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Database: PDB
Entry: 5UUM
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Original site: 5UUM 
HEADER    APOPTOSIS                               17-FEB-17   5UUM              
TITLE     HUMAN MCL-1 IN COMPLEX WITH A BFL-1-SPECIFIC SELECTED PEPTIDE         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INDUCED MYELOID LEUKEMIA CELL DIFFERENTIATION PROTEIN MCL- 
COMPND   3 1;                                                                   
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: UNP RESIDUES 172-325;                                      
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;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: BFL-1 SPECIFIC PEPTIDE FS2;                                
COMPND  11 CHAIN: C, D;                                                         
COMPND  12 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 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  11 ORGANISM_TAXID: 32630                                                
KEYWDS    APOPTOSIS REGULATORY PROTEINS, PEPTIDE LIBRARY, PROTEIN BINDING,      
KEYWDS   2 PROTEIN STRUCTURE, PROTO-ONCOGENE, SPECIFICITY, BCL2A1, BCL2 RELATED 
KEYWDS   3 PROTEIN A1, PEPTIDE INHIBITOR, APOPTOSIS                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.JENSON,R.A.GRANT,A.E.KEATING                                      
REVDAT   3   01-JAN-20 5UUM    1       REMARK                                   
REVDAT   2   27-SEP-17 5UUM    1       REMARK                                   
REVDAT   1   21-JUN-17 5UUM    0                                                
JRNL        AUTH   J.M.JENSON,J.A.RYAN,R.A.GRANT,A.LETAI,A.E.KEATING            
JRNL        TITL   EPISTATIC MUTATIONS IN PUMA BH3 DRIVE AN ALTERNATE BINDING   
JRNL        TITL 2 MODE TO POTENTLY AND SELECTIVELY INHIBIT ANTI-APOPTOTIC      
JRNL        TITL 3 BFL-1.                                                       
JRNL        REF    ELIFE                         V.   6       2017              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   28594323                                                     
JRNL        DOI    10.7554/ELIFE.25541                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1_2575                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.33                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 16695                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1670                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 27.3316 -  5.3579    1.00     1297   145  0.2224 0.2560        
REMARK   3     2  5.3579 -  4.2579    1.00     1276   141  0.1925 0.2030        
REMARK   3     3  4.2579 -  3.7212    1.00     1247   138  0.1767 0.2077        
REMARK   3     4  3.7212 -  3.3817    1.00     1274   142  0.1941 0.2111        
REMARK   3     5  3.3817 -  3.1397    1.00     1248   139  0.2163 0.2519        
REMARK   3     6  3.1397 -  2.9548    1.00     1242   137  0.2381 0.3282        
REMARK   3     7  2.9548 -  2.8070    1.00     1257   141  0.2359 0.2871        
REMARK   3     8  2.8070 -  2.6849    1.00     1253   139  0.2500 0.2936        
REMARK   3     9  2.6849 -  2.5816    1.00     1228   136  0.2382 0.2535        
REMARK   3    10  2.5816 -  2.4926    1.00     1257   140  0.2512 0.3012        
REMARK   3    11  2.4926 -  2.4147    1.00     1244   139  0.2587 0.2962        
REMARK   3    12  2.4147 -  2.3457    0.96     1202   133  0.2840 0.3594        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.240           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.16                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           2931                                  
REMARK   3   ANGLE     :  0.497           3943                                  
REMARK   3   CHIRALITY :  0.033            435                                  
REMARK   3   PLANARITY :  0.003            510                                  
REMARK   3   DIHEDRAL  : 11.705           1769                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5UUM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000226461.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-NOV-16                          
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                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16700                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.346                              
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     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.15000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.87200                            
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: 3PK1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M ZINC SULFATE, 0.1 M IMIDAZOLE      
REMARK 280  (PH 6.5), AND 3% 6-AMINOHEXANOIC ACID, VAPOR DIFFUSION, HANGING     
REMARK 280  DROP, TEMPERATURE 298.0K                                            
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       66.30850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.38000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       66.30850            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       31.38000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9600 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -141.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9770 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -143.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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     ACE C     0                                                      
REMARK 465     NH2 C    24                                                      
REMARK 465     ACE D     0                                                      
REMARK 465     NH2 D    24                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    VAL A   297     HG1  THR A   301              1.53            
REMARK 500   O    VAL B   297     HG1  THR B   301              1.59            
REMARK 500   OE2  GLU A   188    HH21  ARG A   214              1.60            
REMARK 500   O    HOH B   545     O    HOH B   564              2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD2  ASP A   304    HH22  ARG D    11     1565     1.59            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 172       75.46     62.23                                   
REMARK 500    THR A 196     -116.87     60.46                                   
REMARK 500    MET A 199     -160.73     57.93                                   
REMARK 500    ARG A 201     -124.36     63.45                                   
REMARK 500    GLU C  22       56.49    -92.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 404  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 224   NE2                                                    
REMARK 620 2 HOH A 551   O   101.7                                              
REMARK 620 N                    1                                               
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 ASP A 236   OD1                                                    
REMARK 620 2 ASP A 242   OD2 102.2                                              
REMARK 620 3 HIS A 277   NE2 105.2 101.5                                        
REMARK 620 N                    1     2                                         
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 252   NE2                                                    
REMARK 620 2 ASP B 304   OD1  71.8                                              
REMARK 620 3 ASP B 323   OD1  97.0  32.7                                        
REMARK 620 4 ASP B 323   OD2  97.9  33.8   1.1                                  
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 GLU A 317   OE1                                                    
REMARK 620 2 HIS A 320   ND1 129.5                                              
REMARK 620 3 GLU A 322   OE2 108.9  98.3                                        
REMARK 620 4 ASP D  15   OD2 152.4  23.7  89.2                                  
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 224   NE2                                                    
REMARK 620 2 HOH B 531   O   100.3                                              
REMARK 620 N                    1                                               
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 ASP B 236   OD2                                                    
REMARK 620 2 ASP B 242   OD2 170.8                                              
REMARK 620 3 HIS B 277   NE2 100.4  84.6                                        
REMARK 620 N                    1     2                                         
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 252   NE2                                                    
REMARK 620 2 ASP A 304   OD1  60.8                                              
REMARK 620 3 ASP A 323   OD1  84.1  32.2                                        
REMARK 620 4 ASP A 323   OD2  85.6  32.7   1.9                                  
REMARK 620 5 GLU A 325   OE1  89.3  38.5   6.3   5.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 317   OE1                                                    
REMARK 620 2 HIS B 320   ND1 113.6                                              
REMARK 620 3 GLU B 322   OE2 115.7 104.7                                        
REMARK 620 4 ASP C  15   OD2 139.4  25.8  89.4                                  
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 ZN A 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 405                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5UUK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UUL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UUP   RELATED DB: PDB                                   
DBREF  5UUM A  172   325  UNP    Q07820   MCL1_HUMAN     172    325             
DBREF  5UUM B  172   325  UNP    Q07820   MCL1_HUMAN     172    325             
DBREF  5UUM C    0    24  PDB    5UUM     5UUM             0     24             
DBREF  5UUM D    0    24  PDB    5UUM     5UUM             0     24             
SEQADV 5UUM GLY A  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5UUM SER A  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5UUM GLY B  170  UNP  Q07820              EXPRESSION TAG                 
SEQADV 5UUM SER B  171  UNP  Q07820              EXPRESSION TAG                 
SEQRES   1 A  156  GLY SER ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE          
SEQRES   2 A  156  SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP          
SEQRES   3 A  156  THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS          
SEQRES   4 A  156  ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN          
SEQRES   5 A  156  ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS          
SEQRES   6 A  156  LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER          
SEQRES   7 A  156  ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN          
SEQRES   8 A  156  TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE          
SEQRES   9 A  156  VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS          
SEQRES  10 A  156  ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL          
SEQRES  11 A  156  ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP          
SEQRES  12 A  156  ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU          
SEQRES   1 B  156  GLY SER ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE          
SEQRES   2 B  156  SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP          
SEQRES   3 B  156  THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS          
SEQRES   4 B  156  ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN          
SEQRES   5 B  156  ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS          
SEQRES   6 B  156  LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER          
SEQRES   7 B  156  ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN          
SEQRES   8 B  156  TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE          
SEQRES   9 B  156  VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS          
SEQRES  10 B  156  ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL          
SEQRES  11 B  156  ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP          
SEQRES  12 B  156  ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU          
SEQRES   1 C   25  ACE GLN TRP VAL ARG GLU ILE ALA ALA GLY LEU ARG ARG          
SEQRES   2 C   25  ALA ALA ASP ASP VAL ASN ALA GLN VAL GLU ARG NH2              
SEQRES   1 D   25  ACE GLN TRP VAL ARG GLU ILE ALA ALA GLY LEU ARG ARG          
SEQRES   2 D   25  ALA ALA ASP ASP VAL ASN ALA GLN VAL GLU ARG NH2              
HET     ZN  A 401       1                                                       
HET     ZN  A 402       1                                                       
HET     ZN  A 403       1                                                       
HET     ZN  A 404       1                                                       
HET    SO4  A 405       5                                                       
HET     ZN  B 401       1                                                       
HET     ZN  B 402       1                                                       
HET     ZN  B 403       1                                                       
HET     ZN  B 404       1                                                       
HET    SO4  B 405       5                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5   ZN    8(ZN 2+)                                                     
FORMUL   9  SO4    2(O4 S 2-)                                                   
FORMUL  15  HOH   *192(H2 O)                                                    
HELIX    1 AA1 ASP A  172  GLY A  192  1                                  21    
HELIX    2 AA2 SER A  202  HIS A  224  1                                  23    
HELIX    3 AA3 HIS A  224  ASN A  239  1                                  16    
HELIX    4 AA4 ASP A  241  PHE A  254  1                                  14    
HELIX    5 AA5 SER A  255  GLY A  257  5                                   3    
HELIX    6 AA6 ASN A  260  ASN A  282  1                                  23    
HELIX    7 AA7 ILE A  287  LYS A  302  1                                  16    
HELIX    8 AA8 LYS A  302  GLN A  309  1                                   8    
HELIX    9 AA9 ARG A  310  PHE A  319  1                                  10    
HELIX   10 AB1 ASP B  172  GLY B  192  1                                  21    
HELIX   11 AB2 GLY B  203  HIS B  224  1                                  22    
HELIX   12 AB3 HIS B  224  ASN B  239  1                                  16    
HELIX   13 AB4 ASP B  241  PHE B  254  1                                  14    
HELIX   14 AB5 SER B  255  GLY B  257  5                                   3    
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  LYS B  302  1                                  17    
HELIX   18 AB9 LYS B  302  GLN B  309  1                                   8    
HELIX   19 AC1 ARG B  310  PHE B  319  1                                  10    
HELIX   20 AC2 TRP C    2  GLU C   22  1                                  21    
HELIX   21 AC3 TRP D    2  GLU D   22  1                                  21    
SSBOND   1 CYS A  286    CYS A  286                          1555   2556  2.04  
LINK         NE2 HIS A 224                ZN    ZN A 404     1555   1555  2.07  
LINK         OD1 ASP A 236                ZN    ZN A 403     1555   1555  1.96  
LINK         OD2 ASP A 242                ZN    ZN A 403     1555   1555  1.98  
LINK         NE2 HIS A 252                ZN    ZN A 401     1555   1555  2.03  
LINK         NE2 HIS A 277                ZN    ZN A 403     1555   1555  2.12  
LINK         OE1 GLU A 317                ZN    ZN A 402     1555   1555  2.19  
LINK         ND1 HIS A 320                ZN    ZN A 402     1555   1555  2.05  
LINK         OE2 GLU A 322                ZN    ZN A 402     1555   1555  1.78  
LINK         NE2 HIS B 224                ZN    ZN B 404     1555   1555  2.09  
LINK         OD2 ASP B 236                ZN    ZN B 403     1555   1555  2.40  
LINK         OD2 ASP B 242                ZN    ZN B 403     1555   1555  2.04  
LINK         NE2 HIS B 252                ZN    ZN B 402     1555   1555  2.01  
LINK         NE2 HIS B 277                ZN    ZN B 403     1555   1555  2.11  
LINK         OE1 GLU B 317                ZN    ZN B 401     1555   1555  2.55  
LINK         ND1 HIS B 320                ZN    ZN B 401     1555   1555  2.15  
LINK         OE2 GLU B 322                ZN    ZN B 401     1555   1555  1.94  
LINK        ZN    ZN A 404                 O   HOH A 551     1555   1555  2.66  
LINK        ZN    ZN B 404                 O   HOH B 531     1555   1555  2.27  
LINK         OD1 ASP A 304                ZN    ZN B 402     1555   1565  1.93  
LINK         OD1 ASP A 323                ZN    ZN B 402     1555   4456  2.66  
LINK         OD2 ASP A 323                ZN    ZN B 402     1555   4456  2.03  
LINK         OE1 GLU A 325                ZN    ZN B 402     1555   4456  2.46  
LINK         OD1 ASP B 304                ZN    ZN A 401     1555   1545  1.97  
LINK         OD1 ASP B 323                ZN    ZN A 401     1555   4445  2.63  
LINK         OD2 ASP B 323                ZN    ZN A 401     1555   4445  2.41  
LINK         OD2 ASP C  15                ZN    ZN B 401     1555   4455  1.95  
LINK         OD2 ASP D  15                ZN    ZN A 402     1555   4446  1.93  
SITE     1 AC1  4 HIS A 252  ASP B 304  ASP B 323  GLU B 325                    
SITE     1 AC2  4 GLU A 317  HIS A 320  GLU A 322  ASP D  15                    
SITE     1 AC3  4 ASP A 236  ASP A 242  HIS A 277  HOH A 553                    
SITE     1 AC4  4 HIS A 224  HOH A 551  ASP C  16  GLN C  20                    
SITE     1 AC5  6 ARG A 248  HIS A 252  HOH A 507  HOH A 536                    
SITE     2 AC5  6 ARG B 300  HOH C 108                                          
SITE     1 AC6  4 GLU B 317  HIS B 320  GLU B 322  ASP C  15                    
SITE     1 AC7  4 ASP A 304  ASP A 323  GLU A 325  HIS B 252                    
SITE     1 AC8  3 ASP B 236  ASP B 242  HIS B 277                               
SITE     1 AC9  4 HIS B 224  HOH B 531  ASP D  16  GLN D  20                    
SITE     1 AD1  5 ARG A 303  HOH A 505  HIS B 252  HOH B 541                    
SITE     2 AD1  5 HOH D 103                                                     
CRYST1  132.617   62.760   48.788  90.00  98.14  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007541  0.000000  0.001079        0.00000                         
SCALE2      0.000000  0.015934  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020706        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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