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Database: PDB
Entry: 4HW2
LinkDB: 4HW2
Original site: 4HW2 
HEADER    APOPTOSIS/INHIBITOR                     07-NOV-12   4HW2              
TITLE     DISCOVERY OF POTENT MCL-1 INHIBITORS USING FRAGMENT-BASED METHODS AND 
TITLE    2 STRUCTURE-BASED DESIGN                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INDUCED MYELOID LEUKEMIA CELL DIFFERENTIATION PROTEIN MCL- 
COMPND   3 1;                                                                   
COMPND   4 CHAIN: A, B, C, D, E, F;                                             
COMPND   5 SYNONYM: BCL-2-LIKE PROTEIN 3, BCL2-L-3, BCL-2-RELATED PROTEIN       
COMPND   6 EAT/MCL1, MCL1/EAT;                                                  
COMPND   7 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: MCL1, BCL2L3;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS  (DE3)-RIL;                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDEST-HISMBP                              
KEYWDS    REGULATION OF APOPTOSIS, MAINTENANCE OF VIABILITY, APOPTOSIS,         
KEYWDS   2 APOPTOSIS-INHIBITOR COMPLEX                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.ZHAO                                                                
REVDAT   2   06-MAR-13 4HW2    1       JRNL                                     
REVDAT   1   09-JAN-13 4HW2    0                                                
JRNL        AUTH   A.FRIBERG,D.VIGIL,B.ZHAO,R.N.DANIELS,J.P.BURKE,              
JRNL        AUTH 2 P.M.GARCIA-BARRANTES,D.CAMPER,B.A.CHAUDER,T.LEE,             
JRNL        AUTH 3 E.T.OLEJNICZAK,S.W.FESIK                                     
JRNL        TITL   DISCOVERY OF POTENT MYELOID CELL LEUKEMIA 1 (MCL-1)          
JRNL        TITL 2 INHIBITORS USING FRAGMENT-BASED METHODS AND STRUCTURE-BASED  
JRNL        TITL 3 DESIGN.                                                      
JRNL        REF    J.MED.CHEM.                   V.  56    15 2013              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   23244564                                                     
JRNL        DOI    10.1021/JM301448P                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.3                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 25097                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2490                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.90                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3151                       
REMARK   3   BIN FREE R VALUE                    : 0.3633                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 234                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7186                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 190                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 4.10                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.23000                                             
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : 0.25000                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.35                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.45                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.40                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.54                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.024                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ANISOTROPIC                               
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4HW2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB075991.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUL-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07816                            
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25097                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.04700                            
REMARK 200  R SYM                      (I) : 0.05700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.29700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG3350, 0.2M MGCL2, PH 6.5, VAPOR   
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
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       60.99850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.16350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       60.99850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.16350            
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, 3, 4, 5, 6                                        
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: C                                     
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: 4                                                       
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: D                                     
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: 5                                                       
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: E                                     
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: 6                                                       
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: F                                     
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   200                                                      
REMARK 465     ARG A   201                                                      
REMARK 465     GLU A   322                                                      
REMARK 465     ASP A   323                                                      
REMARK 465     GLU B   322                                                      
REMARK 465     ASP B   323                                                      
REMARK 465     VAL C   321                                                      
REMARK 465     GLU C   322                                                      
REMARK 465     ASP C   323                                                      
REMARK 465     GLU D   322                                                      
REMARK 465     ASP D   323                                                      
REMARK 465     GLU E   322                                                      
REMARK 465     ASP E   323                                                      
REMARK 465     VAL F   321                                                      
REMARK 465     GLU F   322                                                      
REMARK 465     ASP F   323                                                      
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     LYS A 194    CG   CD   CE   NZ                                   
REMARK 470     LYS A 197    CG   CD   CE   NZ                                   
REMARK 470     MET A 199    CG   SD   CE                                        
REMARK 470     LYS C 194    CG   CD   CE   NZ                                   
REMARK 470     ASP C 195    CG   OD1  OD2                                       
REMARK 470     LYS C 197    CG   CD   CE   NZ                                   
REMARK 470     ARG C 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 236    CG   OD1  OD2                                       
REMARK 470     ARG D 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D 236    CG   OD1  OD2                                       
REMARK 470     ASP E 236    CG   OD1  OD2                                       
REMARK 470     LYS F 194    CG   CD   CE   NZ                                   
REMARK 470     LYS F 197    CG   CD   CE   NZ                                   
REMARK 470     ARG F 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLY E 200   N   -  CA  -  C   ANGL. DEV. =  20.7 DEGREES          
REMARK 500    ARG F 215   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG F 215   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.3 DEGREES          
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    ASP A 172     -128.21     55.68                                   
REMARK 500    THR A 191      155.10     92.85                                   
REMARK 500    ALA A 193      150.44     83.47                                   
REMARK 500    ASP B 172     -134.19     51.32                                   
REMARK 500    ALA B 193      174.97     77.47                                   
REMARK 500    ASP C 172     -123.99     55.67                                   
REMARK 500    THR C 191      169.88     69.64                                   
REMARK 500    LYS C 197       11.49    118.04                                   
REMARK 500    ARG C 201      -73.42    -50.13                                   
REMARK 500    ASP D 172     -109.62     34.15                                   
REMARK 500    THR D 191      -51.55     60.38                                   
REMARK 500    ALA D 193     -158.00    -51.87                                   
REMARK 500    MET D 199      -61.35     63.65                                   
REMARK 500    SER D 202       39.25     71.74                                   
REMARK 500    PHE D 318      -25.48   -172.40                                   
REMARK 500    ASP E 172     -118.19     54.38                                   
REMARK 500    THR E 191       -2.63     68.57                                   
REMARK 500    ASP F 172     -125.84     46.24                                   
REMARK 500    THR F 191      -98.72   -125.58                                   
REMARK 500    THR F 196      -72.10    -82.86                                   
REMARK 500    LYS F 197      151.64    -16.33                                   
REMARK 500    SER F 202       29.82    158.80                                   
REMARK 500    GLU F 240      -23.01    -23.97                                   
REMARK 500    VAL F 258     -102.37   -106.56                                   
REMARK 500    THR F 259      144.53    133.45                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG B 248         0.29    SIDE CHAIN                              
REMARK 500    ARG C 215         0.29    SIDE CHAIN                              
REMARK 500    ARG F 176         0.30    SIDE CHAIN                              
REMARK 500    ARG F 215         0.20    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19H A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19H B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19H C 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19H D 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19H E 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19H F 400                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4HW3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4HW4   RELATED DB: PDB                                   
DBREF  4HW2 A  172   323  UNP    Q07820   MCL1_HUMAN     172    323             
DBREF  4HW2 B  172   323  UNP    Q07820   MCL1_HUMAN     172    323             
DBREF  4HW2 C  172   323  UNP    Q07820   MCL1_HUMAN     172    323             
DBREF  4HW2 D  172   323  UNP    Q07820   MCL1_HUMAN     172    323             
DBREF  4HW2 E  172   323  UNP    Q07820   MCL1_HUMAN     172    323             
DBREF  4HW2 F  172   323  UNP    Q07820   MCL1_HUMAN     172    323             
SEQADV 4HW2 GLY A  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4HW2 GLY B  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4HW2 GLY C  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4HW2 GLY D  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4HW2 GLY E  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4HW2 GLY F  171  UNP  Q07820              EXPRESSION TAG                 
SEQRES   1 A  153  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 A  153  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 A  153  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 A  153  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 A  153  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 A  153  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 A  153  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 A  153  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 A  153  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 A  153  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 A  153  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 A  153  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP                      
SEQRES   1 B  153  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 B  153  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 B  153  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 B  153  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 B  153  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 B  153  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 B  153  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 B  153  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 B  153  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 B  153  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 B  153  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 B  153  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP                      
SEQRES   1 C  153  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 C  153  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 C  153  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 C  153  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 C  153  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 C  153  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 C  153  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 C  153  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 C  153  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 C  153  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 C  153  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 C  153  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP                      
SEQRES   1 D  153  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 D  153  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 D  153  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 D  153  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 D  153  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 D  153  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 D  153  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 D  153  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 D  153  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 D  153  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 D  153  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 D  153  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP                      
SEQRES   1 E  153  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 E  153  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 E  153  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 E  153  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 E  153  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 E  153  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 E  153  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 E  153  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 E  153  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 E  153  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 E  153  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 E  153  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP                      
SEQRES   1 F  153  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 F  153  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 F  153  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 F  153  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 F  153  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 F  153  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 F  153  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 F  153  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 F  153  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 F  153  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 F  153  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 F  153  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP                      
HET    19H  A 401      26                                                       
HET    PGE  A 402      10                                                       
HET    19H  B 401      26                                                       
HET    PGE  B 402      10                                                       
HET    PGE  B 403      10                                                       
HET    EDO  B 404       4                                                       
HET    19H  C 400      26                                                       
HET    19H  D 400      26                                                       
HET    19H  E 400      26                                                       
HET    19H  F 400      26                                                       
HETNAM     19H 6-CHLORO-3-[3-(4-CHLORO-3,5-DIMETHYLPHENOXY)PROPYL]-1H-          
HETNAM   2 19H  INDOLE-2-CARBOXYLIC ACID                                        
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   7  19H    6(C20 H19 CL2 N O3)                                          
FORMUL   8  PGE    3(C6 H14 O4)                                                 
FORMUL  12  EDO    C2 H6 O2                                                     
HELIX    1   1 ASP A  172  ALA A  190  1                                  19    
HELIX    2   2 ALA A  204  HIS A  224  1                                  21    
HELIX    3   3 HIS A  224  ASP A  236  1                                  13    
HELIX    4   4 ASN A  239  LYS A  244  1                                   6    
HELIX    5   5 LEU A  246  SER A  255  1                                  10    
HELIX    6   6 ASN A  260  ILE A  281  1                                  22    
HELIX    7   7 GLN A  283  SER A  285  5                                   3    
HELIX    8   8 CYS A  286  GLN A  309  1                                  24    
HELIX    9   9 GLY A  311  PHE A  319  1                                   9    
HELIX   10  10 ASP B  172  ALA B  190  1                                  19    
HELIX   11  11 SER B  202  HIS B  224  1                                  23    
HELIX   12  12 HIS B  224  ASP B  236  1                                  13    
HELIX   13  13 ASN B  239  SER B  245  1                                   7    
HELIX   14  14 LEU B  246  SER B  255  1                                  10    
HELIX   15  15 ASN B  260  ILE B  281  1                                  22    
HELIX   16  16 GLN B  283  SER B  285  5                                   3    
HELIX   17  17 CYS B  286  LYS B  302  1                                  17    
HELIX   18  18 LYS B  302  GLN B  309  1                                   8    
HELIX   19  19 ARG B  310  PHE B  319  1                                  10    
HELIX   20  20 ASP C  172  ALA C  190  1                                  19    
HELIX   21  21 SER C  202  HIS C  224  1                                  23    
HELIX   22  22 HIS C  224  ASP C  236  1                                  13    
HELIX   23  23 ASN C  239  LYS C  244  1                                   6    
HELIX   24  24 SER C  245  SER C  255  1                                  11    
HELIX   25  25 ASN C  260  ILE C  281  1                                  22    
HELIX   26  26 GLN C  283  SER C  285  5                                   3    
HELIX   27  27 CYS C  286  LYS C  302  1                                  17    
HELIX   28  28 LYS C  302  GLN C  309  1                                   8    
HELIX   29  29 ARG C  310  PHE C  319  1                                  10    
HELIX   30  30 ASP D  172  ALA D  190  1                                  19    
HELIX   31  31 SER D  202  HIS D  224  1                                  23    
HELIX   32  32 HIS D  224  ASP D  236  1                                  13    
HELIX   33  33 ASN D  239  SER D  245  1                                   7    
HELIX   34  34 LEU D  246  SER D  255  1                                  10    
HELIX   35  35 ASN D  260  ILE D  281  1                                  22    
HELIX   36  36 GLN D  283  SER D  285  5                                   3    
HELIX   37  37 CYS D  286  LYS D  302  1                                  17    
HELIX   38  38 LYS D  302  GLN D  309  1                                   8    
HELIX   39  39 ARG D  310  GLU D  317  1                                   8    
HELIX   40  40 ASP E  172  ALA E  190  1                                  19    
HELIX   41  41 ALA E  204  HIS E  224  1                                  21    
HELIX   42  42 HIS E  224  ASP E  236  1                                  13    
HELIX   43  43 ASN E  239  LYS E  244  1                                   6    
HELIX   44  44 LEU E  246  SER E  255  1                                  10    
HELIX   45  45 ASN E  260  ILE E  281  1                                  22    
HELIX   46  46 GLN E  283  SER E  285  5                                   3    
HELIX   47  47 CYS E  286  LYS E  302  1                                  17    
HELIX   48  48 LYS E  302  GLN E  309  1                                   8    
HELIX   49  49 ARG E  310  PHE E  319  1                                  10    
HELIX   50  50 ASP F  172  THR F  191  1                                  20    
HELIX   51  51 ALA F  204  HIS F  224  1                                  21    
HELIX   52  52 HIS F  224  ASP F  236  1                                  13    
HELIX   53  53 ASN F  239  SER F  245  1                                   7    
HELIX   54  54 LEU F  246  SER F  255  1                                  10    
HELIX   55  55 ASN F  260  ILE F  281  1                                  22    
HELIX   56  56 GLN F  283  SER F  285  5                                   3    
HELIX   57  57 CYS F  286  LYS F  302  1                                  17    
HELIX   58  58 LYS F  302  GLN F  309  1                                   8    
HELIX   59  59 ARG F  310  HIS F  320  1                                  11    
CISPEP   1 ALA B  193    LYS B  194          0       -20.90                     
CISPEP   2 ALA D  193    LYS D  194          0        24.72                     
SITE     1 AC1 11 ALA A 227  PHE A 228  VAL A 249  MET A 250                    
SITE     2 AC1 11 VAL A 253  PHE A 254  ARG A 263  LEU A 267                    
SITE     3 AC1 11 PHE A 270  GLY A 271  ILE A 294                               
SITE     1 AC2  1 HIS A 224                                                     
SITE     1 AC3  8 ALA B 227  PHE B 228  MET B 250  VAL B 253                    
SITE     2 AC3  8 PHE B 254  ARG B 263  LEU B 267  PHE B 270                    
SITE     1 AC4  2 HIS B 224  THR B 266                                          
SITE     1 AC5  4 ASN B 223  HIS B 224  GLY B 262  PHE B 318                    
SITE     1 AC6  4 ASN B 223  HIS B 224  THR B 226  ALA B 227                    
SITE     1 AC7  9 ALA C 227  PHE C 228  MET C 231  VAL C 253                    
SITE     2 AC7  9 PHE C 254  ARG C 263  LEU C 267  PHE C 270                    
SITE     3 AC7  9 GLY C 271                                                     
SITE     1 AC8  9 PHE D 228  MET D 231  LEU D 246  VAL D 253                    
SITE     2 AC8  9 PHE D 254  ARG D 263  LEU D 267  PHE D 270                    
SITE     3 AC8  9 GLY D 271                                                     
SITE     1 AC9  9 ALA E 227  MET E 231  LEU E 246  MET E 250                    
SITE     2 AC9  9 VAL E 253  PHE E 254  ARG E 263  LEU E 267                    
SITE     3 AC9  9 PHE E 270                                                     
SITE     1 BC1 11 LYS E 194  ARG E 207  ALA F 227  PHE F 228                    
SITE     2 BC1 11 MET F 231  MET F 250  VAL F 253  PHE F 254                    
SITE     3 BC1 11 ARG F 263  LEU F 267  PHE F 270                               
CRYST1  121.997  134.327   62.043  90.00  90.00  90.00 P 21 21 2    24          
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      0.008197  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007445  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016118        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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