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Database: PDB
Entry: 5VKC
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HEADER    SIGNALING PROTEIN/INHIBITOR             21-APR-17   5VKC              
TITLE     CRYSTAL STRUCTURE OF MCL-1 IN COMPLEX WITH A BIM COMPETITIVE INHIBITOR
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INDUCED MYELOID LEUKEMIA CELL DIFFERENTIATION PROTEIN MCL- 
COMPND   3 1;                                                                   
COMPND   4 CHAIN: A, B;                                                         
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                                         
KEYWDS    MCL-1, SIGNALING PROTEIN-INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.A.JUDGE,A.J.SOUERS                                                  
REVDAT   2   23-AUG-17 5VKC    1       REMARK                                   
REVDAT   1   03-MAY-17 5VKC    0                                                
JRNL        AUTH   M.BRUNCKO,L.WANG,G.S.SHEPPARD,D.C.PHILLIPS,S.K.TAHIR,J.XUE,  
JRNL        AUTH 2 S.ERICKSON,S.FIDANZE,E.FRY,L.HASVOLD,G.J.JENKINS,S.JIN,      
JRNL        AUTH 3 R.A.JUDGE,P.J.KOVAR,D.MADAR,P.NIMMER,C.PARK,A.M.PETROS,      
JRNL        AUTH 4 S.H.ROSENBERG,M.L.SMITH,X.SONG,C.SUN,Z.F.TAO,X.WANG,Y.XIAO,  
JRNL        AUTH 5 H.ZHANG,C.TSE,J.D.LEVERSON,S.W.ELMORE,A.J.SOUERS             
JRNL        TITL   STRUCTURE-GUIDED DESIGN OF A SERIES OF MCL-1 INHIBITORS WITH 
JRNL        TITL 2 HIGH AFFINITY AND SELECTIVITY.                               
JRNL        REF    J. MED. CHEM.                 V.  58  2180 2015              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   25679114                                                     
JRNL        DOI    10.1021/JM501258M                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.31 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.7                                        
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) : 2.31                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.81                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 18180                          
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)  : 0.202                          
REMARK   3   R VALUE            (WORKING SET)  : 0.201                          
REMARK   3   FREE R VALUE                      : 0.222                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.130                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 933                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 9                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.31                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.45                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 97.34                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2891                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2160                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2750                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2150                   
REMARK   3   BIN FREE R VALUE                        : 0.2370                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.88                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 141                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2324                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 124                                     
REMARK   3   SOLVENT ATOMS            : 124                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 46.53                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.95                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.57550                                             
REMARK   3    B22 (A**2) : -3.57550                                             
REMARK   3    B33 (A**2) : 7.15090                                              
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) : 0.300               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.255               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.188               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.267               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.193               
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      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2526   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3426   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 898    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 58     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 418    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2526   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 5      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 304    ; 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   : 2908   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.08                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.34                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 20.45                    
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 5VKC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-APR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227559.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JUN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.8                                
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-G                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97856                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18293                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 500.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.11800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 7%(W/V) PEG 8000, 0.1M TRIS-HCL, PH      
REMARK 280  8.8, 0.2M ZINC ACETATE, VAPOR DIFFUSION, TEMPERATURE 277K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.93333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       30.46667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1440 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -229.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   170                                                      
REMARK 465     SER A   171                                                      
REMARK 465     ASP A   195                                                      
REMARK 465     THR A   196                                                      
REMARK 465     LYS A   197                                                      
REMARK 465     PRO A   198                                                      
REMARK 465     MET A   199                                                      
REMARK 465     GLY A   200                                                      
REMARK 465     ARG A   201                                                      
REMARK 465     ASP A   323                                                      
REMARK 465     LEU A   324                                                      
REMARK 465     GLU A   325                                                      
REMARK 465     GLY A   326                                                      
REMARK 465     GLY B   170                                                      
REMARK 465     SER B   171                                                      
REMARK 465     ASP B   195                                                      
REMARK 465     THR B   196                                                      
REMARK 465     LYS B   197                                                      
REMARK 465     PRO B   198                                                      
REMARK 465     MET B   199                                                      
REMARK 465     GLY B   200                                                      
REMARK 465     ARG B   201                                                      
REMARK 465     ASP B   323                                                      
REMARK 465     LEU B   324                                                      
REMARK 465     GLU B   325                                                      
REMARK 465     GLY B   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    ASP A 173      -75.85     62.37                                   
REMARK 500    ASP A 236       79.07     40.10                                   
REMARK 500    ASP B 173      -75.66     59.66                                   
REMARK 500    ASP B 236       78.93     40.14                                   
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 556        DISTANCE = 11.98 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 224   NE2                                                    
REMARK 620 2 GLU A 288   OE1  65.7                                              
REMARK 620 3 GLU A 288   OE2  66.9   4.2                                        
REMARK 620 4 HOH A 506   O    99.1 105.9 101.7                                  
REMARK 620 5 HOH A 529   O   109.7  50.5  51.9 122.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 407  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 241   OD2                                                    
REMARK 620 2 ASP B 242   OD1  39.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 406  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 242   OD1                                                    
REMARK 620 2 ASP B 241   OD2  65.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 405  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 252   ND1                                                    
REMARK 620 2 HOH A 515   O   102.3                                              
REMARK 620 3 GLU B 292   OE2  27.3  82.7                                        
REMARK 620 4 ASP B 296   OD2  29.3  81.2   2.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 404  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 252   NE2                                                    
REMARK 620 2 ASP A 256   OD2 117.0                                              
REMARK 620 3 HOH A 537   O   110.7 105.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 408  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 320   NE2                                                    
REMARK 620 2 HOH A 540   O   102.3                                              
REMARK 620 3 9EA B 401   N47 103.5 106.0                                        
REMARK 620 4 HOH B 541   O   106.4 136.9  97.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 224   NE2                                                    
REMARK 620 2 HOH B 518   O    99.3                                              
REMARK 620 3 GLU B 288   OE1  67.1 106.8                                        
REMARK 620 4 GLU B 288   OE2  68.1 102.7   4.2                                  
REMARK 620 5 HOH B 543   O   109.8 123.3  49.7  51.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 403  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 252   ND1                                                    
REMARK 620 2 HOH B 532   O   100.6                                              
REMARK 620 3 GLU A 292   OE2  77.6  67.8                                        
REMARK 620 4 ASP A 296   OD2  82.5  65.8   5.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 404  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 252   NE2                                                    
REMARK 620 2 ASP B 256   OD2 119.4                                              
REMARK 620 3 HOH B 533   O   112.2  97.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 403  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 9EA A 401   N47                                                    
REMARK 620 2 HIS B 320   NE2  76.7                                              
REMARK 620 3 HOH B 537   O    99.9 112.6                                        
REMARK 620 4 HOH B 550   O   107.4  48.2 138.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9EA A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 406                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 407                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 408                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9EA B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 404                  
DBREF  5VKC A  174   326  UNP    Q07820   MCL1_HUMAN     174    326             
DBREF  5VKC B  174   326  UNP    Q07820   MCL1_HUMAN     174    326             
SEQADV 5VKC GLY A  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5VKC SER A  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5VKC MET A  172  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5VKC ASP A  173  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5VKC GLY B  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5VKC SER B  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5VKC MET B  172  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5VKC ASP B  173  UNP  Q07820              EXPRESSION TAG                 
SEQRES   1 A  157  GLY SER MET ASP LEU TYR ARG GLN SER LEU GLU ILE ILE          
SEQRES   2 A  157  SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP          
SEQRES   3 A  157  THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS          
SEQRES   4 A  157  ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN          
SEQRES   5 A  157  ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS          
SEQRES   6 A  157  LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER          
SEQRES   7 A  157  ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN          
SEQRES   8 A  157  TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE          
SEQRES   9 A  157  VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS          
SEQRES  10 A  157  ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL          
SEQRES  11 A  157  ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP          
SEQRES  12 A  157  ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU          
SEQRES  13 A  157  GLY                                                          
SEQRES   1 B  157  GLY SER MET ASP LEU TYR ARG GLN SER LEU GLU ILE ILE          
SEQRES   2 B  157  SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP          
SEQRES   3 B  157  THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS          
SEQRES   4 B  157  ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN          
SEQRES   5 B  157  ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS          
SEQRES   6 B  157  LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER          
SEQRES   7 B  157  ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN          
SEQRES   8 B  157  TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE          
SEQRES   9 B  157  VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS          
SEQRES  10 B  157  ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL          
SEQRES  11 B  157  ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP          
SEQRES  12 B  157  ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU          
SEQRES  13 B  157  GLY                                                          
HET    9EA  A 401      57                                                       
HET     ZN  A 402       1                                                       
HET     ZN  A 403       1                                                       
HET     ZN  A 404       1                                                       
HET     ZN  A 405       1                                                       
HET     ZN  A 406       1                                                       
HET     ZN  A 407       1                                                       
HET     ZN  A 408       1                                                       
HET    9EA  B 401      57                                                       
HET     ZN  B 402       1                                                       
HET     ZN  B 403       1                                                       
HET     ZN  B 404       1                                                       
HETNAM     9EA 7-(3-{[4-(4-ACETYLPIPERAZIN-1-YL)PHENOXY]METHYL}-1,5-            
HETNAM   2 9EA  DIMETHYL-1H-PYRAZOL-4-YL)-3-{3-[(NAPHTHALEN-1-YL)               
HETNAM   3 9EA  OXY]PROPYL}-1-[(PYRIDIN-3-YL)METHYL]-1H-INDOLE-2-               
HETNAM   4 9EA  CARBOXYLIC ACID                                                 
HETNAM      ZN ZINC ION                                                         
FORMUL   3  9EA    2(C46 H46 N6 O5)                                             
FORMUL   4   ZN    10(ZN 2+)                                                    
FORMUL  15  HOH   *124(H2 O)                                                    
HELIX    1 AA1 ASP A  173  GLY A  192  1                                  20    
HELIX    2 AA2 GLY A  203  HIS A  224  1                                  22    
HELIX    3 AA3 HIS A  224  ASP A  236  1                                  13    
HELIX    4 AA4 ASN A  239  SER A  245  1                                   7    
HELIX    5 AA5 SER A  245  ASP A  256  1                                  12    
HELIX    6 AA6 ASN A  260  ILE A  281  1                                  22    
HELIX    7 AA7 GLN A  283  SER A  285  5                                   3    
HELIX    8 AA8 CYS A  286  GLN A  309  1                                  24    
HELIX    9 AA9 ARG A  310  PHE A  319  1                                  10    
HELIX   10 AB1 ASP B  173  GLY B  192  1                                  20    
HELIX   11 AB2 GLY B  203  HIS B  224  1                                  22    
HELIX   12 AB3 HIS B  224  ASP B  236  1                                  13    
HELIX   13 AB4 ASN B  239  SER B  245  1                                   7    
HELIX   14 AB5 SER B  245  ASP B  256  1                                  12    
HELIX   15 AB6 ASN B  260  ILE B  281  1                                  22    
HELIX   16 AB7 GLN B  283  SER B  285  5                                   3    
HELIX   17 AB8 CYS B  286  GLN B  309  1                                  24    
HELIX   18 AB9 ARG B  310  PHE B  319  1                                  10    
LINK         NE2 HIS A 224                ZN    ZN A 402     1555   1555  2.11  
LINK         OD2 ASP A 241                ZN    ZN A 407     1555   1555  2.48  
LINK         OD1 ASP A 242                ZN    ZN A 406     1555   1555  2.22  
LINK         ND1 HIS A 252                ZN    ZN A 405     1555   1555  1.92  
LINK         NE2 HIS A 252                ZN    ZN A 404     1555   1555  2.11  
LINK         OD2 ASP A 256                ZN    ZN A 404     1555   1555  2.08  
LINK         NE2 HIS A 320                ZN    ZN A 408     1555   1555  2.07  
LINK         NE2 HIS B 224                ZN    ZN B 402     1555   1555  2.13  
LINK         ND1 HIS B 252                ZN    ZN B 403     1555   1555  1.92  
LINK         NE2 HIS B 252                ZN    ZN B 404     1555   1555  2.11  
LINK         OD2 ASP B 256                ZN    ZN B 404     1555   1555  2.03  
LINK         N47 9EA A 401                ZN    ZN A 403     1555   1555  2.16  
LINK        ZN    ZN A 404                 O   HOH A 537     1555   1555  2.07  
LINK        ZN    ZN A 405                 O   HOH A 515     1555   1555  2.25  
LINK        ZN    ZN A 408                 O   HOH A 540     1555   1555  2.26  
LINK        ZN    ZN A 408                 N47 9EA B 401     1555   1555  2.20  
LINK        ZN    ZN A 408                 O   HOH B 541     1555   1555  1.89  
LINK        ZN    ZN B 402                 O   HOH B 518     1555   1555  2.09  
LINK        ZN    ZN B 403                 O   HOH B 532     1555   1555  2.33  
LINK        ZN    ZN B 404                 O   HOH B 533     1555   1555  1.89  
LINK         OE1 GLU A 288                ZN    ZN A 402     1555   2564  2.44  
LINK         OE2 GLU A 288                ZN    ZN A 402     1555   2564  2.04  
LINK         OE2 GLU A 292                ZN    ZN B 403     1555   2564  2.09  
LINK         OD2 ASP A 296                ZN    ZN B 403     1555   2564  2.02  
LINK         OD2 ASP B 241                ZN    ZN A 406     1555   3455  2.52  
LINK         OD1 ASP B 242                ZN    ZN A 407     1555   3455  2.15  
LINK         OE1 GLU B 288                ZN    ZN B 402     1555   3355  2.46  
LINK         OE2 GLU B 288                ZN    ZN B 402     1555   3355  2.07  
LINK         OE2 GLU B 292                ZN    ZN A 405     1555   3455  2.09  
LINK         OD2 ASP B 296                ZN    ZN A 405     1555   3455  1.96  
LINK         NE2 HIS B 320                ZN    ZN A 403     1555   1565  1.99  
LINK        ZN    ZN A 402                 O   HOH A 506     1555   3455  2.05  
LINK        ZN    ZN A 402                 O   HOH A 529     1555   3455  2.18  
LINK        ZN    ZN A 403                 O   HOH B 537     1555   1545  1.89  
LINK        ZN    ZN A 403                 O   HOH B 550     1555   1545  2.23  
LINK        ZN    ZN B 402                 O   HOH B 543     1555   2574  2.17  
SITE     1 AC1 15 HIS A 224  ALA A 227  MET A 250  VAL A 253                    
SITE     2 AC1 15 GLY A 262  ARG A 263  THR A 266  LEU A 267                    
SITE     3 AC1 15 PHE A 270  PHE A 319   ZN A 403  HOH A 506                    
SITE     4 AC1 15 HOH A 509  HOH A 512  HIS B 320                               
SITE     1 AC2  4 HIS A 224  GLU A 288  HOH A 506  HOH A 529                    
SITE     1 AC3  4 9EA A 401  HIS B 320  HOH B 537  HOH B 550                    
SITE     1 AC4  3 HIS A 252  ASP A 256  HOH A 537                               
SITE     1 AC5  5 ARG A 248  HIS A 252  HOH A 515  GLU B 292                    
SITE     2 AC5  5 ASP B 296                                                     
SITE     1 AC6  2 ASP A 242  ASP B 241                                          
SITE     1 AC7  2 ASP A 241  ASP B 242                                          
SITE     1 AC8  4 HIS A 320  HOH A 540  9EA B 401  HOH B 541                    
SITE     1 AC9 16 HIS A 320   ZN A 408  HIS B 224  ALA B 227                    
SITE     2 AC9 16 MET B 250  VAL B 253  GLY B 262  ARG B 263                    
SITE     3 AC9 16 THR B 266  LEU B 267  PHE B 270  PHE B 319                    
SITE     4 AC9 16 HOH B 502  HOH B 518  HOH B 538  HOH B 541                    
SITE     1 AD1  4 HIS B 224  GLU B 288  HOH B 518  HOH B 543                    
SITE     1 AD2  5 GLU A 292  ASP A 296  ARG B 248  HIS B 252                    
SITE     2 AD2  5 HOH B 532                                                     
SITE     1 AD3  4 GLU A 322  HIS B 252  ASP B 256  HOH B 533                    
CRYST1   63.920   63.920   91.400  90.00  90.00 120.00 P 32          6          
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      0.015645  0.009032  0.000000        0.00000                         
SCALE2      0.000000  0.018065  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010941        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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