3GEN_ligand
  SciTegic09242217043D

 50 54  0  0  0  0            999 V2000
  -19.2787    4.7680  -16.8325 N   0  0
  -18.2349    5.0273  -17.6558 C   0  0
  -18.3629    4.6274  -18.9316 N   0  0
  -17.4071    4.9527  -19.8146 C   0  0
  -16.3050    5.6446  -19.5314 N   0  0
  -16.1410    5.9862  -18.2457 C   0  0
  -17.0937    5.6723  -17.2479 C   0  0
  -15.0823    6.6685  -17.6581 N   0  0
  -13.8896    7.1437  -18.3874 C   0  0
  -12.5907    6.5187  -17.8730 C   0  0
  -11.4835    7.5058  -18.2604 C   0  0
  -12.1805    8.8251  -18.6303 C   0  0
  -13.6574    8.6479  -18.2694 C   0  0
  -15.3970    6.7621  -16.3507 C   0  0
  -16.5858    6.1393  -16.0167 C   0  0
  -17.1663    6.0013  -14.6560 C   0  0
  -17.2788    7.1049  -13.8384 C   0  0
  -17.8215    6.9898  -12.5660 C   0  0
  -18.2667    5.7663  -12.0838 C   0  0
  -18.1357    4.6525  -12.9008 C   0  0
  -17.5917    4.7756  -14.1761 C   0  0
  -18.7353    5.6107  -10.7843 O   0  0
  -19.6300    6.5633  -10.3033 C   0  0
  -19.5087    6.9562   -8.9767 C   0  0
  -20.4307    7.8285   -8.4137 C   0  0
  -21.4878    8.3087   -9.1749 C   0  0
  -21.6099    7.9289  -10.5055 C   0  0
  -20.6806    7.0658  -11.0712 C   0  0
  -17.5327    4.6166  -20.8331 H   0  0
  -13.9751    6.9059  -19.4498 H   0  0
  -12.4223    5.5227  -18.2819 H   0  0
  -12.6174    6.4221  -16.7874 H   0  0
  -10.7818    7.6393  -17.4366 H   0  0
  -10.9146    7.1362  -19.1137 H   0  0
  -11.7338    9.6852  -18.1306 H   0  0
  -12.0921    8.9900  -19.7046 H   0  0
  -13.8291    8.9881  -17.2477 H   0  0
  -14.3211    9.2127  -18.9234 H   0  0
  -14.7674    7.2657  -15.6314 H   0  0
  -16.9496    8.0775  -14.1778 H   0  0
  -17.8800    7.8584  -11.9432 H   0  0
  -18.4490    3.6847  -12.5390 H   0  0
  -17.4973    3.8874  -14.7841 H   0  0
  -18.6883    6.5819   -8.3836 H   0  0
  -20.3183    8.1410   -7.3860 H   0  0
  -22.2068    8.9831   -8.7325 H   0  0
  -22.4248    8.3064  -11.1053 H   0  0
  -20.8012    6.7705  -12.1035 H   0  0
  -20.0646    4.2449  -17.1646 H   0  0
  -19.2905    5.0871  -15.8855 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  4 29  1  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
  9 30  1  0
 10 11  1  0
 10 31  1  0
 10 32  1  0
 11 12  1  0
 11 33  1  0
 11 34  1  0
 12 13  1  0
 12 35  1  0
 12 36  1  0
 13 37  1  0
 13 38  1  0
 14 15  2  0
 14 39  1  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 17 40  1  0
 18 19  2  0
 18 41  1  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 20 42  1  0
 21 43  1  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 24 44  1  0
 25 26  2  0
 25 45  1  0
 26 27  1  0
 26 46  1  0
 27 28  2  0
 27 47  1  0
 28 48  1  0
  1 49  1  0
  1 50  1  0
M  END
> <Name>
3GEN_ligand

> <TopHits>
10

> <-CDOCKER_ENERGY>
21.3557726

> <-CDOCKER_INTERACTION_ENERGY>
55.8387881

> <POSE_NUMBER>
1

> <CHARMm Energy>
0.97763

> <ChiRotor E-elec>
-2.6883

> <ChiRotor E-total>
-21.3158

> <ChiRotor E-vdw>
-31.6052

> <ChiRotor RMSD>
2.23148

> <Dihedral Energy>
25.2207

> <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>
0.02245

> <Initial RMS Gradient>
24.8347

> <Ionization pH>
7.4

> <IonizationIndex>
1

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

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

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

> <Refined Residues>
6

> <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

> <__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

> <Initial Potential Energy>
36.2529

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

> <Potential Energy>
0.97763

> <RMS Gradient>
0.08795

> <Van der Waals Energy>
4.00237

> <Electrostatic Energy>
-40.9001

> <Angle Energy>
11.6399

> <At pH>
7.4

> <OBJECTID>
9223372036858118157

> <Bond Energy>
0.99233

$$$$
3GEN_ligand
  SciTegic09242217043D

 50 54  0  0  0  0            999 V2000
  -19.2694    4.8024  -16.9619 N   0  0
  -18.1944    5.0645  -17.7427 C   0  0
  -18.2855    4.6863  -19.0292 N   0  0
  -17.2933    5.0100  -19.8709 C   0  0
  -16.1851    5.6700  -19.5372 N   0  0
  -16.0616    5.9968  -18.2433 C   0  0
  -17.0595    5.6906  -17.2854 C   0  0
  -15.0151    6.6554  -17.6063 N   0  0
  -13.7741    7.1107  -18.2672 C   0  0
  -12.5140    6.5034  -17.6419 C   0  0
  -11.3910    7.5059  -17.9317 C   0  0
  -12.0638    8.8238  -18.3431 C   0  0
  -13.5664    8.6194  -18.1475 C   0  0
  -15.3881    6.7589  -16.3174 C   0  0
  -16.5924    6.1443  -16.0313 C   0  0
  -17.2053    6.0048  -14.6845 C   0  0
  -17.3197    7.1025  -13.8564 C   0  0
  -17.8544    6.9763  -12.5814 C   0  0
  -18.2909    5.7463  -12.1073 C   0  0
  -18.1652    4.6407  -12.9360 C   0  0
  -17.6422    4.7787  -14.2179 C   0  0
  -18.7536    5.5811  -10.8079 O   0  0
  -19.6430    6.5352  -10.3198 C   0  0
  -19.5275    6.9003   -8.9855 C   0  0
  -20.4445    7.7702   -8.4111 C   0  0
  -21.4971    8.2685   -9.1667 C   0  0
  -21.6125    7.9201  -10.5060 C   0  0
  -20.6833    7.0654  -11.0846 C   0  0
  -17.3914    4.6989  -20.9002 H   0  0
  -13.7868    6.8497  -19.3266 H   0  0
  -12.2908    5.5084  -18.0300 H   0  0
  -12.6338    6.4104  -16.5621 H   0  0
  -10.7558    7.6396  -17.0558 H   0  0
  -10.7587    7.1482  -18.7434 H   0  0
  -11.6953    9.6734  -17.7692 H   0  0
  -11.8523    9.0258  -19.3934 H   0  0
  -13.8493    8.9653  -17.1533 H   0  0
  -14.1657    9.1703  -18.8730 H   0  0
  -14.7880    7.2625  -15.5736 H   0  0
  -16.9934    8.0794  -14.1851 H   0  0
  -17.9067    7.8388  -11.9471 H   0  0
  -18.4703    3.6671  -12.5827 H   0  0
  -17.5581    3.8968  -14.8350 H   0  0
  -18.7201    6.5009   -8.3913 H   0  0
  -20.3358    8.0592   -7.3764 H   0  0
  -22.2192    8.9336   -8.7155 H   0  0
  -22.4243    8.3093  -11.1025 H   0  0
  -20.7997    6.7953  -12.1243 H   0  0
  -19.3217    5.1333  -16.0200 H   0  0
  -20.0381    4.2707  -17.3198 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  4 29  1  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
  9 30  1  0
 10 11  1  0
 10 31  1  0
 10 32  1  0
 11 12  1  0
 11 33  1  0
 11 34  1  0
 12 13  1  0
 12 35  1  0
 12 36  1  0
 13 37  1  0
 13 38  1  0
 14 15  2  0
 14 39  1  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 17 40  1  0
 18 19  2  0
 18 41  1  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 20 42  1  0
 21 43  1  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 24 44  1  0
 25 26  2  0
 25 45  1  0
 26 27  1  0
 26 46  1  0
 27 28  2  0
 27 47  1  0
 28 48  1  0
  1 49  1  0
  1 50  1  0
M  END
> <Name>
3GEN_ligand

> <TopHits>
10

> <-CDOCKER_ENERGY>
21.2972459

> <-CDOCKER_INTERACTION_ENERGY>
55.8670868

> <POSE_NUMBER>
2

> <CHARMm Energy>
0.97763

> <ChiRotor E-elec>
-2.6883

> <ChiRotor E-total>
-21.3158

> <ChiRotor E-vdw>
-31.6052

> <ChiRotor RMSD>
2.23148

> <Dihedral Energy>
25.2207

> <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>
0.02245

> <Initial RMS Gradient>
24.8347

> <Ionization pH>
7.4

> <IonizationIndex>
1

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

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

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

> <Refined Residues>
6

> <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

> <__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

> <Initial Potential Energy>
36.2529

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

> <Potential Energy>
0.97763

> <RMS Gradient>
0.08795

> <Van der Waals Energy>
4.00237

> <Electrostatic Energy>
-40.9001

> <Angle Energy>
11.6399

> <At pH>
7.4

> <OBJECTID>
9223372036858118157

> <Bond Energy>
0.99233

$$$$
3GEN_ligand
  SciTegic09242217043D

 50 54  0  0  0  0            999 V2000
  -19.2370    4.8023  -17.0089 N   0  0
  -18.1699    5.0647  -17.7998 C   0  0
  -18.2734    4.6808  -19.0824 N   0  0
  -17.2937    5.0047  -19.9377 C   0  0
  -16.1920    5.6841  -19.6236 N   0  0
  -16.0522    6.0102  -18.3306 C   0  0
  -17.0322    5.6966  -17.3576 C   0  0
  -14.9973    6.6729  -17.7115 N   0  0
  -13.7793    7.1417  -18.4040 C   0  0
  -12.4966    6.5117  -17.8576 C   0  0
  -11.4085    7.4807  -18.3103 C   0  0
  -12.0425    8.8661  -18.1639 C   0  0
  -13.5605    8.6565  -18.2874 C   0  0
  -15.3419    6.7598  -16.4126 C   0  0
  -16.5463    6.1504  -16.1104 C   0  0
  -17.1501    6.0114  -14.7587 C   0  0
  -17.2508    7.1071  -13.9255 C   0  0
  -17.7881    6.9831  -12.6496 C   0  0
  -18.2455    5.7557  -12.1838 C   0  0
  -18.1370    4.6539  -13.0207 C   0  0
  -17.6003    4.7884  -14.2971 C   0  0
  -18.6919    5.5761  -10.8792 O   0  0
  -19.5648    6.5247  -10.3516 C   0  0
  -19.4206    6.8582   -9.0112 C   0  0
  -20.3321    7.7033   -8.3928 C   0  0
  -21.4009    8.2195   -9.1136 C   0  0
  -21.5413    7.9070  -10.4594 C   0  0
  -20.6208    7.0722  -11.0802 C   0  0
  -17.3948    4.6748  -20.9606 H   0  0
  -13.8349    6.8971  -19.4668 H   0  0
  -12.3367    5.4983  -18.2243 H   0  0
  -12.5183    6.4728  -16.7678 H   0  0
  -10.4869    7.3810  -17.7390 H   0  0
  -11.1716    7.2964  -19.3588 H   0  0
  -11.8064    9.2700  -17.1788 H   0  0
  -11.6572    9.5680  -18.9048 H   0  0
  -14.0588    9.0703  -17.4098 H   0  0
  -13.9686    9.1655  -19.1612 H   0  0
  -14.7202    7.2489  -15.6770 H   0  0
  -16.9128    8.0823  -14.2511 H   0  0
  -17.8223    7.8417  -12.0078 H   0  0
  -18.4561    3.6830  -12.6725 H   0  0
  -17.5247    3.9064  -14.9159 H   0  0
  -18.5964    6.4495   -8.4482 H   0  0
  -20.2046    7.9602   -7.3519 H   0  0
  -22.1151    8.8687   -8.6282 H   0  0
  -22.3674    8.3102  -11.0265 H   0  0
  -20.7574    6.8284  -12.1231 H   0  0
  -19.2662    5.0933  -16.0527 H   0  0
  -20.0261    4.3087  -17.3756 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  4 29  1  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
  9 30  1  0
 10 11  1  0
 10 31  1  0
 10 32  1  0
 11 12  1  0
 11 33  1  0
 11 34  1  0
 12 13  1  0
 12 35  1  0
 12 36  1  0
 13 37  1  0
 13 38  1  0
 14 15  2  0
 14 39  1  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 17 40  1  0
 18 19  2  0
 18 41  1  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 20 42  1  0
 21 43  1  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 24 44  1  0
 25 26  2  0
 25 45  1  0
 26 27  1  0
 26 46  1  0
 27 28  2  0
 27 47  1  0
 28 48  1  0
  1 49  1  0
  1 50  1  0
M  END
> <Name>
3GEN_ligand

> <TopHits>
10

> <-CDOCKER_ENERGY>
21.1372472

> <-CDOCKER_INTERACTION_ENERGY>
55.7164158

> <POSE_NUMBER>
3

> <CHARMm Energy>
0.97763

> <ChiRotor E-elec>
-2.6883

> <ChiRotor E-total>
-21.3158

> <ChiRotor E-vdw>
-31.6052

> <ChiRotor RMSD>
2.23148

> <Dihedral Energy>
25.2207

> <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>
0.02245

> <Initial RMS Gradient>
24.8347

> <Ionization pH>
7.4

> <IonizationIndex>
1

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

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

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

> <Refined Residues>
6

> <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

> <__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

> <Initial Potential Energy>
36.2529

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

> <Potential Energy>
0.97763

> <RMS Gradient>
0.08795

> <Van der Waals Energy>
4.00237

> <Electrostatic Energy>
-40.9001

> <Angle Energy>
11.6399

> <At pH>
7.4

> <OBJECTID>
9223372036858118157

> <Bond Energy>
0.99233

$$$$
3GEN_ligand
  SciTegic09242217043D

 50 54  0  0  0  0            999 V2000
  -19.1904    4.8222  -17.0082 N   0  0
  -18.1348    5.0943  -17.8128 C   0  0
  -18.2479    4.7013  -19.0926 N   0  0
  -17.2784    5.0321  -19.9564 C   0  0
  -16.1833    5.7282  -19.6569 N   0  0
  -16.0362    6.0689  -18.3700 C   0  0
  -17.0000    5.7438  -17.3857 C   0  0
  -14.9876    6.7605  -17.7720 N   0  0
  -13.7991    7.2574  -18.5035 C   0  0
  -12.5117    6.5814  -18.0278 C   0  0
  -12.0152    7.4182  -16.8464 C   0  0
  -12.6271    8.8167  -17.0209 C   0  0
  -13.5606    8.7446  -18.2380 C   0  0
  -15.3157    6.8403  -16.4664 C   0  0
  -16.5065    6.2098  -16.1473 C   0  0
  -17.0985    6.0613  -14.7914 C   0  0
  -17.5404    4.8316  -14.3381 C   0  0
  -18.0971    4.6875  -13.0721 C   0  0
  -18.2176    5.7840  -12.2318 C   0  0
  -17.7525    7.0147  -12.6804 C   0  0
  -17.2029    7.1493  -13.9493 C   0  0
  -18.6908    5.5997  -10.9392 O   0  0
  -19.5964    6.5346  -10.4465 C   0  0
  -19.5081    6.8663   -9.1016 C   0  0
  -20.4453    7.7107   -8.5226 C   0  0
  -21.4905    8.2173   -9.2837 C   0  0
  -21.5803    7.8984  -10.6326 C   0  0
  -20.6291    7.0718  -11.2163 C   0  0
  -17.3843    4.6955  -20.9762 H   0  0
  -13.9255    7.0805  -19.5728 H   0  0
  -11.7718    6.6295  -18.8280 H   0  0
  -12.6465    5.5280  -17.7788 H   0  0
  -12.3554    6.9765  -15.9094 H   0  0
  -10.9266    7.4513  -16.8083 H   0  0
  -13.1811    9.0957  -16.1245 H   0  0
  -11.8577    9.5753  -17.1671 H   0  0
  -14.4875    9.3012  -18.0960 H   0  0
  -13.0530    9.1788  -19.0998 H   0  0
  -14.7005    7.3412  -15.7340 H   0  0
  -17.4569    3.9551  -14.9626 H   0  0
  -18.4267    3.7157  -12.7356 H   0  0
  -17.7951    7.8694  -12.0331 H   0  0
  -16.8641    8.1265  -14.2671 H   0  0
  -18.7063    6.4571   -8.5048 H   0  0
  -20.3585    7.9705   -7.4784 H   0  0
  -22.2271    8.8634   -8.8268 H   0  0
  -22.3909    8.2904  -11.2303 H   0  0
  -20.7276    6.8251  -12.2638 H   0  0
  -19.2048    5.1047  -16.0496 H   0  0
  -19.9848    4.3283  -17.3636 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  4 29  1  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
  9 30  1  0
 10 11  1  0
 10 31  1  0
 10 32  1  0
 11 12  1  0
 11 33  1  0
 11 34  1  0
 12 13  1  0
 12 35  1  0
 12 36  1  0
 13 37  1  0
 13 38  1  0
 14 15  2  0
 14 39  1  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 17 40  1  0
 18 19  2  0
 18 41  1  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 20 42  1  0
 21 43  1  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 24 44  1  0
 25 26  2  0
 25 45  1  0
 26 27  1  0
 26 46  1  0
 27 28  2  0
 27 47  1  0
 28 48  1  0
  1 49  1  0
  1 50  1  0
M  END
> <Name>
3GEN_ligand

> <TopHits>
10

> <-CDOCKER_ENERGY>
21.038997

> <-CDOCKER_INTERACTION_ENERGY>
55.6964506

> <POSE_NUMBER>
4

> <CHARMm Energy>
0.97763

> <ChiRotor E-elec>
-2.6883

> <ChiRotor E-total>
-21.3158

> <ChiRotor E-vdw>
-31.6052

> <ChiRotor RMSD>
2.23148

> <Dihedral Energy>
25.2207

> <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>
0.02245

> <Initial RMS Gradient>
24.8347

> <Ionization pH>
7.4

> <IonizationIndex>
1

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

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

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

> <Refined Residues>
6

> <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

> <__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

> <Initial Potential Energy>
36.2529

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

> <Potential Energy>
0.97763

> <RMS Gradient>
0.08795

> <Van der Waals Energy>
4.00237

> <Electrostatic Energy>
-40.9001

> <Angle Energy>
11.6399

> <At pH>
7.4

> <OBJECTID>
9223372036858118157

> <Bond Energy>
0.99233

$$$$
3GEN_ligand
  SciTegic09242217043D

 50 54  0  0  0  0            999 V2000
  -19.3402    4.7542  -16.8274 N   0  0
  -18.2850    4.9929  -17.6401 C   0  0
  -18.4014    4.5660  -18.9065 N   0  0
  -17.4469    4.8836  -19.7921 C   0  0
  -16.3500    5.5866  -19.5167 N   0  0
  -16.1923    5.9460  -18.2357 C   0  0
  -17.1466    5.6440  -17.2370 C   0  0
  -15.1400    6.6374  -17.6523 N   0  0
  -13.9433    7.1004  -18.3793 C   0  0
  -12.6487    6.4903  -17.8188 C   0  0
  -11.6193    7.6254  -17.7781 C   0  0
  -12.2595    8.8016  -18.5191 C   0  0
  -13.7581    8.6157  -18.3046 C   0  0
  -15.4603    6.7535  -16.3492 C   0  0
  -16.6445    6.1258  -16.0101 C   0  0
  -17.2209    5.9930  -14.6493 C   0  0
  -17.3251    7.0944  -13.8264 C   0  0
  -17.8613    6.9774  -12.5514 C   0  0
  -18.3072    5.7518  -12.0723 C   0  0
  -18.1773    4.6403  -12.8918 C   0  0
  -17.6456    4.7670  -14.1699 C   0  0
  -18.7845    5.5932  -10.7772 O   0  0
  -19.6752    6.5531  -10.3009 C   0  0
  -20.7127    7.0770  -11.0741 C   0  0
  -21.6443    7.9351  -10.5038 C   0  0
  -21.5286    8.2995   -9.1684 C   0  0
  -20.4768    7.8081   -8.4071 C   0  0
  -19.5627    6.9290   -8.9696 C   0  0
  -17.5707    4.5313  -20.8052 H   0  0
  -14.0095    6.8306  -19.4360 H   0  0
  -12.3106    5.6655  -18.4462 H   0  0
  -12.7912    6.0877  -16.8157 H   0  0
  -11.4322    7.9039  -16.7405 H   0  0
  -10.6656    7.3347  -18.2170 H   0  0
  -11.8996    9.7682  -18.1651 H   0  0
  -12.0355    8.7280  -19.5834 H   0  0
  -14.0343    8.9943  -17.3194 H   0  0
  -14.3634    9.1395  -19.0451 H   0  0
  -14.8353    7.2737  -15.6388 H   0  0
  -16.9928    8.0682  -14.1606 H   0  0
  -17.9162    7.8432  -11.9220 H   0  0
  -18.4827    3.6686  -12.5349 H   0  0
  -17.5635    3.8795  -14.7791 H   0  0
  -20.8277    6.8023  -12.1126 H   0  0
  -22.4582    8.3180  -11.1024 H   0  0
  -22.2484    8.9693   -8.7226 H   0  0
  -20.3648    8.1116   -7.3772 H   0  0
  -18.7581    6.5323   -8.3705 H   0  0
  -20.1447    4.2757  -17.1804 H   0  0
  -19.3453    5.0458  -15.8711 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  4 29  1  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
  9 30  1  0
 10 11  1  0
 10 31  1  0
 10 32  1  0
 11 12  1  0
 11 33  1  0
 11 34  1  0
 12 13  1  0
 12 35  1  0
 12 36  1  0
 13 37  1  0
 13 38  1  0
 14 15  2  0
 14 39  1  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 17 40  1  0
 18 19  2  0
 18 41  1  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 20 42  1  0
 21 43  1  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 24 44  1  0
 25 26  2  0
 25 45  1  0
 26 27  1  0
 26 46  1  0
 27 28  2  0
 27 47  1  0
 28 48  1  0
  1 49  1  0
  1 50  1  0
M  END
> <Name>
3GEN_ligand

> <TopHits>
10

> <-CDOCKER_ENERGY>
21.0085813

> <-CDOCKER_INTERACTION_ENERGY>
55.6848904

> <POSE_NUMBER>
5

> <CHARMm Energy>
0.97763

> <ChiRotor E-elec>
-2.6883

> <ChiRotor E-total>
-21.3158

> <ChiRotor E-vdw>
-31.6052

> <ChiRotor RMSD>
2.23148

> <Dihedral Energy>
25.2207

> <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>
0.02245

> <Initial RMS Gradient>
24.8347

> <Ionization pH>
7.4

> <IonizationIndex>
1

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

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

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

> <Refined Residues>
6

> <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

> <__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

> <Initial Potential Energy>
36.2529

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

> <Potential Energy>
0.97763

> <RMS Gradient>
0.08795

> <Van der Waals Energy>
4.00237

> <Electrostatic Energy>
-40.9001

> <Angle Energy>
11.6399

> <At pH>
7.4

> <OBJECTID>
9223372036858118157

> <Bond Energy>
0.99233

$$$$
3GEN_ligand
  SciTegic09242217043D

 50 54  0  0  0  0            999 V2000
  -19.2216    4.7759  -16.9794 N   0  0
  -18.1595    5.0770  -17.7639 C   0  0
  -18.2590    4.7266  -19.0572 N   0  0
  -17.2797    5.0795  -19.9026 C   0  0
  -16.1852    5.7615  -19.5695 N   0  0
  -16.0542    6.0652  -18.2708 C   0  0
  -17.0303    5.7156  -17.3065 C   0  0
  -15.0127    6.7388  -17.6422 N   0  0
  -13.8180    7.2602  -18.3429 C   0  0
  -12.5362    6.5817  -17.8543 C   0  0
  -12.0114    7.4331  -16.6933 C   0  0
  -12.7162    8.7945  -16.7900 C   0  0
  -13.5957    8.7436  -18.0446 C   0  0
  -15.3523    6.7772  -16.3400 C   0  0
  -16.5515    6.1516  -16.0509 C   0  0
  -17.1539    5.9919  -14.7026 C   0  0
  -17.2649    7.0808  -13.8636 C   0  0
  -17.8125    6.9502  -12.5951 C   0  0
  -18.2626    5.7191  -12.1366 C   0  0
  -18.1392    4.6205  -12.9757 C   0  0
  -17.5953    4.7624  -14.2480 C   0  0
  -18.7274    5.5418  -10.8404 O   0  0
  -19.6057    6.4962  -10.3329 C   0  0
  -19.4724    6.8517   -8.9971 C   0  0
  -20.3932    7.7002   -8.3981 C   0  0
  -21.4628    8.1949   -9.1327 C   0  0
  -21.5881    7.8665  -10.4763 C   0  0
  -20.6569    7.0312  -11.0785 C   0  0
  -17.3770    4.7761  -20.9343 H   0  0
  -13.9271    7.1051  -19.4177 H   0  0
  -11.8028    6.5862  -18.6605 H   0  0
  -12.6948    5.5397  -17.5807 H   0  0
  -12.2370    6.9591  -15.7379 H   0  0
  -10.9291    7.5423  -16.7511 H   0  0
  -13.3297    8.9576  -15.9041 H   0  0
  -12.0043    9.6183  -16.8373 H   0  0
  -14.5269    9.2999  -17.9302 H   0  0
  -13.0537    9.1923  -18.8775 H   0  0
  -14.7393    7.2446  -15.5847 H   0  0
  -16.9289    8.0581  -14.1814 H   0  0
  -17.8644    7.8097  -11.9559 H   0  0
  -18.4525    3.6456  -12.6326 H   0  0
  -17.5078    3.8833  -14.8693 H   0  0
  -18.6513    6.4561   -8.4192 H   0  0
  -20.2763    7.9698   -7.3590 H   0  0
  -22.1922    8.8387   -8.6623 H   0  0
  -22.4150    8.2508  -11.0554 H   0  0
  -20.7832    6.7742  -12.1199 H   0  0
  -19.2430    5.0245  -16.0116 H   0  0
  -20.0141    4.2961  -17.3593 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  4 29  1  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
  9 30  1  0
 10 11  1  0
 10 31  1  0
 10 32  1  0
 11 12  1  0
 11 33  1  0
 11 34  1  0
 12 13  1  0
 12 35  1  0
 12 36  1  0
 13 37  1  0
 13 38  1  0
 14 15  2  0
 14 39  1  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 17 40  1  0
 18 19  2  0
 18 41  1  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 20 42  1  0
 21 43  1  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 24 44  1  0
 25 26  2  0
 25 45  1  0
 26 27  1  0
 26 46  1  0
 27 28  2  0
 27 47  1  0
 28 48  1  0
  1 49  1  0
  1 50  1  0
M  END
> <Name>
3GEN_ligand

> <TopHits>
10

> <-CDOCKER_ENERGY>
20.9519036

> <-CDOCKER_INTERACTION_ENERGY>
55.6888854

> <POSE_NUMBER>
6

> <CHARMm Energy>
0.97763

> <ChiRotor E-elec>
-2.6883

> <ChiRotor E-total>
-21.3158

> <ChiRotor E-vdw>
-31.6052

> <ChiRotor RMSD>
2.23148

> <Dihedral Energy>
25.2207

> <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>
0.02245

> <Initial RMS Gradient>
24.8347

> <Ionization pH>
7.4

> <IonizationIndex>
1

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

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

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

> <Refined Residues>
6

> <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

> <__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

> <Initial Potential Energy>
36.2529

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

> <Potential Energy>
0.97763

> <RMS Gradient>
0.08795

> <Van der Waals Energy>
4.00237

> <Electrostatic Energy>
-40.9001

> <Angle Energy>
11.6399

> <At pH>
7.4

> <OBJECTID>
9223372036858118157

> <Bond Energy>
0.99233

$$$$
3GEN_ligand
  SciTegic09242217043D

 50 54  0  0  0  0            999 V2000
  -19.3221    4.7655  -16.7790 N   0  0
  -18.2594    5.0753  -17.5592 C   0  0
  -18.3430    4.7280  -18.8557 N   0  0
  -17.3609    5.1057  -19.6882 C   0  0
  -16.2866    5.8130  -19.3392 N   0  0
  -16.1714    6.1157  -18.0371 C   0  0
  -17.1469    5.7282  -17.0866 C   0  0
  -15.1647    6.8254  -17.3822 N   0  0
  -13.9840    7.4498  -18.0118 C   0  0
  -14.3207    8.5773  -18.9821 C   0  0
  -13.0137    8.8075  -19.7461 C   0  0
  -12.2708    7.4608  -19.7295 C   0  0
  -13.0947    6.5221  -18.8383 C   0  0
  -15.5096    6.8181  -16.0838 C   0  0
  -16.6916    6.1563  -15.8199 C   0  0
  -17.2993    5.9737  -14.4800 C   0  0
  -17.6606    4.7279  -14.0032 C   0  0
  -18.1994    4.5817  -12.7277 C   0  0
  -18.4049    5.6898  -11.9166 C   0  0
  -18.0308    6.9360  -12.4016 C   0  0
  -17.4878    7.0739  -13.6701 C   0  0
  -18.9099    5.5195  -10.6320 O   0  0
  -19.7794    6.5020  -10.1616 C   0  0
  -19.6249    6.9332   -8.8515 C   0  0
  -20.5019    7.8628   -8.3103 C   0  0
  -21.5537    8.3537   -9.0715 C   0  0
  -21.7107    7.9339  -10.3855 C   0  0
  -20.8230    7.0184  -10.9325 C   0  0
  -17.4409    4.8068  -20.7225 H   0  0
  -13.3711    7.8752  -17.2153 H   0  0
  -14.6807    9.4678  -18.4685 H   0  0
  -15.0967    8.2591  -19.6776 H   0  0
  -13.1890    9.1712  -20.7586 H   0  0
  -12.4152    9.5586  -19.2285 H   0  0
  -12.1645    7.0492  -20.7336 H   0  0
  -11.2655    7.5890  -19.3263 H   0  0
  -13.7131    5.8954  -19.4771 H   0  0
  -12.4772    5.8664  -18.2241 H   0  0
  -14.9107    7.2877  -15.3167 H   0  0
  -17.5226    3.8465  -14.6129 H   0  0
  -18.4496    3.5964  -12.3639 H   0  0
  -18.1503    7.8029  -11.7823 H   0  0
  -17.2158    8.0631  -14.0121 H   0  0
  -18.8147    6.5441   -8.2540 H   0  0
  -20.3618    8.2078   -7.2967 H   0  0
  -22.2430    9.0649   -8.6412 H   0  0
  -22.5222    8.3162  -10.9867 H   0  0
  -20.9699    6.7025  -11.9549 H   0  0
  -20.1080    4.2788  -17.1628 H   0  0
  -19.3510    5.0138  -15.8112 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  4 29  1  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
  9 30  1  0
 10 11  1  0
 10 31  1  0
 10 32  1  0
 11 12  1  0
 11 33  1  0
 11 34  1  0
 12 13  1  0
 12 35  1  0
 12 36  1  0
 13 37  1  0
 13 38  1  0
 14 15  2  0
 14 39  1  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 17 40  1  0
 18 19  2  0
 18 41  1  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 20 42  1  0
 21 43  1  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 24 44  1  0
 25 26  2  0
 25 45  1  0
 26 27  1  0
 26 46  1  0
 27 28  2  0
 27 47  1  0
 28 48  1  0
  1 49  1  0
  1 50  1  0
M  END
> <Name>
3GEN_ligand

> <TopHits>
10

> <-CDOCKER_ENERGY>
20.8838901

> <-CDOCKER_INTERACTION_ENERGY>
56.2456217

> <POSE_NUMBER>
7

> <CHARMm Energy>
0.97763

> <ChiRotor E-elec>
-2.6883

> <ChiRotor E-total>
-21.3158

> <ChiRotor E-vdw>
-31.6052

> <ChiRotor RMSD>
2.23148

> <Dihedral Energy>
25.2207

> <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>
0.02245

> <Initial RMS Gradient>
24.8347

> <Ionization pH>
7.4

> <IonizationIndex>
1

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

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

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

> <Refined Residues>
6

> <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

> <__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

> <Initial Potential Energy>
36.2529

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

> <Potential Energy>
0.97763

> <RMS Gradient>
0.08795

> <Van der Waals Energy>
4.00237

> <Electrostatic Energy>
-40.9001

> <Angle Energy>
11.6399

> <At pH>
7.4

> <OBJECTID>
9223372036858118157

> <Bond Energy>
0.99233

$$$$
3GEN_ligand
  SciTegic09242217043D

 50 54  0  0  0  0            999 V2000
  -19.2147    4.6967  -16.9574 N   0  0
  -18.1666    5.0586  -17.7350 C   0  0
  -18.2276    4.6753  -19.0221 N   0  0
  -17.2769    5.1034  -19.8659 C   0  0
  -16.2531    5.8911  -19.5385 N   0  0
  -16.1575    6.2295  -18.2439 C   0  0
  -17.0977    5.7943  -17.2796 C   0  0
  -15.2022    7.0307  -17.6218 N   0  0
  -14.0883    7.7007  -18.3344 C   0  0
  -13.1175    6.6640  -18.9262 C   0  0
  -11.9245    6.5675  -17.9640 C   0  0
  -12.2180    7.5338  -16.8147 C   0  0
  -13.2016    8.5404  -17.4083 C   0  0
  -15.5404    7.0312  -16.3184 C   0  0
  -16.6612    6.2782  -16.0258 C   0  0
  -17.2356    6.0633  -14.6746 C   0  0
  -17.3726    7.1316  -13.8121 C   0  0
  -17.8916    6.9539  -12.5382 C   0  0
  -18.2990    5.7005  -12.1012 C   0  0
  -18.1450    4.6230  -12.9642 C   0  0
  -17.6215    4.8093  -14.2394 C   0  0
  -18.7616    5.4864  -10.8084 O   0  0
  -19.6001    6.4556  -10.2620 C   0  0
  -19.4026    6.8097   -8.9350 C   0  0
  -20.2710    7.6889   -8.3030 C   0  0
  -21.3542    8.2136   -8.9955 C   0  0
  -21.5412    7.8889  -10.3323 C   0  0
  -20.6618    7.0226  -10.9684 C   0  0
  -17.3404    4.7766  -20.8930 H   0  0
  -14.5199    8.3330  -19.1120 H   0  0
  -12.7720    6.9886  -19.9085 H   0  0
  -13.5887    5.6932  -19.0605 H   0  0
  -11.7643    5.5495  -17.6081 H   0  0
  -11.0172    6.8788  -18.4804 H   0  0
  -12.6893    6.9944  -15.9934 H   0  0
  -11.3160    8.0028  -16.4214 H   0  0
  -13.7532    9.1087  -16.6604 H   0  0
  -12.6471    9.2650  -18.0053 H   0  0
  -14.9901    7.5636  -15.5569 H   0  0
  -17.0790    8.1280  -14.1144 H   0  0
  -17.9638    7.7984  -11.8816 H   0  0
  -18.4240    3.6301  -12.6452 H   0  0
  -17.5082    3.9478  -14.8814 H   0  0
  -18.5678    6.3924   -8.3950 H   0  0
  -20.1023    7.9622   -7.2722 H   0  0
  -22.0444    8.8791   -8.4969 H   0  0
  -22.3744    8.3052  -10.8789 H   0  0
  -20.8313    6.7762  -12.0066 H   0  0
  -19.2620    4.9376  -15.9887 H   0  0
  -19.9745    4.1736  -17.3459 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  4 29  1  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
  9 30  1  0
 10 11  1  0
 10 31  1  0
 10 32  1  0
 11 12  1  0
 11 33  1  0
 11 34  1  0
 12 13  1  0
 12 35  1  0
 12 36  1  0
 13 37  1  0
 13 38  1  0
 14 15  2  0
 14 39  1  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 17 40  1  0
 18 19  2  0
 18 41  1  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 20 42  1  0
 21 43  1  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 24 44  1  0
 25 26  2  0
 25 45  1  0
 26 27  1  0
 26 46  1  0
 27 28  2  0
 27 47  1  0
 28 48  1  0
  1 49  1  0
  1 50  1  0
M  END
> <Name>
3GEN_ligand

> <TopHits>
10

> <-CDOCKER_ENERGY>
20.8462876

> <-CDOCKER_INTERACTION_ENERGY>
56.2442635

> <POSE_NUMBER>
8

> <CHARMm Energy>
0.97763

> <ChiRotor E-elec>
-2.6883

> <ChiRotor E-total>
-21.3158

> <ChiRotor E-vdw>
-31.6052

> <ChiRotor RMSD>
2.23148

> <Dihedral Energy>
25.2207

> <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>
0.02245

> <Initial RMS Gradient>
24.8347

> <Ionization pH>
7.4

> <IonizationIndex>
1

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

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

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

> <Refined Residues>
6

> <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

> <__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

> <Initial Potential Energy>
36.2529

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

> <Potential Energy>
0.97763

> <RMS Gradient>
0.08795

> <Van der Waals Energy>
4.00237

> <Electrostatic Energy>
-40.9001

> <Angle Energy>
11.6399

> <At pH>
7.4

> <OBJECTID>
9223372036858118157

> <Bond Energy>
0.99233

$$$$
3GEN_ligand
  SciTegic09242217043D

 50 54  0  0  0  0            999 V2000
  -19.1707    4.8646  -17.1107 N   0  0
  -18.0958    5.1522  -17.8826 C   0  0
  -18.1884    4.8084  -19.1788 N   0  0
  -17.1862    5.1376  -20.0061 C   0  0
  -16.0838    5.7983  -19.6591 N   0  0
  -15.9665    6.1050  -18.3598 C   0  0
  -16.9623    5.7710  -17.4093 C   0  0
  -14.9266    6.7685  -17.7170 N   0  0
  -13.7122    7.2772  -18.3968 C   0  0
  -12.4396    6.6658  -17.8035 C   0  0
  -12.0225    7.5904  -16.6530 C   0  0
  -12.7521    8.9262  -16.8747 C   0  0
  -13.5399    8.7810  -18.1810 C   0  0
  -15.2857    6.8119  -16.4202 C   0  0
  -16.4921    6.1953  -16.1457 C   0  0
  -17.1071    6.0307  -14.8021 C   0  0
  -17.2025    7.1118  -13.9501 C   0  0
  -17.7631    6.9780  -12.6860 C   0  0
  -18.2430    5.7507  -12.2441 C   0  0
  -18.1319    4.6585  -13.0947 C   0  0
  -17.5721    4.8045  -14.3606 C   0  0
  -18.7230    5.5686  -10.9513 O   0  0
  -19.6102    6.5181  -10.4460 C   0  0
  -19.5147    6.8448   -9.0986 C   0  0
  -20.4388    7.6999   -8.5124 C   0  0
  -21.4807    8.2210   -9.2679 C   0  0
  -21.5820    7.9028  -10.6154 C   0  0
  -20.6422    7.0683  -11.2076 C   0  0
  -17.2637    4.8327  -21.0378 H   0  0
  -13.7669    7.0573  -19.4636 H   0  0
  -11.6549    6.6638  -18.5615 H   0  0
  -12.5821    5.6324  -17.4899 H   0  0
  -12.3117    7.1581  -15.6944 H   0  0
  -10.9411    7.7239  -16.6284 H   0  0
  -13.4337    9.1228  -16.0463 H   0  0
  -12.0584    9.7654  -16.9190 H   0  0
  -14.4898    9.3189  -18.1672 H   0  0
  -12.9446    9.1898  -18.9987 H   0  0
  -14.6826    7.2744  -15.6544 H   0  0
  -16.8405    8.0847  -14.2536 H   0  0
  -17.7959    7.8307  -12.0354 H   0  0
  -18.4748    3.6858  -12.7712 H   0  0
  -17.4864    3.9296  -14.9875 H   0  0
  -18.7181    6.4259   -8.5029 H   0  0
  -20.3436    7.9599   -7.4684 H   0  0
  -22.2065    8.8761   -8.8078 H   0  0
  -22.3900    8.3062  -11.2080 H   0  0
  -20.7493    6.8234  -12.2548 H   0  0
  -19.9543    4.3775  -17.4978 H   0  0
  -19.2085    5.1303  -16.1486 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  4 29  1  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
  9 30  1  0
 10 11  1  0
 10 31  1  0
 10 32  1  0
 11 12  1  0
 11 33  1  0
 11 34  1  0
 12 13  1  0
 12 35  1  0
 12 36  1  0
 13 37  1  0
 13 38  1  0
 14 15  2  0
 14 39  1  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 17 40  1  0
 18 19  2  0
 18 41  1  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 20 42  1  0
 21 43  1  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 24 44  1  0
 25 26  2  0
 25 45  1  0
 26 27  1  0
 26 46  1  0
 27 28  2  0
 27 47  1  0
 28 48  1  0
  1 49  1  0
  1 50  1  0
M  END
> <Name>
3GEN_ligand

> <TopHits>
10

> <-CDOCKER_ENERGY>
20.8150036

> <-CDOCKER_INTERACTION_ENERGY>
55.3472774

> <POSE_NUMBER>
9

> <CHARMm Energy>
0.97763

> <ChiRotor E-elec>
-2.6883

> <ChiRotor E-total>
-21.3158

> <ChiRotor E-vdw>
-31.6052

> <ChiRotor RMSD>
2.23148

> <Dihedral Energy>
25.2207

> <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>
0.02245

> <Initial RMS Gradient>
24.8347

> <Ionization pH>
7.4

> <IonizationIndex>
1

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

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

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

> <Refined Residues>
6

> <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

> <__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

> <Initial Potential Energy>
36.2529

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

> <Potential Energy>
0.97763

> <RMS Gradient>
0.08795

> <Van der Waals Energy>
4.00237

> <Electrostatic Energy>
-40.9001

> <Angle Energy>
11.6399

> <At pH>
7.4

> <OBJECTID>
9223372036858118157

> <Bond Energy>
0.99233

$$$$
3GEN_ligand
  SciTegic09242217043D

 50 54  0  0  0  0            999 V2000
  -19.3337    4.7985  -16.7358 N   0  0
  -18.2745    5.1066  -17.5211 C   0  0
  -18.3696    4.7626  -18.8176 N   0  0
  -17.3881    5.1283  -19.6571 C   0  0
  -16.3027    5.8220  -19.3163 N   0  0
  -16.1766    6.1220  -18.0146 C   0  0
  -17.1523    5.7496  -17.0585 C   0  0
  -15.1548    6.8126  -17.3631 N   0  0
  -13.9567    7.3969  -17.9935 C   0  0
  -14.2474    8.5003  -19.0043 C   0  0
  -12.9149    8.6788  -19.7360 C   0  0
  -12.1985    7.3196  -19.6483 C   0  0
  -13.0816    6.4211  -18.7751 C   0  0
  -15.4995    6.8242  -16.0655 C   0  0
  -16.6859    6.1751  -15.7954 C   0  0
  -17.2918    5.9912  -14.4554 C   0  0
  -17.6511    4.7401  -13.9928 C   0  0
  -18.1907    4.5781  -12.7221 C   0  0
  -18.4014    5.6761  -11.8998 C   0  0
  -18.0383    6.9305  -12.3726 C   0  0
  -17.4853    7.0823  -13.6360 C   0  0
  -18.8897    5.4766  -10.6137 O   0  0
  -19.7063    6.4678  -10.0741 C   0  0
  -19.4616    6.8710   -8.7695 C   0  0
  -20.2912    7.7927   -8.1469 C   0  0
  -21.3828    8.3147   -8.8285 C   0  0
  -21.6266    7.9295  -10.1399 C   0  0
  -20.7889    7.0145  -10.7647 C   0  0
  -17.4775    4.8321  -20.6912 H   0  0
  -13.3453    7.8263  -17.1992 H   0  0
  -14.6037    9.4133  -18.5298 H   0  0
  -15.0088    8.1756  -19.7123 H   0  0
  -13.0578    9.0052  -20.7656 H   0  0
  -12.3157    9.4384  -19.2313 H   0  0
  -12.0494    6.8797  -20.6343 H   0  0
  -11.2151    7.4392  -19.1917 H   0  0
  -13.7106    5.8115  -19.4209 H   0  0
  -12.5079    5.7495  -18.1350 H   0  0
  -14.8937    7.2930  -15.3043 H   0  0
  -17.5106    3.8651  -14.6109 H   0  0
  -18.4333    3.5868  -12.3693 H   0  0
  -18.1692    7.7941  -11.7513 H   0  0
  -17.2150    8.0759  -13.9656 H   0  0
  -18.6165    6.4616   -8.2398 H   0  0
  -20.0817    8.1071   -7.1343 H   0  0
  -22.0346    9.0255   -8.3411 H   0  0
  -22.4715    8.3355  -10.6772 H   0  0
  -21.0020    6.7233  -11.7826 H   0  0
  -20.1259    4.3271  -17.1235 H   0  0
  -19.3537    5.0319  -15.7638 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  4 29  1  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
  9 30  1  0
 10 11  1  0
 10 31  1  0
 10 32  1  0
 11 12  1  0
 11 33  1  0
 11 34  1  0
 12 13  1  0
 12 35  1  0
 12 36  1  0
 13 37  1  0
 13 38  1  0
 14 15  2  0
 14 39  1  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 17 40  1  0
 18 19  2  0
 18 41  1  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 20 42  1  0
 21 43  1  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 24 44  1  0
 25 26  2  0
 25 45  1  0
 26 27  1  0
 26 46  1  0
 27 28  2  0
 27 47  1  0
 28 48  1  0
  1 49  1  0
  1 50  1  0
M  END
> <Name>
3GEN_ligand

> <TopHits>
10

> <-CDOCKER_ENERGY>
20.713143

> <-CDOCKER_INTERACTION_ENERGY>
56.0604951

> <POSE_NUMBER>
10

> <CHARMm Energy>
0.97763

> <ChiRotor E-elec>
-2.6883

> <ChiRotor E-total>
-21.3158

> <ChiRotor E-vdw>
-31.6052

> <ChiRotor RMSD>
2.23148

> <Dihedral Energy>
25.2207

> <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>
0.02245

> <Initial RMS Gradient>
24.8347

> <Ionization pH>
7.4

> <IonizationIndex>
1

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

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

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

> <Refined Residues>
6

> <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

> <__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

> <Initial Potential Energy>
36.2529

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

> <Potential Energy>
0.97763

> <RMS Gradient>
0.08795

> <Van der Waals Energy>
4.00237

> <Electrostatic Energy>
-40.9001

> <Angle Energy>
11.6399

> <At pH>
7.4

> <OBJECTID>
9223372036858118157

> <Bond Energy>
0.99233

$$$$
