0  1  0  0
  -16.9447    6.9058  -14.0340 C   0  0  0  1  0  0
  -16.9211    7.4620  -12.7754 C   0  0  0  1  0  0
  -17.6912    6.9495  -11.7496 C   0  0  0  1  0  0
  -18.4828    5.8481  -11.9181 C   0  0  0  1  0  0
  -18.4791    5.2354  -13.1618 C   0  0  0  1  0  0
  -17.7463    5.7859  -14.2173 C   0  0  0  1  0  0
  -19.1693    5.3941  -10.8016 O   0  0  0  1  0  0
  -19.9675    6.3806  -10.2199 C   0  0  0  1  0  0
  -19.7274    6.7689   -8.9084 C   0  0  0  1  0  0
  -20.5087    7.7494   -8.3122 C   0  0  0  1  0  0
  -21.5553    8.3286   -9.0179 C   0  0  0  1  0  0
  -21.7889    7.9566  -10.3352 C   0  0  0  1  0  0
  -20.9870    6.9997  -10.9396 C   0  0  0  1  0  0
  -16.2074   11.0503  -13.0742 H   0  0
  -17.2956    9.8307  -13.6409 H   0  0
  -13.2220   11.6010  -16.3114 H   0  0
  -13.1113    6.7505  -18.0305 H   0  0
  -13.3496    8.7786  -19.2600 H   0  0
  -15.0787    8.5117  -19.5001 H   0  0
  -14.0036    7.6827  -21.5832 H   0  0
  -12.7915    6.8404  -20.6378 H   0  0
  -15.7475    6.1744  -20.7988 H   0  0
  -14.4129    5.0907  -21.0218 H   0  0
  -14.2564    4.8367  -18.6118 H   0  0
  -15.8324    5.5983  -18.6431 H   0  0
  -16.0503    5.7765  -16.4876 H   0  0
  -16.2965    8.2982  -12.5301 H   0  0
  -17.6351    7.3158  -10.7474 H   0  0
  -19.0450    4.3322  -13.3075 H   0  0
  -17.8121    5.2915  -15.1755 H   0  0
  -18.9152    6.3176   -8.3624 H   0  0
  -20.2981    8.0624   -7.3004 H   0  0
  -22.1834    9.0698   -8.5440 H   0  0
  -22.5945    8.4024  -10.8979 H   0  0
  -21.1710    6.7280  -11.9691 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372148527267856

> <LigScore1_Dreiding>
3.05

> <LigScore2_Dreiding>
5.52

> <-PLP1>
93.1

> <-PLP2>
84.23

> <Jain>
5.04

> <-PMF>
111.82

> <-PMF04>
40.15

> <AbsoluteEnergy>
149.211

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
23

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
3.163

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
93

> <LibDockScore>
81.685

> <HotSpots>
-15.00,10.92,-16.29,A,23,4
-16.20,6.52,-15.49,A,24,14
-21.80,7.92,-10.89,A,54,28

> <-In-Situ Starting Energy>
-701.448

> <-In-Situ Final Energy>
8.728

> <In-Situ Gradient>
0.009

> <Favorable A:LEU408>
1

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
2

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
1

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
1

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
1

> <Favorable A:ARG525>
1

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
2

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
1

> <Favorable A:PHE540>
1

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
1

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
2

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
1

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
1

> <Hydrophobic A:LEU528>
2

> <Hydrophobic A:PHE540>
1

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
1

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
1

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
   -9.2279   11.1382  -12.4791 N   0  0  0  1  0  0
   -9.6093   11.6388  -11.2819 C   0  0  0  1  0  0
   -8.6436   11.7020  -10.3422 N   0  0  0  1  0  0
   -8.9531   12.2195   -9.1379 C   0  0  0  1  0  0
  -10.1741   12.6001   -8.7699 N   0  0  0  1  0  0
  -11.1398   12.5156   -9.6982 C   0  0  0  1  0  0
  -10.8945   12.0479  -11.0117 C   0  0  0  1  0  0
  -12.4915   12.8295   -9.5767 N   0  0  0  1  0  0
  -13.1290   13.3049   -8.3272 C   0  0  0  1  0  0
  -13.0165   12.2796   -7.1812 C   0  0  0  1  0  0
  -14.4227   12.1072   -6.5978 C   0  0  0  1  0  0
  -15.2047   13.3289   -7.0691 C   0  0  0  1  0  0
  -14.6299   13.6203   -8.4500 C   0  0  0  1  0  0
  -13.0174   12.5987  -10.7956 C   0  0  0  1  0  0
  -12.1144   12.1215  -11.7260 C   0  0  0  1  0  0
  -12.4174   11.7634  -13.1396 C   0  0  0  1  0  0
  -11.6227   12.1850  -14.1909 C   0  0  0  1  0  0
  -11.8964   11.7930  -15.4993 C   0  0  0  1  0  0
  -12.9725   10.9601  -15.7723 C   0  0  0  1  0  0
  -13.8068   10.5838  -14.7270 C   0  0  0  1  0  0
  -13.5289   10.9928  -13.4269 C   0  0  0  1  0  0
  -13.2052   10.5351  -17.0716 O   0  0  0  1  0  0
  -13.2104    9.1564  -17.2605 C   0  0  0  1  0  0
  -14.1022    8.6304  -18.1873 C   0  0  0  1  0  0
  -14.1311    7.2653  -18.4427 C   0  0  0  1  0  0
  -13.2596    6.4164  -17.7736 C   0  0  0  1  0  0
  -12.3586    6.9344  -16.8527 C   0  0  0  1  0  0
  -12.3281    8.3002  -16.5996 C   0  0  0  1  0  0
   -8.2601   10.9918  -12.6776 H   0  0
   -9.8940   10.8986  -13.1858 H   0  0
   -8.1593   12.3312   -8.4125 H   0  0
  -12.6237   14.2222   -8.0179 H   0  0
  -12.3280   12.6590   -6.4268 H   0  0
  -12.6242   11.3184   -7.5155 H   0  0
  -14.8721   11.2099   -7.0203 H   0  0
  -14.4206   11.9972   -5.5133 H   0  0
  -16.2829   13.1755   -7.0929 H   0  0
  -15.0048   14.1625   -6.4025 H   0  0
  -14.8137   14.6467   -8.7670 H   0  0
  -15.1233   12.9568   -9.1590 H   0  0
  -14.0557   12.7646  -11.0397 H   0  0
  -10.7741   12.8296  -14.0117 H   0  0
  -11.2671   12.1221  -16.3123 H   0  0
  -14.6755    9.9747  -14.9264 H   0  0
  -14.2033   10.6888  -12.6392 H   0  0
  -14.7799    9.2902  -18.7067 H   0  0
  -14.8286    6.8655  -19.1640 H   0  0
  -13.2784    5.3547  -17.9718 H   0  0
  -11.6775    6.2760  -16.3337 H   0  0
  -11.6021    8.6819  -15.8965 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372152822235152

> <LigScore1_Dreiding>
2.49

> <LigScore2_Dreiding>
5.03

> <-PLP1>
72.74

> <-PLP2>
62.46

> <Jain>
1.86

> <-PMF>
90.71

> <-PMF04>
31.93

> <AbsoluteEnergy>
149.211

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
23

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
3.163

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
95

> <LibDockScore>
79.308

> <HotSpots>
-16.00,13.72,-7.29,A,87,12
-15.00,13.92,-8.49,A,79,13
-12.60,6.32,-17.69,A,17,26

> <-In-Situ Starting Energy>
-774.821

> <-In-Situ Final Energy>
19.602

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
0

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
1

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
1

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
0

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
0

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
1

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
1

> <Favorable A:LEU528>
0

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
1

> <Favorable A:PHE540>
0

> <Favorable A:LEU542>
1

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
1

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
0

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
1

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
0

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
0

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
1

> <Hydrophobic A:LEU528>
0

> <Hydrophobic A:PHE540>
0

> <Hydrophobic A:LEU542>
1

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
1

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
1

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
1

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
1

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -16.7437    5.7485  -20.0619 N   0  0  0  1  0  0
  -17.2693    5.5923  -18.8262 C   0  0  0  1  0  0
  -18.4857    5.0234  -18.8033 N   0  0  0  1  0  0
  -19.0899    4.8466  -17.6207 C   0  0  0  1  0  0
  -18.5501    5.1333  -16.4459 N   0  0  0  1  0  0
  -17.3371    5.6957  -16.4562 C   0  0  0  1  0  0
  -16.6408    5.9719  -17.6597 C   0  0  0  1  0  0
  -16.5504    6.0955  -15.3743 N   0  0  0  1  0  0
  -16.8532    5.9156  -13.9365 C   0  0  0  1  0  0
  -18.1366    5.1852  -13.5209 C   0  0  0  1  0  0
  -18.2362    5.5092  -12.0349 C   0  0  0  1  0  0
  -17.7787    6.9557  -11.9274 C   0  0  0  1  0  0
  -16.9359    7.2449  -13.1801 C   0  0  0  1  0  0
  -15.4618    6.6606  -15.9259 C   0  0  0  1  0  0
  -15.4175    6.5893  -17.3047 C   0  0  0  1  0  0
  -14.2970    7.0600  -18.1614 C   0  0  0  1  0  0
  -12.9951    6.7380  -17.8249 C   0  0  0  1  0  0
  -11.9271    7.1460  -18.6168 C   0  0  0  1  0  0
  -12.1479    7.8647  -19.7804 C   0  0  0  1  0  0
  -13.4535    8.2182  -20.1022 C   0  0  0  1  0  0
  -14.5130    7.8253  -19.2900 C   0  0  0  1  0  0
  -11.0637    8.2457  -20.5593 O   0  0  0  1  0  0
  -11.1543    7.9964  -21.9268 C   0  0  0  1  0  0
  -11.8648    6.9254  -22.4719 C   0  0  0  1  0  0
  -11.9440    6.7657  -23.8496 C   0  0  0  1  0  0
  -11.2960    7.6598  -24.6915 C   0  0  0  1  0  0
  -10.5458    8.6967  -24.1537 C   0  0  0  1  0  0
  -10.4643    8.8508  -22.7758 C   0  0  0  1  0  0
  -17.3504    5.6504  -20.8574 H   0  0
  -15.7771    5.9565  -20.2024 H   0  0
  -20.0849    4.4444  -17.6283 H   0  0
  -16.0214    5.3422  -13.5252 H   0  0
  -18.1104    4.1136  -13.7222 H   0  0
  -19.0096    5.6037  -14.0229 H   0  0
  -19.2233    5.4112  -11.6123 H   0  0
  -17.5947    4.8420  -11.4675 H   0  0
  -18.6556    7.5963  -11.8965 H   0  0
  -17.2474    7.1165  -10.9966 H   0  0
  -15.9504    7.6414  -12.9423 H   0  0
  -17.4437    7.9877  -13.7969 H   0  0
  -14.6819    7.1226  -15.3380 H   0  0
  -12.7818    6.1577  -16.9383 H   0  0
  -10.9160    6.8875  -18.3481 H   0  0
  -13.6354    8.7963  -20.9918 H   0  0
  -15.5126    8.1378  -19.5484 H   0  0
  -12.3417    6.1975  -21.8321 H   0  0
  -12.5027    5.9403  -24.2656 H   0  0
  -11.3602    7.5400  -25.7636 H   0  0
  -10.0216    9.3789  -24.8076 H   0  0
   -9.8584    9.6356  -22.3516 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372157117202448

> <LigScore1_Dreiding>
3.42

> <LigScore2_Dreiding>
5.2

> <-PLP1>
80.72

> <-PLP2>
77.48

> <Jain>
5.76

> <-PMF>
77.47

> <-PMF04>
19.1

> <AbsoluteEnergy>
147.754

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
18

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
1.707

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
97

> <LibDockScore>
76.896

> <HotSpots>
-18.40,4.72,-11.29,A,50,11
-16.20,6.52,-15.49,A,24,14
-14.40,5.92,-18.29,A,15,17

> <-In-Situ Starting Energy>
-192.479

> <-In-Situ Final Energy>
14.634

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
1

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
4

> <Favorable A:ALA428>
2

> <Favorable A:LYS430>
1

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
0

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
1

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
2

> <Favorable A:CYS481>
0

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
2

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
0

> <Favorable A:PHE540>
0

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
1

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
4

> <Hydrophobic A:ALA428>
2

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
0

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
2

> <Hydrophobic A:PHE540>
0

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
1

> <HydrogenBond A:MET477>
2

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -10.0369   10.1734  -10.6617 N   0  0  0  1  0  0
  -10.8181    9.5779  -11.5896 C   0  0  0  1  0  0
  -10.5382    8.2864  -11.8287 N   0  0  0  1  0  0
  -11.2905    7.6173  -12.7169 C   0  0  0  1  0  0
  -12.3624    8.1207  -13.3322 N   0  0  0  1  0  0
  -12.6228    9.4225  -13.1165 C   0  0  0  1  0  0
  -11.8497   10.2121  -12.2360 C   0  0  0  1  0  0
  -13.6505   10.2107  -13.6326 N   0  0  0  1  0  0
  -14.7136    9.7219  -14.5418 C   0  0  0  1  0  0
  -16.0477    9.7026  -13.7861 C   0  0  0  1  0  0
  -16.6137   11.0990  -14.0082 C   0  0  0  1  0  0
  -16.3133   11.3390  -15.4779 C   0  0  0  1  0  0
  -14.9448   10.6844  -15.7269 C   0  0  0  1  0  0
  -13.4558   11.4420  -13.1076 C   0  0  0  1  0  0
  -12.3891   11.5159  -12.2366 C   0  0  0  1  0  0
  -11.9282   12.6944  -11.4603 C   0  0  0  1  0  0
  -12.8024   13.3858  -10.6408 C   0  0  0  1  0  0
  -12.3427   14.3992   -9.8017 C   0  0  0  1  0  0
  -10.9886   14.7061   -9.7679 C   0  0  0  1  0  0
  -10.1318   14.0868  -10.6687 C   0  0  0  1  0  0
  -10.6089   13.0995  -11.5198 C   0  0  0  1  0  0
  -10.4794   15.5600   -8.8084 O   0  0  0  1  0  0
   -9.6729   14.8739   -7.9063 C   0  0  0  1  0  0
  -10.1446   13.7634   -7.2071 C   0  0  0  1  0  0
   -9.3129   13.0821   -6.3273 C   0  0  0  1  0  0
   -8.0046   13.5074   -6.1404 C   0  0  0  1  0  0
   -7.5321   14.6131   -6.8342 C   0  0  0  1  0  0
   -8.3683   15.3017   -7.7055 C   0  0  0  1  0  0
   -9.2745    9.6603  -10.2761 H   0  0
  -10.2166   11.1078  -10.3528 H   0  0
  -11.0065    6.5987  -12.9393 H   0  0
  -14.4739    8.7159  -14.8908 H   0  0
  -15.9405    9.4406  -12.7363 H   0  0
  -16.7160    8.9668  -14.2360 H   0  0
  -17.6639   11.1987  -13.7864 H   0  0
  -16.1085   11.8188  -13.3702 H   0  0
  -16.3776   12.3759  -15.7840 H   0  0
  -17.0835   10.8340  -16.0425 H   0  0
  -14.9376   10.1554  -16.6795 H   0  0
  -14.1637   11.4432  -15.7853 H   0  0
  -14.0676   12.3045  -13.3338 H   0  0
  -13.8561   13.1310  -10.6310 H   0  0
  -13.0195   14.9010   -9.1228 H   0  0
   -9.0842   14.3490  -10.6764 H   0  0
   -9.9161   12.6161  -12.1952 H   0  0
  -11.1679   13.4406   -7.3265 H   0  0
   -9.6907   12.2334   -5.7760 H   0  0
   -7.3561   12.9941   -5.4439 H   0  0
   -6.5135   14.9390   -6.6836 H   0  0
   -8.0118   16.1711   -8.2360 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372161412169744

> <LigScore1_Dreiding>
2.09

> <LigScore2_Dreiding>
4.75

> <-PLP1>
94.5

> <-PLP2>
80.47

> <Jain>
3.62

> <-PMF>
116.84

> <-PMF04>
49.35

> <AbsoluteEnergy>
147.442

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
16

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
1.395

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
98

> <LibDockScore>
76.707

> <HotSpots>
-16.80,9.32,-14.09,A,31,10
-16.60,11.32,-15.29,A,27,12
-9.00,13.52,-7.09,A,99,28

> <-In-Situ Starting Energy>
-56713.848

> <-In-Situ Final Energy>
16.62

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
0

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
1

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
0

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
2

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
0

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
1

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
1

> <Favorable A:LEU528>
1

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
1

> <Favorable A:PHE540>
0

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
1

> <Favorable A:TYR551>
1

> <Favorable A:LYS558>
1

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
2

> <Charge A:ASP539>
1

> <Hydrophobic A:LEU408>
0

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
1

> <Hydrophobic A:VAL416>
0

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
0

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
0

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
1

> <Hydrophobic A:LEU528>
1

> <Hydrophobic A:PHE540>
0

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
1

> <Hydrophobic A:TYR551>
1

> <Hydrophobic A:LYS558>
1

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
1

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -15.8310    9.9222  -13.5078 N   0  0  0  1  0  0
  -14.9230    9.4709  -14.4010 C   0  0  0  1  0  0
  -13.8434   10.2537  -14.5322 N   0  0  0  1  0  0
  -12.9527    9.9728  -15.4889 C   0  0  0  1  0  0
  -13.0454    8.9357  -16.3171 N   0  0  0  1  0  0
  -14.0908    8.1070  -16.1549 C   0  0  0  1  0  0
  -15.0673    8.3185  -15.1480 C   0  0  0  1  0  0
  -14.4436    6.9652  -16.8849 N   0  0  0  1  0  0
  -13.7339    6.3588  -18.0386 C   0  0  0  1  0  0
  -14.5581    6.5673  -19.3114 C   0  0  0  1  0  0
  -14.1093    7.9335  -19.8339 C   0  0  0  1  0  0
  -12.6531    8.1036  -19.3826 C   0  0  0  1  0  0
  -12.3697    6.9454  -18.4180 C   0  0  0  1  0  0
  -15.5775    6.5223  -16.3136 C   0  0  0  1  0  0
  -15.9769    7.2287  -15.1988 C   0  0  0  1  0  0
  -17.1172    6.8872  -14.2997 C   0  0  0  1  0  0
  -17.1307    7.2936  -12.9865 C   0  0  0  1  0  0
  -18.2687    7.1873  -12.2079 C   0  0  0  1  0  0
  -19.4403    6.6500  -12.7210 C   0  0  0  1  0  0
  -19.3683    6.0818  -13.9841 C   0  0  0  1  0  0
  -18.2083    6.1662  -14.7491 C   0  0  0  1  0  0
  -20.6831    6.7169  -12.0820 O   0  0  0  1  0  0
  -20.7416    7.0809  -10.7421 C   0  0  0  1  0  0
  -21.6616    8.0514  -10.3774 C   0  0  0  1  0  0
  -21.6716    8.5472   -9.0806 C   0  0  0  1  0  0
  -20.7533    8.0795   -8.1531 C   0  0  0  1  0  0
  -19.9146    7.0254   -8.4786 C   0  0  0  1  0  0
  -19.9374    6.5005   -9.7631 C   0  0  0  1  0  0
  -15.5884   10.6408  -12.8470 H   0  0
  -16.7647    9.5700  -13.4789 H   0  0
  -12.1034   10.6327  -15.5949 H   0  0
  -13.6161    5.2972  -17.8181 H   0  0
  -15.6355    6.5124  -19.1533 H   0  0
  -14.2992    5.8018  -20.0428 H   0  0
  -14.2053    8.0057  -20.9154 H   0  0
  -14.7256    8.7137  -19.3854 H   0  0
  -12.5154    9.0688  -18.8957 H   0  0
  -11.9663    8.0679  -20.2291 H   0  0
  -11.8171    6.1810  -18.9583 H   0  0
  -11.7436    7.2151  -17.5687 H   0  0
  -16.1173    5.6692  -16.6974 H   0  0
  -16.2581    7.7230  -12.5339 H   0  0
  -18.2317    7.5880  -11.2170 H   0  0
  -20.2433    5.6118  -14.3956 H   0  0
  -18.2330    5.7478  -15.7448 H   0  0
  -22.3411    8.4391  -11.1218 H   0  0
  -22.3726    9.3147   -8.7943 H   0  0
  -20.6984    8.5335   -7.1751 H   0  0
  -19.2339    6.6328   -7.7388 H   0  0
  -19.2803    5.6848  -10.0243 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372165707137040

> <LigScore1_Dreiding>
3.53

> <LigScore2_Dreiding>
5.8

> <-PLP1>
86.35

> <-PLP2>
78.36

> <Jain>
4.3

> <-PMF>
117.05

> <-PMF04>
39.95

> <AbsoluteEnergy>
162.605

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
49

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
16.558

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
99

> <LibDockScore>
73.01

> <HotSpots>
-12.60,6.32,-17.69,A,17,10
-19.40,6.32,-13.69,A,35,20
-21.60,6.32,-8.29,A,80,27

> <-In-Situ Starting Energy>
-1444.257

> <-In-Situ Final Energy>
6.747

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
1

> <Favorable A:THR410>
0

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
0

> <Favorable A:VAL416>
2

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
1

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
1

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
1

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
0

> <Favorable A:ARG525>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
2

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
1

> <Favorable A:PHE540>
1

> <Favorable A:LEU542>
1

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
1

> <Charge A:LYS430>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
1

> <Hydrophobic A:THR410>
0

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
2

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
1

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
1

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
2

> <Hydrophobic A:PHE540>
1

> <Hydrophobic A:LEU542>
1

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
0

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
0

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
1

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -10.8425    9.7226  -10.9651 N   0  0  0  1  0  0
  -10.9139    8.8941  -12.0334 C   0  0  0  1  0  0
  -10.6333    7.6051  -11.7935 N   0  0  0  1  0  0
  -10.6489    6.7470  -12.8230 C   0  0  0  1  0  0
  -10.9485    7.0766  -14.0822 N   0  0  0  1  0  0
  -11.2406    8.3663  -14.3227 C   0  0  0  1  0  0
  -11.2547    9.3205  -13.2904 C   0  0  0  1  0  0
  -11.5740    9.0060  -15.5204 N   0  0  0  1  0  0
  -11.6208    8.3192  -16.8294 C   0  0  0  1  0  0
  -12.5742    7.1228  -16.8726 C   0  0  0  1  0  0
  -12.8596    6.8845  -18.3596 C   0  0  0  1  0  0
  -12.4870    8.1869  -19.0850 C   0  0  0  1  0  0
  -12.1007    9.1886  -17.9926 C   0  0  0  1  0  0
  -11.8111   10.3012  -15.1893 C   0  0  0  1  0  0
  -11.6543   10.5479  -13.8369 C   0  0  0  1  0  0
  -11.8777   11.7644  -13.0254 C   0  0  0  1  0  0
  -13.0543   11.8502  -12.3199 C   0  0  0  1  0  0
  -13.2118   12.8019  -11.3312 C   0  0  0  1  0  0
  -12.2001   13.7108  -11.0490 C   0  0  0  1  0  0
  -11.0793   13.7244  -11.8738 C   0  0  0  1  0  0
  -10.9256   12.7544  -12.8680 C   0  0  0  1  0  0
  -12.2902   14.5537   -9.9474 O   0  0  0  1  0  0
  -12.7153   13.8560   -8.8175 C   0  0  0  1  0  0
  -11.9087   12.8734   -8.2483 C   0  0  0  1  0  0
  -12.3822   12.1007   -7.1934 C   0  0  0  1  0  0
  -13.6640   12.3088   -6.6996 C   0  0  0  1  0  0
  -14.4642   13.3002   -7.2515 C   0  0  0  1  0  0
  -13.9872   14.0732   -8.3035 C   0  0  0  1  0  0
  -10.5707    9.3648  -10.0756 H   0  0
  -11.0609   10.6960  -11.0520 H   0  0
  -10.3913    5.7181  -12.6141 H   0  0
  -10.6156    7.9619  -17.0579 H   0  0
  -13.5021    7.3710  -16.3561 H   0  0
  -12.1527    6.2418  -16.3890 H   0  0
  -12.2495    6.0620  -18.7358 H   0  0
  -13.9035    6.6135  -18.5198 H   0  0
  -13.3012    8.5593  -19.7073 H   0  0
  -11.6327    8.0046  -19.7389 H   0  0
  -11.3463    9.9023  -18.3243 H   0  0
  -12.9880    9.7498  -17.6976 H   0  0
  -12.1001   11.0652  -15.8970 H   0  0
  -13.8724   11.1647  -12.4966 H   0  0
  -14.1396   12.8097  -10.7778 H   0  0
  -10.3016   14.4518  -11.6956 H   0  0
  -10.0157   12.7308  -13.4509 H   0  0
  -10.9177   12.7037   -8.6402 H   0  0
  -11.7574   11.3349   -6.7568 H   0  0
  -14.0351   11.7052   -5.8835 H   0  0
  -15.4554   13.4807   -6.8631 H   0  0
  -14.6082   14.8457   -8.7263 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372170002104336

> <LigScore1_Dreiding>
2.17

> <LigScore2_Dreiding>
4.89

> <-PLP1>
74.19

> <-PLP2>
65.61

> <Jain>
1.52

> <-PMF>
97.37

> <-PMF04>
31.6

> <AbsoluteEnergy>
154.407

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
43

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
8.36

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
100

> <LibDockScore>
63.007

> <HotSpots>
-10.00,6.32,-12.49,P,52,3
-14.40,7.72,-18.49,A,11,12
-15.00,13.92,-8.49,A,79,28

> <-In-Situ Starting Energy>
-447.663

> <-In-Situ Final Energy>
10.067

> <In-Situ Gradient>
0.001

> <Favorable A:LEU408>
0

> <Favorable A:THR410>
1

> <Favorable A:GLY411>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:GLY414>
1

> <Favorable A:VAL416>
2

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
1

> <Favorable A:MET449>
0

> <Favorable A:VAL458>
0

> <Favorable A:LEU460>
0

> <Favorable A:ILE472>
0

> <Favorable A:THR474>
0

> <Favorable A:GLU475>
0

> <Favorable A:TYR476>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
0

> <Favorable A:ARG525>
1

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
0

> <Favorable A:SER538>
0

> <Favorable A:ASP539>
1

> <Favorable A:PHE540>
0

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Favorable A:LYS558>
0

> <Unfavorable A:GLY414>
0

> <Unfavorable A:LYS430>
0

> <Unfavorable A:SER538>
0

> <Charge A:LYS430>
1

> <Charge A:ASP539>
1

> <Hydrophobic A:LEU408>
0

> <Hydrophobic A:THR410>
1

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
2

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
0

> <Hydrophobic A:MET449>
0

> <Hydrophobic A:VAL458>
0

> <Hydrophobic A:LEU460>
0

> <Hydrophobic A:ILE472>
0

> <Hydrophobic A:TYR476>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
0

> <Hydrophobic A:PHE540>
0

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <Hydrophobic A:LYS558>
0

> <HydrogenBond A:LEU408>
0

> <HydrogenBond A:THR410>
0

> <HydrogenBond A:GLY411>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLY414>
1

> <HydrogenBond A:ALA428>
0

> <HydrogenBond A:LYS430>
0

> <HydrogenBond A:ILE472>
0

> <HydrogenBond A:THR474>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ARG525>
1

> <HydrogenBond A:ASN526>
0

> <HydrogenBond A:SER538>
0

> <HydrogenBond A:ASP539>
0

> <Other A:CYS481>
0

$$$$
