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Database: PDB
Entry: 2W3L
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HEADER    APOPTOSIS                               13-NOV-08   2W3L              
TITLE     CRYSTAL STRUCTURE OF CHIMAERIC BCL2-XL AND PHENYL                     
TITLE    2 TETRAHYDROISOQUINOLINE AMIDE COMPLEX                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APOPTOSIS REGULATOR BCL-2;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 9-33,92-206;                                      
COMPND   5 SYNONYM: BCL2-XL;                                                    
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    APOPTOSIS                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.PORTER,A.PAYNE,B.DE CANDOLE,D.FORD,B.HUTCHINSON,G.TREVITT,J.TURNER, 
AUTHOR   2 C.EDWARDS,C.WATKINS,I.WHITCOMBE,J.DAVIS,C.STUBBERFIELD,M.FISHER,     
AUTHOR   3 M.LAMERS                                                             
REVDAT   3   28-JUN-17 2W3L    1       REMARK                                   
REVDAT   2   23-DEC-08 2W3L    1       JRNL                                     
REVDAT   1   09-DEC-08 2W3L    0                                                
JRNL        AUTH   J.PORTER,A.PAYNE,B.DE CANDOLE,D.FORD,B.HUTCHINSON,G.TREVITT, 
JRNL        AUTH 2 J.TURNER,C.EDWARDS,C.WATKINS,I.WHITCOMBE,J.DAVIS,            
JRNL        AUTH 3 C.STUBBERFIELD                                               
JRNL        TITL   TETRAHYDROISOQUINOLINE AMIDE SUBSTITUTED PHENYL PYRAZOLES AS 
JRNL        TITL 2 SELECTIVE BCL-2 INHIBITORS.                                  
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  19   230 2009              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   19027294                                                     
JRNL        DOI    10.1016/J.BMCL.2008.10.113                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 18688                          
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) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1012                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1340                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 71                           
REMARK   3   BIN FREE R VALUE                    : 0.3030                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2318                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 84                                      
REMARK   3   SOLVENT ATOMS            : 223                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.91000                                              
REMARK   3    B22 (A**2) : -1.96000                                             
REMARK   3    B33 (A**2) : -0.95000                                             
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): 0.261         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.210         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.149         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.425         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2476 ; 0.018 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3357 ; 1.718 ; 1.951       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   279 ; 6.395 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   133 ;31.187 ;22.632       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   370 ;16.501 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;15.933 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   327 ; 0.118 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1987 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1204 ; 0.213 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1702 ; 0.316 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   263 ; 0.242 ; 0.500       
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):    68 ; 0.204 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    30 ; 0.257 ; 0.500       
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):  1435 ; 1.253 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2224 ; 1.976 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1234 ; 3.095 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1133 ; 4.798 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2W3L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-NOV-08.                  
REMARK 100 THE DEPOSITION ID IS D_1290038090.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-MAR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
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 MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : VARIMAX-HF                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU (RAXIS4)                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22774                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.910                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.010                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.970                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       34.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.33500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.16000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       35.33500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.16000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: PQS                                                   
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     ASP A    35                                                      
REMARK 465     SER B   164                                                      
REMARK 465     MET B   165                                                      
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     ARG A  12    CZ   NH1  NH2                                       
REMARK 470     LYS A  17    CG   CD   CE   NZ                                   
REMARK 470     GLN A  25    CD   OE1  NE2                                       
REMARK 470     LYS A  54    CE   NZ                                             
REMARK 470     LYS B  17    CG   CD   CE   NZ                                   
REMARK 470     ARG B  26    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B  65    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B  76    CB   OG                                             
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    HOH A  2019     O    HOH A  2020              2.14            
REMARK 500   O    GLU A   124     O    HOH A  2095              2.17            
REMARK 500   OE1  GLN A   149     O    HOH A  2108              2.19            
REMARK 500   OH   TYR B    18     OE2  GLU B   111              2.19            
REMARK 500   OE1  GLU A   119     O    HOH A  2092              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  2056     O    HOH B  2025     2564     2.08            
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    SER A  76       61.90    -57.59                                   
REMARK 500    HIS A  79       51.88     38.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 TYR B  161     GLY B  162                   47.20                    
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 A2021        DISTANCE =  6.56 ANGSTROMS                       
REMARK 525    HOH B2019        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH B2024        DISTANCE =  6.32 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DRO A1166                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DRO B1164                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1YSW   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF THE ANTI-APOPTOTIC PROTEIN BCL-2COMPLEXED      
REMARK 900 WITH AN ACYL- SULFONAMIDE-BASED LIGAND                               
REMARK 900 RELATED ID: 1G5M   RELATED DB: PDB                                   
REMARK 900 HUMAN BCL-2, ISOFORM 1                                               
REMARK 900 RELATED ID: 1GJH   RELATED DB: PDB                                   
REMARK 900 HUMAN BCL-2, ISOFORM 2                                               
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE AUTHORS SUGGEST THE FLEXIBLE LOOP BETWEEN N- AND C-TERMINUS      
REMARK 999 IS A CHIMERA                                                         
DBREF  2W3L A    9    33  UNP    P10415   BCL2_HUMAN       9     33             
DBREF  2W3L A   34    50  PDB    2W3L     2W3L            34     50             
DBREF  2W3L A   51   165  UNP    P10415   BCL2_HUMAN      92    206             
DBREF  2W3L B    9    33  UNP    P10415   BCL2_HUMAN       9     33             
DBREF  2W3L B   34    50  PDB    2W3L     2W3L            34     50             
DBREF  2W3L B   51   165  UNP    P10415   BCL2_HUMAN      92    206             
SEQADV 2W3L LYS A   54  UNP  P10415    LEU    95 CONFLICT                       
SEQADV 2W3L GLU A   58  UNP  P10415    GLN    99 CONFLICT                       
SEQADV 2W3L GLY A   77  UNP  P10415    GLN   118 CONFLICT                       
SEQADV 2W3L LYS B   54  UNP  P10415    LEU    95 CONFLICT                       
SEQADV 2W3L GLU B   58  UNP  P10415    GLN    99 CONFLICT                       
SEQADV 2W3L GLY B   77  UNP  P10415    GLN   118 CONFLICT                       
SEQRES   1 A  144  TYR ASP ASN ARG GLU ILE VAL MET LYS TYR ILE HIS TYR          
SEQRES   2 A  144  LYS LEU SER GLN ARG GLY TYR GLU TRP ASP ALA GLY ALA          
SEQRES   3 A  144  ASP SER GLU VAL VAL HIS LYS THR LEU ARG GLU ALA GLY          
SEQRES   4 A  144  ASP ASP PHE SER ARG ARG TYR ARG ARG ASP PHE ALA GLU          
SEQRES   5 A  144  MET SER SER GLY LEU HIS LEU THR PRO PHE THR ALA ARG          
SEQRES   6 A  144  GLY ARG PHE ALA THR VAL VAL GLU GLU LEU PHE ARG ASP          
SEQRES   7 A  144  GLY VAL ASN TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE          
SEQRES   8 A  144  GLY GLY VAL MET CYS VAL GLU SER VAL ASN ARG GLU MET          
SEQRES   9 A  144  SER PRO LEU VAL ASP ASN ILE ALA LEU TRP MET THR GLU          
SEQRES  10 A  144  TYR LEU ASN ARG HIS LEU HIS THR TRP ILE GLN ASP ASN          
SEQRES  11 A  144  GLY GLY TRP ASP ALA PHE VAL GLU LEU TYR GLY PRO SER          
SEQRES  12 A  144  MET                                                          
SEQRES   1 B  144  TYR ASP ASN ARG GLU ILE VAL MET LYS TYR ILE HIS TYR          
SEQRES   2 B  144  LYS LEU SER GLN ARG GLY TYR GLU TRP ASP ALA GLY ALA          
SEQRES   3 B  144  ASP SER GLU VAL VAL HIS LYS THR LEU ARG GLU ALA GLY          
SEQRES   4 B  144  ASP ASP PHE SER ARG ARG TYR ARG ARG ASP PHE ALA GLU          
SEQRES   5 B  144  MET SER SER GLY LEU HIS LEU THR PRO PHE THR ALA ARG          
SEQRES   6 B  144  GLY ARG PHE ALA THR VAL VAL GLU GLU LEU PHE ARG ASP          
SEQRES   7 B  144  GLY VAL ASN TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE          
SEQRES   8 B  144  GLY GLY VAL MET CYS VAL GLU SER VAL ASN ARG GLU MET          
SEQRES   9 B  144  SER PRO LEU VAL ASP ASN ILE ALA LEU TRP MET THR GLU          
SEQRES  10 B  144  TYR LEU ASN ARG HIS LEU HIS THR TRP ILE GLN ASP ASN          
SEQRES  11 B  144  GLY GLY TRP ASP ALA PHE VAL GLU LEU TYR GLY PRO SER          
SEQRES  12 B  144  MET                                                          
HET    DRO  A1166      42                                                       
HET    DRO  B1164      42                                                       
HETNAM     DRO 1-(2-{[(3S)-3-(AMINOMETHYL)-3,4-DIHYDROISOQUINOLIN-              
HETNAM   2 DRO  2(1H)-YL]CARBONYL}PHENYL)-4-CHLORO-5-METHYL-N,N-                
HETNAM   3 DRO  DIPHENYL-1H-PYRAZOLE-3-CARBOXAMIDE                              
FORMUL   3  DRO    2(C34 H30 CL N5 O2)                                          
FORMUL   5  HOH   *223(H2 O)                                                    
HELIX    1   1 ASP A   10  ARG A   26  1                                  17    
HELIX    2   2 SER A   49  TYR A   67  1                                  19    
HELIX    3   3 TYR A   67  SER A   76  1                                  10    
HELIX    4   4 THR A   84  PHE A   97  1                                  14    
HELIX    5   5 ASN A  102  ARG A  123  1                                  22    
HELIX    6   6 PRO A  127  LEU A  144  1                                  18    
HELIX    7   7 LEU A  144  ASN A  151  1                                   8    
HELIX    8   8 GLY A  153  TYR A  161  1                                   9    
HELIX    9   9 ASP B   10  GLN B   25  1                                  16    
HELIX   10  10 SER B   49  TYR B   67  1                                  19    
HELIX   11  11 TYR B   67  SER B   76  1                                  10    
HELIX   12  12 THR B   84  ARG B   98  1                                  15    
HELIX   13  13 ASN B  102  ARG B  123  1                                  22    
HELIX   14  14 PRO B  127  LEU B  144  1                                  18    
HELIX   15  15 LEU B  144  ASN B  151  1                                   8    
HELIX   16  16 GLY B  153  GLY B  162  1                                  10    
SITE     1 AC1  9 PHE A  63  TYR A  67  ASP A  70  MET A  74                    
SITE     2 AC1  9 VAL A  92  GLU A  95  LEU A  96  ALA A 108                    
SITE     3 AC1  9 PHE A 112                                                     
SITE     1 AC2 10 PHE B  63  TYR B  67  ASP B  70  PHE B  71                    
SITE     2 AC2 10 MET B  74  GLU B  95  LEU B  96  ALA B 108                    
SITE     3 AC2 10 PHE B 112  HOH B2102                                          
CRYST1   68.000   68.320   70.670  90.00  90.00  90.00 P 21 21 21    8          
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      0.014706  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014637  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014150        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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