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Database: PDB
Entry: 4WMR
LinkDB: 4WMR
Original site: 4WMR 
HEADER    APOPTOSIS/INHIBITOR                     09-OCT-14   4WMR              
TITLE     STRUCTURE OF MCL1 BOUND TO BRD INHIBITOR LIGAND 1 AT 1.7A             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INDUCED MYELOID LEUKEMIA CELL DIFFERENTIATION PROTEIN MCL- 
COMPND   3 1;                                                                   
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: BCL-2-LIKE PROTEIN 3,BCL2-L-3,BCL-2-RELATED PROTEIN         
COMPND   6 EAT/MCL1,MCL1/EAT;                                                   
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MCL1, BCL2L3;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    APOPTOSIS, PROTEIN-PROTEIN INTERACTION                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.C.CLIFTON,T.E.EDWARDS                                               
REVDAT   1   06-MAY-15 4WMR    0                                                
JRNL        AUTH   M.C.CLIFTON,D.M.DRANOW,A.LEED,B.FULROTH,J.W.FAIRMAN,         
JRNL        AUTH 2 J.ABENDROTH,K.A.ATKINS,E.WALLACE,D.FAN,G.XU,Z.J.NI,          
JRNL        AUTH 3 D.DANIELS,J.VAN DRIE,G.WEI,A.B.BURGIN,T.R.GOLUB,B.K.HUBBARD, 
JRNL        AUTH 4 M.H.SERRANO-WU                                               
JRNL        TITL   A MALTOSE-BINDING PROTEIN FUSION CONSTRUCT YIELDS A ROBUST   
JRNL        TITL 2 CRYSTALLOGRAPHY PLATFORM FOR MCL1.                           
JRNL        REF    PLOS ONE                      V.  10 25010 2015              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   25909780                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0125010                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.17                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 14163                          
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) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 715                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 887                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.92                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 42                           
REMARK   3   BIN FREE R VALUE                    : 0.2450                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1146                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 68                                      
REMARK   3   SOLVENT ATOMS            : 123                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.47                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.12000                                              
REMARK   3    B22 (A**2) : -0.28000                                             
REMARK   3    B33 (A**2) : 0.15000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.01000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.123         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.115         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.070         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.862         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1280 ; 0.006 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1167 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1758 ; 1.420 ; 1.996       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2666 ; 0.756 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   167 ; 4.100 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    55 ;33.056 ;23.455       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   200 ;11.731 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;19.460 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   193 ; 0.058 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1475 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   313 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   617 ; 0.639 ; 1.264       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   616 ; 0.637 ; 1.264       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   774 ; 1.163 ; 1.891       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   -10        A  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.3290 -14.0102  12.0942              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0113 T22:   0.0117                                     
REMARK   3      T33:   0.0065 T12:  -0.0023                                     
REMARK   3      T13:   0.0041 T23:  -0.0008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7746 L22:   1.3929                                     
REMARK   3      L33:   0.5302 L12:  -0.4200                                     
REMARK   3      L13:   0.1847 L23:  -0.0980                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0009 S12:  -0.0185 S13:  -0.0497                       
REMARK   3      S21:   0.0844 S22:  -0.0126 S23:   0.0638                       
REMARK   3      S31:  -0.0031 S32:  -0.0536 S33:   0.0134                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED HYDROGENS       
REMARK   3  HAVE BEEN ADDED IN THE RIDING POSITIONS                             
REMARK   4                                                                      
REMARK   4 4WMR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-OCT-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000204092.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JUL-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E+ SUPERBRIGHT           
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944+                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14163                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 9.100                              
REMARK 200  R MERGE                    (I) : 0.04500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 30.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MG/ML MCL1, 16% PEG8000, 20%          
REMARK 280  GLYCEROL, 40MM KH2PO4, 2MM LIGAND 1, 2MM ZINC CHLORIDE, 9.98 MG/    
REMARK 280  ML MCL1, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       36.38500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       19.20500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       36.38500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       19.20500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -228.0 KCAL/MOL                       
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 KCAL/MOL                        
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   BIOMT1   2 -1.000000  0.000000  0.000000      -10.54286            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       47.16606            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 ZN    ZN A 403  LIES ON A SPECIAL POSITION.                          
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A 172    OG                                                  
REMARK 470     LYS A 194    CG   CD   CE   NZ                                   
REMARK 470     LYS A 197    CG   CD   CE   NZ                                   
REMARK 470     ARG A 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 202    OG                                                  
REMARK 470     LYS A 208    CG   CD   CE   NZ                                   
REMARK 470     ARG A 233    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 234    CG   CD   CE   NZ                                   
REMARK 470     GLU A 240    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 241    CG   OD1  OD2                                       
REMARK 470     LYS A 244    CG   CD   CE   NZ                                   
REMARK 470     ARG A 248    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 303    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 308    CG   CD   CE   NZ                                   
REMARK 470     GLU A 317    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500  ZN     ZN A   402     O4   POP A   406              1.61            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 201      -72.18    -68.27                                   
REMARK 500    HIS A 320       55.54     36.46                                   
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 615        DISTANCE =  6.10 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 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 224   ND1                                                    
REMARK 620 2 POP A 405   O2  107.5                                              
REMARK 620 3 865 A 404   N46 112.8 118.4                                        
REMARK 620 4 POP A 405   O5  106.5 103.8 106.8                                  
REMARK 620 N                    1     2     3                                   
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 252   NE2                                                    
REMARK 620 2 ASP A 256   OD2 110.0                                              
REMARK 620 3 POP A 406   O2  107.8 113.3                                        
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 POP A 405   O3                                                     
REMARK 620 2 POP A 405   O6  105.0                                              
REMARK 620 3 POP A 405   O6  116.2 107.8                                        
REMARK 620 4 POP A 405   O3  107.2 116.2 105.0                                  
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 ZN 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 865 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue POP A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue POP A 406                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4WMS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4WMT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4WMU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4WMV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4WMW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4WMX   RELATED DB: PDB                                   
DBREF  4WMR A  173   321  UNP    Q07820   MCL1_HUMAN     173    321             
SEQADV 4WMR SER A  172  UNP  Q07820              EXPRESSION TAG                 
SEQRES   1 A  150  SER GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER ARG          
SEQRES   2 A  150  TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR LYS          
SEQRES   3 A  150  PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA LEU          
SEQRES   4 A  150  GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG ASN          
SEQRES   5 A  150  HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU ASP          
SEQRES   6 A  150  ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG VAL          
SEQRES   7 A  150  MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP GLY          
SEQRES   8 A  150  ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL ALA          
SEQRES   9 A  150  LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE GLU          
SEQRES  10 A  150  PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG THR          
SEQRES  11 A  150  LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP GLY          
SEQRES  12 A  150  PHE VAL GLU PHE PHE HIS VAL                                  
HET     ZN  A 401       1                                                       
HET     ZN  A 402       1                                                       
HET     ZN  A 403       1                                                       
HET    865  A 404      47                                                       
HET    POP  A 405       9                                                       
HET    POP  A 406       9                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     865 7-[2-(1H-IMIDAZOL-1-YL)-4-METHYLPYRIDIN-3-YL]-3-[3-              
HETNAM   2 865  (NAPHTHALEN-1-YLOXY)PROPYL]-1-[2-OXO-2-(PIPERAZIN-1-            
HETNAM   3 865  YL)ETHYL]-1H-INDOLE-2-CARBOXYLIC ACID                           
HETNAM     POP PYROPHOSPHATE 2-                                                 
FORMUL   2   ZN    3(ZN 2+)                                                     
FORMUL   5  865    C37 H36 N6 O4                                                
FORMUL   6  POP    2(H2 O7 P2 2-)                                               
FORMUL   8  HOH   *123(H2 O)                                                    
HELIX    1 AA1 SER A  172  GLY A  192  1                                  21    
HELIX    2 AA2 SER A  202  HIS A  224  1                                  23    
HELIX    3 AA3 HIS A  224  ASP A  236  1                                  13    
HELIX    4 AA4 ASN A  239  ASP A  256  1                                  18    
HELIX    5 AA5 ASN A  260  ILE A  281  1                                  22    
HELIX    6 AA6 GLN A  283  SER A  285  5                                   3    
HELIX    7 AA7 CYS A  286  LYS A  302  1                                  17    
HELIX    8 AA8 LYS A  302  GLN A  309  1                                   8    
HELIX    9 AA9 ARG A  310  HIS A  320  1                                  11    
LINK         ND1 HIS A 224                ZN    ZN A 401     1555   1555  2.06  
LINK         NE2 HIS A 252                ZN    ZN A 402     1555   1555  2.12  
LINK         OD2 ASP A 256                ZN    ZN A 402     1555   1555  2.02  
LINK        ZN    ZN A 401                 O2  POP A 405     1555   1555  1.88  
LINK        ZN    ZN A 401                 N46 865 A 404     1555   1555  2.00  
LINK        ZN    ZN A 401                 O5  POP A 405     1555   1555  1.85  
LINK        ZN    ZN A 402                 O2  POP A 406     1555   1555  2.29  
LINK        ZN    ZN A 403                 O3  POP A 405     1555   1555  1.85  
LINK        ZN    ZN A 403                 O6  POP A 405     1555   1555  2.00  
LINK        ZN    ZN A 403                 O6  POP A 405     1555   2555  2.00  
LINK        ZN    ZN A 403                 O3  POP A 405     1555   2555  1.85  
SITE     1 AC1  3 HIS A 224  865 A 404  POP A 405                               
SITE     1 AC2  3 HIS A 252  ASP A 256  POP A 406                               
SITE     1 AC3  1 POP A 405                                                     
SITE     1 AC4 17 HIS A 224  THR A 226  ALA A 227  LEU A 246                    
SITE     2 AC4 17 MET A 250  VAL A 253  ARG A 263  THR A 266                    
SITE     3 AC4 17 LEU A 267  PHE A 270  GLY A 271   ZN A 401                    
SITE     4 AC4 17 POP A 405  HOH A 560  HOH A 584  HOH A 587                    
SITE     5 AC4 17 HOH A 601                                                     
SITE     1 AC5  8 HIS A 224   ZN A 401   ZN A 403  865 A 404                    
SITE     2 AC5  8 HOH A 512  HOH A 518  HOH A 560  HOH A 601                    
SITE     1 AC6  7 SER A 172  HIS A 252  ASP A 256  ARG A 300                    
SITE     2 AC6  7  ZN A 402  HOH A 540  HOH A 617                               
CRYST1   72.770   38.410   48.330  90.00 102.60  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013742  0.000000  0.003070        0.00000                         
SCALE2      0.000000  0.026035  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021201        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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