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Database: PDB
Entry: 5N4W
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HEADER    LIGASE                                  11-FEB-17   5N4W              
TITLE     CRYSTAL STRUCTURE OF THE CUL2-RBX1-ELOBC-VHL UBIQUITIN LIGASE COMPLEX 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CULLIN-2;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CUL-2;                                                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: VON HIPPEL-LINDAU DISEASE TUMOR SUPPRESSOR;                
COMPND   8 CHAIN: V;                                                            
COMPND   9 SYNONYM: PROTEIN G7,PVHL;                                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RBX1;                          
COMPND  13 CHAIN: R;                                                            
COMPND  14 SYNONYM: PROTEIN ZYP,RING FINGER PROTEIN 75,RING-BOX PROTEIN 1,RBX1, 
COMPND  15 REGULATOR OF CULLINS 1;                                              
COMPND  16 EC: 6.3.2.-;                                                         
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: ELONGIN-B;                                                 
COMPND  20 CHAIN: B;                                                            
COMPND  21 SYNONYM: ELOB,ELONGIN 18 KDA SUBUNIT,RNA POLYMERASE II TRANSCRIPTION 
COMPND  22 FACTOR SIII SUBUNIT B,SIII P18,TRANSCRIPTION ELONGATION FACTOR B     
COMPND  23 POLYPEPTIDE 2;                                                       
COMPND  24 ENGINEERED: YES;                                                     
COMPND  25 MOL_ID: 5;                                                           
COMPND  26 MOLECULE: ELONGIN-C;                                                 
COMPND  27 CHAIN: C;                                                            
COMPND  28 SYNONYM: ELOC,ELONGIN 15 KDA SUBUNIT,RNA POLYMERASE II TRANSCRIPTION 
COMPND  29 FACTOR SIII SUBUNIT C,SIII P15,TRANSCRIPTION ELONGATION FACTOR B     
COMPND  30 POLYPEPTIDE 1;                                                       
COMPND  31 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: CUL2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF21;                                   
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: VHL;                                                           
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 MOL_ID: 3;                                                           
SOURCE  19 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  20 ORGANISM_COMMON: HUMAN;                                              
SOURCE  21 ORGANISM_TAXID: 9606;                                                
SOURCE  22 GENE: RBX1, RNF75, ROC1;                                             
SOURCE  23 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  24 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  26 EXPRESSION_SYSTEM_CELL_LINE: SF21;                                   
SOURCE  27 MOL_ID: 4;                                                           
SOURCE  28 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  29 ORGANISM_COMMON: HUMAN;                                              
SOURCE  30 ORGANISM_TAXID: 9606;                                                
SOURCE  31 GENE: ELOB, TCEB2;                                                   
SOURCE  32 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  33 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  34 MOL_ID: 5;                                                           
SOURCE  35 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  36 ORGANISM_COMMON: HUMAN;                                              
SOURCE  37 ORGANISM_TAXID: 9606;                                                
SOURCE  38 GENE: ELOC, TCEB1;                                                   
SOURCE  39 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  40 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CULLIN RING, E3 UBIQUITIN LIGASE, VHL, LIGASE, CULLIN-2               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.A.F.CARDOTE,M.S.GADD,A.CIULLI                                       
REVDAT   4   24-APR-19 5N4W    1       SOURCE                                   
REVDAT   3   24-OCT-18 5N4W    1       REMARK LINK                              
REVDAT   2   21-JUN-17 5N4W    1       JRNL                                     
REVDAT   1   07-JUN-17 5N4W    0                                                
JRNL        AUTH   T.A.F.CARDOTE,M.S.GADD,A.CIULLI                              
JRNL        TITL   CRYSTAL STRUCTURE OF THE CUL2-RBX1-ELOBC-VHL UBIQUITIN       
JRNL        TITL 2 LIGASE COMPLEX.                                              
JRNL        REF    STRUCTURE                     V.  25   901 2017              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   28591624                                                     
JRNL        DOI    10.1016/J.STR.2017.04.009                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11_2558: ???)                              
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) : 3.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 95.48                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 34407                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.304                           
REMARK   3   R VALUE            (WORKING SET) : 0.302                           
REMARK   3   FREE R VALUE                     : 0.346                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.240                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1802                            
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 95.5096 -  9.1678    0.99     2523   132  0.2378 0.2543        
REMARK   3     2  9.1678 -  7.2776    1.00     2510   144  0.2965 0.4164        
REMARK   3     3  7.2776 -  6.3579    1.00     2534   132  0.3463 0.3968        
REMARK   3     4  6.3579 -  5.7767    0.99     2479   139  0.3654 0.3823        
REMARK   3     5  5.7767 -  5.3627    0.99     2555   126  0.3389 0.3884        
REMARK   3     6  5.3627 -  5.0465    0.99     2513   129  0.3019 0.3205        
REMARK   3     7  5.0465 -  4.7938    1.00     2485   162  0.2974 0.3758        
REMARK   3     8  4.7938 -  4.5851    0.99     2493   159  0.3068 0.3149        
REMARK   3     9  4.5851 -  4.4086    1.00     2568   134  0.3103 0.3438        
REMARK   3    10  4.4086 -  4.2565    1.00     2506   142  0.3215 0.3607        
REMARK   3    11  4.2565 -  4.1234    0.98     2448   135  0.3410 0.3982        
REMARK   3    12  4.1234 -  4.0055    0.99     2509   133  0.3506 0.3771        
REMARK   3    13  4.0055 -  3.9001    0.99     2482   135  0.3973 0.4026        
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)     : 0.680            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 40.040           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 200.0                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 191.0                          
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           7855                                  
REMARK   3   ANGLE     :  0.692          10574                                  
REMARK   3   CHIRALITY :  0.043           1195                                  
REMARK   3   PLANARITY :  0.004           1346                                  
REMARK   3   DIHEDRAL  :  3.499           5127                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 163)                    
REMARK   3    ORIGIN FOR THE GROUP (A): -22.3345   3.0801 -61.2783              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0689 T22:   2.2287                                     
REMARK   3      T33:   1.4286 T12:  -0.3334                                     
REMARK   3      T13:  -0.6835 T23:   0.0869                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4416 L22:   2.6024                                     
REMARK   3      L33:   0.9859 L12:  -0.9161                                     
REMARK   3      L13:  -0.4704 L23:   0.0327                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.4110 S12:  -0.8893 S13:  -0.4805                       
REMARK   3      S21:  -0.5002 S22:  -0.4473 S23:   0.0407                       
REMARK   3      S31:   0.5873 S32:   0.2498 S33:   0.7896                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 164 THROUGH 277 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.7137  -6.9799 -34.8271              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8643 T22:   1.2219                                     
REMARK   3      T33:   0.3861 T12:  -0.2563                                     
REMARK   3      T13:  -0.1499 T23:  -0.4484                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6601 L22:   1.8008                                     
REMARK   3      L33:   4.4624 L12:   1.5957                                     
REMARK   3      L13:   1.5672 L23:  -0.7209                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5151 S12:   0.4970 S13:  -1.5810                       
REMARK   3      S21:  -0.3201 S22:  -0.4902 S23:  -0.6268                       
REMARK   3      S31:   1.9262 S32:  -0.1380 S33:  -1.9091                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 278 THROUGH 384 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  28.4750   3.9890 -10.4271              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0145 T22:   0.6923                                     
REMARK   3      T33:   0.6978 T12:  -0.1987                                     
REMARK   3      T13:  -0.0458 T23:   0.2188                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6025 L22:   4.3182                                     
REMARK   3      L33:   4.0187 L12:   2.2955                                     
REMARK   3      L13:   3.0674 L23:   3.5745                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5896 S12:   0.0704 S13:   1.0121                       
REMARK   3      S21:   0.5913 S22:  -0.6006 S23:  -0.5931                       
REMARK   3      S31:   1.1456 S32:  -0.2406 S33:  -0.1875                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 385 THROUGH 745 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  44.5049  34.3277   8.3282              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2817 T22:   0.9750                                     
REMARK   3      T33:   1.2739 T12:  -0.0270                                     
REMARK   3      T13:  -0.1324 T23:   0.0145                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3887 L22:   2.7737                                     
REMARK   3      L33:   1.1465 L12:   2.3656                                     
REMARK   3      L13:   1.2059 L23:  -0.6650                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4383 S12:  -0.4654 S13:  -0.5272                       
REMARK   3      S21:   0.7327 S22:  -0.1995 S23:  -0.2278                       
REMARK   3      S31:  -0.4248 S32:   0.0227 S33:  -0.2087                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'V' AND (RESID 157 THROUGH 169 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.4166  36.3384 -64.3799              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.7599 T22:   4.9135                                     
REMARK   3      T33:   1.7178 T12:   2.2711                                     
REMARK   3      T13:  -0.0416 T23:   0.5893                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8190 L22:   0.6587                                     
REMARK   3      L33:   2.3176 L12:   1.3946                                     
REMARK   3      L13:   1.6200 L23:   1.0974                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0845 S12:   0.0787 S13:   0.2800                       
REMARK   3      S21:  -0.5578 S22:  -0.0792 S23:   0.4548                       
REMARK   3      S31:  -0.2568 S32:   0.2531 S33:   0.2607                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'V' AND (RESID 170 THROUGH 174 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -41.6138  38.7758 -65.2808              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.9341 T22:   4.1075                                     
REMARK   3      T33:   4.4692 T12:   1.2560                                     
REMARK   3      T13:   1.6627 T23:  -0.1328                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2834 L22:   0.0010                                     
REMARK   3      L33:   1.6384 L12:  -0.0082                                     
REMARK   3      L13:  -0.6799 L23:   0.0144                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3704 S12:  -0.0463 S13:   0.1389                       
REMARK   3      S21:   0.2860 S22:   0.0839 S23:  -0.0599                       
REMARK   3      S31:   0.5034 S32:  -0.0416 S33:   0.1952                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'V' AND (RESID 175 THROUGH 184 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -38.6655  28.7954 -67.2672              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8979 T22:   3.7251                                     
REMARK   3      T33:   5.7989 T12:  -0.4477                                     
REMARK   3      T13:  -0.2185 T23:   0.4033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0940 L22:   3.9026                                     
REMARK   3      L33:   1.9340 L12:  -1.1519                                     
REMARK   3      L13:   0.1177 L23:  -0.3047                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.4182 S12:  -3.7635 S13:   0.4264                       
REMARK   3      S21:  -0.5461 S22:   0.7130 S23:   0.0162                       
REMARK   3      S31:   0.6000 S32:  -0.9840 S33:  -2.0622                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'V' AND (RESID 185 THROUGH 193 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -34.7566  31.7704 -58.7414              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.3408 T22:   4.6010                                     
REMARK   3      T33:   1.8977 T12:   2.5002                                     
REMARK   3      T13:  -0.0999 T23:  -0.3595                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8289 L22:   6.8594                                     
REMARK   3      L33:   3.6211 L12:  -6.4760                                     
REMARK   3      L13:  -1.9960 L23:   3.8285                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.3507 S12:   1.5725 S13:   1.1976                       
REMARK   3      S21:  -1.6292 S22:  -0.7883 S23:  -0.9787                       
REMARK   3      S31:   0.0909 S32:  -0.3411 S33:   0.5941                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'R' AND (RESID 17 THROUGH 39 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  60.0442  45.0616  12.0342              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0551 T22:   1.4693                                     
REMARK   3      T33:   1.9921 T12:  -0.2412                                     
REMARK   3      T13:  -0.2591 T23:   0.3776                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4695 L22:   5.0819                                     
REMARK   3      L33:   4.1034 L12:  -3.3631                                     
REMARK   3      L13:   1.5711 L23:   0.6260                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2816 S12:  -1.0039 S13:   1.1395                       
REMARK   3      S21:   0.1591 S22:  -0.7327 S23:  -1.4716                       
REMARK   3      S31:   0.7498 S32:   0.8090 S33:   0.2479                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'R' AND (RESID 40 THROUGH 102 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  26.0964  49.7187  15.3168              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1877 T22:   1.7940                                     
REMARK   3      T33:   4.1069 T12:   0.1148                                     
REMARK   3      T13:  -0.3588 T23:  -1.1907                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9618 L22:   5.1236                                     
REMARK   3      L33:   6.0420 L12:   1.7897                                     
REMARK   3      L13:   1.6618 L23:   0.7178                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.2555 S12:  -0.6793 S13:   1.1224                       
REMARK   3      S21:  -0.4194 S22:  -1.2611 S23:   0.8705                       
REMARK   3      S31:   0.2689 S32:  -2.4303 S33:   1.5632                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 97 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.3664  36.4351 -85.7069              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.9877 T22:   3.2780                                     
REMARK   3      T33:   2.0168 T12:  -0.0367                                     
REMARK   3      T13:   0.2935 T23:   0.0999                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6330 L22:   3.5227                                     
REMARK   3      L33:   0.1523 L12:   2.8189                                     
REMARK   3      L13:   0.8571 L23:   0.6830                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.1701 S12:  -0.8976 S13:   1.7102                       
REMARK   3      S21:  -0.5568 S22:  -0.0118 S23:  -0.3669                       
REMARK   3      S31:  -2.0484 S32:  -1.7834 S33:  -0.1751                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 17 THROUGH 112 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -15.5196  27.7148 -72.2335              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9334 T22:   2.6424                                     
REMARK   3      T33:   1.0703 T12:  -0.3529                                     
REMARK   3      T13:  -0.3580 T23:   0.6579                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9764 L22:   2.6639                                     
REMARK   3      L33:   4.2153 L12:  -0.8038                                     
REMARK   3      L13:   1.4942 L23:   0.9370                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5457 S12:   1.5225 S13:   1.5369                       
REMARK   3      S21:  -1.0610 S22:   0.5154 S23:  -0.2467                       
REMARK   3      S31:  -2.1753 S32:   0.2148 S33:   0.5464                       
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 5N4W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003519.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-AUG-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.928                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DIALS                              
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34407                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 95.481                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.11400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.73200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
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: HOMOLOGY MODEL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 7.6, 0.15 M AMMONIUM       
REMARK 280  SULPHATE, 15% POLYETHYLENEGLYCOL 4000 AND 3% 1,4-DIOXANE OR 4%      
REMARK 280  ACETONITRILE. THE SAMPLE WAS CRYSTALLISED IN THE PRESENCE OF A      
REMARK 280  19-MER PEPTIDE MIMICKING THE SUBSTRATE HIF-1ALPHA - RESIDUES 559-   
REMARK 280  577 (DEALAPYIPMDDDFQLRSF, WITH THE MUTATIONS L559D AND M561A AND    
REMARK 280  P564 IS HYDROXYPROLINE)., VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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      119.44250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      119.44250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       43.01900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       95.48100            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       43.01900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       95.48100            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      119.44250            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       43.01900            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       95.48100            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      119.44250            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       43.01900            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       95.48100            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
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: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10350 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 56520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -174.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, V, R, B, 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 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    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     LYS A   117                                                      
REMARK 465     LEU A   118                                                      
REMARK 465     THR A   119                                                      
REMARK 465     GLU A   120                                                      
REMARK 465     ALA A   121                                                      
REMARK 465     ASP A   122                                                      
REMARK 465     LEU A   123                                                      
REMARK 465     GLN A   124                                                      
REMARK 465     TYR A   125                                                      
REMARK 465     GLY A   126                                                      
REMARK 465     TYR A   127                                                      
REMARK 465     GLY A   128                                                      
REMARK 465     GLY A   129                                                      
REMARK 465     VAL A   130                                                      
REMARK 465     ASP A   131                                                      
REMARK 465     MET A   132                                                      
REMARK 465     ASN A   133                                                      
REMARK 465     GLU A   134                                                      
REMARK 465     TYR A   194                                                      
REMARK 465     LYS A   195                                                      
REMARK 465     LYS A   196                                                      
REMARK 465     LYS A   197                                                      
REMARK 465     LYS A   291                                                      
REMARK 465     LYS A   382                                                      
REMARK 465     LYS A   404                                                      
REMARK 465     ILE A   501                                                      
REMARK 465     ASP A   502                                                      
REMARK 465     LEU A   503                                                      
REMARK 465     GLY A   504                                                      
REMARK 465     ILE A   505                                                      
REMARK 465     SER A   524                                                      
REMARK 465     SER A   525                                                      
REMARK 465     THR A   526                                                      
REMARK 465     PHE A   527                                                      
REMARK 465     ALA A   528                                                      
REMARK 465     ILE A   529                                                      
REMARK 465     TYR A   568                                                      
REMARK 465     GLY A   570                                                      
REMARK 465     TYR A   573                                                      
REMARK 465     LEU A   585                                                      
REMARK 465     LEU A   586                                                      
REMARK 465     ALA A   587                                                      
REMARK 465     PHE A   588                                                      
REMARK 465     ASN A   589                                                      
REMARK 465     ASN A   590                                                      
REMARK 465     THR A   593                                                      
REMARK 465     LYS A   615                                                      
REMARK 465     HIS A   625                                                      
REMARK 465     ASP A   626                                                      
REMARK 465     SER A   627                                                      
REMARK 465     GLU A   628                                                      
REMARK 465     LYS A   629                                                      
REMARK 465     GLU A   630                                                      
REMARK 465     ASP A   631                                                      
REMARK 465     ILE A   632                                                      
REMARK 465     ASP A   633                                                      
REMARK 465     ALA A   634                                                      
REMARK 465     SER A   645                                                      
REMARK 465     SER A   646                                                      
REMARK 465     LYS A   647                                                      
REMARK 465     ARG A   648                                                      
REMARK 465     THR A   649                                                      
REMARK 465     LYS A   650                                                      
REMARK 465     PHE A   651                                                      
REMARK 465     LYS A   652                                                      
REMARK 465     ILE A   653                                                      
REMARK 465     THR A   654                                                      
REMARK 465     THR A   655                                                      
REMARK 465     SER A   656                                                      
REMARK 465     MET A   657                                                      
REMARK 465     GLN A   658                                                      
REMARK 465     LYS A   659                                                      
REMARK 465     ASP A   660                                                      
REMARK 465     GLN A   729                                                      
REMARK 465     MET V    54                                                      
REMARK 465     GLU V    55                                                      
REMARK 465     ALA V    56                                                      
REMARK 465     GLY V    57                                                      
REMARK 465     ARG V    58                                                      
REMARK 465     PRO V    59                                                      
REMARK 465     ARG V    60                                                      
REMARK 465     PRO V    61                                                      
REMARK 465     VAL V    62                                                      
REMARK 465     LEU V    63                                                      
REMARK 465     ARG V    64                                                      
REMARK 465     SER V    65                                                      
REMARK 465     VAL V    66                                                      
REMARK 465     ASN V    67                                                      
REMARK 465     SER V    68                                                      
REMARK 465     ARG V    69                                                      
REMARK 465     GLU V    70                                                      
REMARK 465     PRO V    71                                                      
REMARK 465     SER V    72                                                      
REMARK 465     GLN V    73                                                      
REMARK 465     VAL V    74                                                      
REMARK 465     ILE V    75                                                      
REMARK 465     PHE V    76                                                      
REMARK 465     CYS V    77                                                      
REMARK 465     ASN V    78                                                      
REMARK 465     ARG V    79                                                      
REMARK 465     SER V    80                                                      
REMARK 465     PRO V    81                                                      
REMARK 465     ARG V    82                                                      
REMARK 465     VAL V    83                                                      
REMARK 465     VAL V    84                                                      
REMARK 465     LEU V    85                                                      
REMARK 465     PRO V    86                                                      
REMARK 465     VAL V    87                                                      
REMARK 465     TRP V    88                                                      
REMARK 465     LEU V    89                                                      
REMARK 465     ASN V    90                                                      
REMARK 465     PHE V    91                                                      
REMARK 465     ASP V    92                                                      
REMARK 465     GLY V    93                                                      
REMARK 465     GLU V    94                                                      
REMARK 465     PRO V    95                                                      
REMARK 465     GLN V    96                                                      
REMARK 465     PRO V    97                                                      
REMARK 465     TYR V    98                                                      
REMARK 465     PRO V    99                                                      
REMARK 465     THR V   100                                                      
REMARK 465     LEU V   101                                                      
REMARK 465     PRO V   102                                                      
REMARK 465     PRO V   103                                                      
REMARK 465     GLY V   104                                                      
REMARK 465     THR V   105                                                      
REMARK 465     GLY V   106                                                      
REMARK 465     ARG V   107                                                      
REMARK 465     ARG V   108                                                      
REMARK 465     ILE V   109                                                      
REMARK 465     HIS V   110                                                      
REMARK 465     SER V   111                                                      
REMARK 465     TYR V   112                                                      
REMARK 465     ARG V   113                                                      
REMARK 465     GLY V   114                                                      
REMARK 465     HIS V   115                                                      
REMARK 465     LEU V   116                                                      
REMARK 465     TRP V   117                                                      
REMARK 465     LEU V   118                                                      
REMARK 465     PHE V   119                                                      
REMARK 465     ARG V   120                                                      
REMARK 465     ASP V   121                                                      
REMARK 465     ALA V   122                                                      
REMARK 465     GLY V   123                                                      
REMARK 465     THR V   124                                                      
REMARK 465     HIS V   125                                                      
REMARK 465     ASP V   126                                                      
REMARK 465     GLY V   127                                                      
REMARK 465     LEU V   128                                                      
REMARK 465     LEU V   129                                                      
REMARK 465     VAL V   130                                                      
REMARK 465     ASN V   131                                                      
REMARK 465     GLN V   132                                                      
REMARK 465     THR V   133                                                      
REMARK 465     GLU V   134                                                      
REMARK 465     LEU V   135                                                      
REMARK 465     PHE V   136                                                      
REMARK 465     VAL V   137                                                      
REMARK 465     PRO V   138                                                      
REMARK 465     SER V   139                                                      
REMARK 465     LEU V   140                                                      
REMARK 465     ASN V   141                                                      
REMARK 465     VAL V   142                                                      
REMARK 465     ASP V   143                                                      
REMARK 465     GLY V   144                                                      
REMARK 465     GLN V   145                                                      
REMARK 465     PRO V   146                                                      
REMARK 465     ILE V   147                                                      
REMARK 465     PHE V   148                                                      
REMARK 465     ALA V   149                                                      
REMARK 465     ASN V   150                                                      
REMARK 465     ILE V   151                                                      
REMARK 465     THR V   152                                                      
REMARK 465     LEU V   153                                                      
REMARK 465     PRO V   154                                                      
REMARK 465     VAL V   155                                                      
REMARK 465     TYR V   156                                                      
REMARK 465     VAL V   194                                                      
REMARK 465     GLN V   195                                                      
REMARK 465     LYS V   196                                                      
REMARK 465     ASP V   197                                                      
REMARK 465     LEU V   198                                                      
REMARK 465     GLU V   199                                                      
REMARK 465     ARG V   200                                                      
REMARK 465     LEU V   201                                                      
REMARK 465     THR V   202                                                      
REMARK 465     GLN V   203                                                      
REMARK 465     GLU V   204                                                      
REMARK 465     ARG V   205                                                      
REMARK 465     ILE V   206                                                      
REMARK 465     ALA V   207                                                      
REMARK 465     HIS V   208                                                      
REMARK 465     GLN V   209                                                      
REMARK 465     ARG V   210                                                      
REMARK 465     MET V   211                                                      
REMARK 465     GLY V   212                                                      
REMARK 465     ASP V   213                                                      
REMARK 465     MET R     1                                                      
REMARK 465     ALA R     2                                                      
REMARK 465     ALA R     3                                                      
REMARK 465     ALA R     4                                                      
REMARK 465     MET R     5                                                      
REMARK 465     ASP R     6                                                      
REMARK 465     VAL R     7                                                      
REMARK 465     ASP R     8                                                      
REMARK 465     THR R     9                                                      
REMARK 465     PRO R    10                                                      
REMARK 465     SER R    11                                                      
REMARK 465     GLY R    12                                                      
REMARK 465     THR R    13                                                      
REMARK 465     ASN R    14                                                      
REMARK 465     SER R    15                                                      
REMARK 465     GLY R    16                                                      
REMARK 465     HIS B    10                                                      
REMARK 465     LYS B    11                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     LYS B    19                                                      
REMARK 465     GLU B    20                                                      
REMARK 465     SER B    21                                                      
REMARK 465     GLY B    61                                                      
REMARK 465     PHE B    62                                                      
REMARK 465     THR B    63                                                      
REMARK 465     VAL B    75                                                      
REMARK 465     GLY B    76                                                      
REMARK 465     LEU B    88                                                      
REMARK 465     CYS B    89                                                      
REMARK 465     ILE B    90                                                      
REMARK 465     GLU B    91                                                      
REMARK 465     GLU B    98                                                      
REMARK 465     LEU B    99                                                      
REMARK 465     PRO B   100                                                      
REMARK 465     ASP B   101                                                      
REMARK 465     VAL B   102                                                      
REMARK 465     MET B   103                                                      
REMARK 465     LYS B   104                                                      
REMARK 465     MET C    16                                                      
REMARK 465     PHE C    52                                                      
REMARK 465     GLU C    54                                                      
REMARK 465     ASN C    55                                                      
REMARK 465     GLU C    56                                                      
REMARK 465     THR C    57                                                      
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     TYR A  58    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL A  76    CG1  CG2                                            
REMARK 470     TYR A  90    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 136    CG   CD1  CD2                                       
REMARK 470     MET A 137    CG   SD   CE                                        
REMARK 470     TRP A 147    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 147    CZ3  CH2                                            
REMARK 470     LYS A 238    CG   CD   CE   NZ                                   
REMARK 470     HIS A 255    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TYR A 378    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 398    CG   CD1  CD2                                       
REMARK 470     PHE A 422    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 442    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A 449    CG   SD   CE                                        
REMARK 470     LYS A 462    CG   CD   CE   NZ                                   
REMARK 470     ILE A 494    CG1  CG2  CD1                                       
REMARK 470     PRO A 530    CG   CD                                             
REMARK 470     GLN A 531    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 532    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 533    CG   CD1  CD2                                       
REMARK 470     GLU A 534    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 535    CG   CD   CE   NZ                                   
REMARK 470     VAL A 537    CB   CG1  CG2                                       
REMARK 470     PHE A 540    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A 542    CG   CD1  CD2                                       
REMARK 470     ARG A 710    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 720    CG   CD   CE   NZ                                   
REMARK 470     TYR A 741    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ALA R  17    CB                                                  
REMARK 470     GLN R  57    CG   CD   OE1  NE2                                  
REMARK 470     TRP R 101    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP R 101    CZ3  CH2                                            
REMARK 470     ARG B   8    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B  12    OG1  CG2                                            
REMARK 470     ASP B  52    CG   OD1  OD2                                       
REMARK 470     ARG B  80    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B  82    CG   OD1  OD2                                       
REMARK 470     PHE B  85    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     ARG C  63    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR C  83    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR C  88    CB   OG1  CG2                                       
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    LEU A   533     N    LYS A   535              1.22            
REMARK 500   NE   ARG A   475     OE2  GLU R    66              2.09            
REMARK 500   C    LEU A   533     N    LYS A   535              2.12            
REMARK 500   O    LEU A   533     CA   LYS A   535              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 530   N   -  CA  -  CB  ANGL. DEV. =   7.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  47      -64.96   -122.95                                   
REMARK 500    PRO A  50       44.95    -82.04                                   
REMARK 500    GLU A  81       -2.80     67.60                                   
REMARK 500    GLU A 138       73.81     59.33                                   
REMARK 500    PRO A 154       -7.29    -55.55                                   
REMARK 500    HIS A 190      -21.54   -141.01                                   
REMARK 500    SER A 257       -7.44    -59.73                                   
REMARK 500    ALA A 272       -7.33     71.46                                   
REMARK 500    GLN A 332       -2.25     65.87                                   
REMARK 500    ASN A 334       57.48     35.62                                   
REMARK 500    ASN A 359       27.28     49.50                                   
REMARK 500    LYS A 386        1.68     58.33                                   
REMARK 500    ASN A 409       -0.98     66.12                                   
REMARK 500    ASN A 496       16.38   -140.40                                   
REMARK 500    GLN A 497     -148.15   -138.37                                   
REMARK 500    THR A 499     -163.04     54.43                                   
REMARK 500    ALA A 514       -0.85     67.14                                   
REMARK 500    LEU A 533     -169.34   -117.69                                   
REMARK 500    GLU A 534      -17.41     -5.83                                   
REMARK 500    LYS A 535     -148.79     73.23                                   
REMARK 500    SER A 536        6.32     92.74                                   
REMARK 500    LYS A 565       71.36     73.92                                   
REMARK 500    THR A 578      -51.22   -123.40                                   
REMARK 500    TYR A 580       62.12     66.18                                   
REMARK 500    SER A 595     -179.59    -68.82                                   
REMARK 500    VAL A 620      -69.54    -96.94                                   
REMARK 500    LYS A 621      -39.07   -135.03                                   
REMARK 500    GLN A 701      -16.85     75.58                                   
REMARK 500    SER A 707       30.02    -88.17                                   
REMARK 500    SER A 734      -61.25    -94.33                                   
REMARK 500    LYS R  26      130.45    -32.84                                   
REMARK 500    THR R  69      103.04   -161.28                                   
REMARK 500    ARG R  99     -168.47   -126.51                                   
REMARK 500    LYS B  46       74.83   -112.86                                   
REMARK 500    ASP B  47      -19.21     60.41                                   
REMARK 500    ASP B  48       -0.31   -149.06                                   
REMARK 500    ALA B  71       72.06   -161.08                                   
REMARK 500    ASP B  82      -67.53    -97.83                                   
REMARK 500    ASP B  83      -50.59   -126.52                                   
REMARK 500    ASP C 111       19.29     59.11                                   
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 R 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS R  45   SG                                                     
REMARK 620 2 CYS R  83   SG   94.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN R 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS R  53   SG                                                     
REMARK 620 2 CYS R  56   SG  112.6                                              
REMARK 620 3 HIS R  82   NE2  65.9  86.0                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN R 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN R 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN R 203                  
DBREF  5N4W A    1   745  UNP    Q13617   CUL2_HUMAN       1    745             
DBREF  5N4W V   54   213  UNP    P40337   VHL_HUMAN       54    213             
DBREF  5N4W R    1   102  UNP    P62877   RBX1_HUMAN       1    102             
DBREF  5N4W B    1   104  UNP    Q15370   ELOB_HUMAN       1    104             
DBREF  5N4W C   17   112  UNP    Q15369   ELOC_HUMAN      17    112             
SEQADV 5N4W GLY A   -2  UNP  Q13617              EXPRESSION TAG                 
SEQADV 5N4W GLY A   -1  UNP  Q13617              EXPRESSION TAG                 
SEQADV 5N4W SER A    0  UNP  Q13617              EXPRESSION TAG                 
SEQADV 5N4W LYS R   18  UNP  P62877    GLY    18 CONFLICT                       
SEQADV 5N4W MET C   16  UNP  Q15369              INITIATING METHIONINE          
SEQRES   1 A  748  GLY GLY SER MET SER LEU LYS PRO ARG VAL VAL ASP PHE          
SEQRES   2 A  748  ASP GLU THR TRP ASN LYS LEU LEU THR THR ILE LYS ALA          
SEQRES   3 A  748  VAL VAL MET LEU GLU TYR VAL GLU ARG ALA THR TRP ASN          
SEQRES   4 A  748  ASP ARG PHE SER ASP ILE TYR ALA LEU CYS VAL ALA TYR          
SEQRES   5 A  748  PRO GLU PRO LEU GLY GLU ARG LEU TYR THR GLU THR LYS          
SEQRES   6 A  748  ILE PHE LEU GLU ASN HIS VAL ARG HIS LEU HIS LYS ARG          
SEQRES   7 A  748  VAL LEU GLU SER GLU GLU GLN VAL LEU VAL MET TYR HIS          
SEQRES   8 A  748  ARG TYR TRP GLU GLU TYR SER LYS GLY ALA ASP TYR MET          
SEQRES   9 A  748  ASP CYS LEU TYR ARG TYR LEU ASN THR GLN PHE ILE LYS          
SEQRES  10 A  748  LYS ASN LYS LEU THR GLU ALA ASP LEU GLN TYR GLY TYR          
SEQRES  11 A  748  GLY GLY VAL ASP MET ASN GLU PRO LEU MET GLU ILE GLY          
SEQRES  12 A  748  GLU LEU ALA LEU ASP MET TRP ARG LYS LEU MET VAL GLU          
SEQRES  13 A  748  PRO LEU GLN ALA ILE LEU ILE ARG MET LEU LEU ARG GLU          
SEQRES  14 A  748  ILE LYS ASN ASP ARG GLY GLY GLU ASP PRO ASN GLN LYS          
SEQRES  15 A  748  VAL ILE HIS GLY VAL ILE ASN SER PHE VAL HIS VAL GLU          
SEQRES  16 A  748  GLN TYR LYS LYS LYS PHE PRO LEU LYS PHE TYR GLN GLU          
SEQRES  17 A  748  ILE PHE GLU SER PRO PHE LEU THR GLU THR GLY GLU TYR          
SEQRES  18 A  748  TYR LYS GLN GLU ALA SER ASN LEU LEU GLN GLU SER ASN          
SEQRES  19 A  748  CYS SER GLN TYR MET GLU LYS VAL LEU GLY ARG LEU LYS          
SEQRES  20 A  748  ASP GLU GLU ILE ARG CYS ARG LYS TYR LEU HIS PRO SER          
SEQRES  21 A  748  SER TYR THR LYS VAL ILE HIS GLU CYS GLN GLN ARG MET          
SEQRES  22 A  748  VAL ALA ASP HIS LEU GLN PHE LEU HIS ALA GLU CYS HIS          
SEQRES  23 A  748  ASN ILE ILE ARG GLN GLU LYS LYS ASN ASP MET ALA ASN          
SEQRES  24 A  748  MET TYR VAL LEU LEU ARG ALA VAL SER THR GLY LEU PRO          
SEQRES  25 A  748  HIS MET ILE GLN GLU LEU GLN ASN HIS ILE HIS ASP GLU          
SEQRES  26 A  748  GLY LEU ARG ALA THR SER ASN LEU THR GLN GLU ASN MET          
SEQRES  27 A  748  PRO THR LEU PHE VAL GLU SER VAL LEU GLU VAL HIS GLY          
SEQRES  28 A  748  LYS PHE VAL GLN LEU ILE ASN THR VAL LEU ASN GLY ASP          
SEQRES  29 A  748  GLN HIS PHE MET SER ALA LEU ASP LYS ALA LEU THR SER          
SEQRES  30 A  748  VAL VAL ASN TYR ARG GLU PRO LYS SER VAL CYS LYS ALA          
SEQRES  31 A  748  PRO GLU LEU LEU ALA LYS TYR CYS ASP ASN LEU LEU LYS          
SEQRES  32 A  748  LYS SER ALA LYS GLY MET THR GLU ASN GLU VAL GLU ASP          
SEQRES  33 A  748  ARG LEU THR SER PHE ILE THR VAL PHE LYS TYR ILE ASP          
SEQRES  34 A  748  ASP LYS ASP VAL PHE GLN LYS PHE TYR ALA ARG MET LEU          
SEQRES  35 A  748  ALA LYS ARG LEU ILE HIS GLY LEU SER MET SER MET ASP          
SEQRES  36 A  748  SER GLU GLU ALA MET ILE ASN LYS LEU LYS GLN ALA CYS          
SEQRES  37 A  748  GLY TYR GLU PHE THR SER LYS LEU HIS ARG MET TYR THR          
SEQRES  38 A  748  ASP MET SER VAL SER ALA ASP LEU ASN ASN LYS PHE ASN          
SEQRES  39 A  748  ASN PHE ILE LYS ASN GLN ASP THR VAL ILE ASP LEU GLY          
SEQRES  40 A  748  ILE SER PHE GLN ILE TYR VAL LEU GLN ALA GLY ALA TRP          
SEQRES  41 A  748  PRO LEU THR GLN ALA PRO SER SER THR PHE ALA ILE PRO          
SEQRES  42 A  748  GLN GLU LEU GLU LYS SER VAL GLN MET PHE GLU LEU PHE          
SEQRES  43 A  748  TYR SER GLN HIS PHE SER GLY ARG LYS LEU THR TRP LEU          
SEQRES  44 A  748  HIS TYR LEU CYS THR GLY GLU VAL LYS MET ASN TYR LEU          
SEQRES  45 A  748  GLY LYS PRO TYR VAL ALA MET VAL THR THR TYR GLN MET          
SEQRES  46 A  748  ALA VAL LEU LEU ALA PHE ASN ASN SER GLU THR VAL SER          
SEQRES  47 A  748  TYR LYS GLU LEU GLN ASP SER THR GLN MET ASN GLU LYS          
SEQRES  48 A  748  GLU LEU THR LYS THR ILE LYS SER LEU LEU ASP VAL LYS          
SEQRES  49 A  748  MET ILE ASN HIS ASP SER GLU LYS GLU ASP ILE ASP ALA          
SEQRES  50 A  748  GLU SER SER PHE SER LEU ASN MET ASN PHE SER SER LYS          
SEQRES  51 A  748  ARG THR LYS PHE LYS ILE THR THR SER MET GLN LYS ASP          
SEQRES  52 A  748  THR PRO GLN GLU MET GLU GLN THR ARG SER ALA VAL ASP          
SEQRES  53 A  748  GLU ASP ARG LYS MET TYR LEU GLN ALA ALA ILE VAL ARG          
SEQRES  54 A  748  ILE MET LYS ALA ARG LYS VAL LEU ARG HIS ASN ALA LEU          
SEQRES  55 A  748  ILE GLN GLU VAL ILE SER GLN SER ARG ALA ARG PHE ASN          
SEQRES  56 A  748  PRO SER ILE SER MET ILE LYS LYS CYS ILE GLU VAL LEU          
SEQRES  57 A  748  ILE ASP LYS GLN TYR ILE GLU ARG SER GLN ALA SER ALA          
SEQRES  58 A  748  ASP GLU TYR SER TYR VAL ALA                                  
SEQRES   1 V  160  MET GLU ALA GLY ARG PRO ARG PRO VAL LEU ARG SER VAL          
SEQRES   2 V  160  ASN SER ARG GLU PRO SER GLN VAL ILE PHE CYS ASN ARG          
SEQRES   3 V  160  SER PRO ARG VAL VAL LEU PRO VAL TRP LEU ASN PHE ASP          
SEQRES   4 V  160  GLY GLU PRO GLN PRO TYR PRO THR LEU PRO PRO GLY THR          
SEQRES   5 V  160  GLY ARG ARG ILE HIS SER TYR ARG GLY HIS LEU TRP LEU          
SEQRES   6 V  160  PHE ARG ASP ALA GLY THR HIS ASP GLY LEU LEU VAL ASN          
SEQRES   7 V  160  GLN THR GLU LEU PHE VAL PRO SER LEU ASN VAL ASP GLY          
SEQRES   8 V  160  GLN PRO ILE PHE ALA ASN ILE THR LEU PRO VAL TYR THR          
SEQRES   9 V  160  LEU LYS GLU ARG CYS LEU GLN VAL VAL ARG SER LEU VAL          
SEQRES  10 V  160  LYS PRO GLU ASN TYR ARG ARG LEU ASP ILE VAL ARG SER          
SEQRES  11 V  160  LEU TYR GLU ASP LEU GLU ASP HIS PRO ASN VAL GLN LYS          
SEQRES  12 V  160  ASP LEU GLU ARG LEU THR GLN GLU ARG ILE ALA HIS GLN          
SEQRES  13 V  160  ARG MET GLY ASP                                              
SEQRES   1 R  102  MET ALA ALA ALA MET ASP VAL ASP THR PRO SER GLY THR          
SEQRES   2 R  102  ASN SER GLY ALA LYS LYS LYS ARG PHE GLU VAL LYS LYS          
SEQRES   3 R  102  TRP ASN ALA VAL ALA LEU TRP ALA TRP ASP ILE VAL VAL          
SEQRES   4 R  102  ASP ASN CYS ALA ILE CYS ARG ASN HIS ILE MET ASP LEU          
SEQRES   5 R  102  CYS ILE GLU CYS GLN ALA ASN GLN ALA SER ALA THR SER          
SEQRES   6 R  102  GLU GLU CYS THR VAL ALA TRP GLY VAL CYS ASN HIS ALA          
SEQRES   7 R  102  PHE HIS PHE HIS CYS ILE SER ARG TRP LEU LYS THR ARG          
SEQRES   8 R  102  GLN VAL CYS PRO LEU ASP ASN ARG GLU TRP GLU                  
SEQRES   1 B  104  MET ASP VAL PHE LEU MET ILE ARG ARG HIS LYS THR THR          
SEQRES   2 B  104  ILE PHE THR ASP ALA LYS GLU SER SER THR VAL PHE GLU          
SEQRES   3 B  104  LEU LYS ARG ILE VAL GLU GLY ILE LEU LYS ARG PRO PRO          
SEQRES   4 B  104  ASP GLU GLN ARG LEU TYR LYS ASP ASP GLN LEU LEU ASP          
SEQRES   5 B  104  ASP GLY LYS THR LEU GLY GLU CYS GLY PHE THR SER GLN          
SEQRES   6 B  104  THR ALA ARG PRO GLN ALA PRO ALA THR VAL GLY LEU ALA          
SEQRES   7 B  104  PHE ARG ALA ASP ASP THR PHE GLU ALA LEU CYS ILE GLU          
SEQRES   8 B  104  PRO PHE SER SER PRO PRO GLU LEU PRO ASP VAL MET LYS          
SEQRES   1 C   97  MET MET TYR VAL LYS LEU ILE SER SER ASP GLY HIS GLU          
SEQRES   2 C   97  PHE ILE VAL LYS ARG GLU HIS ALA LEU THR SER GLY THR          
SEQRES   3 C   97  ILE LYS ALA MET LEU SER GLY PRO GLY GLN PHE ALA GLU          
SEQRES   4 C   97  ASN GLU THR ASN GLU VAL ASN PHE ARG GLU ILE PRO SER          
SEQRES   5 C   97  HIS VAL LEU SER LYS VAL CYS MET TYR PHE THR TYR LYS          
SEQRES   6 C   97  VAL ARG TYR THR ASN SER SER THR GLU ILE PRO GLU PHE          
SEQRES   7 C   97  PRO ILE ALA PRO GLU ILE ALA LEU GLU LEU LEU MET ALA          
SEQRES   8 C   97  ALA ASN PHE LEU ASP CYS                                      
HET     ZN  R 201       1                                                       
HET     ZN  R 202       1                                                       
HET     ZN  R 203       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   6   ZN    3(ZN 2+)                                                     
HELIX    1 AA1 ASP A   11  VAL A   25  1                                  15    
HELIX    2 AA2 MET A   26  GLU A   28  5                                   3    
HELIX    3 AA3 ALA A   33  PHE A   39  1                                   7    
HELIX    4 AA4 PHE A   39  ALA A   44  1                                   6    
HELIX    5 AA5 LEU A   53  SER A   79  1                                  27    
HELIX    6 AA6 GLN A   82  GLU A   93  1                                  12    
HELIX    7 AA7 TYR A   94  TYR A  105  1                                  12    
HELIX    8 AA8 TYR A  105  GLN A  111  1                                   7    
HELIX    9 AA9 GLU A  138  VAL A  152  1                                  15    
HELIX   10 AB1 PRO A  154  ASN A  169  1                                  16    
HELIX   11 AB2 ASN A  177  SER A  187  1                                  11    
HELIX   12 AB3 LEU A  200  PHE A  207  1                                   8    
HELIX   13 AB4 PHE A  207  GLN A  228  1                                  22    
HELIX   14 AB5 ASN A  231  LEU A  254  1                                  24    
HELIX   15 AB6 HIS A  255  SER A  257  5                                   3    
HELIX   16 AB7 SER A  258  MET A  270  1                                  13    
HELIX   17 AB8 HIS A  274  ILE A  286  1                                  13    
HELIX   18 AB9 ASP A  293  ALA A  303  1                                  11    
HELIX   19 AC1 GLY A  307  THR A  327  1                                  21    
HELIX   20 AC2 MET A  335  LEU A  358  1                                  24    
HELIX   21 AC3 GLN A  362  VAL A  376  1                                  15    
HELIX   22 AC4 LYS A  386  LYS A  400  1                                  15    
HELIX   23 AC5 GLU A  410  TYR A  424  1                                  15    
HELIX   24 AC6 ASP A  427  HIS A  445  1                                  19    
HELIX   25 AC7 SER A  450  CYS A  465  1                                  16    
HELIX   26 AC8 THR A  470  LYS A  495  1                                  26    
HELIX   27 AC9 VAL A  537  PHE A  548  1                                  12    
HELIX   28 AD1 THR A  613  ILE A  614  5                                   2    
HELIX   29 AD2 SER A  616  ASP A  619  5                                   4    
HELIX   30 AD3 PRO A  662  ARG A  669  1                                   8    
HELIX   31 AD4 SER A  670  ARG A  691  1                                  22    
HELIX   32 AD5 ARG A  695  ILE A  700  1                                   6    
HELIX   33 AD6 GLN A  701  SER A  707  1                                   7    
HELIX   34 AD7 SER A  714  ILE A  726  1                                  13    
HELIX   35 AD8 LEU V  158  ARG V  167  1                                  10    
HELIX   36 AD9 CYS R   53  GLN R   60  1                                   8    
HELIX   37 AE1 PHE R   81  ARG R   91  1                                  11    
HELIX   38 AE2 THR B   23  LYS B   36  1                                  14    
HELIX   39 AE3 PRO B   38  ASP B   40  5                                   3    
HELIX   40 AE4 LYS C   32  LEU C   37  1                                   6    
HELIX   41 AE5 SER C   39  SER C   47  1                                   9    
HELIX   42 AE6 PRO C   66  TYR C   83  1                                  18    
HELIX   43 AE7 ILE C   99  LEU C  110  1                                  12    
SHEET    1 AA1 3 PHE A 507  LEU A 512  0                                        
SHEET    2 AA1 3 TRP R  27  ALA R  34  1  O  ALA R  31   N  TYR A 510           
SHEET    3 AA1 3 LYS A 552  LEU A 556 -1  N  LYS A 552   O  ALA R  34           
SHEET    1 AA2 2 ILE A 731  GLU A 732  0                                        
SHEET    2 AA2 2 SER A 742  TYR A 743 -1  O  SER A 742   N  GLU A 732           
SHEET    1 AA3 2 VAL R  70  ALA R  71  0                                        
SHEET    2 AA3 2 PHE R  79  HIS R  80 -1  O  PHE R  79   N  ALA R  71           
SHEET    1 AA4 2 GLN B  42  ARG B  43  0                                        
SHEET    2 AA4 2 ALA B  78  PHE B  79 -1  O  ALA B  78   N  ARG B  43           
SHEET    1 AA5 3 ILE C  30  VAL C  31  0                                        
SHEET    2 AA5 3 VAL C  19  LEU C  21 -1  N  VAL C  19   O  VAL C  31           
SHEET    3 AA5 3 GLU C  59  VAL C  60  1  O  VAL C  60   N  LYS C  20           
LINK         SG  CYS R  45                ZN    ZN R 201     1555   1555  2.68  
LINK         SG  CYS R  53                ZN    ZN R 202     1555   1555  2.45  
LINK         SG  CYS R  56                ZN    ZN R 202     1555   1555  2.36  
LINK         SG  CYS R  75                ZN    ZN R 203     1555   1555  2.52  
LINK         NE2 HIS R  82                ZN    ZN R 202     1555   1555  2.32  
LINK         SG  CYS R  83                ZN    ZN R 201     1555   1555  2.88  
CISPEP   1 TYR A   49    PRO A   50          0       -25.53                     
CISPEP   2 GLU A  174    ASP A  175          0         0.44                     
CISPEP   3 GLY A  360    ASP A  361          0        -5.10                     
CISPEP   4 SER A  383    VAL A  384          0        -1.48                     
CISPEP   5 VAL A  384    CYS A  385          0         3.51                     
CISPEP   6 VAL R   38    VAL R   39          0        10.13                     
SITE     1 AC1  4 CYS R  42  CYS R  45  HIS R  80  CYS R  83                    
SITE     1 AC2  4 CYS R  53  CYS R  56  CYS R  68  HIS R  82                    
SITE     1 AC3  4 CYS R  75  HIS R  77  CYS R  94  ASP R  97                    
CRYST1   86.038  190.962  238.885  90.00  90.00  90.00 C 2 2 21      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      0.011623  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005237  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004186        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system