3GEN_ligand
  SciTegic09242217553D

 50 54  0  0  0  0            999 V2000
  -19.2400    4.7697  -16.7750 N   0  0
  -18.1979    5.0296  -17.6009 C   0  0
  -18.3177    4.6088  -18.8744 N   0  0
  -17.3471    4.9150  -19.7509 C   0  0
  -16.2399    5.6015  -19.4555 N   0  0
  -16.1024    5.9966  -18.1775 C   0  0
  -17.0734    5.7047  -17.1906 C   0  0
  -15.0707    6.7256  -17.5870 N   0  0
  -13.8783    7.2208  -18.3146 C   0  0  2  0  0  0
  -12.5784    6.6581  -17.7340 C   0  0
  -12.1438    7.6328  -16.6345 C   0  0
  -12.8518    8.9643  -16.9307 C   0  0
  -13.7211    8.7365  -18.1739 C   0  0
  -15.4172    6.8492  -16.2875 C   0  0
  -16.6083    6.2264  -15.9663 C   0  0
  -17.2472    6.1197  -14.6300 C   0  0
  -17.8063    7.2173  -14.0045 C   0  0
  -18.4393    7.0941  -12.7692 C   0  0
  -18.4842    5.8578  -12.1216 C   0  0
  -17.8870    4.7713  -12.7400 C   0  0
  -17.2932    4.8982  -13.9886 C   0  0
  -18.9982    5.6441  -10.8475 O   0  0
  -19.9743    6.5121  -10.3875 C   0  0
  -19.7750    7.1247   -9.1581 C   0  0
  -20.7329    7.9882   -8.6480 C   0  0
  -21.9008    8.2279   -9.3581 C   0  0
  -22.1169    7.5978  -10.5770 C   0  0
  -21.1587    6.7305  -11.0876 C   0  0
  -20.0341    4.2540  -17.1011 H   0  0
  -19.2397    5.0853  -15.8268 H   0  0
  -17.4728    4.5761  -20.7677 H   0  0
  -13.9557    6.9503  -19.3690 H   0  0
  -11.8160    6.6381  -18.5131 H   0  0
  -12.6888    5.6366  -17.3741 H   0  0
  -11.0597    7.7471  -16.6087 H   0  0
  -12.4475    7.2585  -15.6559 H   0  0
  -12.1363    9.7709  -17.0949 H   0  0
  -13.4706    9.2529  -16.0802 H   0  0
  -14.6766    9.2590  -18.1223 H   0  0
  -13.1933    9.1175  -19.0486 H   0  0
  -14.8214    7.3770  -15.5584 H   0  0
  -17.7620    8.1930  -14.4698 H   0  0
  -18.8575    7.9808  -12.3142 H   0  0
  -17.9174    3.8061  -12.2578 H   0  0
  -16.8694    4.0164  -14.4476 H   0  0
  -18.8679    6.9356   -8.6037 H   0  0
  -20.5574    8.4872   -7.7066 H   0  0
  -22.6377    8.8993   -8.9466 H   0  0
  -23.0317    7.7754  -11.1239 H   0  0
  -21.3404    6.2212  -12.0232 H   0  0
  1  2  1  0
  1 29  1  0
  1 30  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  4 31  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 32  1  0
 10 11  1  0
 10 33  1  0
 10 34  1  0
 11 12  1  0
 11 35  1  0
 11 36  1  0
 12 13  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 15  2  0
 14 41  1  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 17 42  1  0
 18 19  2  0
 18 43  1  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 20 44  1  0
 21 45  1  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 24 46  1  0
 25 26  2  0
 25 47  1  0
 26 27  1  0
 26 48  1  0
 27 28  2  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372096987660304

> <LigScore1_Dreiding>
4.31

> <LigScore2_Dreiding>
6.79

> <-PLP1>
114.73

> <-PLP2>
109.57

> <Jain>
8.27

> <-PMF>
113.83

> <-PMF04>
43.12

> <-CDOCKER_ENERGY>
20.793

> <-CDOCKER_INTERACTION_ENERGY>
56.216

> <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

> <ChiRotor E-total>
-21.315771
-68.896721

> <ChiRotor E-elec>
-2.688296
-17.862387

> <ChiRotor E-vdw>
-31.605207
-72.761116

> <pI>
6.32

> <At pH>
7.4

> <Net Charge>
-4.97

> <ChiFlex Energy>
-59.535

> <Side Chain Conformation>
4

> <Residues Side-Chain Conformations>
A:LEU408 A:ALA428 A:LYS430 A:MET449 A:THR474 A:GLU475 A:MET477 A:SER538 A:ASP539 A:PHE540

> <Protein Conformation>
4

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <NumberOfIonizations>
1

> <__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

> <MOL_NUMBER>
1

> <LibDockScore>
100.137

> <LibDock Pose>
1

> <Refined Residues>
9

> <__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

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

> <Rotated Residues>
A:ALA428,A:ASP539,A:GLU475,A:LEU408,A:LYS430,A:MET449,A:MET477,A:PHE540,A:SER538,A:THR474

> <Receptor.Positions>
-10.627 1.547 -19.716 atno 269
-10.838966 1.356604 -18.763379 atno 270
-11.136 2.809 -20.243 atno 271
-11.087409 2.781907 -21.33233 atno 272
-12.591 3.008 -19.818 atno 273
-12.633601 3.110781 -18.732578 atno 274
-12.968222 3.946314 -20.228136 atno 275
-13.531624 1.862534 -20.232207 atno 276
-13.186939 0.944848 -19.756586 atno 277
-14.949827 2.145536 -19.723035 atno 278
-15.403483 2.942016 -20.307071 atno 279
-15.594796 1.273505 -19.792443 atno 280
-14.949206 2.45828 -18.681211 atno 281
-13.533816 1.646602 -21.754017 atno 282
-14.243792 0.878065 -22.05142 atno 283
-12.555436 1.331011 -22.114403 atno 284
-13.804533 2.562896 -22.279048 atno 285
-10.29 4 -19.805 atno 286
-10.313 5.055 -20.437 atno 287
-19.792 -0.299 -16.749 atno 585
-20.564906 -0.016041 -16.188071 atno 586
-18.479 0.235 -16.414 atno 587
-17.742206 -0.200208 -17.090559 atno 588
-18.46 1.755 -16.537 atno 589
-19.047944 2.214874 -15.74435 atno 590
-18.875324 2.05218 -17.499097 atno 591
-17.445242 2.15175 -16.472671 atno 592
-18.171 -0.182 -14.983 atno 593
-19.064 -0.211 -14.137 atno 594
-15.724 0.924 -12.005 atno 614
-16.667292 1.071665 -11.703809 atno 615
-14.772 1.844 -11.395 atno 616
-13.989011 2.047694 -12.128374 atno 617
-15.466 3.153 -11.002 atno 618
-15.509587 3.727838 -11.920347 atno 619
-16.48856 2.925442 -10.717915 atno 620
-14.849911 4.032284 -9.924997 atno 621
-14.968466 3.504003 -8.98135 atno 622
-13.78298 4.186267 -10.090531 atno 623
-15.596869 5.370101 -9.845726 atno 624
-16.670088 5.185537 -9.888019 atno 625
-15.427745 5.801321 -8.865496 atno 626
-15.193119 6.37019 -10.942464 atno 627
-14.153216 6.676896 -10.823751 atno 628
-15.276988 5.923372 -11.931692 atno 629
-16.020086 7.573464 -10.942463 atno 630
-15.762024 8.197179 -11.734311 atno 631
-17.023229 7.311855 -11.039049 atno 632
-15.899542 8.111306 -10.060912 atno 633
-14.169 1.166 -10.173 atno 634
-14.88 0.843 -9.223 atno 635
-27.476 6.614 -2.937 atno 914
-26.741236 6.3562 -2.307466 atno 915
-27.209 6.837 -4.358 atno 916
-27.600089 7.829089 -4.586976 atno 917
-25.706 6.799 -4.623 atno 918
-25.317131 5.837794 -4.286897 atno 919
-25.50698 6.853826 -5.694208 atno 920
-24.935936 7.923243 -3.91586 atno 921
-25.143299 8.880115 -4.395681 atno 922
-25.251002 8.036519 -2.879409 atno 923
-23.157115 7.617823 -3.930172 atno 924
-22.785083 8.138611 -5.613445 atno 925
-23.308092 7.507676 -6.33202 atno 926
-23.119362 9.163247 -5.764632 atno 927
-21.712546 8.088908 -5.801262 atno 928
-27.933 5.844 -5.266 atno 929
-28.302 6.184 -6.394 atno 930
-21.505 0.745 -12.85 atno 1340
-20.629344 0.562333 -13.283504 atno 1341
-22.408 1.74 -13.413 atno 1342
-23.345341 1.696856 -12.856498 atno 1343
-21.823 3.185 -13.321 atno 1344
-21.733863 3.452023 -12.267623 atno 1345
-22.668817 4.105021 -13.910003 atno 1346
-22.752393 3.9004 -14.834189 atno 1347
-20.455751 3.284336 -13.983502 atno 1348
-20.057836 4.292545 -13.98068 atno 1349
-19.722672 2.613978 -13.534537 atno 1350
-20.589934 3.024302 -15.023182 atno 1351
-22.769 1.474 -14.872 atno 1352
-22.155 0.653 -15.56 atno 1353
-23.793 2.191 -15.315 atno 1354
-24.293473 2.759051 -14.663765 atno 1355
-24.101 2.398 -16.713 atno 1356
-24.592778 1.496949 -17.08055 atno 1357
-25.026 3.612 -16.766 atno 1358
-25.766643 3.516634 -15.971184 atno 1359
-24.483881 4.53608 -16.558931 atno 1360
-25.776936 3.737381 -18.104475 atno 1361
-25.070668 3.903255 -18.916729 atno 1362
-26.28546 2.803426 -18.337436 atno 1363
-26.82864 4.871986 -18.112946 atno 1364
-27.678218 4.873063 -19.003034 atno 1365
-26.789714 5.749414 -17.249613 atno 1366
-22.819 2.676 -17.507 atno 1367
-21.954 3.419 -17.046 atno 1368
-20.874 4.369 -20.555 atno 1390
-20.29798 4.428076 -19.758843 atno 1391
-21.029 5.583 -21.354 atno 1392
-22.020004 5.588001 -21.811894 atno 1393
-20.919 6.817 -20.453 atno 1394
-19.976127 6.764975 -19.906539 atno 1395
-20.85428 7.719426 -21.062155 atno 1396
-22.055554 6.992066 -19.444726 atno 1397
-22.306616 6.059486 -18.938249 atno 1398
-21.732157 7.679276 -18.669205 atno 1399
-23.498846 7.741412 -20.212045 atno 1400
-24.617309 6.356665 -20.008512 atno 1401
-24.230302 5.479782 -20.525531 atno 1402
-24.676181 6.123958 -18.947778 atno 1403
-25.610857 6.58709 -20.386235 atno 1404
-19.983 5.606 -22.475 atno 1405
-18.847 6.053 -22.28 atno 1406
-22.097 12.549 -13.491 atno 2387
-21.554499 13.353254 -13.751076 atno 2388
-21.416 11.41 -12.883 atno 2389
-22.179618 10.699821 -12.559404 atno 2390
-20.457 10.787 -13.9 atno 2391
-19.495638 11.311512 -13.922815 atno 2392
-20.236941 9.753942 -13.627892 atno 2393
-20.986851 10.790682 -15.209822 atno 2394
-21.364328 11.639903 -15.407666 atno 2395
-20.647 11.853 -11.641 atno 2396
-20.505 13.053 -11.387 atno 2397
-20.161 10.872 -10.875 atno 2398
-20.143159 9.952599 -11.266922 atno 2399
-19.352 11.108 -9.671 atno 2400
-19.222188 10.126808 -9.215021 atno 2401
-17.982 11.697 -10.048 atno 2402
-17.45339 12.070012 -9.168431 atno 2403
-18.073562 12.53977 -10.734125 atno 2404
-17.101912 10.602162 -10.689726 atno 2405
-17.381302 10.189183 -11.816012 atno 2406
-16.150407 10.158192 -10.046794 atno 2407
-20.047 11.999 -8.641 atno 2408
-19.382 12.654 -7.819 atno 2409
-21.379 12.014 -8.67 atno 2410
-21.846255 11.319518 -9.213628 atno 2411
-22.132 12.941 -7.828 atno 2412
-21.706316 13.926354 -8.017038 atno 2413
-23.624 12.986 -8.196 atno 2414
-24.200252 13.518628 -7.438715 atno 2415
-23.734677 13.583363 -9.101589 atno 2416
-24.26071 11.646258 -8.460192 atno 2417
-24.751492 10.863303 -7.421409 atno 2418
-24.656142 11.195648 -6.400044 atno 2419
-24.391037 11.184729 -9.766522 atno 2420
-24.009043 11.768327 -10.59126 atno 2421
-25.369479 9.647407 -7.67844 atno 2422
-25.730177 9.040561 -6.862837 atno 2423
-25.024824 9.978049 -10.027092 atno 2424
-25.134749 9.639469 -11.048077 atno 2425
-25.517293 9.208328 -8.984976 atno 2426
-26.009286 8.268384 -9.190102 atno 2427
-21.939 12.649 -6.35 atno 2428
-22.196 11.537 -5.893 atno 2429

> <Heavy atom RMSD to 3GEN_ligand_origInal 7>
0.548

> <Scoring Rotated Receptor Atoms>
157

> <Favorable A:LEU408>
1

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:VAL416>
4

> <Favorable A:ALA428>
3

> <Favorable A:LYS430>
2

> <Favorable A:GLU475>
1

> <Favorable A:MET477>
2

> <Favorable A:CYS481>
0

> <Favorable A:ASP521>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
2

> <Favorable A:ASP539>
0

> <Favorable A:PHE540>
2

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Charge A:LYS430>
1

> <Charge A:ASP521>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
1

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
4

> <Hydrophobic A:ALA428>
3

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
2

> <Hydrophobic A:PHE540>
2

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLU475>
1

> <HydrogenBond A:MET477>
2

> <HydrogenBond A:ASN526>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242217553D

 50 54  0  0  0  0            999 V2000
  -11.7006   11.8828  -14.4571 N   0  0
  -11.7299   12.5845  -13.2989 C   0  0
  -10.8495   13.6026  -13.2089 N   0  0
  -10.7842   14.3057  -12.0671 C   0  0
  -11.5575   14.1021  -11.0010 N   0  0
  -12.4424   13.0937  -11.0876 C   0  0
  -12.5745   12.2900  -12.2490 C   0  0
  -13.3387   12.6451  -10.1229 N   0  0
  -13.4878   13.2403   -8.7754 C   0  0  2  0  0  0
  -13.2470   12.2060   -7.6605 C   0  0
  -14.6145   11.9608   -7.0285 C   0  0
  -15.3255   13.3016   -7.1660 C   0  0
  -14.9070   13.7921   -8.5485 C   0  0
  -13.9803   11.6033  -10.6899 C   0  0
  -13.5886   11.3364  -11.9917 C   0  0
  -14.1282   10.2686  -12.8805 C   0  0
  -14.5125   10.5329  -14.1835 C   0  0
  -14.9979    9.5243  -15.0107 C   0  0
  -15.1186    8.2204  -14.5356 C   0  0
  -14.7610    7.9604  -13.2209 C   0  0
  -14.2671    8.9765  -12.4074 C   0  0
  -15.6439    7.1869  -15.3023 O   0  0
  -15.0938    6.9909  -16.5648 C   0  0
  -13.7386    7.1739  -16.8414 C   0  0
  -13.2438    6.9159  -18.1140 C   0  0
  -14.0995    6.4848  -19.1194 C   0  0
  -15.4446    6.2796  -18.8441 C   0  0
  -15.9351    6.5215  -17.5673 C   0  0
  -12.2477   11.0558  -14.5764 H   0  0
  -11.1202   12.1863  -15.2116 H   0  0
  -10.0539   15.0998  -12.0089 H   0  0
  -12.7749   14.0570   -8.6437 H   0  0
  -12.5803   12.6305   -6.9094 H   0  0
  -12.7843   11.2838   -8.0127 H   0  0
  -14.5512   11.6115   -5.9973 H   0  0
  -15.1492   11.2140   -7.6129 H   0  0
  -14.9564   13.9815   -6.3997 H   0  0
  -16.4077   13.2359   -7.0606 H   0  0
  -15.6051   13.4027   -9.2904 H   0  0
  -14.9405   14.8774   -8.6139 H   0  0
  -14.7364   11.0335  -10.1683 H   0  0
  -14.4451   11.5364  -14.5800 H   0  0
  -15.2880    9.7677  -16.0205 H   0  0
  -14.8581    6.9570  -12.8343 H   0  0
  -13.9904    8.7341  -11.3912 H   0  0
  -13.0525    7.4974  -16.0727 H   0  0
  -12.1915    7.0478  -18.3215 H   0  0
  -13.7158    6.2987  -20.1114 H   0  0
  -16.1074    5.9299  -19.6229 H   0  0
  -16.9798    6.3531  -17.3510 H   0  0
  1  2  1  0
  1 29  1  0
  1 30  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  4 31  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 32  1  0
 10 11  1  0
 10 33  1  0
 10 34  1  0
 11 12  1  0
 11 35  1  0
 11 36  1  0
 12 13  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 15  2  0
 14 41  1  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 17 42  1  0
 18 19  2  0
 18 43  1  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 20 44  1  0
 21 45  1  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 24 46  1  0
 25 26  2  0
 25 47  1  0
 26 27  1  0
 26 48  1  0
 27 28  2  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372101282627600

> <LigScore1_Dreiding>
2.14

> <LigScore2_Dreiding>
5.31

> <-PLP1>
81.21

> <-PLP2>
71.97

> <Jain>
2.29

> <-PMF>
120.3

> <-PMF04>
49.45

> <-CDOCKER_ENERGY>
8.381

> <-CDOCKER_INTERACTION_ENERGY>
42.473

> <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

> <ChiRotor E-total>
-21.315771
-78.144691

> <ChiRotor E-elec>
-2.688296
-14.523658

> <ChiRotor E-vdw>
-31.605207
-81.277954

> <pI>
6.32

> <At pH>
7.4

> <Net Charge>
-4.97

> <ChiFlex Energy>
-57.802

> <Side Chain Conformation>
7

> <Residues Side-Chain Conformations>
A:LEU408 A:ALA428 A:LYS430 A:MET449 A:THR474 A:GLU475 A:MET477 A:SER538 A:ASP539 A:PHE540

> <Protein Conformation>
7

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <NumberOfIonizations>
1

> <__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

> <MOL_NUMBER>
1

> <LibDockScore>
74.492

> <LibDock Pose>
1

> <Refined Residues>
9

> <__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

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

> <Rotated Residues>
A:ALA428,A:ASP539,A:GLU475,A:LEU408,A:LYS430,A:MET449,A:MET477,A:PHE540,A:SER538,A:THR474

> <Receptor.Positions>
-10.627 1.547 -19.716 atno 269
-10.813254 1.323773 -18.766356 atno 270
-11.136 2.809 -20.243 atno 271
-11.085179 2.781095 -21.332464 atno 272
-12.591 3.008 -19.818 atno 273
-12.635649 3.086753 -18.730103 atno 274
-12.948244 3.965973 -20.200313 atno 275
-13.565934 1.906908 -20.272631 atno 276
-13.252969 0.962871 -19.827001 atno 277
-14.978281 2.225789 -19.759462 atno 278
-15.683268 1.429381 -19.982719 atno 279
-14.987052 2.357234 -18.680861 atno 280
-15.360354 3.144927 -20.204511 atno 281
-13.572204 1.734228 -21.799349 atno 282
-14.306595 0.994722 -22.114522 atno 283
-13.814207 2.672118 -22.299619 atno 284
-12.603398 1.397367 -22.166918 atno 285
-10.29 4 -19.805 atno 286
-10.313 5.055 -20.437 atno 287
-19.792 -0.299 -16.749 atno 585
-20.55559 0.006062 -16.184967 atno 586
-18.479 0.235 -16.414 atno 587
-17.744065 -0.200165 -17.092252 atno 588
-18.46 1.755 -16.537 atno 589
-18.955269 2.240278 -15.699112 atno 590
-18.945873 2.082753 -17.455537 atno 591
-17.436375 2.135063 -16.557505 atno 592
-18.171 -0.182 -14.983 atno 593
-19.064 -0.211 -14.137 atno 594
-15.724 0.924 -12.005 atno 614
-16.664681 1.094383 -11.710608 atno 615
-14.772 1.844 -11.395 atno 616
-13.989083 2.0562 -12.126397 atno 617
-15.466 3.153 -11.002 atno 618
-15.968455 3.029602 -10.048279 atno 619
-14.68421 3.888209 -10.804967 atno 620
-16.466012 3.762196 -11.997117 atno 621
-16.000963 3.866714 -12.976742 atno 622
-17.321935 3.098885 -12.128242 atno 623
-16.949196 5.132598 -11.482609 atno 624
-17.468402 4.995712 -10.532861 atno 625
-16.083466 5.7566 -11.260306 atno 626
-17.866467 5.884926 -12.455133 atno 627
-17.399569 5.983675 -13.4357 atno 628
-18.800001 5.340502 -12.58679 atno 629
-18.197663 7.23063 -11.984926 atno 630
-18.852646 7.693305 -12.649623 atno 631
-18.651444 7.17362 -11.050671 atno 632
-17.339733 7.813165 -11.899131 atno 633
-14.169 1.166 -10.173 atno 634
-14.88 0.843 -9.223 atno 635
-27.476 6.614 -2.937 atno 914
-26.758642 6.351562 -2.289359 atno 915
-27.209 6.837 -4.358 atno 916
-27.598037 7.832181 -4.575994 atno 917
-25.706 6.799 -4.623 atno 918
-25.306595 5.844519 -4.27999 atno 919
-25.5249 6.835219 -5.698615 atno 920
-24.912463 7.937604 -3.974714 atno 921
-25.263199 8.909456 -4.323259 atno 922
-25.04257 7.932996 -2.894138 atno 923
-23.156801 7.767095 -4.36329 atno 924
-22.484376 9.11838 -3.379498 atno 925
-21.883592 9.773009 -4.010314 atno 926
-23.277922 9.705224 -2.92094 atno 927
-21.829787 8.72149 -2.603663 atno 928
-27.933 5.844 -5.266 atno 929
-28.302 6.184 -6.394 atno 930
-21.505 0.745 -12.85 atno 1340
-20.660277 0.500096 -13.31134 atno 1341
-22.408 1.74 -13.413 atno 1342
-23.347397 1.694539 -12.859903 atno 1343
-21.823 3.185 -13.321 atno 1344
-22.607086 3.885352 -13.634877 atno 1345
-20.706041 3.283831 -14.190439 atno 1346
-20.423215 4.187574 -14.278482 atno 1347
-21.38826 3.546595 -11.893023 atno 1348
-21.126376 4.601392 -11.808954 atno 1349
-22.185249 3.350445 -11.177507 atno 1350
-20.517105 2.964798 -11.591777 atno 1351
-22.769 1.474 -14.872 atno 1352
-22.155 0.653 -15.56 atno 1353
-23.793 2.191 -15.315 atno 1354
-24.305512 2.749567 -14.665901 atno 1355
-24.101 2.398 -16.713 atno 1356
-24.597357 1.493852 -17.06526 atno 1357
-25.026 3.612 -16.766 atno 1358
-25.706286 3.578787 -15.914128 atno 1359
-24.456115 4.535943 -16.652332 atno 1360
-25.882543 3.652301 -18.043901 atno 1361
-25.247777 3.647366 -18.929579 atno 1362
-26.490774 2.749067 -18.100523 atno 1363
-26.82792 4.873897 -18.114746 atno 1364
-27.712754 4.877152 -18.967667 atno 1365
-26.674563 5.814311 -17.332138 atno 1366
-22.819 2.676 -17.507 atno 1367
-21.954 3.419 -17.046 atno 1368
-20.874 4.369 -20.555 atno 1390
-20.052151 4.331753 -19.992143 atno 1391
-21.029 5.583 -21.354 atno 1392
-22.019998 5.592641 -21.811487 atno 1393
-20.919 6.817 -20.453 atno 1394
-19.960729 6.780551 -19.932329 atno 1395
-20.890617 7.722742 -21.059971 atno 1396
-22.033138 6.960537 -19.408492 atno 1397
-22.2433 6.022613 -18.894389 atno 1398
-21.705427 7.647295 -18.63111 atno 1399
-23.529246 7.673648 -20.114744 atno 1400
-24.547002 6.193666 -20.154898 atno 1401
-24.402268 5.634892 -19.233178 atno 1402
-24.271339 5.557282 -20.994538 atno 1403
-25.60094 6.458575 -20.223818 atno 1404
-19.983 5.606 -22.475 atno 1405
-18.847 6.053 -22.28 atno 1406
-22.097 12.549 -13.491 atno 2387
-21.513626 13.314568 -13.78334 atno 2388
-21.416 11.41 -12.883 atno 2389
-22.171257 10.685779 -12.574706 atno 2390
-20.457 10.787 -13.9 atno 2391
-20.988905 10.587391 -14.828605 atno 2392
-19.68045 11.52488 -14.143346 atno 2393
-19.895095 9.572123 -13.409101 atno 2394
-19.058216 9.389497 -13.828262 atno 2395
-20.647 11.853 -11.641 atno 2396
-20.505 13.053 -11.387 atno 2397
-20.161 10.872 -10.875 atno 2398
-20.301063 9.932132 -11.162472 atno 2399
-19.352 11.108 -9.671 atno 2400
-19.218001 10.12984 -9.209891 atno 2401
-17.982 11.697 -10.048 atno 2402
-17.304123 11.687058 -9.193649 atno 2403
-18.068511 12.731203 -10.386901 atno 2404
-17.375773 10.832032 -11.175778 atno 2405
-17.131858 9.645729 -10.948866 atno 2406
-17.169997 11.347578 -12.276379 atno 2407
-20.047 11.999 -8.641 atno 2408
-19.382 12.654 -7.819 atno 2409
-21.379 12.014 -8.67 atno 2410
-21.853861 11.295603 -9.168478 atno 2411
-22.132 12.941 -7.828 atno 2412
-21.702876 13.92529 -8.015872 atno 2413
-23.624 12.986 -8.196 atno 2414
-23.746632 13.618729 -9.075499 atno 2415
-24.219668 13.462559 -7.416994 atno 2416
-24.200412 11.631399 -8.534642 atno 2417
-24.182542 11.169463 -9.849327 atno 2418
-23.759564 11.782166 -10.633216 atno 2419
-24.756157 10.82059 -7.548058 atno 2420
-24.781085 11.155971 -6.523085 atno 2421
-24.703221 9.923469 -10.17264 atno 2422
-24.683461 9.578697 -11.196897 atno 2423
-25.278367 9.57331 -7.868184 atno 2424
-25.70262 8.951326 -7.093933 atno 2425
-25.252999 9.123731 -9.181188 atno 2426
-25.660439 8.155059 -9.432468 atno 2427
-21.939 12.649 -6.35 atno 2428
-22.196 11.537 -5.893 atno 2429

> <Heavy atom RMSD to 3GEN_ligand_origInal 7>
9.831

> <Scoring Rotated Receptor Atoms>
157

> <Favorable A:LEU408>
1

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:VAL416>
1

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
1

> <Favorable A:GLU475>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
0

> <Favorable A:ASP521>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
1

> <Favorable A:ASP539>
1

> <Favorable A:PHE540>
0

> <Favorable A:LEU542>
1

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
1

> <Charge A:LYS430>
1

> <Charge A:ASP521>
0

> <Charge A:ASP539>
1

> <Hydrophobic A:LEU408>
1

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
1

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
1

> <Hydrophobic A:PHE540>
0

> <Hydrophobic A:LEU542>
1

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
1

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ASN526>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242217553D

 50 54  0  0  0  0            999 V2000
  -14.6819   12.2609  -10.2652 N   0  0
  -14.0414   12.4485   -9.0918 C   0  0
  -14.8184   12.8103   -8.0514 N   0  0
  -14.2469   12.9844   -6.8508 C   0  0
  -12.9474   12.8268   -6.5983 N   0  0
  -12.1646   12.4865   -7.6350 C   0  0
  -12.6827   12.2837   -8.9379 C   0  0
  -10.7852   12.2762   -7.6576 N   0  0
   -9.8920   12.4218   -6.4852 C   0  0  2  0  0  0
   -8.8067   13.4827   -6.6607 C   0  0
   -7.8152   13.1832   -5.5343 C   0  0
   -7.9109   11.6694   -5.2822 C   0  0
   -9.0936   11.1649   -6.1263 C   0  0
  -10.4991   11.9437   -8.9314 C   0  0
  -11.5966   11.9388   -9.7770 C   0  0
  -11.5869   11.6319  -11.2341 C   0  0
  -10.9749   10.4808  -11.6960 C   0  0
  -10.9278   10.1880  -13.0563 C   0  0
  -11.5006   11.0546  -13.9842 C   0  0
  -12.1199   12.2081  -13.5208 C   0  0
  -12.1667   12.4853  -12.1569 C   0  0
  -11.4123   10.8353  -15.3534 O   0  0
  -11.8213    9.5834  -15.8000 C   0  0
  -12.9810    8.9729  -15.3258 C   0  0
  -13.3879    7.7501  -15.8428 C   0  0
  -12.6345    7.1237  -16.8278 C   0  0
  -11.4842    7.7328  -17.3112 C   0  0
  -11.0854    8.9636  -16.8028 C   0  0
  -14.2152   11.9260  -11.0813 H   0  0
  -15.6590   12.4581  -10.3407 H   0  0
  -14.8852   13.2702   -6.0289 H   0  0
  -10.4803   12.7052   -5.6131 H   0  0
   -9.1985   14.4978   -6.6105 H   0  0
   -8.3080   13.3623   -7.6231 H   0  0
   -8.1133   13.7207   -4.6342 H   0  0
   -6.8058   13.5115   -5.7787 H   0  0
   -8.0731   11.4766   -4.2224 H   0  0
   -6.9866   11.1602   -5.5469 H   0  0
   -8.7133   10.6956   -7.0333 H   0  0
   -9.6984   10.4248   -5.6013 H   0  0
   -9.4965   11.7100   -9.2592 H   0  0
  -10.5206    9.7859  -11.0023 H   0  0
  -10.4283    9.2905  -13.3890 H   0  0
  -12.5706   12.8908  -14.2261 H   0  0
  -12.6614   13.3921  -11.8357 H   0  0
  -13.5837    9.4493  -14.5663 H   0  0
  -14.2939    7.2897  -15.4752 H   0  0
  -12.9489    6.1685  -17.2230 H   0  0
  -10.9028    7.2509  -18.0849 H   0  0
  -10.1942    9.4392  -17.1846 H   0  0
  1  2  1  0
  1 29  1  0
  1 30  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  4 31  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 32  1  0
 10 11  1  0
 10 33  1  0
 10 34  1  0
 11 12  1  0
 11 35  1  0
 11 36  1  0
 12 13  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 15  2  0
 14 41  1  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 17 42  1  0
 18 19  2  0
 18 43  1  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 20 44  1  0
 21 45  1  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 24 46  1  0
 25 26  2  0
 25 47  1  0
 26 27  1  0
 26 48  1  0
 27 28  2  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372105577594896

> <LigScore1_Dreiding>
2.61

> <LigScore2_Dreiding>
5.22

> <-PLP1>
77.66

> <-PLP2>
68.94

> <Jain>
2.1

> <-PMF>
111.34

> <-PMF04>
51.32

> <-CDOCKER_ENERGY>
4.622

> <-CDOCKER_INTERACTION_ENERGY>
39.015

> <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

> <ChiRotor E-total>
-21.315771
-76.451744

> <ChiRotor E-elec>
-2.688296
-14.438707

> <ChiRotor E-vdw>
-31.605207
-80.52388

> <pI>
6.32

> <At pH>
7.4

> <Net Charge>
-4.97

> <ChiFlex Energy>
-58.336

> <Side Chain Conformation>
6

> <Residues Side-Chain Conformations>
A:LEU408 A:ALA428 A:LYS430 A:MET449 A:THR474 A:GLU475 A:MET477 A:SER538 A:ASP539 A:PHE540

> <Protein Conformation>
6

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <NumberOfIonizations>
1

> <__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

> <MOL_NUMBER>
1

> <LibDockScore>
72.457

> <LibDock Pose>
2

> <Refined Residues>
9

> <__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

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

> <Rotated Residues>
A:ALA428,A:ASP539,A:GLU475,A:LEU408,A:LYS430,A:MET449,A:MET477,A:PHE540,A:SER538,A:THR474

> <Receptor.Positions>
-10.627 1.547 -19.716 atno 269
-10.80912 1.350906 -18.758897 atno 270
-11.136 2.809 -20.243 atno 271
-11.086438 2.781612 -21.332408 atno 272
-12.591 3.008 -19.818 atno 273
-12.635486 3.089913 -18.730352 atno 274
-12.950265 3.9631 -20.205012 atno 275
-13.561926 1.901195 -20.268774 atno 276
-13.245179 0.960048 -19.819738 atno 277
-14.975755 2.214921 -19.75677 atno 278
-15.676537 1.413137 -19.973074 atno 279
-14.984504 2.353911 -18.679186 atno 280
-15.363921 3.128032 -20.208579 atno 281
-13.567018 1.722725 -21.794953 atno 282
-14.298104 0.979137 -22.107912 atno 283
-13.812609 2.657646 -22.298978 atno 284
-12.596773 1.388435 -22.161027 atno 285
-10.29 4 -19.805 atno 286
-10.313 5.055 -20.437 atno 287
-19.792 -0.299 -16.749 atno 585
-20.553415 0.007736 -16.182946 atno 586
-18.479 0.235 -16.414 atno 587
-17.742846 -0.199537 -17.091412 atno 588
-18.46 1.755 -16.537 atno 589
-18.971574 2.23677 -15.707118 atno 590
-18.931949 2.083039 -17.462574 atno 591
-17.436582 2.134449 -16.542755 atno 592
-18.171 -0.182 -14.983 atno 593
-19.064 -0.211 -14.137 atno 594
-15.724 0.924 -12.005 atno 614
-16.666166 1.079009 -11.706807 atno 615
-14.772 1.844 -11.395 atno 616
-13.988083 2.055316 -12.124784 atno 617
-15.466 3.153 -11.002 atno 618
-16.058952 3.024997 -10.107202 atno 619
-14.689654 3.869306 -10.728953 atno 620
-16.32496 3.757815 -12.125872 atno 621
-15.814478 3.624408 -13.079601 atno 622
-17.265992 3.21122 -12.206697 atno 623
-16.604216 5.258682 -11.942319 atno 624
-15.660786 5.806615 -11.960657 atno 625
-17.175674 5.615226 -12.800348 atno 626
-17.36561 5.59361 -10.653712 atno 627
-18.305295 5.040682 -10.608956 atno 628
-16.779245 5.315977 -9.778002 atno 629
-17.680733 7.016482 -10.54023 atno 630
-18.185085 7.196178 -9.647814 atno 631
-16.810274 7.589691 -10.553891 atno 632
-18.2789 7.310461 -11.336664 atno 633
-14.169 1.166 -10.173 atno 634
-14.88 0.843 -9.223 atno 635
-27.476 6.614 -2.937 atno 914
-26.756275 6.353083 -2.291726 atno 915
-27.209 6.837 -4.358 atno 916
-27.596875 7.832496 -4.576416 atno 917
-25.706 6.799 -4.623 atno 918
-25.306306 5.844849 -4.27943 atno 919
-25.525329 6.834416 -5.698715 atno 920
-24.912102 7.938256 -3.976277 atno 921
-25.265555 8.910055 -4.322215 atno 922
-25.038484 7.931661 -2.895275 atno 923
-23.157543 7.770892 -4.371522 atno 924
-22.482017 9.115682 -3.380941 atno 925
-21.876693 9.76991 -4.007857 atno 926
-23.274373 9.704918 -2.923453 atno 927
-21.83158 8.713454 -2.604344 atno 928
-27.933 5.844 -5.266 atno 929
-28.302 6.184 -6.394 atno 930
-21.505 0.745 -12.85 atno 1340
-20.644466 0.536152 -13.301789 atno 1341
-22.408 1.74 -13.413 atno 1342
-23.347622 1.693983 -12.860082 atno 1343
-21.823 3.185 -13.321 atno 1344
-22.590879 3.889341 -13.662736 atno 1345
-20.682428 3.27461 -14.159523 atno 1346
-20.346778 4.164982 -14.178603 atno 1347
-21.424798 3.550769 -11.882432 atno 1348
-21.169958 4.606759 -11.79042 atno 1349
-22.236568 3.351135 -11.185706 atno 1350
-20.559311 2.972029 -11.560244 atno 1351
-22.769 1.474 -14.872 atno 1352
-22.155 0.653 -15.56 atno 1353
-23.793 2.191 -15.315 atno 1354
-24.313077 2.742471 -14.665616 atno 1355
-24.101 2.398 -16.713 atno 1356
-24.597469 1.493613 -17.065264 atno 1357
-25.026 3.612 -16.766 atno 1358
-25.722606 3.558307 -15.928483 atno 1359
-24.461988 4.535183 -16.622119 atno 1360
-25.857368 3.678561 -18.059934 atno 1361
-25.202679 3.743349 -18.928742 atno 1362
-26.427535 2.756398 -18.173694 atno 1363
-26.85015 4.864857 -18.092797 atno 1364
-27.713649 4.878228 -18.968869 atno 1365
-26.753942 5.768476 -17.260982 atno 1366
-22.819 2.676 -17.507 atno 1367
-21.954 3.419 -17.046 atno 1368
-20.874 4.369 -20.555 atno 1390
-20.05339 4.337907 -19.989364 atno 1391
-21.029 5.583 -21.354 atno 1392
-22.020147 5.592791 -21.811099 atno 1393
-20.919 6.817 -20.453 atno 1394
-20.872593 7.721205 -21.061229 atno 1395
-19.968357 6.772035 -19.919338 atno 1396
-22.045502 6.976783 -19.426036 atno 1397
-21.72351 7.669839 -18.652517 atno 1398
-22.271509 6.042245 -18.911992 atno 1399
-23.520377 7.697248 -20.164728 atno 1400
-24.59573 6.266527 -20.035716 atno 1401
-24.537558 5.879465 -19.020634 atno 1402
-25.629534 6.535264 -20.244046 atno 1403
-24.273305 5.481791 -20.718266 atno 1404
-19.983 5.606 -22.475 atno 1405
-18.847 6.053 -22.28 atno 1406
-22.097 12.549 -13.491 atno 2387
-21.546994 13.346619 -13.757774 atno 2388
-21.416 11.41 -12.883 atno 2389
-22.168952 10.684649 -12.570744 atno 2390
-20.457 10.787 -13.9 atno 2391
-19.49379 11.308382 -13.924411 atno 2392
-20.242443 9.748372 -13.645781 atno 2393
-21.007502 10.819387 -15.201893 atno 2394
-21.361365 11.680371 -15.390565 atno 2395
-20.647 11.853 -11.641 atno 2396
-20.505 13.053 -11.387 atno 2397
-20.161 10.872 -10.875 atno 2398
-20.363895 9.938688 -11.153308 atno 2399
-19.352 11.108 -9.671 atno 2400
-19.217337 10.128704 -9.21251 atno 2401
-17.982 11.697 -10.048 atno 2402
-17.371281 11.748147 -9.146846 atno 2403
-18.067706 12.70719 -10.45274 atno 2404
-17.298902 10.770126 -11.076081 atno 2405
-16.829273 9.696716 -10.689584 atno 2406
-17.250949 11.126924 -12.253927 atno 2407
-20.047 11.999 -8.641 atno 2408
-19.382 12.654 -7.819 atno 2409
-21.379 12.014 -8.67 atno 2410
-21.874492 11.293681 -9.146135 atno 2411
-22.132 12.941 -7.828 atno 2412
-21.703311 13.925282 -8.016588 atno 2413
-23.624 12.986 -8.196 atno 2414
-24.219667 13.461888 -7.416566 atno 2415
-23.746766 13.619528 -9.074905 atno 2416
-24.201446 11.630654 -8.534781 atno 2417
-24.754888 10.821661 -7.549996 atno 2418
-24.780642 11.153974 -6.524523 atno 2419
-24.182965 11.171763 -9.851447 atno 2420
-23.761382 11.784854 -10.634259 atno 2421
-25.278169 9.570817 -7.872266 atno 2422
-25.701451 8.949757 -7.097307 atno 2423
-24.703408 9.924847 -10.176042 atno 2424
-24.683984 9.581677 -11.199768 atno 2425
-25.252206 9.12503 -9.18307 atno 2426
-25.659532 8.155301 -9.436809 atno 2427
-21.939 12.649 -6.35 atno 2428
-22.196 11.537 -5.893 atno 2429

> <Heavy atom RMSD to 3GEN_ligand_origInal 7>
11.676

> <Scoring Rotated Receptor Atoms>
157

> <Favorable A:LEU408>
0

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
2

> <Favorable A:VAL416>
1

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
0

> <Favorable A:GLU475>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
0

> <Favorable A:ASP521>
1

> <Favorable A:ASN526>
1

> <Favorable A:LEU528>
0

> <Favorable A:ASP539>
0

> <Favorable A:PHE540>
0

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
1

> <Favorable A:TYR551>
2

> <Charge A:LYS430>
0

> <Charge A:ASP521>
1

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
0

> <Hydrophobic A:PHE413>
2

> <Hydrophobic A:VAL416>
1

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
0

> <Hydrophobic A:PHE540>
0

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
1

> <Hydrophobic A:TYR551>
2

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ASN526>
1

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242217553D

 50 54  0  0  0  0            999 V2000
  -11.1709   12.5712  -14.7506 N   0  0
  -11.4264   11.6714  -15.7296 C   0  0
  -11.1119   12.0533  -16.9839 N   0  0
  -11.3832   11.2195  -18.0005 C   0  0
  -11.9575   10.0208  -17.8736 N   0  0
  -12.2602    9.6295  -16.6227 C   0  0
  -11.9846   10.4356  -15.4908 C   0  0
  -12.8707    8.4489  -16.1914 N   0  0
  -13.3552    7.3595  -17.0673 C   0  0  2  0  0  0
  -12.2743    6.7600  -17.9890 C   0  0
  -12.7303    7.0638  -19.4183 C   0  0
  -14.2508    7.1424  -19.3281 C   0  0
  -14.5067    7.8144  -17.9818 C   0  0
  -12.9172    8.5390  -14.8483 C   0  0
  -12.3878    9.7126  -14.3454 C   0  0
  -12.2773   10.1004  -12.9158 C   0  0
  -11.0480   10.3990  -12.3602 C   0  0
  -10.9378   10.7771  -11.0268 C   0  0
  -12.0663   10.8749  -10.2241 C   0  0
  -13.3036   10.5433  -10.7771 C   0  0
  -13.3989   10.1603  -12.1108 C   0  0
  -11.8845   11.2343   -8.8936 O   0  0
  -12.9343   11.8988   -8.2752 C   0  0
  -13.3646   11.4358   -7.0395 C   0  0
  -14.3964   12.0810   -6.3739 C   0  0
  -14.9965   13.1982   -6.9394 C   0  0
  -14.5597   13.6751   -8.1671 C   0  0
  -13.5259   13.0313   -8.8339 C   0  0
  -10.7162   13.4316  -14.9764 H   0  0
  -11.4359   12.3953  -13.8029 H   0  0
  -11.1222   11.5480  -18.9959 H   0  0
  -13.7293    6.5610  -16.4252 H   0  0
  -12.2393    5.6788  -17.8472 H   0  0
  -11.2705    7.1369  -17.7873 H   0  0
  -12.3987    6.3182  -20.1385 H   0  0
  -12.3340    8.0283  -19.7371 H   0  0
  -14.6731    6.1360  -19.3269 H   0  0
  -14.6925    7.6922  -20.1587 H   0  0
  -14.4884    8.8949  -18.1246 H   0  0
  -15.4826    7.5569  -17.5703 H   0  0
  -13.3310    7.7622  -14.2222 H   0  0
  -10.1487   10.3401  -12.9581 H   0  0
   -9.9690   11.0019  -10.6070 H   0  0
  -14.2065   10.5662  -10.1849 H   0  0
  -14.3749    9.9195  -12.5093 H   0  0
  -12.8978   10.5651   -6.6024 H   0  0
  -14.7250   11.7096   -5.4156 H   0  0
  -15.8001   13.7039   -6.4265 H   0  0
  -15.0174   14.5543   -8.5947 H   0  0
  -13.1866   13.4172   -9.7841 H   0  0
  1  2  1  0
  1 29  1  0
  1 30  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  4 31  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 32  1  0
 10 11  1  0
 10 33  1  0
 10 34  1  0
 11 12  1  0
 11 35  1  0
 11 36  1  0
 12 13  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 15  2  0
 14 41  1  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 17 42  1  0
 18 19  2  0
 18 43  1  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 20 44  1  0
 21 45  1  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 24 46  1  0
 25 26  2  0
 25 47  1  0
 26 27  1  0
 26 48  1  0
 27 28  2  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372109872562192

> <LigScore1_Dreiding>
1.92

> <LigScore2_Dreiding>
5.08

> <-PLP1>
72.82

> <-PLP2>
65.51

> <Jain>
1.64

> <-PMF>
90.36

> <-PMF04>
35.79

> <-CDOCKER_ENERGY>
2.764

> <-CDOCKER_INTERACTION_ENERGY>
37.288

> <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

> <ChiRotor E-total>
-21.315771
-76.92672

> <ChiRotor E-elec>
-2.688296
-15.404712

> <ChiRotor E-vdw>
-31.605207
-78.963089

> <pI>
6.32

> <At pH>
7.4

> <Net Charge>
-4.97

> <ChiFlex Energy>
-62.777

> <Side Chain Conformation>
2

> <Residues Side-Chain Conformations>
A:LEU408 A:ALA428 A:LYS430 A:MET449 A:THR474 A:GLU475 A:MET477 A:SER538 A:ASP539 A:PHE540

> <Protein Conformation>
2

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <NumberOfIonizations>
1

> <__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

> <MOL_NUMBER>
1

> <LibDockScore>
70.027

> <LibDock Pose>
3

> <Refined Residues>
9

> <__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

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

> <Rotated Residues>
A:ALA428,A:ASP539,A:GLU475,A:LEU408,A:LYS430,A:MET449,A:MET477,A:PHE540,A:SER538,A:THR474

> <Receptor.Positions>
-10.627 1.547 -19.716 atno 269
-10.80595 1.358041 -18.757071 atno 270
-11.136 2.809 -20.243 atno 271
-11.086736 2.783529 -21.332223 atno 272
-12.591 3.008 -19.818 atno 273
-12.635048 3.087648 -18.73015 atno 274
-12.948949 3.965318 -20.201216 atno 275
-13.563254 1.903579 -20.270483 atno 276
-13.247176 0.961054 -19.823859 atno 277
-14.975926 2.218232 -19.756198 atno 278
-15.678029 1.417873 -19.973802 atno 279
-14.982982 2.354782 -18.678246 atno 280
-15.363065 3.133095 -20.205376 atno 281
-13.569978 1.728736 -21.796977 atno 282
-14.302282 0.986653 -22.110818 atno 283
-13.814945 2.665175 -22.298494 atno 284
-12.600403 1.394221 -22.164656 atno 285
-10.29 4 -19.805 atno 286
-10.313 5.055 -20.437 atno 287
-19.792 -0.299 -16.749 atno 585
-20.5532 0.011851 -16.185747 atno 586
-18.479 0.235 -16.414 atno 587
-17.742862 -0.199408 -17.091559 atno 588
-18.46 1.755 -16.537 atno 589
-18.978539 2.237446 -15.711564 atno 590
-18.926504 2.07928 -17.466778 atno 591
-17.437274 2.13661 -16.535423 atno 592
-18.171 -0.182 -14.983 atno 593
-19.064 -0.211 -14.137 atno 594
-15.724 0.924 -12.005 atno 614
-16.665087 1.080072 -11.702631 atno 615
-14.772 1.844 -11.395 atno 616
-13.988247 2.054086 -12.125365 atno 617
-15.466 3.153 -11.002 atno 618
-16.11582 2.984317 -10.157883 atno 619
-14.692408 3.824945 -10.62669 atno 620
-16.244085 3.891055 -12.102327 atno 621
-15.631715 3.976875 -12.998158 atno 622
-17.128952 3.320457 -12.387196 atno 623
-16.651526 5.295497 -11.61766 atno 624
-17.355072 5.200519 -10.789319 atno 625
-15.773333 5.800961 -11.213401 atno 626
-17.256484 6.184533 -12.710888 atno 627
-16.561586 6.289038 -13.544944 atno 628
-18.175436 5.744896 -13.099548 atno 629
-17.572028 7.529985 -12.228413 atno 630
-17.954852 8.107826 -13.003477 atno 631
-18.273551 7.475044 -11.463185 atno 632
-16.719343 7.999541 -11.856102 atno 633
-14.169 1.166 -10.173 atno 634
-14.88 0.843 -9.223 atno 635
-27.476 6.614 -2.937 atno 914
-26.759035 6.340731 -2.293978 atno 915
-27.209 6.837 -4.358 atno 916
-27.601752 7.82865 -4.586328 atno 917
-25.706 6.799 -4.623 atno 918
-25.528273 6.82886 -5.699399 atno 919
-25.30318 5.847676 -4.275333 atno 920
-24.912261 7.944403 -3.987304 atno 921
-25.008499 7.919419 -2.903515 atno 922
-25.289138 8.915265 -4.310408 atno 923
-23.167592 7.807061 -4.434945 atno 924
-22.467297 9.080584 -3.370419 atno 925
-21.87191 8.621557 -2.581149 atno 926
-23.248325 9.699016 -2.932049 atno 927
-21.806751 9.724263 -3.951348 atno 928
-27.933 5.844 -5.266 atno 929
-28.302 6.184 -6.394 atno 930
-21.505 0.745 -12.85 atno 1340
-20.635692 0.555937 -13.294112 atno 1341
-22.408 1.74 -13.413 atno 1342
-23.347547 1.694018 -12.860113 atno 1343
-21.823 3.185 -13.321 atno 1344
-22.593949 3.888423 -13.658028 atno 1345
-20.686381 3.277176 -14.164576 atno 1346
-20.359272 4.170141 -14.192674 atno 1347
-21.419896 3.549711 -11.88391 atno 1348
-21.16365 4.605408 -11.792633 atno 1349
-22.229716 3.350632 -11.184601 atno 1350
-20.55389 2.970042 -11.564846 atno 1351
-22.769 1.474 -14.872 atno 1352
-22.155 0.653 -15.56 atno 1353
-23.793 2.191 -15.315 atno 1354
-24.309784 2.744773 -14.664978 atno 1355
-24.101 2.398 -16.713 atno 1356
-24.59759 1.493798 -17.065763 atno 1357
-25.026 3.612 -16.766 atno 1358
-25.728576 3.551377 -15.933956 atno 1359
-24.464186 4.534777 -16.611715 atno 1360
-25.847424 3.686915 -18.0658 atno 1361
-25.185863 3.773791 -18.927406 atno 1362
-26.404526 2.759345 -18.198523 atno 1363
-26.855523 4.860517 -18.089311 atno 1364
-27.71401 4.874035 -18.970407 atno 1365
-26.775625 5.754612 -17.245643 atno 1366
-22.819 2.676 -17.507 atno 1367
-21.954 3.419 -17.046 atno 1368
-20.874 4.369 -20.555 atno 1390
-20.059895 4.33484 -19.980697 atno 1391
-21.029 5.583 -21.354 atno 1392
-22.019629 5.59247 -21.812194 atno 1393
-20.919 6.817 -20.453 atno 1394
-19.969639 6.770363 -19.917231 atno 1395
-20.869199 7.720886 -21.06146 atno 1396
-22.047261 6.97994 -19.429018 atno 1397
-22.277616 6.045353 -18.916827 atno 1398
-21.725386 7.672968 -18.655431 atno 1399
-23.516784 7.702986 -20.174793 atno 1400
-24.607152 6.28914 -20.001306 atno 1401
-24.268253 5.46638 -20.628938 atno 1402
-24.57946 5.957269 -18.965452 atno 1403
-25.63187 6.549689 -20.258637 atno 1404
-19.983 5.606 -22.475 atno 1405
-18.847 6.053 -22.28 atno 1406
-22.097 12.549 -13.491 atno 2387
-21.559171 13.346452 -13.779634 atno 2388
-21.416 11.41 -12.883 atno 2389
-22.170824 10.685917 -12.570041 atno 2390
-20.457 10.787 -13.9 atno 2391
-19.492963 11.307025 -13.921844 atno 2392
-20.245704 9.747769 -13.646129 atno 2393
-21.003941 10.821037 -15.203159 atno 2394
-21.363264 11.680351 -15.389422 atno 2395
-20.647 11.853 -11.641 atno 2396
-20.505 13.053 -11.387 atno 2397
-20.161 10.872 -10.875 atno 2398
-20.38369 9.93903 -11.140589 atno 2399
-19.352 11.108 -9.671 atno 2400
-19.216569 10.128569 -9.213111 atno 2401
-17.982 11.697 -10.048 atno 2402
-17.360787 11.83851 -9.162415 atno 2403
-18.079684 12.67215 -10.52824 atno 2404
-17.251566 10.718787 -10.994469 atno 2405
-17.180439 10.988164 -12.192876 atno 2406
-16.77631 9.683237 -10.525045 atno 2407
-20.047 11.999 -8.641 atno 2408
-19.382 12.654 -7.819 atno 2409
-21.379 12.014 -8.67 atno 2410
-21.876256 11.326756 -9.192853 atno 2411
-22.132 12.941 -7.828 atno 2412
-21.70611 13.926039 -8.017998 atno 2413
-23.624 12.986 -8.196 atno 2414
-23.745866 13.612774 -9.079885 atno 2415
-24.216989 13.470407 -7.419764 atno 2416
-24.206383 11.631383 -8.523019 atno 2417
-24.759197 10.826865 -7.528025 atno 2418
-24.775015 11.168088 -6.504185 atno 2419
-24.200398 11.161864 -9.834936 atno 2420
-23.780511 11.768355 -10.624446 atno 2421
-25.288438 9.581129 -7.837496 atno 2422
-25.708959 8.964378 -7.057069 atno 2423
-24.729245 9.917362 -10.147866 atno 2424
-24.719704 9.56673 -11.17028 atno 2425
-25.275812 9.124174 -9.147589 atno 2426
-25.690006 8.156786 -9.391081 atno 2427
-21.939 12.649 -6.35 atno 2428
-22.196 11.537 -5.893 atno 2429

> <Heavy atom RMSD to 3GEN_ligand_origInal 7>
7.318

> <Scoring Rotated Receptor Atoms>
157

> <Favorable A:LEU408>
1

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
1

> <Favorable A:VAL416>
1

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
0

> <Favorable A:GLU475>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
1

> <Favorable A:ASP521>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
0

> <Favorable A:ASP539>
1

> <Favorable A:PHE540>
0

> <Favorable A:LEU542>
1

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
1

> <Charge A:LYS430>
0

> <Charge A:ASP521>
0

> <Charge A:ASP539>
1

> <Hydrophobic A:LEU408>
1

> <Hydrophobic A:PHE413>
1

> <Hydrophobic A:VAL416>
1

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
0

> <Hydrophobic A:CYS481>
1

> <Hydrophobic A:LEU528>
0

> <Hydrophobic A:PHE540>
0

> <Hydrophobic A:LEU542>
1

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
1

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ASN526>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242217553D

 50 54  0  0  0  0            999 V2000
  -16.1699    6.3121  -17.3604 N   0  0
  -15.9355    6.0535  -18.6698 C   0  0
  -16.8849    5.3510  -19.3169 N   0  0
  -16.7005    5.0622  -20.6166 C   0  0
  -15.6431    5.4317  -21.3427 N   0  0
  -14.6974    6.1387  -20.7016 C   0  0
  -14.8013    6.4696  -19.3298 C   0  0
  -13.5101    6.6673  -21.2059 N   0  0
  -13.1008    6.5363  -22.6261 C   0  0  2  0  0  0
  -12.8591    5.0668  -23.0121 C   0  0
  -11.7272    5.0843  -24.0348 C   0  0
  -10.8460    6.2457  -23.5871 C   0  0
  -11.8225    7.2949  -23.0480 C   0  0
  -12.9111    7.2639  -20.1507 C   0  0
  -13.6360    7.1783  -18.9754 C   0  0
  -13.2677    7.7039  -17.6360 C   0  0
  -13.9170    8.8000  -17.1028 C   0  0
  -13.6196    9.2540  -15.8215 C   0  0
  -12.6696    8.6044  -15.0427 C   0  0
  -11.9780    7.5283  -15.6056 C   0  0
  -12.2781    7.0927  -16.8934 C   0  0
  -12.4415    9.0794  -13.7534 O   0  0
  -12.0656    8.1084  -12.8396 C   0  0
  -10.7516    8.0531  -12.3982 C   0  0
  -10.3415    7.0234  -11.5622 C   0  0
  -11.2509    6.0638  -11.1398 C   0  0
  -12.5811    6.1584  -11.5254 C   0  0
  -12.9891    7.1784  -12.3762 C   0  0
  -15.5314    6.8517  -16.8124 H   0  0
  -16.9966    5.9590  -16.9237 H   0  0
  -17.4615    4.4774  -21.1098 H   0  0
  -13.9178    6.9248  -23.2380 H   0  0
  -13.7572    4.5804  -23.3946 H   0  0
  -12.5296    4.5021  -22.1422 H   0  0
  -12.1268    5.2866  -25.0286 H   0  0
  -11.1863    4.1379  -24.0765 H   0  0
  -10.2186    6.6322  -24.3912 H   0  0
  -10.1869    5.9169  -22.7836 H   0  0
  -11.3624    7.8867  -22.2599 H   0  0
  -12.0716    7.9939  -23.8484 H   0  0
  -11.9553    7.7647  -20.1966 H   0  0
  -14.6692    9.3191  -17.6790 H   0  0
  -14.1453   10.1071  -15.4176 H   0  0
  -11.2024    7.0113  -15.0608 H   0  0
  -11.7368    6.2464  -17.2938 H   0  0
  -10.0462    8.7973  -12.7358 H   0  0
   -9.3135    6.9692  -11.2411 H   0  0
  -10.9298    5.2572  -10.4968 H   0  0
  -13.2940    5.4265  -11.1802 H   0  0
  -14.0180    7.2355  -12.6979 H   0  0
  1  2  1  0
  1 29  1  0
  1 30  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  4 31  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 32  1  0
 10 11  1  0
 10 33  1  0
 10 34  1  0
 11 12  1  0
 11 35  1  0
 11 36  1  0
 12 13  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 15  2  0
 14 41  1  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 17 42  1  0
 18 19  2  0
 18 43  1  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 20 44  1  0
 21 45  1  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 24 46  1  0
 25 26  2  0
 25 47  1  0
 26 27  1  0
 26 48  1  0
 27 28  2  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372114167529488

> <LigScore1_Dreiding>
1.81

> <LigScore2_Dreiding>
4.87

> <-PLP1>
89.4

> <-PLP2>
79.95

> <Jain>
3.39

> <-PMF>
53.21

> <-PMF04>
1.58

> <-CDOCKER_ENERGY>
2.432

> <-CDOCKER_INTERACTION_ENERGY>
39.69

> <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

> <ChiRotor E-total>
-21.315771
-68.43322

> <ChiRotor E-elec>
-2.688296
-15.142503

> <ChiRotor E-vdw>
-31.605207
-76.720222

> <pI>
6.32

> <At pH>
7.4

> <Net Charge>
-4.97

> <ChiFlex Energy>
-58.352

> <Side Chain Conformation>
5

> <Residues Side-Chain Conformations>
A:LEU408 A:ALA428 A:LYS430 A:MET449 A:THR474 A:GLU475 A:MET477 A:SER538 A:ASP539 A:PHE540

> <Protein Conformation>
5

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <NumberOfIonizations>
1

> <__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

> <MOL_NUMBER>
1

> <LibDockScore>
73.961

> <LibDock Pose>
1

> <Refined Residues>
9

> <__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

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

> <Rotated Residues>
A:ALA428,A:ASP539,A:GLU475,A:LEU408,A:LYS430,A:MET449,A:MET477,A:PHE540,A:SER538,A:THR474

> <Receptor.Positions>
-10.627 1.547 -19.716 atno 269
-10.802429 1.336749 -18.761136 atno 270
-11.136 2.809 -20.243 atno 271
-11.067236 2.788878 -21.330093 atno 272
-12.591 3.008 -19.818 atno 273
-12.553074 3.036771 -18.727024 atno 274
-12.953539 4.013606 -19.983241 atno 275
-13.532559 1.819559 -20.098211 atno 276
-13.143161 0.997946 -19.497857 atno 277
-14.959591 2.075401 -19.594571 atno 278
-15.532989 1.153648 -19.51683 atno 279
-14.965925 2.547754 -18.617775 atno 280
-15.499301 2.736781 -20.261251 atno 281
-13.526094 1.324479 -21.549505 atno 282
-13.631439 0.253052 -21.535873 atno 283
-14.358272 1.703728 -22.137911 atno 284
-12.601644 1.536636 -22.081737 atno 285
-10.29 4 -19.805 atno 286
-10.313 5.055 -20.437 atno 287
-19.792 -0.299 -16.749 atno 585
-20.549726 -0.015243 -16.166379 atno 586
-18.479 0.235 -16.414 atno 587
-17.742877 -0.198793 -17.091772 atno 588
-18.46 1.755 -16.537 atno 589
-18.961994 2.239462 -15.702418 atno 590
-18.942206 2.084873 -17.456233 atno 591
-17.437999 2.13769 -16.556283 atno 592
-18.171 -0.182 -14.983 atno 593
-19.064 -0.211 -14.137 atno 594
-15.724 0.924 -12.005 atno 614
-16.665735 1.069361 -11.70286 atno 615
-14.772 1.844 -11.395 atno 616
-13.988408 2.05328 -12.125606 atno 617
-15.466 3.153 -11.002 atno 618
-16.1476 2.972909 -10.18761 atno 619
-14.698775 3.807526 -10.584756 atno 620
-16.194552 3.928621 -12.111055 atno 621
-15.55354 4.022577 -12.985183 atno 622
-17.079416 3.380547 -12.437321 atno 623
-16.591254 5.33088 -11.609043 atno 624
-17.340021 5.231665 -10.821809 atno 625
-15.723632 5.801986 -11.14445 atno 626
-17.112105 6.268444 -12.70555 atno 627
-16.359374 6.394298 -13.484297 atno 628
-18.007144 5.855923 -13.172706 atno 629
-17.444704 7.599649 -12.19567 atno 630
-17.768098 8.213848 -12.970641 atno 631
-18.197622 7.526281 -11.482544 atno 632
-16.614778 8.045527 -11.750074 atno 633
-14.169 1.166 -10.173 atno 634
-14.88 0.843 -9.223 atno 635
-27.476 6.614 -2.937 atno 914
-26.759967 6.351164 -2.288037 atno 915
-27.209 6.837 -4.358 atno 916
-27.597107 7.832362 -4.576685 atno 917
-25.706 6.799 -4.623 atno 918
-25.306335 5.844752 -4.279644 atno 919
-25.525113 6.834761 -5.698668 atno 920
-24.912509 7.938134 -3.97559 atno 921
-25.265045 8.909892 -4.322573 atno 922
-25.040464 7.932284 -2.894768 atno 923
-23.157454 7.769941 -4.367963 atno 924
-22.483685 9.117268 -3.379669 atno 925
-21.880387 9.772058 -4.007935 atno 926
-23.276746 9.705112 -2.921566 atno 927
-21.831419 8.717133 -2.603536 atno 928
-27.933 5.844 -5.266 atno 929
-28.302 6.184 -6.394 atno 930
-21.505 0.745 -12.85 atno 1340
-20.642314 0.534108 -13.29721 atno 1341
-22.408 1.74 -13.413 atno 1342
-23.346829 1.695871 -12.859424 atno 1343
-21.823 3.185 -13.321 atno 1344
-22.592684 3.88877 -13.660034 atno 1345
-20.68468 3.276306 -14.162764 atno 1346
-20.354869 4.167877 -14.188551 atno 1347
-21.422441 3.550488 -11.883324 atno 1348
-21.166399 4.606239 -11.792191 atno 1349
-22.233657 3.352043 -11.185543 atno 1350
-20.557246 2.970939 -11.561817 atno 1351
-22.769 1.474 -14.872 atno 1352
-22.155 0.653 -15.56 atno 1353
-23.793 2.191 -15.315 atno 1354
-24.29238 2.761983 -14.666902 atno 1355
-24.101 2.398 -16.713 atno 1356
-24.597257 1.493775 -17.065556 atno 1357
-25.026 3.612 -16.766 atno 1358
-25.726433 3.550987 -15.932134 atno 1359
-24.465198 4.535708 -16.613677 atno 1360
-25.850974 3.685444 -18.063501 atno 1361
-25.191157 3.785971 -18.924989 atno 1362
-26.397844 2.752428 -18.201076 atno 1363
-26.872888 4.847139 -18.078414 atno 1364
-27.713537 4.872735 -18.976414 atno 1365
-26.821148 5.720964 -17.211498 atno 1366
-22.819 2.676 -17.507 atno 1367
-21.954 3.419 -17.046 atno 1368
-20.874 4.369 -20.555 atno 1390
-20.249184 4.441178 -19.794854 atno 1391
-21.029 5.583 -21.354 atno 1392
-22.019808 5.592709 -21.81191 atno 1393
-20.919 6.817 -20.453 atno 1394
-19.967861 6.773526 -19.920193 atno 1395
-20.872306 7.720543 -21.062161 atno 1396
-22.043591 6.979296 -19.425554 atno 1397
-22.270501 6.044712 -18.912326 atno 1398
-21.720375 7.676159 -18.655884 atno 1399
-23.515344 7.696397 -20.172099 atno 1400
-24.620637 6.306932 -19.920766 atno 1401
-24.625058 6.0547 -18.86219 atno 1402
-25.63478 6.54914 -20.234867 atno 1403
-24.267024 5.437185 -20.471758 atno 1404
-19.983 5.606 -22.475 atno 1405
-18.847 6.053 -22.28 atno 1406
-22.097 12.549 -13.491 atno 2387
-21.540627 13.338297 -13.766854 atno 2388
-21.416 11.41 -12.883 atno 2389
-22.171756 10.685025 -12.576306 atno 2390
-20.457 10.787 -13.9 atno 2391
-19.499575 11.318509 -13.936169 atno 2392
-20.230721 9.753334 -13.636354 atno 2393
-21.019573 10.798062 -15.196849 atno 2394
-21.361715 11.661446 -15.401634 atno 2395
-20.647 11.853 -11.641 atno 2396
-20.505 13.053 -11.387 atno 2397
-20.161 10.872 -10.875 atno 2398
-20.279976 9.9352 -11.18184 atno 2399
-19.352 11.108 -9.671 atno 2400
-19.216129 10.128476 -9.213869 atno 2401
-17.982 11.697 -10.048 atno 2402
-17.363152 11.850783 -9.162943 atno 2403
-18.078181 12.664202 -10.543772 atno 2404
-17.258132 10.700945 -10.981871 atno 2405
-16.636501 9.761397 -10.482943 atno 2406
-17.341693 10.8552 -12.201672 atno 2407
-20.047 11.999 -8.641 atno 2408
-19.382 12.654 -7.819 atno 2409
-21.379 12.014 -8.67 atno 2410
-21.873957 11.284217 -9.129936 atno 2411
-22.132 12.941 -7.828 atno 2412
-21.702621 13.925034 -8.016385 atno 2413
-23.624 12.986 -8.196 atno 2414
-24.219662 13.462562 -7.416986 atno 2415
-23.746684 13.618705 -9.07551 atno 2416
-24.200445 11.631334 -8.533499 atno 2417
-24.756799 10.820795 -7.548919 atno 2418
-24.782971 11.156586 -6.523166 atno 2419
-24.181284 11.16833 -9.849918 atno 2420
-23.757925 11.78138 -10.632716 atno 2421
-25.277796 9.572976 -7.868353 atno 2422
-25.702695 8.951008 -7.094177 atno 2423
-24.700214 9.922761 -10.172301 atno 2424
-24.679775 9.576991 -11.196454 atno 2425
-25.251141 9.122404 -9.180789 atno 2426
-25.657311 8.153671 -9.432253 atno 2427
-21.939 12.649 -6.35 atno 2428
-22.196 11.537 -5.893 atno 2429

> <Heavy atom RMSD to 3GEN_ligand_origInal 7>
6.261

> <Scoring Rotated Receptor Atoms>
157

> <Favorable A:LEU408>
3

> <Favorable A:GLN412>
0

> <Favorable A:PHE413>
0

> <Favorable A:VAL416>
2

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
1

> <Favorable A:GLU475>
0

> <Favorable A:MET477>
1

> <Favorable A:CYS481>
0

> <Favorable A:ASP521>
0

> <Favorable A:ASN526>
0

> <Favorable A:LEU528>
1

> <Favorable A:ASP539>
0

> <Favorable A:PHE540>
0

> <Favorable A:LEU542>
0

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
0

> <Charge A:LYS430>
0

> <Charge A:ASP521>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
3

> <Hydrophobic A:PHE413>
0

> <Hydrophobic A:VAL416>
2

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
1

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
1

> <Hydrophobic A:PHE540>
0

> <Hydrophobic A:LEU542>
0

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
0

> <HydrogenBond A:GLN412>
0

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
1

> <HydrogenBond A:ASN526>
0

> <Other A:CYS481>
0

$$$$
3GEN_ligand
  SciTegic09242217553D

 50 54  0  0  0  0            999 V2000
   -8.5878   11.4425  -12.6242 N   0  0
   -9.0615   11.7405  -11.3898 C   0  0
   -8.1445   11.8366  -10.4030 N   0  0
   -8.5477   12.2337   -9.1825 C   0  0
   -9.8070   12.5277   -8.8545 N   0  0
  -10.7287   12.3920   -9.8243 C   0  0
  -10.3967   11.9585  -11.1310 C   0  0
  -12.0989   12.6398   -9.7636 N   0  0
  -12.7819   13.1455   -8.5461 C   0  0  1  0  0  0
  -14.2937   13.4003   -8.7049 C   0  0
  -14.9784   12.2060   -8.0472 C   0  0
  -14.0722   11.8799   -6.8628 C   0  0
  -12.6549   12.1400   -7.3797 C   0  0
  -12.5704   12.3244  -10.9914 C   0  0
  -11.6001   11.8664  -11.8683 C   0  0
  -11.8021   11.3840  -13.2635 C   0  0
  -12.5212   12.1319  -14.1780 C   0  0
  -12.6957   11.6865  -15.4866 C   0  0
  -12.1798   10.4645  -15.8940 C   0  0
  -11.4620    9.7068  -14.9741 C   0  0
  -11.2790   10.1699  -13.6752 C   0  0
  -12.3574   10.0528  -17.2077 O   0  0
  -12.9172    8.7896  -17.3779 C   0  0
  -13.9371    8.3084  -16.5565 C   0  0
  -14.4837    7.0515  -16.7829 C   0  0
  -14.0209    6.2712  -17.8342 C   0  0
  -13.0171    6.7523  -18.6645 C   0  0
  -12.4733    8.0108  -18.4398 C   0  0
   -7.6133   11.2662  -12.7598 H   0  0
   -9.1946   11.3971  -13.4176 H   0  0
   -7.7971   12.3231   -8.4109 H   0  0
  -12.3066   14.0895   -8.2712 H   0  0
  -14.6261   13.5718   -9.7271 H   0  0
  -14.5574   14.2967   -8.1404 H   0  0
  -15.0041   11.3624   -8.7401 H   0  0
  -16.0019   12.4305   -7.7462 H   0  0
  -14.2034   10.8610   -6.4986 H   0  0
  -14.2947   12.5603   -6.0397 H   0  0
  -12.0051   12.5181   -6.5897 H   0  0
  -12.2226   11.1983   -7.7237 H   0  0
  -13.6113   12.4079  -11.2727 H   0  0
  -12.9591   13.0794  -13.8920 H   0  0
  -13.2430   12.2840  -16.1984 H   0  0
  -11.0312    8.7603  -15.2661 H   0  0
  -10.7135    9.5566  -12.9872 H   0  0
  -14.3228    8.9066  -15.7449 H   0  0
  -15.2684    6.6830  -16.1404 H   0  0
  -14.4446    5.2929  -18.0104 H   0  0
  -12.6589    6.1507  -19.4862 H   0  0
  -11.6960    8.3816  -19.0912 H   0  0
  1  2  1  0
  1 29  1  0
  1 30  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  4 31  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 32  1  0
 10 11  1  0
 10 33  1  0
 10 34  1  0
 11 12  1  0
 11 35  1  0
 11 36  1  0
 12 13  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 15  2  0
 14 41  1  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 17 42  1  0
 18 19  2  0
 18 43  1  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 20 44  1  0
 21 45  1  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 24 46  1  0
 25 26  2  0
 25 47  1  0
 26 27  1  0
 26 48  1  0
 27 28  2  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372118462496784

> <LigScore1_Dreiding>
2.56

> <LigScore2_Dreiding>
5.14

> <-PLP1>
61.61

> <-PLP2>
53.32

> <Jain>
1.38

> <-PMF>
82.52

> <-PMF04>
30.07

> <-CDOCKER_ENERGY>
2.146

> <-CDOCKER_INTERACTION_ENERGY>
37.512

> <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

> <ChiRotor E-total>
-21.315771
-47.702034

> <ChiRotor E-elec>
-2.688296
-15.107075

> <ChiRotor E-vdw>
-31.605207
-62.202942

> <pI>
6.32

> <At pH>
7.4

> <Net Charge>
-4.97

> <ChiFlex Energy>
-62.833

> <Side Chain Conformation>
1

> <Residues Side-Chain Conformations>
A:LEU408 A:ALA428 A:LYS430 A:MET449 A:THR474 A:GLU475 A:MET477 A:SER538 A:ASP539 A:PHE540

> <Protein Conformation>
1

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <NumberOfIonizations>
1

> <__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

> <MOL_NUMBER>
1

> <LibDockScore>
70.642

> <LibDock Pose>
3

> <Refined Residues>
9

> <__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

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

> <Rotated Residues>
A:ALA428,A:ASP539,A:GLU475,A:LEU408,A:LYS430,A:MET449,A:MET477,A:PHE540,A:SER538,A:THR474

> <Receptor.Positions>
-10.627 1.547 -19.716 atno 269
-10.806332 1.323089 -18.765077 atno 270
-11.136 2.809 -20.243 atno 271
-11.085225 2.781061 -21.332559 atno 272
-12.591 3.008 -19.818 atno 273
-12.637233 3.087389 -18.730248 atno 274
-12.948323 3.964641 -20.203055 atno 275
-13.563908 1.905355 -20.274292 atno 276
-13.257545 0.96456 -19.817426 atno 277
-14.981713 2.230691 -19.781039 atno 278
-15.685131 1.433701 -20.005756 atno 279
-15.00552 2.370373 -18.704333 atno 280
-15.356896 3.146264 -20.238839 atno 281
-13.554767 1.718937 -21.799448 atno 282
-14.288997 0.979579 -22.115492 atno 283
-13.787614 2.653142 -22.310799 atno 284
-12.583755 1.374678 -22.153986 atno 285
-10.29 4 -19.805 atno 286
-10.313 5.055 -20.437 atno 287
-19.792 -0.299 -16.749 atno 585
-20.55638 -0.017599 -16.174965 atno 586
-18.479 0.235 -16.414 atno 587
-17.743004 -0.199409 -17.091511 atno 588
-18.46 1.755 -16.537 atno 589
-18.97436 2.237559 -15.709037 atno 590
-18.930895 2.079784 -17.464453 atno 591
-17.436922 2.134909 -16.54222 atno 592
-18.171 -0.182 -14.983 atno 593
-19.064 -0.211 -14.137 atno 594
-15.724 0.924 -12.005 atno 614
-16.658437 1.07358 -11.681857 atno 615
-14.772 1.844 -11.395 atno 616
-13.988765 2.053068 -12.126154 atno 617
-15.466 3.153 -11.002 atno 618
-16.125946 2.985861 -10.166092 atno 619
-14.694656 3.823512 -10.619596 atno 620
-16.227347 3.886065 -12.117319 atno 621
-15.611113 3.944213 -13.012606 atno 622
-17.119847 3.324741 -12.396623 atno 623
-16.614402 5.306228 -11.665779 atno 624
-17.334474 5.240709 -10.848841 atno 625
-15.734136 5.803724 -11.256097 atno 626
-17.181693 6.18025 -12.790342 atno 627
-16.460992 6.268032 -13.60472 atno 628
-18.090649 5.738841 -13.199504 atno 629
-17.504476 7.534579 -12.340453 atno 630
-17.861592 8.101414 -13.134259 atno 631
-18.229507 7.495435 -11.594177 atno 632
-16.662782 8.005216 -11.947299 atno 633
-14.169 1.166 -10.173 atno 634
-14.88 0.843 -9.223 atno 635
-27.476 6.614 -2.937 atno 914
-26.759449 6.347061 -2.290397 atno 915
-27.209 6.837 -4.358 atno 916
-27.601755 7.828569 -4.586866 atno 917
-25.706 6.799 -4.623 atno 918
-25.30559 5.84594 -4.277255 atno 919
-25.524851 6.832871 -5.698678 atno 920
-24.914431 7.940406 -3.977278 atno 921
-25.26967 8.911217 -4.324164 atno 922
-25.041221 7.934522 -2.896263 atno 923
-23.15937 7.776647 -4.371061 atno 924
-22.488073 9.120226 -3.376067 atno 925
-21.886656 9.779764 -4.001158 atno 926
-23.282308 9.703703 -2.91432 atno 927
-21.834404 8.717387 -2.602526 atno 928
-27.933 5.844 -5.266 atno 929
-28.302 6.184 -6.394 atno 930
-21.505 0.745 -12.85 atno 1340
-20.634311 0.550808 -13.288768 atno 1341
-22.408 1.74 -13.413 atno 1342
-23.34753 1.694248 -12.860122 atno 1343
-21.823 3.185 -13.321 atno 1344
-22.593632 3.888455 -13.658648 atno 1345
-20.685758 3.27733 -14.163745 atno 1346
-20.357487 4.169928 -14.18963 atno 1347
-21.421067 3.549681 -11.883545 atno 1348
-21.165626 4.605532 -11.791769 atno 1349
-22.231179 3.349926 -11.184809 atno 1350
-20.55495 2.970458 -11.563988 atno 1351
-22.769 1.474 -14.872 atno 1352
-22.155 0.653 -15.56 atno 1353
-23.793 2.191 -15.315 atno 1354
-24.312066 2.744035 -14.666077 atno 1355
-24.101 2.398 -16.713 atno 1356
-24.597063 1.493573 -17.065659 atno 1357
-25.026 3.612 -16.766 atno 1358
-25.733046 3.544573 -15.938253 atno 1359
-24.467538 4.535388 -16.603776 atno 1360
-25.839425 3.691464 -18.070325 atno 1361
-25.172143 3.808417 -18.923756 atno 1362
-26.375793 2.75458 -18.222924 atno 1363
-26.873002 4.842479 -18.083539 atno 1364
-27.702208 4.870052 -18.992054 atno 1365
-26.84111 5.705834 -17.205397 atno 1366
-22.819 2.676 -17.507 atno 1367
-21.954 3.419 -17.046 atno 1368
-20.874 4.369 -20.555 atno 1390
-20.053155 4.337561 -19.98968 atno 1391
-21.029 5.583 -21.354 atno 1392
-22.019934 5.592725 -21.811616 atno 1393
-20.919 6.817 -20.453 atno 1394
-20.863412 7.720437 -21.061657 atno 1395
-19.972055 6.767548 -19.913227 atno 1396
-22.051047 6.984631 -19.434314 atno 1397
-21.730331 7.67787 -18.660412 atno 1398
-22.288924 6.049846 -18.925688 atno 1399
-23.511662 7.711152 -20.192515 atno 1400
-24.631042 6.333567 -19.938496 atno 1401
-24.69615 6.132477 -18.870778 atno 1402
-25.622534 6.552314 -20.330284 atno 1403
-24.243343 5.439175 -20.42416 atno 1404
-19.983 5.606 -22.475 atno 1405
-18.847 6.053 -22.28 atno 1406
-22.097 12.549 -13.491 atno 2387
-21.543731 13.350705 -13.736853 atno 2388
-21.416 11.41 -12.883 atno 2389
-22.172404 10.687102 -12.571773 atno 2390
-20.457 10.787 -13.9 atno 2391
-19.497802 11.315645 -13.93421 atno 2392
-20.234243 9.752575 -13.636383 atno 2393
-21.018659 10.799207 -15.197449 atno 2394
-21.36031 11.662215 -15.401422 atno 2395
-20.647 11.853 -11.641 atno 2396
-20.505 13.053 -11.387 atno 2397
-20.161 10.872 -10.875 atno 2398
-20.307581 9.93318 -11.16245 atno 2399
-19.352 11.108 -9.671 atno 2400
-19.257928 10.113721 -9.224946 atno 2401
-17.982 11.697 -10.048 atno 2402
-17.801267 11.619803 -9.056175 atno 2403
-17.999204 12.723885 -10.416741 atno 2404
-17.262642 10.689797 -10.97386 atno 2405
-17.067291 11.001383 -12.148281 atno 2406
-16.925297 9.596568 -10.518689 atno 2407
-20.047 11.999 -8.641 atno 2408
-19.382 12.654 -7.819 atno 2409
-21.379 12.014 -8.67 atno 2410
-21.871699 11.319626 -9.187734 atno 2411
-22.132 12.941 -7.828 atno 2412
-21.705624 13.925817 -8.018053 atno 2413
-23.624 12.986 -8.196 atno 2414
-24.219879 13.461776 -7.416693 atno 2415
-23.747035 13.619153 -9.075141 atno 2416
-24.199864 11.63087 -8.534344 atno 2417
-24.749706 10.817254 -7.548612 atno 2418
-24.772224 11.150659 -6.522197 atno 2419
-24.185358 11.171823 -9.851262 atno 2420
-23.767505 11.786736 -10.634962 atno 2421
-25.269577 9.568884 -7.868902 atno 2422
-25.689273 8.944219 -7.093779 atno 2423
-24.703854 9.924565 -10.174708 atno 2424
-24.687051 9.581885 -11.199242 atno 2425
-25.247711 9.121657 -9.181932 atno 2426
-25.653121 8.152147 -9.433982 atno 2427
-21.939 12.649 -6.35 atno 2428
-22.196 11.537 -5.893 atno 2429

> <Heavy atom RMSD to 3GEN_ligand_origInal 7>
11.041

> <Scoring Rotated Receptor Atoms>
157

> <Favorable A:LEU408>
0

> <Favorable A:GLN412>
1

> <Favorable A:PHE413>
1

> <Favorable A:VAL416>
1

> <Favorable A:ALA428>
0

> <Favorable A:LYS430>
0

> <Favorable A:GLU475>
0

> <Favorable A:MET477>
0

> <Favorable A:CYS481>
1

> <Favorable A:ASP521>
0

> <Favorable A:ASN526>
1

> <Favorable A:LEU528>
0

> <Favorable A:ASP539>
0

> <Favorable A:PHE540>
0

> <Favorable A:LEU542>
1

> <Favorable A:VAL546>
0

> <Favorable A:TYR551>
1

> <Charge A:LYS430>
0

> <Charge A:ASP521>
0

> <Charge A:ASP539>
0

> <Hydrophobic A:LEU408>
0

> <Hydrophobic A:PHE413>
1

> <Hydrophobic A:VAL416>
1

> <Hydrophobic A:ALA428>
0

> <Hydrophobic A:LYS430>
0

> <Hydrophobic A:CYS481>
0

> <Hydrophobic A:LEU528>
0

> <Hydrophobic A:PHE540>
0

> <Hydrophobic A:LEU542>
1

> <Hydrophobic A:VAL546>
0

> <Hydrophobic A:TYR551>
1

> <HydrogenBond A:GLN412>
1

> <HydrogenBond A:GLU475>
0

> <HydrogenBond A:MET477>
0

> <HydrogenBond A:ASN526>
1

> <Other A:CYS481>
1

$$$$
