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Database: PDB
Entry: 4OQ5
LinkDB: 4OQ5
Original site: 4OQ5 
HEADER    APOPTOSIS/INHIBITOR                     07-FEB-14   4OQ5              
TITLE     CRYSTAL STRUCTURE OF HUMAN MCL-1 BOUND TO INHIBITOR 4-(4-             
TITLE    2 METHYLNAPHTHALEN-1-YL)-2-{[(4-PHENOXYPHENYL)SULFONYL]AMINO}BENZOIC   
TITLE    3 ACID                                                                 
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 FRAGMENT: UNP RESIDUES 174-326;                                      
COMPND   6 SYNONYM: BCL-2-LIKE PROTEIN 3, BCL2-L-3, BCL-2-RELATED PROTEIN       
COMPND   7 EAT/MCL1, MCL1/EAT;                                                  
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: MCL1, BCL2L3;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    APOPTOSIS-INHIBITOR COMPLEX                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.M.PETROS,S.L.SWANN,D.SONG,K.SWINGER,C.PARK,H.ZHANG,M.D.WENDT,       
AUTHOR   2 A.R.KUNZER,A.J.SOUERS,C.SUN                                          
REVDAT   1   12-MAR-14 4OQ5    0                                                
JRNL        AUTH   A.M.PETROS,S.L.SWANN,D.SONG,K.SWINGER,C.PARK,H.ZHANG,        
JRNL        AUTH 2 M.D.WENDT,A.R.KUNZER,A.J.SOUERS,C.SUN                        
JRNL        TITL   FRAGMENT-BASED DISCOVERY OF POTENT INHIBITORS OF THE         
JRNL        TITL 2 ANTI-APOPTOTIC MCL-1 PROTEIN.                                
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  24  1484 2014              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   24582986                                                     
JRNL        DOI    10.1016/J.BMCL.2014.02.010                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.86 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.4                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.86                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.15                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 26737                          
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)  : 0.200                          
REMARK   3   R VALUE            (WORKING SET)  : 0.198                          
REMARK   3   FREE R VALUE                      : 0.239                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.010                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1340                           
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               : 13                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.86                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.98                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 98.21                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2601                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2187                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2478                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2170                   
REMARK   3   BIN FREE R VALUE                        : 0.2536                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.73                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 123                      
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            : 7240                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 222                                     
REMARK   3   SOLVENT ATOMS            : 154                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 73.89                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 60.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.63980                                             
REMARK   3    B22 (A**2) : 2.98960                                              
REMARK   3    B33 (A**2) : 2.65010                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.31050                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.348               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.354               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 7728   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 10480  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2768   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 180    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1264   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 7728   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 946    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 9646   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.17                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.27                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.12                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4OQ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-FEB-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB084810.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
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                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26737                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.855                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : 2.85                     
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: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M MES, 30%   
REMARK 280  W/V PEG5000 MME, PH 6.5, VAPOR DIFFUSION, SITTING DROP,             
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       54.87500            
REMARK 290   SMTRY3   2  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 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 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 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 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 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 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   164                                                      
REMARK 465     THR A   165                                                      
REMARK 465     LEU A   166                                                      
REMARK 465     VAL A   167                                                      
REMARK 465     PRO A   168                                                      
REMARK 465     ARG A   169                                                      
REMARK 465     GLY A   170                                                      
REMARK 465     SER A   171                                                      
REMARK 465     ILE A   264                                                      
REMARK 465     ASP A   323                                                      
REMARK 465     LEU A   324                                                      
REMARK 465     GLU A   325                                                      
REMARK 465     GLY A   326                                                      
REMARK 465     GLY B   164                                                      
REMARK 465     THR B   165                                                      
REMARK 465     LEU B   166                                                      
REMARK 465     VAL B   167                                                      
REMARK 465     PRO B   168                                                      
REMARK 465     ARG B   169                                                      
REMARK 465     GLY B   170                                                      
REMARK 465     SER B   171                                                      
REMARK 465     ASP B   323                                                      
REMARK 465     LEU B   324                                                      
REMARK 465     GLU B   325                                                      
REMARK 465     GLY B   326                                                      
REMARK 465     GLY C   164                                                      
REMARK 465     THR C   165                                                      
REMARK 465     LEU C   166                                                      
REMARK 465     VAL C   167                                                      
REMARK 465     PRO C   168                                                      
REMARK 465     ARG C   169                                                      
REMARK 465     GLY C   170                                                      
REMARK 465     SER C   171                                                      
REMARK 465     VAL C   321                                                      
REMARK 465     GLU C   322                                                      
REMARK 465     ASP C   323                                                      
REMARK 465     LEU C   324                                                      
REMARK 465     GLU C   325                                                      
REMARK 465     GLY C   326                                                      
REMARK 465     GLY D   164                                                      
REMARK 465     THR D   165                                                      
REMARK 465     LEU D   166                                                      
REMARK 465     VAL D   167                                                      
REMARK 465     PRO D   168                                                      
REMARK 465     ARG D   169                                                      
REMARK 465     GLY D   170                                                      
REMARK 465     SER D   171                                                      
REMARK 465     VAL D   321                                                      
REMARK 465     GLU D   322                                                      
REMARK 465     ASP D   323                                                      
REMARK 465     LEU D   324                                                      
REMARK 465     GLU D   325                                                      
REMARK 465     GLY D   326                                                      
REMARK 465     GLY E   164                                                      
REMARK 465     THR E   165                                                      
REMARK 465     LEU E   166                                                      
REMARK 465     VAL E   167                                                      
REMARK 465     PRO E   168                                                      
REMARK 465     ARG E   169                                                      
REMARK 465     GLY E   170                                                      
REMARK 465     SER E   171                                                      
REMARK 465     ASP E   323                                                      
REMARK 465     LEU E   324                                                      
REMARK 465     GLU E   325                                                      
REMARK 465     GLY E   326                                                      
REMARK 465     GLY F   164                                                      
REMARK 465     THR F   165                                                      
REMARK 465     LEU F   166                                                      
REMARK 465     VAL F   167                                                      
REMARK 465     PRO F   168                                                      
REMARK 465     ARG F   169                                                      
REMARK 465     GLY F   170                                                      
REMARK 465     SER F   171                                                      
REMARK 465     VAL F   321                                                      
REMARK 465     GLU F   322                                                      
REMARK 465     ASP F   323                                                      
REMARK 465     LEU F   324                                                      
REMARK 465     GLU F   325                                                      
REMARK 465     GLY F   326                                                      
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    LYS A 197      -92.34   -145.15                                   
REMARK 500    ARG A 201       86.85     55.39                                   
REMARK 500    SER A 255     -124.23    -83.91                                   
REMARK 500    ASP A 256      -57.40     59.47                                   
REMARK 500    VAL A 321     -105.76   -106.46                                   
REMARK 500    LYS B 197      -92.23   -144.98                                   
REMARK 500    ARG B 201       86.75     55.31                                   
REMARK 500    SER B 255     -125.33    -84.99                                   
REMARK 500    ASP B 256      -62.40     60.53                                   
REMARK 500    VAL B 321      -93.49   -121.20                                   
REMARK 500    LYS C 197      -92.75   -145.23                                   
REMARK 500    SER C 202       70.04     53.40                                   
REMARK 500    ASP C 256      107.47     71.73                                   
REMARK 500    LYS D 197      -92.95   -145.38                                   
REMARK 500    ARG D 201     -132.59     77.97                                   
REMARK 500    SER D 255     -127.23    -84.95                                   
REMARK 500    ASP D 256      -60.29     58.56                                   
REMARK 500    LYS E 197      -93.68   -145.83                                   
REMARK 500    ARG E 201       85.05     55.42                                   
REMARK 500    SER E 202       70.10     53.96                                   
REMARK 500    SER E 255     -123.18    -84.89                                   
REMARK 500    ASP E 256       96.24     29.19                                   
REMARK 500    PHE E 319       62.00   -105.71                                   
REMARK 500    VAL E 321     -124.44    -95.83                                   
REMARK 500    LYS F 197      -92.59   -145.36                                   
REMARK 500    ARG F 201       85.93     54.81                                   
REMARK 500    SER F 202       70.35     53.25                                   
REMARK 500    SER F 255     -124.91    -84.70                                   
REMARK 500    ASP F 256       97.67     24.80                                   
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 526        DISTANCE =  7.18 ANGSTROMS                       
REMARK 525    HOH A 527        DISTANCE =  8.02 ANGSTROMS                       
REMARK 525    HOH B 507        DISTANCE = 10.50 ANGSTROMS                       
REMARK 525    HOH C 510        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH C 518        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH D 503        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH D 515        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH D 516        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH D 517        DISTANCE =  6.85 ANGSTROMS                       
REMARK 525    HOH D 519        DISTANCE =  8.78 ANGSTROMS                       
REMARK 525    HOH E 511        DISTANCE = 12.71 ANGSTROMS                       
REMARK 525    HOH E 513        DISTANCE = 12.62 ANGSTROMS                       
REMARK 525    HOH E 519        DISTANCE =  9.93 ANGSTROMS                       
REMARK 525    HOH E 520        DISTANCE = 21.61 ANGSTROMS                       
REMARK 525    HOH E 522        DISTANCE = 14.02 ANGSTROMS                       
REMARK 525    HOH E 524        DISTANCE =  8.26 ANGSTROMS                       
REMARK 525    HOH F 508        DISTANCE = 16.17 ANGSTROMS                       
REMARK 525    HOH F 517        DISTANCE =  8.07 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2UU A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2UU B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2UU C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2UU D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2UU E 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2UU F 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4OQ6   RELATED DB: PDB                                   
REMARK 900 HUMAN MCL-1 BOUND TO INHIBITOR 36                                    
DBREF  4OQ5 A  174   326  UNP    Q07820   MCL1_HUMAN     174    326             
DBREF  4OQ5 B  174   326  UNP    Q07820   MCL1_HUMAN     174    326             
DBREF  4OQ5 C  174   326  UNP    Q07820   MCL1_HUMAN     174    326             
DBREF  4OQ5 D  174   326  UNP    Q07820   MCL1_HUMAN     174    326             
DBREF  4OQ5 E  174   326  UNP    Q07820   MCL1_HUMAN     174    326             
DBREF  4OQ5 F  174   326  UNP    Q07820   MCL1_HUMAN     174    326             
SEQADV 4OQ5 GLY A  164  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 THR A  165  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 LEU A  166  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 VAL A  167  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 PRO A  168  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 ARG A  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 GLY A  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 SER A  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 MET A  172  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 ASP A  173  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 GLY B  164  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 THR B  165  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 LEU B  166  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 VAL B  167  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 PRO B  168  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 ARG B  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 GLY B  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 SER B  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 MET B  172  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 ASP B  173  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 GLY C  164  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 THR C  165  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 LEU C  166  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 VAL C  167  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 PRO C  168  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 ARG C  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 GLY C  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 SER C  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 MET C  172  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 ASP C  173  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 GLY D  164  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 THR D  165  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 LEU D  166  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 VAL D  167  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 PRO D  168  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 ARG D  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 GLY D  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 SER D  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 MET D  172  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 ASP D  173  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 GLY E  164  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 THR E  165  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 LEU E  166  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 VAL E  167  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 PRO E  168  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 ARG E  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 GLY E  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 SER E  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 MET E  172  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 ASP E  173  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 GLY F  164  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 THR F  165  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 LEU F  166  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 VAL F  167  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 PRO F  168  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 ARG F  169  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 GLY F  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 SER F  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 MET F  172  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4OQ5 ASP F  173  UNP  Q07820              EXPRESSION TAG                 
SEQRES   1 A  163  GLY THR LEU VAL PRO ARG GLY SER MET ASP LEU TYR ARG          
SEQRES   2 A  163  GLN SER LEU GLU ILE ILE SER ARG TYR LEU ARG GLU GLN          
SEQRES   3 A  163  ALA THR GLY ALA LYS ASP THR LYS PRO MET GLY ARG SER          
SEQRES   4 A  163  GLY ALA THR SER ARG LYS ALA LEU GLU THR LEU ARG ARG          
SEQRES   5 A  163  VAL GLY ASP GLY VAL GLN ARG ASN HIS GLU THR ALA PHE          
SEQRES   6 A  163  GLN GLY MET LEU ARG LYS LEU ASP ILE LYS ASN GLU ASP          
SEQRES   7 A  163  ASP VAL LYS SER LEU SER ARG VAL MET ILE HIS VAL PHE          
SEQRES   8 A  163  SER ASP GLY VAL THR ASN TRP GLY ARG ILE VAL THR LEU          
SEQRES   9 A  163  ILE SER PHE GLY ALA PHE VAL ALA LYS HIS LEU LYS THR          
SEQRES  10 A  163  ILE ASN GLN GLU SER CYS ILE GLU PRO LEU ALA GLU SER          
SEQRES  11 A  163  ILE THR ASP VAL LEU VAL ARG THR LYS ARG ASP TRP LEU          
SEQRES  12 A  163  VAL LYS GLN ARG GLY TRP ASP GLY PHE VAL GLU PHE PHE          
SEQRES  13 A  163  HIS VAL GLU ASP LEU GLU GLY                                  
SEQRES   1 B  163  GLY THR LEU VAL PRO ARG GLY SER MET ASP LEU TYR ARG          
SEQRES   2 B  163  GLN SER LEU GLU ILE ILE SER ARG TYR LEU ARG GLU GLN          
SEQRES   3 B  163  ALA THR GLY ALA LYS ASP THR LYS PRO MET GLY ARG SER          
SEQRES   4 B  163  GLY ALA THR SER ARG LYS ALA LEU GLU THR LEU ARG ARG          
SEQRES   5 B  163  VAL GLY ASP GLY VAL GLN ARG ASN HIS GLU THR ALA PHE          
SEQRES   6 B  163  GLN GLY MET LEU ARG LYS LEU ASP ILE LYS ASN GLU ASP          
SEQRES   7 B  163  ASP VAL LYS SER LEU SER ARG VAL MET ILE HIS VAL PHE          
SEQRES   8 B  163  SER ASP GLY VAL THR ASN TRP GLY ARG ILE VAL THR LEU          
SEQRES   9 B  163  ILE SER PHE GLY ALA PHE VAL ALA LYS HIS LEU LYS THR          
SEQRES  10 B  163  ILE ASN GLN GLU SER CYS ILE GLU PRO LEU ALA GLU SER          
SEQRES  11 B  163  ILE THR ASP VAL LEU VAL ARG THR LYS ARG ASP TRP LEU          
SEQRES  12 B  163  VAL LYS GLN ARG GLY TRP ASP GLY PHE VAL GLU PHE PHE          
SEQRES  13 B  163  HIS VAL GLU ASP LEU GLU GLY                                  
SEQRES   1 C  163  GLY THR LEU VAL PRO ARG GLY SER MET ASP LEU TYR ARG          
SEQRES   2 C  163  GLN SER LEU GLU ILE ILE SER ARG TYR LEU ARG GLU GLN          
SEQRES   3 C  163  ALA THR GLY ALA LYS ASP THR LYS PRO MET GLY ARG SER          
SEQRES   4 C  163  GLY ALA THR SER ARG LYS ALA LEU GLU THR LEU ARG ARG          
SEQRES   5 C  163  VAL GLY ASP GLY VAL GLN ARG ASN HIS GLU THR ALA PHE          
SEQRES   6 C  163  GLN GLY MET LEU ARG LYS LEU ASP ILE LYS ASN GLU ASP          
SEQRES   7 C  163  ASP VAL LYS SER LEU SER ARG VAL MET ILE HIS VAL PHE          
SEQRES   8 C  163  SER ASP GLY VAL THR ASN TRP GLY ARG ILE VAL THR LEU          
SEQRES   9 C  163  ILE SER PHE GLY ALA PHE VAL ALA LYS HIS LEU LYS THR          
SEQRES  10 C  163  ILE ASN GLN GLU SER CYS ILE GLU PRO LEU ALA GLU SER          
SEQRES  11 C  163  ILE THR ASP VAL LEU VAL ARG THR LYS ARG ASP TRP LEU          
SEQRES  12 C  163  VAL LYS GLN ARG GLY TRP ASP GLY PHE VAL GLU PHE PHE          
SEQRES  13 C  163  HIS VAL GLU ASP LEU GLU GLY                                  
SEQRES   1 D  163  GLY THR LEU VAL PRO ARG GLY SER MET ASP LEU TYR ARG          
SEQRES   2 D  163  GLN SER LEU GLU ILE ILE SER ARG TYR LEU ARG GLU GLN          
SEQRES   3 D  163  ALA THR GLY ALA LYS ASP THR LYS PRO MET GLY ARG SER          
SEQRES   4 D  163  GLY ALA THR SER ARG LYS ALA LEU GLU THR LEU ARG ARG          
SEQRES   5 D  163  VAL GLY ASP GLY VAL GLN ARG ASN HIS GLU THR ALA PHE          
SEQRES   6 D  163  GLN GLY MET LEU ARG LYS LEU ASP ILE LYS ASN GLU ASP          
SEQRES   7 D  163  ASP VAL LYS SER LEU SER ARG VAL MET ILE HIS VAL PHE          
SEQRES   8 D  163  SER ASP GLY VAL THR ASN TRP GLY ARG ILE VAL THR LEU          
SEQRES   9 D  163  ILE SER PHE GLY ALA PHE VAL ALA LYS HIS LEU LYS THR          
SEQRES  10 D  163  ILE ASN GLN GLU SER CYS ILE GLU PRO LEU ALA GLU SER          
SEQRES  11 D  163  ILE THR ASP VAL LEU VAL ARG THR LYS ARG ASP TRP LEU          
SEQRES  12 D  163  VAL LYS GLN ARG GLY TRP ASP GLY PHE VAL GLU PHE PHE          
SEQRES  13 D  163  HIS VAL GLU ASP LEU GLU GLY                                  
SEQRES   1 E  163  GLY THR LEU VAL PRO ARG GLY SER MET ASP LEU TYR ARG          
SEQRES   2 E  163  GLN SER LEU GLU ILE ILE SER ARG TYR LEU ARG GLU GLN          
SEQRES   3 E  163  ALA THR GLY ALA LYS ASP THR LYS PRO MET GLY ARG SER          
SEQRES   4 E  163  GLY ALA THR SER ARG LYS ALA LEU GLU THR LEU ARG ARG          
SEQRES   5 E  163  VAL GLY ASP GLY VAL GLN ARG ASN HIS GLU THR ALA PHE          
SEQRES   6 E  163  GLN GLY MET LEU ARG LYS LEU ASP ILE LYS ASN GLU ASP          
SEQRES   7 E  163  ASP VAL LYS SER LEU SER ARG VAL MET ILE HIS VAL PHE          
SEQRES   8 E  163  SER ASP GLY VAL THR ASN TRP GLY ARG ILE VAL THR LEU          
SEQRES   9 E  163  ILE SER PHE GLY ALA PHE VAL ALA LYS HIS LEU LYS THR          
SEQRES  10 E  163  ILE ASN GLN GLU SER CYS ILE GLU PRO LEU ALA GLU SER          
SEQRES  11 E  163  ILE THR ASP VAL LEU VAL ARG THR LYS ARG ASP TRP LEU          
SEQRES  12 E  163  VAL LYS GLN ARG GLY TRP ASP GLY PHE VAL GLU PHE PHE          
SEQRES  13 E  163  HIS VAL GLU ASP LEU GLU GLY                                  
SEQRES   1 F  163  GLY THR LEU VAL PRO ARG GLY SER MET ASP LEU TYR ARG          
SEQRES   2 F  163  GLN SER LEU GLU ILE ILE SER ARG TYR LEU ARG GLU GLN          
SEQRES   3 F  163  ALA THR GLY ALA LYS ASP THR LYS PRO MET GLY ARG SER          
SEQRES   4 F  163  GLY ALA THR SER ARG LYS ALA LEU GLU THR LEU ARG ARG          
SEQRES   5 F  163  VAL GLY ASP GLY VAL GLN ARG ASN HIS GLU THR ALA PHE          
SEQRES   6 F  163  GLN GLY MET LEU ARG LYS LEU ASP ILE LYS ASN GLU ASP          
SEQRES   7 F  163  ASP VAL LYS SER LEU SER ARG VAL MET ILE HIS VAL PHE          
SEQRES   8 F  163  SER ASP GLY VAL THR ASN TRP GLY ARG ILE VAL THR LEU          
SEQRES   9 F  163  ILE SER PHE GLY ALA PHE VAL ALA LYS HIS LEU LYS THR          
SEQRES  10 F  163  ILE ASN GLN GLU SER CYS ILE GLU PRO LEU ALA GLU SER          
SEQRES  11 F  163  ILE THR ASP VAL LEU VAL ARG THR LYS ARG ASP TRP LEU          
SEQRES  12 F  163  VAL LYS GLN ARG GLY TRP ASP GLY PHE VAL GLU PHE PHE          
SEQRES  13 F  163  HIS VAL GLU ASP LEU GLU GLY                                  
HET    2UU  A 401      57                                                       
HET    2UU  B 401      57                                                       
HET    2UU  C 401      57                                                       
HET    2UU  D 401      57                                                       
HET    2UU  E 401      57                                                       
HET    2UU  F 401      57                                                       
HETNAM     2UU 4-(4-METHYLNAPHTHALEN-1-YL)-2-{[(4-PHENOXYPHENYL)                
HETNAM   2 2UU  SULFONYL]AMINO}BENZOIC ACID                                     
FORMUL   7  2UU    6(C30 H23 N O5 S)                                            
FORMUL  13  HOH   *154(H2 O)                                                    
HELIX    1   1 MET A  172  GLY A  192  1                                  21    
HELIX    2   2 SER A  202  HIS A  224  1                                  23    
HELIX    3   3 HIS A  224  ASP A  236  1                                  13    
HELIX    4   4 ASN A  239  SER A  255  1                                  17    
HELIX    5   5 GLY A  262  ARG A  263  5                                   2    
HELIX    6   6 VAL A  265  VAL A  265  5                                   1    
HELIX    7   7 THR A  266  ILE A  281  1                                  16    
HELIX    8   8 GLN A  283  SER A  285  5                                   3    
HELIX    9   9 CYS A  286  GLN A  309  1                                  24    
HELIX   10  10 ARG A  310  HIS A  320  1                                  11    
HELIX   11  11 ASP B  173  GLY B  192  1                                  20    
HELIX   12  12 SER B  202  HIS B  224  1                                  23    
HELIX   13  13 HIS B  224  ASP B  236  1                                  13    
HELIX   14  14 ASN B  239  SER B  245  1                                   7    
HELIX   15  15 SER B  245  SER B  255  1                                  11    
HELIX   16  16 ASN B  260  ILE B  281  1                                  22    
HELIX   17  17 GLN B  283  SER B  285  5                                   3    
HELIX   18  18 CYS B  286  GLN B  309  1                                  24    
HELIX   19  19 ARG B  310  HIS B  320  1                                  11    
HELIX   20  20 ASP C  173  GLY C  192  1                                  20    
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  SER C  255  1                                  17    
HELIX   24  24 ASN C  260  ILE C  281  1                                  22    
HELIX   25  25 GLN C  283  SER C  285  5                                   3    
HELIX   26  26 CYS C  286  GLN C  309  1                                  24    
HELIX   27  27 ARG C  310  HIS C  320  1                                  11    
HELIX   28  28 ASP D  173  GLY D  192  1                                  20    
HELIX   29  29 SER D  202  HIS D  224  1                                  23    
HELIX   30  30 HIS D  224  ASP D  236  1                                  13    
HELIX   31  31 ASN D  239  SER D  255  1                                  17    
HELIX   32  32 ASN D  260  ILE D  281  1                                  22    
HELIX   33  33 GLN D  283  SER D  285  5                                   3    
HELIX   34  34 CYS D  286  GLN D  309  1                                  24    
HELIX   35  35 ARG D  310  PHE D  319  1                                  10    
HELIX   36  36 ASP E  173  GLY E  192  1                                  20    
HELIX   37  37 SER E  202  HIS E  224  1                                  23    
HELIX   38  38 HIS E  224  ASP E  236  1                                  13    
HELIX   39  39 ASN E  239  SER E  255  1                                  17    
HELIX   40  40 ASN E  260  ILE E  281  1                                  22    
HELIX   41  41 GLN E  283  SER E  285  5                                   3    
HELIX   42  42 CYS E  286  GLN E  309  1                                  24    
HELIX   43  43 ARG E  310  PHE E  319  1                                  10    
HELIX   44  44 ASP F  173  GLY F  192  1                                  20    
HELIX   45  45 SER F  202  HIS F  224  1                                  23    
HELIX   46  46 HIS F  224  ASP F  236  1                                  13    
HELIX   47  47 ASN F  239  SER F  255  1                                  17    
HELIX   48  48 ASN F  260  ILE F  281  1                                  22    
HELIX   49  49 GLN F  283  SER F  285  5                                   3    
HELIX   50  50 CYS F  286  GLN F  309  1                                  24    
HELIX   51  51 ARG F  310  PHE F  319  1                                  10    
SITE     1 AC1 14 PHE A 228  MET A 231  LEU A 235  MET A 250                    
SITE     2 AC1 14 VAL A 253  ARG A 263  THR A 266  LEU A 267                    
SITE     3 AC1 14 PHE A 270  ALA F 227  GLY F 230  MET F 231                    
SITE     4 AC1 14 LYS F 234  2UU F 401                                          
SITE     1 AC2 13 PHE B 228  MET B 231  LEU B 235  ARG B 263                    
SITE     2 AC2 13 THR B 266  LEU B 267  PHE B 270  GLY B 271                    
SITE     3 AC2 13 ALA E 227  GLY E 230  LYS E 234  2UU E 401                    
SITE     4 AC2 13 HOH E 527                                                     
SITE     1 AC3 15 PHE C 228  MET C 231  LEU C 235  VAL C 253                    
SITE     2 AC3 15 PHE C 254  ARG C 263  THR C 266  LEU C 267                    
SITE     3 AC3 15 PHE C 270  LEU C 290  THR D 226  ALA D 227                    
SITE     4 AC3 15 GLY D 230  MET D 231  LYS D 234                               
SITE     1 AC4 14 THR C 226  ALA C 227  LYS C 234  PHE D 228                    
SITE     2 AC4 14 MET D 231  LEU D 235  MET D 250  VAL D 253                    
SITE     3 AC4 14 PHE D 254  ARG D 263  THR D 266  LEU D 267                    
SITE     4 AC4 14 PHE D 270  LEU D 290                                          
SITE     1 AC5 16 THR B 226  ALA B 227  MET B 231  2UU B 401                    
SITE     2 AC5 16 PHE E 228  MET E 231  LYS E 234  LEU E 235                    
SITE     3 AC5 16 MET E 250  VAL E 253  PHE E 254  ARG E 263                    
SITE     4 AC5 16 THR E 266  LEU E 267  PHE E 270  LEU E 290                    
SITE     1 AC6 14 THR A 226  ALA A 227  MET A 231  2UU A 401                    
SITE     2 AC6 14 HOH A 517  MET F 231  LEU F 235  MET F 250                    
SITE     3 AC6 14 VAL F 253  PHE F 254  ARG F 263  THR F 266                    
SITE     4 AC6 14 LEU F 267  PHE F 270                                          
CRYST1   71.112  109.750   76.544  90.00  93.31  90.00 P 1 21 1     12          
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      0.014062  0.000000  0.000813        0.00000                         
SCALE2      0.000000  0.009112  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013086        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system