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Database: PDB
Entry: 6R7N
LinkDB: 6R7N
Original site: 6R7N 
HEADER    LIGASE                                  29-MAR-19   6R7N              
TITLE     STRUCTURAL BASIS OF CULLIN-2 RING E3 LIGASE REGULATION BY THE COP9    
TITLE    2 SIGNALOSOME                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COP9 SIGNALOSOME COMPLEX SUBUNIT 1;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SIGNALOSOME SUBUNIT 1,G PROTEIN PATHWAY SUPPRESSOR 1,GPS-1, 
COMPND   5 JAB1-CONTAINING SIGNALOSOME SUBUNIT 1,PROTEIN MFH;                   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: COP9 SIGNALOSOME COMPLEX SUBUNIT 4;                        
COMPND   9 CHAIN: D;                                                            
COMPND  10 SYNONYM: SIGNALOSOME SUBUNIT 4,JAB1-CONTAINING SIGNALOSOME SUBUNIT 4;
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: COP9 SIGNALOSOME COMPLEX SUBUNIT 8;                        
COMPND  14 CHAIN: H;                                                            
COMPND  15 SYNONYM: SIGNALOSOME SUBUNIT 8,COP9 HOMOLOG,HCOP9,JAB1-CONTAINING    
COMPND  16 SIGNALOSOME SUBUNIT 8;                                               
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: ELONGIN-B;                                                 
COMPND  20 CHAIN: P;                                                            
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: Q;                                                            
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;                                                     
COMPND  32 MOL_ID: 6;                                                           
COMPND  33 MOLECULE: RBX1 E3 UBIQUITIN-PROTEIN LIGASE;                          
COMPND  34 CHAIN: R;                                                            
COMPND  35 ENGINEERED: YES;                                                     
COMPND  36 MOL_ID: 7;                                                           
COMPND  37 MOLECULE: COP9 SIGNALOSOME COMPLEX SUBUNIT 3;                        
COMPND  38 CHAIN: C;                                                            
COMPND  39 SYNONYM: SIGNALOSOME SUBUNIT 3,JAB1-CONTAINING SIGNALOSOME SUBUNIT 3;
COMPND  40 ENGINEERED: YES;                                                     
COMPND  41 MOL_ID: 8;                                                           
COMPND  42 MOLECULE: CSN7B_HUMAN;                                               
COMPND  43 CHAIN: G;                                                            
COMPND  44 ENGINEERED: YES;                                                     
COMPND  45 MOL_ID: 9;                                                           
COMPND  46 MOLECULE: CULLIN-2;                                                  
COMPND  47 CHAIN: O;                                                            
COMPND  48 SYNONYM: CUL-2;                                                      
COMPND  49 ENGINEERED: YES;                                                     
COMPND  50 MOL_ID: 10;                                                          
COMPND  51 MOLECULE: COP9 SIGNALOSOME COMPLEX SUBUNIT 2;                        
COMPND  52 CHAIN: B;                                                            
COMPND  53 SYNONYM: SIGNALOSOME SUBUNIT 2,ALIEN HOMOLOG,JAB1-CONTAINING         
COMPND  54 SIGNALOSOME SUBUNIT 2,THYROID RECEPTOR-INTERACTING PROTEIN 15,TRIP-  
COMPND  55 15;                                                                  
COMPND  56 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: GPS1, COPS1, CSN1;                                             
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: COPS4, CSN4;                                                   
SOURCE  13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: COPS8, CSN8;                                                   
SOURCE  20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  24 ORGANISM_COMMON: HUMAN;                                              
SOURCE  25 ORGANISM_TAXID: 9606;                                                
SOURCE  26 GENE: ELOB, TCEB2;                                                   
SOURCE  27 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  29 MOL_ID: 5;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  31 ORGANISM_COMMON: HUMAN;                                              
SOURCE  32 ORGANISM_TAXID: 9606;                                                
SOURCE  33 GENE: ELOC, TCEB1;                                                   
SOURCE  34 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  35 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  36 MOL_ID: 6;                                                           
SOURCE  37 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  38 ORGANISM_TAXID: 9606;                                                
SOURCE  39 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  40 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  41 MOL_ID: 7;                                                           
SOURCE  42 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  43 ORGANISM_COMMON: HUMAN;                                              
SOURCE  44 ORGANISM_TAXID: 9606;                                                
SOURCE  45 GENE: COPS3, CSN3;                                                   
SOURCE  46 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  47 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  48 MOL_ID: 8;                                                           
SOURCE  49 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  50 ORGANISM_TAXID: 9606;                                                
SOURCE  51 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  52 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  53 MOL_ID: 9;                                                           
SOURCE  54 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  55 ORGANISM_COMMON: HUMAN;                                              
SOURCE  56 ORGANISM_TAXID: 9606;                                                
SOURCE  57 GENE: CUL2;                                                          
SOURCE  58 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  59 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  60 MOL_ID: 10;                                                          
SOURCE  61 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  62 ORGANISM_COMMON: HUMAN;                                              
SOURCE  63 ORGANISM_TAXID: 9606;                                                
SOURCE  64 GENE: COPS2, CSN2, TRIP15;                                           
SOURCE  65 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  66 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    CULLIN-RING E3 LIGASES (CRLS) COP9 SIGNALOSOME (CSN) DENEDDYLATION    
KEYWDS   2 VHL TUMOUR SUPPRESSOR SUBSTRATE RECEPTOR, LIGASE                     
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    S.V.FAULL,A.M.C.LAU,C.MARTENS,Z.AHDASH,H.YEBENES,C.SCHMIDT,F.BEURON,  
AUTHOR   2 N.B.CRONIN,E.P.MORRIS,A.POLITIS                                      
REVDAT   2   04-SEP-19 6R7N    1       JRNL                                     
REVDAT   1   28-AUG-19 6R7N    0                                                
JRNL        AUTH   S.V.FAULL,A.M.C.LAU,C.MARTENS,Z.AHDASH,K.HANSEN,H.YEBENES,   
JRNL        AUTH 2 C.SCHMIDT,F.BEURON,N.B.CRONIN,E.P.MORRIS,A.POLITIS           
JRNL        TITL   STRUCTURAL BASIS OF CULLIN 2 RING E3 LIGASE REGULATION BY    
JRNL        TITL 2 THE COP9 SIGNALOSOME.                                        
JRNL        REF    NAT COMMUN                    V.  10  3814 2019              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   31444342                                                     
JRNL        DOI    10.1038/S41467-019-11772-Y                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    6.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NULL                                      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : FLEXIBLE FIT                        
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 6.500                          
REMARK   3   NUMBER OF PARTICLES               : 22471                          
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 6R7N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-MAR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292101367.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : CNS (COP9 SIGNALOSOME) WITH       
REMARK 245                                    CSN5/CSN6 THE CATALYTIC           
REMARK 245                                    HETERODIMER COMPLEXED WITH CUL2   
REMARK 245                                    (CUL2, ELONGINB, ELONGINGC,       
REMARK 245                                    RBX1 AND VDL)                     
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : 1800.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 3000.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 45.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
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: DECAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, H, P, Q, R, C, G, O, B          
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    41                                                      
REMARK 465     PRO A    42                                                      
REMARK 465     LEU A    43                                                      
REMARK 465     PRO A    44                                                      
REMARK 465     VAL A    45                                                      
REMARK 465     GLN A    46                                                      
REMARK 465     VAL A    47                                                      
REMARK 465     PHE A    48                                                      
REMARK 465     ASN A    49                                                      
REMARK 465     LEU A    50                                                      
REMARK 465     GLN A    51                                                      
REMARK 465     GLY A    52                                                      
REMARK 465     ALA A    53                                                      
REMARK 465     VAL A    54                                                      
REMARK 465     GLU A    55                                                      
REMARK 465     PRO A    56                                                      
REMARK 465     MET A    57                                                      
REMARK 465     GLN A    58                                                      
REMARK 465     ILE A    59                                                      
REMARK 465     ASP A    60                                                      
REMARK 465     VAL A    61                                                      
REMARK 465     ASP A    62                                                      
REMARK 465     PRO A    63                                                      
REMARK 465     GLN A    64                                                      
REMARK 465     GLU A    65                                                      
REMARK 465     ASP A    66                                                      
REMARK 465     PRO A    67                                                      
REMARK 465     GLN A    68                                                      
REMARK 465     ASN A    69                                                      
REMARK 465     ALA A    70                                                      
REMARK 465     PRO A    71                                                      
REMARK 465     ASP A    72                                                      
REMARK 465     VAL A    73                                                      
REMARK 465     ASN A    74                                                      
REMARK 465     TYR A    75                                                      
REMARK 465     VAL A    76                                                      
REMARK 465     ARG A   142A                                                     
REMARK 465     SER A   142B                                                     
REMARK 465     SER A   142C                                                     
REMARK 465     LEU A   142D                                                     
REMARK 465     ASP A   150                                                      
REMARK 465     ALA A   151                                                      
REMARK 465     ILE A   152                                                      
REMARK 465     PRO A   153                                                      
REMARK 465     GLU A   154                                                      
REMARK 465     SER A   155                                                      
REMARK 465     GLY A   156                                                      
REMARK 465     VAL A   157                                                      
REMARK 465     GLU A   158                                                      
REMARK 465     PRO A   159                                                      
REMARK 465     PRO A   506                                                      
REMARK 465     ARG A   507                                                      
REMARK 465     GLU A   508                                                      
REMARK 465     GLY A   509                                                      
REMARK 465     SER A   510                                                      
REMARK 465     GLN A   511                                                      
REMARK 465     GLY A   512                                                      
REMARK 465     GLU A   513                                                      
REMARK 465     LEU A   514                                                      
REMARK 465     THR A   515                                                      
REMARK 465     PRO A   516                                                      
REMARK 465     ALA A   517                                                      
REMARK 465     ASN A   518                                                      
REMARK 465     SER A   519                                                      
REMARK 465     GLN A   520                                                      
REMARK 465     SER A   521                                                      
REMARK 465     ARG A   522                                                      
REMARK 465     MET A   523                                                      
REMARK 465     SER A   524                                                      
REMARK 465     THR A   525                                                      
REMARK 465     ASN A   526                                                      
REMARK 465     MET A   527                                                      
REMARK 465     VAL H   168                                                      
REMARK 465     ALA H   169                                                      
REMARK 465     GLY H   170                                                      
REMARK 465     ALA H   171                                                      
REMARK 465     LEU H   172                                                      
REMARK 465     ASP H   173                                                      
REMARK 465     VAL H   174                                                      
REMARK 465     SER H   175                                                      
REMARK 465     PHE H   176                                                      
REMARK 465     ASN H   177                                                      
REMARK 465     LYS H   178                                                      
REMARK 465     PHE H   179                                                      
REMARK 465     ILE H   180                                                      
REMARK 465     PRO H   181                                                      
REMARK 465     LEU H   182                                                      
REMARK 465     SER H   183                                                      
REMARK 465     GLU H   184                                                      
REMARK 465     PRO H   185                                                      
REMARK 465     ALA H   186                                                      
REMARK 465     PRO H   187                                                      
REMARK 465     VAL H   188                                                      
REMARK 465     PRO H   189                                                      
REMARK 465     PRO H   190                                                      
REMARK 465     ILE H   191                                                      
REMARK 465     PRO H   192                                                      
REMARK 465     ASN H   193                                                      
REMARK 465     GLU H   194                                                      
REMARK 465     GLN H   195                                                      
REMARK 465     GLN H   196                                                      
REMARK 465     ASN H   209                                                      
REMARK 465     MET Q     1                                                      
REMARK 465     ASP Q     2                                                      
REMARK 465     GLY Q     3                                                      
REMARK 465     GLU Q     4                                                      
REMARK 465     GLU Q     5                                                      
REMARK 465     LYS Q     6                                                      
REMARK 465     THR Q     7                                                      
REMARK 465     TYR Q     8                                                      
REMARK 465     GLY Q     9                                                      
REMARK 465     GLY Q    10                                                      
REMARK 465     CYS Q    11                                                      
REMARK 465     GLU Q    12                                                      
REMARK 465     GLY Q    13                                                      
REMARK 465     PRO Q    14                                                      
REMARK 465     ASP Q    15                                                      
REMARK 465     ALA Q    16                                                      
REMARK 465     GLY Q    50                                                      
REMARK 465     GLN Q    51                                                      
REMARK 465     PHE Q    52                                                      
REMARK 465     ALA Q    53                                                      
REMARK 465     GLU Q    54                                                      
REMARK 465     ASN Q    55                                                      
REMARK 465     GLU Q    56                                                      
REMARK 465     THR Q    57                                                      
REMARK 465     ALA O   121                                                      
REMARK 465     ASP O   122                                                      
REMARK 465     LEU O   123                                                      
REMARK 465     GLN O   124                                                      
REMARK 465     TYR O   125                                                      
REMARK 465     GLY O   126                                                      
REMARK 465     TYR O   127                                                      
REMARK 465     GLY O   128                                                      
REMARK 465     GLY O   129                                                      
REMARK 465     VAL O   130                                                      
REMARK 465     ASP O   131                                                      
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     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 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    GLU Q    64     CE2  TYR O    49              0.52            
REMARK 500   NE2  GLN D   390     CB   LYS G     6              0.60            
REMARK 500   CA   VAL A   418     CZ   ARG B   401              0.62            
REMARK 500   CG   PRO D   393     CG   LEU G    46              0.62            
REMARK 500   CD1  LEU O   159     CG1  VAL O   184              0.63            
REMARK 500   OE2  GLU D   394     C    LEU G    46              0.68            
REMARK 500   OD1  ASP A   454     OG1  THR C   316              0.68            
REMARK 500   CA   GLU D   394     CA   GLU G    45              0.69            
REMARK 500   CA   VAL O   574     CD1  TYR B    16              0.70            
REMARK 500   N    ALA D   397     OE1  GLU G    45              0.72            
REMARK 500   CD2  LEU O   164     CZ   PHE O   207              0.75            
REMARK 500   N    VAL O   574     CD1  TYR B    16              0.75            
REMARK 500   CB   LEU O    84     CG1  VAL O   180              0.77            
REMARK 500   NZ   LYS O   565     N    GLU B    13              0.77            
REMARK 500   O    PRO Q    66     CE   MET O     1              0.80            
REMARK 500   CA   VAL A   418     NE   ARG B   401              0.84            
REMARK 500   CE   MET O   151     CA   VAL O   191              0.84            
REMARK 500   CA   VAL O   574     CG   TYR B    16              0.85            
REMARK 500   SD   MET O   151     CG2  VAL O   191              0.85            
REMARK 500   CB   VAL O   574     CG   TYR B    16              0.87            
REMARK 500   OE2  GLU D   394     N    LEU G    47              0.90            
REMARK 500   CG   GLN D   390     O    GLN G     5              0.95            
REMARK 500   O    GLU Q    64     CZ   TYR O    49              0.96            
REMARK 500   O    PRO D   393     CG   GLU G    45              0.96            
REMARK 500   NE2  GLN D   380     CD1  PHE G   156              0.97            
REMARK 500   C    VAL A   418     CZ   ARG B   401              0.97            
REMARK 500   CE   MET O   151     CB   VAL O   191              1.00            
REMARK 500   CB   GLU D   394     C    GLY G    44              1.01            
REMARK 500   CA   GLU D   394     N    GLU G    45              1.02            
REMARK 500   CB   VAL O   574     CB   TYR B    16              1.03            
REMARK 500   O    ASN Q    61     SG   CYS O    46              1.03            
REMARK 500   CB   HIS A   456     CG2  THR C   316              1.04            
REMARK 500   OG1  THR D   391     CD1  ILE G   162              1.04            
REMARK 500   NE2  GLN D   390     CG   LYS G     6              1.04            
REMARK 500   CB   GLU D   394     N    GLU G    45              1.05            
REMARK 500   CB   THR D   396     OE2  GLU G    45              1.09            
REMARK 500   SD   MET A   478     NE2  GLN B   430              1.10            
REMARK 500   O    LEU H    25     CB   ARG C   119              1.10            
REMARK 500   CG   MET O   151     CG2  VAL O   191              1.11            
REMARK 500   N    ALA O   575     CE2  TYR B    16              1.11            
REMARK 500   C    PRO Q    66     CE   MET O     1              1.12            
REMARK 500   CG2  ILE O   160     CZ   PHE O   188              1.13            
REMARK 500   SD   MET O   151     CB   VAL O   191              1.14            
REMARK 500   CE2  TYR O    87     OG   SER O   187              1.20            
REMARK 500   C    GLU Q    64     CZ   TYR O    49              1.20            
REMARK 500   CG   LEU O   164     CE1  PHE O   207              1.22            
REMARK 500   CB   VAL A   418     NE   ARG B   401              1.25            
REMARK 500   NE2  GLN O   156     CD1  ILE O   206              1.26            
REMARK 500   CD   GLU D   394     N    LEU G    47              1.27            
REMARK 500   CA   ILE Q    65     OH   TYR O    49              1.30            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     382 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASP C 387   C     GLU C 388   N       0.156                       
REMARK 500    HIS B 413   C     GLN B 414   N       0.172                       
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    LEU P  99   C   -  N   -  CA  ANGL. DEV. =  17.0 DEGREES          
REMARK 500    SER O 656   C   -  N   -  CA  ANGL. DEV. =  18.2 DEGREES          
REMARK 500    LEU O 694   CB  -  CA  -  C   ANGL. DEV. = -14.2 DEGREES          
REMARK 500    GLU B  14   CB  -  CA  -  C   ANGL. DEV. =  13.0 DEGREES          
REMARK 500    GLY B  65   C   -  N   -  CA  ANGL. DEV. =  14.2 DEGREES          
REMARK 500    TRP B  67   CA  -  CB  -  CG  ANGL. DEV. = -29.6 DEGREES          
REMARK 500    PHE B  85   C   -  N   -  CA  ANGL. DEV. =  24.5 DEGREES          
REMARK 500    PRO B 229   C   -  N   -  CD  ANGL. DEV. = -12.7 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    SER A  92     -168.75   -163.95                                   
REMARK 500    ASN A 250       68.32   -100.33                                   
REMARK 500    PRO A 265       39.07    -85.05                                   
REMARK 500    ARG A 271      -33.81   -131.47                                   
REMARK 500    ASP A 275       82.46     61.14                                   
REMARK 500    SER A 276       77.09     70.38                                   
REMARK 500    GLN A 277      121.31    -38.24                                   
REMARK 500    ILE A 281      -55.54   -124.75                                   
REMARK 500    LEU A 308       42.00   -102.89                                   
REMARK 500    HIS A 313      -64.92    -93.87                                   
REMARK 500    LEU A 319      -33.76   -130.61                                   
REMARK 500    MET D  52       50.80    -92.01                                   
REMARK 500    LEU D 132      -72.53   -104.53                                   
REMARK 500    GLU D 133       14.49   -145.76                                   
REMARK 500    ALA D 366     -169.24   -160.81                                   
REMARK 500    GLU H  26      -63.92   -104.10                                   
REMARK 500    THR H  92       37.72    -97.99                                   
REMARK 500    THR H 158       -9.30     72.71                                   
REMARK 500    LYS P  36       62.60     64.19                                   
REMARK 500    ALA P  71       79.84   -156.60                                   
REMARK 500    ASP P  83       25.48   -140.14                                   
REMARK 500    LEU P  99      111.58    -37.83                                   
REMARK 500    ASP Q  25       33.83    -99.67                                   
REMARK 500    HIS Q  35       40.09   -106.93                                   
REMARK 500    PHE Q  62       46.35   -140.58                                   
REMARK 500    PHE R  22       63.78     65.23                                   
REMARK 500    ALA R  29     -169.34   -122.33                                   
REMARK 500    ALA R  43        0.75    -63.47                                   
REMARK 500    ASN R  76      -21.46     69.42                                   
REMARK 500    PHE R  79     -163.03   -117.82                                   
REMARK 500    ASN R  98       64.78     60.87                                   
REMARK 500    GLN C  18     -154.98   -121.70                                   
REMARK 500    SER C  31      -67.01     64.08                                   
REMARK 500    GLU C  33      -80.01     60.99                                   
REMARK 500    LEU C  46      -24.09   -143.03                                   
REMARK 500    LEU C  49      -60.49   -106.45                                   
REMARK 500    ASP C  50       44.07   -158.31                                   
REMARK 500    VAL C  51      -22.62     63.57                                   
REMARK 500    GLN C  52      177.73     66.68                                   
REMARK 500    MET C  68      -60.94     91.32                                   
REMARK 500    PRO C  69      -16.90    -47.99                                   
REMARK 500    SER C  70       52.58   -148.66                                   
REMARK 500    VAL C  71     -176.19     49.46                                   
REMARK 500    PRO C  72       -9.09    -58.94                                   
REMARK 500    SER C  86      -82.32    -65.16                                   
REMARK 500    ASN C  89      -97.58     40.95                                   
REMARK 500    HIS C  92       45.93    -91.33                                   
REMARK 500    ARG C 114     -104.23    -78.22                                   
REMARK 500    LYS C 115      -99.05   -143.14                                   
REMARK 500    PRO C 117       54.45   -101.94                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     118 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU A  266     ILE A  267                 -140.80                    
REMARK 500 GLN A  277     THR A  278                  146.36                    
REMARK 500 SER D   58     LEU D   59                 -142.16                    
REMARK 500 GLU D  133     THR D  134                 -148.47                    
REMARK 500 PRO H   28     GLY H   29                  149.33                    
REMARK 500 PHE P   79     ARG P   80                 -140.36                    
REMARK 500 GLU R   23     VAL R   24                 -145.43                    
REMARK 500 ILE R   37     VAL R   38                 -145.61                    
REMARK 500 CYS R   45     ARG R   46                 -147.78                    
REMARK 500 CYS R   75     ASN R   76                  148.40                    
REMARK 500 MET C   68     PRO C   69                  -55.30                    
REMARK 500 LYS G  164     LYS G  165                 -136.02                    
REMARK 500 LYS G  165     ASP G  166                  143.61                    
REMARK 500 LYS B  123     GLN B  124                 -148.13                    
REMARK 500 GLY B  191     THR B  192                  149.17                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    MET C  68        -10.66                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-4744   RELATED DB: EMDB                              
REMARK 900 STRUCTURAL BASIS OF CULLIN-2 RING E3 LIGASE REGULATION BY THE COP9   
REMARK 900 SIGNALOSOME                                                          
DBREF  6R7N A   41   527  UNP    Q13098   CSN1_HUMAN       1    491             
DBREF  6R7N D    1   406  UNP    Q9BT78   CSN4_HUMAN       1    406             
DBREF  6R7N H   11   209  UNP    Q99627   CSN8_HUMAN      11    209             
DBREF  6R7N P    1   104  UNP    Q15370   ELOB_HUMAN       1    104             
DBREF  6R7N Q    1   112  UNP    Q15369   ELOC_HUMAN       1    112             
DBREF  6R7N R   17   102  PDB    6R7N     6R7N            17    102             
DBREF  6R7N C    3   403  UNP    Q9UNS2   CSN3_HUMAN       3    403             
DBREF  6R7N G    1   215  PDB    6R7N     6R7N             1    215             
DBREF  6R7N O    1   745  UNP    Q13617   CUL2_HUMAN      20    764             
DBREF  6R7N B    1   443  UNP    P61201   CSN2_HUMAN       1    443             
SEQRES   1 A  491  MET PRO LEU PRO VAL GLN VAL PHE ASN LEU GLN GLY ALA          
SEQRES   2 A  491  VAL GLU PRO MET GLN ILE ASP VAL ASP PRO GLN GLU ASP          
SEQRES   3 A  491  PRO GLN ASN ALA PRO ASP VAL ASN TYR VAL VAL GLU ASN          
SEQRES   4 A  491  PRO SER LEU ASP LEU GLU GLN TYR ALA ALA SER TYR SER          
SEQRES   5 A  491  GLY LEU MET ARG ILE GLU ARG LEU GLN PHE ILE ALA ASP          
SEQRES   6 A  491  HIS CYS PRO THR LEU ARG VAL GLU ALA LEU LYS MET ALA          
SEQRES   7 A  491  LEU SER PHE VAL GLN ARG THR PHE ASN VAL ASP MET TYR          
SEQRES   8 A  491  GLU GLU ILE HIS ARG LYS LEU SER GLU ALA THR ARG SER          
SEQRES   9 A  491  SER LEU ARG GLU LEU GLN ASN ALA PRO ASP ALA ILE PRO          
SEQRES  10 A  491  GLU SER GLY VAL GLU PRO PRO ALA LEU ASP THR ALA TRP          
SEQRES  11 A  491  VAL GLU ALA THR ARG LYS LYS ALA LEU LEU LYS LEU GLU          
SEQRES  12 A  491  LYS LEU ASP THR ASP LEU LYS ASN TYR LYS GLY ASN SER          
SEQRES  13 A  491  ILE LYS GLU SER ILE ARG ARG GLY HIS ASP ASP LEU GLY          
SEQRES  14 A  491  ASP HIS TYR LEU ASP CYS GLY ASP LEU SER ASN ALA LEU          
SEQRES  15 A  491  LYS CYS TYR SER ARG ALA ARG ASP TYR CYS THR SER ALA          
SEQRES  16 A  491  LYS HIS VAL ILE ASN MET CYS LEU ASN VAL ILE LYS VAL          
SEQRES  17 A  491  SER VAL TYR LEU GLN ASN TRP SER HIS VAL LEU SER TYR          
SEQRES  18 A  491  VAL SER LYS ALA GLU SER THR PRO GLU ILE ALA GLU GLN          
SEQRES  19 A  491  ARG GLY GLU ARG ASP SER GLN THR GLN ALA ILE LEU THR          
SEQRES  20 A  491  LYS LEU LYS CYS ALA ALA GLY LEU ALA GLU LEU ALA ALA          
SEQRES  21 A  491  ARG LYS TYR LYS GLN ALA ALA LYS CYS LEU LEU LEU ALA          
SEQRES  22 A  491  SER PHE ASP HIS CYS ASP PHE PRO GLU LEU LEU SER PRO          
SEQRES  23 A  491  SER ASN VAL ALA ILE TYR GLY GLY LEU CYS ALA LEU ALA          
SEQRES  24 A  491  THR PHE ASP ARG GLN GLU LEU GLN ARG ASN VAL ILE SER          
SEQRES  25 A  491  SER SER SER PHE LYS LEU PHE LEU GLU LEU GLU PRO GLN          
SEQRES  26 A  491  VAL ARG ASP ILE ILE PHE LYS PHE TYR GLU SER LYS TYR          
SEQRES  27 A  491  ALA SER CYS LEU LYS MET LEU ASP GLU MET LYS ASP ASN          
SEQRES  28 A  491  LEU LEU LEU ASP MET TYR LEU ALA PRO HIS VAL ARG THR          
SEQRES  29 A  491  LEU TYR THR GLN ILE ARG ASN ARG ALA LEU ILE GLN TYR          
SEQRES  30 A  491  PHE SER PRO TYR VAL SER ALA ASP MET HIS ARG MET ALA          
SEQRES  31 A  491  ALA ALA PHE ASN THR THR VAL ALA ALA LEU GLU ASP GLU          
SEQRES  32 A  491  LEU THR GLN LEU ILE LEU GLU GLY LEU ILE SER ALA ARG          
SEQRES  33 A  491  VAL ASP SER HIS SER LYS ILE LEU TYR ALA ARG ASP VAL          
SEQRES  34 A  491  ASP GLN ARG SER THR THR PHE GLU LYS SER LEU LEU MET          
SEQRES  35 A  491  GLY LYS GLU PHE GLN ARG ARG ALA LYS ALA MET MET LEU          
SEQRES  36 A  491  ARG ALA ALA VAL LEU ARG ASN GLN ILE HIS VAL LYS SER          
SEQRES  37 A  491  PRO PRO ARG GLU GLY SER GLN GLY GLU LEU THR PRO ALA          
SEQRES  38 A  491  ASN SER GLN SER ARG MET SER THR ASN MET                      
SEQRES   1 D  406  MET ALA ALA ALA VAL ARG GLN ASP LEU ALA GLN LEU MET          
SEQRES   2 D  406  ASN SER SER GLY SER HIS LYS ASP LEU ALA GLY LYS TYR          
SEQRES   3 D  406  ARG GLN ILE LEU GLU LYS ALA ILE GLN LEU SER GLY ALA          
SEQRES   4 D  406  GLU GLN LEU GLU ALA LEU LYS ALA PHE VAL GLU ALA MET          
SEQRES   5 D  406  VAL ASN GLU ASN VAL SER LEU VAL ILE SER ARG GLN LEU          
SEQRES   6 D  406  LEU THR ASP PHE CYS THR HIS LEU PRO ASN LEU PRO ASP          
SEQRES   7 D  406  SER THR ALA LYS GLU ILE TYR HIS PHE THR LEU GLU LYS          
SEQRES   8 D  406  ILE GLN PRO ARG VAL ILE SER PHE GLU GLU GLN VAL ALA          
SEQRES   9 D  406  SER ILE ARG GLN HIS LEU ALA SER ILE TYR GLU LYS GLU          
SEQRES  10 D  406  GLU ASP TRP ARG ASN ALA ALA GLN VAL LEU VAL GLY ILE          
SEQRES  11 D  406  PRO LEU GLU THR GLY GLN LYS GLN TYR ASN VAL ASP TYR          
SEQRES  12 D  406  LYS LEU GLU THR TYR LEU LYS ILE ALA ARG LEU TYR LEU          
SEQRES  13 D  406  GLU ASP ASP ASP PRO VAL GLN ALA GLU ALA TYR ILE ASN          
SEQRES  14 D  406  ARG ALA SER LEU LEU GLN ASN GLU SER THR ASN GLU GLN          
SEQRES  15 D  406  LEU GLN ILE HIS TYR LYS VAL CYS TYR ALA ARG VAL LEU          
SEQRES  16 D  406  ASP TYR ARG ARG LYS PHE ILE GLU ALA ALA GLN ARG TYR          
SEQRES  17 D  406  ASN GLU LEU SER TYR LYS THR ILE VAL HIS GLU SER GLU          
SEQRES  18 D  406  ARG LEU GLU ALA LEU LYS HIS ALA LEU HIS CYS THR ILE          
SEQRES  19 D  406  LEU ALA SER ALA GLY GLN GLN ARG SER ARG MET LEU ALA          
SEQRES  20 D  406  THR LEU PHE LYS ASP GLU ARG CYS GLN GLN LEU ALA ALA          
SEQRES  21 D  406  TYR GLY ILE LEU GLU LYS MET TYR LEU ASP ARG ILE ILE          
SEQRES  22 D  406  ARG GLY ASN GLN LEU GLN GLU PHE ALA ALA MET LEU MET          
SEQRES  23 D  406  PRO HIS GLN LYS ALA THR THR ALA ASP GLY SER SER ILE          
SEQRES  24 D  406  LEU ASP ARG ALA VAL ILE GLU HIS ASN LEU LEU SER ALA          
SEQRES  25 D  406  SER LYS LEU TYR ASN ASN ILE THR PHE GLU GLU LEU GLY          
SEQRES  26 D  406  ALA LEU LEU GLU ILE PRO ALA ALA LYS ALA GLU LYS ILE          
SEQRES  27 D  406  ALA SER GLN MET ILE THR GLU GLY ARG MET ASN GLY PHE          
SEQRES  28 D  406  ILE ASP GLN ILE ASP GLY ILE VAL HIS PHE GLU THR ARG          
SEQRES  29 D  406  GLU ALA LEU PRO THR TRP ASP LYS GLN ILE GLN SER LEU          
SEQRES  30 D  406  CYS PHE GLN VAL ASN ASN LEU LEU GLU LYS ILE SER GLN          
SEQRES  31 D  406  THR ALA PRO GLU TRP THR ALA GLN ALA MET GLU ALA GLN          
SEQRES  32 D  406  MET ALA GLN                                                  
SEQRES   1 H  199  PHE SER PHE LYS LYS LEU LEU ASP GLN CYS GLU ASN GLN          
SEQRES   2 H  199  GLU LEU GLU ALA PRO GLY GLY ILE ALA THR PRO PRO VAL          
SEQRES   3 H  199  TYR GLY GLN LEU LEU ALA LEU TYR LEU LEU HIS ASN ASP          
SEQRES   4 H  199  MET ASN ASN ALA ARG TYR LEU TRP LYS ARG ILE PRO PRO          
SEQRES   5 H  199  ALA ILE LYS SER ALA ASN SER GLU LEU GLY GLY ILE TRP          
SEQRES   6 H  199  SER VAL GLY GLN ARG ILE TRP GLN ARG ASP PHE PRO GLY          
SEQRES   7 H  199  ILE TYR THR THR ILE ASN ALA HIS GLN TRP SER GLU THR          
SEQRES   8 H  199  VAL GLN PRO ILE MET GLU ALA LEU ARG ASP ALA THR ARG          
SEQRES   9 H  199  ARG ARG ALA PHE ALA LEU VAL SER GLN ALA TYR THR SER          
SEQRES  10 H  199  ILE ILE ALA ASP ASP PHE ALA ALA PHE VAL GLY LEU PRO          
SEQRES  11 H  199  VAL GLU GLU ALA VAL LYS GLY ILE LEU GLU GLN GLY TRP          
SEQRES  12 H  199  GLN ALA ASP SER THR THR ARG MET VAL LEU PRO ARG LYS          
SEQRES  13 H  199  PRO VAL ALA GLY ALA LEU ASP VAL SER PHE ASN LYS PHE          
SEQRES  14 H  199  ILE PRO LEU SER GLU PRO ALA PRO VAL PRO PRO ILE PRO          
SEQRES  15 H  199  ASN GLU GLN GLN LEU ALA ARG LEU THR ASP TYR VAL ALA          
SEQRES  16 H  199  PHE LEU GLU ASN                                              
SEQRES   1 P  104  MET ASP VAL PHE LEU MET ILE ARG ARG HIS LYS THR THR          
SEQRES   2 P  104  ILE PHE THR ASP ALA LYS GLU SER SER THR VAL PHE GLU          
SEQRES   3 P  104  LEU LYS ARG ILE VAL GLU GLY ILE LEU LYS ARG PRO PRO          
SEQRES   4 P  104  ASP GLU GLN ARG LEU TYR LYS ASP ASP GLN LEU LEU ASP          
SEQRES   5 P  104  ASP GLY LYS THR LEU GLY GLU CYS GLY PHE THR SER GLN          
SEQRES   6 P  104  THR ALA ARG PRO GLN ALA PRO ALA THR VAL GLY LEU ALA          
SEQRES   7 P  104  PHE ARG ALA ASP ASP THR PHE GLU ALA LEU CYS ILE GLU          
SEQRES   8 P  104  PRO PHE SER SER PRO PRO GLU LEU PRO ASP VAL MET LYS          
SEQRES   1 Q  112  MET ASP GLY GLU GLU LYS THR TYR GLY GLY CYS GLU GLY          
SEQRES   2 Q  112  PRO ASP ALA MET TYR VAL LYS LEU ILE SER SER ASP GLY          
SEQRES   3 Q  112  HIS GLU PHE ILE VAL LYS ARG GLU HIS ALA LEU THR SER          
SEQRES   4 Q  112  GLY THR ILE LYS ALA MET LEU SER GLY PRO GLY GLN PHE          
SEQRES   5 Q  112  ALA GLU ASN GLU THR ASN GLU VAL ASN PHE ARG GLU ILE          
SEQRES   6 Q  112  PRO SER HIS VAL LEU SER LYS VAL CYS MET TYR PHE THR          
SEQRES   7 Q  112  TYR LYS VAL ARG TYR THR ASN SER SER THR GLU ILE PRO          
SEQRES   8 Q  112  GLU PHE PRO ILE ALA PRO GLU ILE ALA LEU GLU LEU LEU          
SEQRES   9 Q  112  MET ALA ALA ASN PHE LEU ASP CYS                              
SEQRES   1 R   86  ALA LYS LYS LYS ARG PHE GLU VAL LYS LYS TRP ASN ALA          
SEQRES   2 R   86  VAL ALA LEU TRP ALA TRP ASP ILE VAL VAL ASP ASN CYS          
SEQRES   3 R   86  ALA ILE CYS ARG ASN HIS ILE MET ASP LEU CYS ILE GLU          
SEQRES   4 R   86  CYS GLN ALA ASN GLN ALA SER ALA THR SER GLU GLU CYS          
SEQRES   5 R   86  THR VAL ALA TRP GLY VAL CYS ASN HIS ALA PHE HIS PHE          
SEQRES   6 R   86  HIS CYS ILE SER ARG TRP LEU LYS THR ARG GLN VAL CYS          
SEQRES   7 R   86  PRO LEU ASP ASN ARG GLU TRP GLU                              
SEQRES   1 C  401  SER ALA LEU GLU GLN PHE VAL ASN SER VAL ARG GLN LEU          
SEQRES   2 C  401  SER ALA GLN GLY GLN MET THR GLN LEU CYS GLU LEU ILE          
SEQRES   3 C  401  ASN LYS SER GLY GLU LEU LEU ALA LYS ASN LEU SER HIS          
SEQRES   4 C  401  LEU ASP THR VAL LEU GLY ALA LEU ASP VAL GLN GLU HIS          
SEQRES   5 C  401  SER LEU GLY VAL LEU ALA VAL LEU PHE VAL LYS PHE SER          
SEQRES   6 C  401  MET PRO SER VAL PRO ASP PHE GLU THR LEU PHE SER GLN          
SEQRES   7 C  401  VAL GLN LEU PHE ILE SER THR CYS ASN GLY GLU HIS ILE          
SEQRES   8 C  401  ARG TYR ALA THR ASP THR PHE ALA GLY LEU CYS HIS GLN          
SEQRES   9 C  401  LEU THR ASN ALA LEU VAL GLU ARG LYS GLN PRO LEU ARG          
SEQRES  10 C  401  GLY ILE GLY ILE LEU LYS GLN ALA ILE ASP LYS MET GLN          
SEQRES  11 C  401  MET ASN THR ASN GLN LEU THR SER ILE HIS ALA ASP LEU          
SEQRES  12 C  401  CYS GLN LEU CYS LEU LEU ALA LYS CYS PHE LYS PRO ALA          
SEQRES  13 C  401  LEU PRO TYR LEU ASP VAL ASP MET MET ASP ILE CYS LYS          
SEQRES  14 C  401  GLU ASN GLY ALA TYR ASP ALA LYS HIS PHE LEU CYS TYR          
SEQRES  15 C  401  TYR TYR TYR GLY GLY MET ILE TYR THR GLY LEU LYS ASN          
SEQRES  16 C  401  PHE GLU ARG ALA LEU TYR PHE TYR GLU GLN ALA ILE THR          
SEQRES  17 C  401  THR PRO ALA MET ALA VAL SER HIS ILE MET LEU GLU SER          
SEQRES  18 C  401  TYR LYS LYS TYR ILE LEU VAL SER LEU ILE LEU LEU GLY          
SEQRES  19 C  401  LYS VAL GLN GLN LEU PRO LYS TYR THR SER GLN ILE VAL          
SEQRES  20 C  401  GLY ARG PHE ILE LYS PRO LEU SER ASN ALA TYR HIS GLU          
SEQRES  21 C  401  LEU ALA GLN VAL TYR SER THR ASN ASN PRO SER GLU LEU          
SEQRES  22 C  401  ARG ASN LEU VAL ASN LYS HIS SER GLU THR PHE THR ARG          
SEQRES  23 C  401  ASP ASN ASN MET GLY LEU VAL LYS GLN CYS LEU SER SER          
SEQRES  24 C  401  LEU TYR LYS LYS ASN ILE GLN ARG LEU THR LYS THR PHE          
SEQRES  25 C  401  LEU THR LEU SER LEU GLN ASP MET ALA SER ARG VAL GLN          
SEQRES  26 C  401  LEU SER GLY PRO GLN GLU ALA GLU LYS TYR VAL LEU HIS          
SEQRES  27 C  401  MET ILE GLU ASP GLY GLU ILE PHE ALA SER ILE ASN GLN          
SEQRES  28 C  401  LYS ASP GLY MET VAL SER PHE HIS ASP ASN PRO GLU LYS          
SEQRES  29 C  401  TYR ASN ASN PRO ALA MET LEU HIS ASN ILE ASP GLN GLU          
SEQRES  30 C  401  MET LEU LYS CYS ILE GLU LEU ASP GLU ARG LEU LYS ALA          
SEQRES  31 C  401  MET ASP GLN GLU ILE THR VAL ASN PRO GLN PHE                  
SEQRES   1 G  215  MET ALA GLY GLU GLN LYS PRO SER SER ASN LEU LEU GLU          
SEQRES   2 G  215  GLN PHE ILE LEU LEU ALA LYS GLY THR SER GLY SER ALA          
SEQRES   3 G  215  LEU THR ALA LEU ILE SER GLN VAL LEU GLU ALA PRO GLY          
SEQRES   4 G  215  VAL TYR VAL PHE GLY GLU LEU LEU GLU LEU ALA ASN VAL          
SEQRES   5 G  215  GLN GLU LEU ALA GLU GLY ALA ASN ALA ALA TYR LEU GLN          
SEQRES   6 G  215  LEU LEU ASN LEU PHE ALA TYR GLY THR TYR PRO ASP TYR          
SEQRES   7 G  215  ILE ALA ASN LYS GLU SER LEU PRO GLU LEU SER THR ALA          
SEQRES   8 G  215  GLN GLN ASN LYS LEU LYS HIS LEU THR ILE VAL SER LEU          
SEQRES   9 G  215  ALA SER ARG MET LYS CYS ILE PRO TYR SER VAL LEU LEU          
SEQRES  10 G  215  LYS ASP LEU GLU MET ARG ASN LEU ARG GLU LEU GLU ASP          
SEQRES  11 G  215  LEU ILE ILE GLU ALA VAL TYR THR ASP ILE ILE GLN GLY          
SEQRES  12 G  215  LYS LEU ASP GLN ARG ASN GLN LEU LEU GLU VAL ASP PHE          
SEQRES  13 G  215  CYS ILE GLY ARG ASP ILE ARG LYS LYS ASP LEU SER ALA          
SEQRES  14 G  215  ILE ALA ARG THR LEU GLN GLU TRP CYS VAL GLY CYS GLU          
SEQRES  15 G  215  VAL VAL LEU SER GLY ILE GLU GLU GLN VAL SER ARG ALA          
SEQRES  16 G  215  ASN GLN HIS LYS GLU GLN GLN LEU GLY LEU LYS GLN GLN          
SEQRES  17 G  215  ILE GLU SER GLU VAL ALA ASN                                  
SEQRES   1 O  745  MET SER LEU LYS PRO ARG VAL VAL ASP PHE ASP GLU THR          
SEQRES   2 O  745  TRP ASN LYS LEU LEU THR THR ILE LYS ALA VAL VAL MET          
SEQRES   3 O  745  LEU GLU TYR VAL GLU ARG ALA THR TRP ASN ASP ARG PHE          
SEQRES   4 O  745  SER ASP ILE TYR ALA LEU CYS VAL ALA TYR PRO GLU PRO          
SEQRES   5 O  745  LEU GLY GLU ARG LEU TYR THR GLU THR LYS ILE PHE LEU          
SEQRES   6 O  745  GLU ASN HIS VAL ARG HIS LEU HIS LYS ARG VAL LEU GLU          
SEQRES   7 O  745  SER GLU GLU GLN VAL LEU VAL MET TYR HIS ARG TYR TRP          
SEQRES   8 O  745  GLU GLU TYR SER LYS GLY ALA ASP TYR MET ASP CYS LEU          
SEQRES   9 O  745  TYR ARG TYR LEU ASN THR GLN PHE ILE LYS LYS ASN LYS          
SEQRES  10 O  745  LEU THR GLU ALA ASP LEU GLN TYR GLY TYR GLY GLY VAL          
SEQRES  11 O  745  ASP MET ASN GLU PRO LEU MET GLU ILE GLY GLU LEU ALA          
SEQRES  12 O  745  LEU ASP MET TRP ARG LYS LEU MET VAL GLU PRO LEU GLN          
SEQRES  13 O  745  ALA ILE LEU ILE ARG MET LEU LEU ARG GLU ILE LYS ASN          
SEQRES  14 O  745  ASP ARG GLY GLY GLU ASP PRO ASN GLN LYS VAL ILE HIS          
SEQRES  15 O  745  GLY VAL ILE ASN SER PHE VAL HIS VAL GLU GLN TYR LYS          
SEQRES  16 O  745  LYS LYS PHE PRO LEU LYS PHE TYR GLN GLU ILE PHE GLU          
SEQRES  17 O  745  SER PRO PHE LEU THR GLU THR GLY GLU TYR TYR LYS GLN          
SEQRES  18 O  745  GLU ALA SER ASN LEU LEU GLN GLU SER ASN CYS SER GLN          
SEQRES  19 O  745  TYR MET GLU LYS VAL LEU GLY ARG LEU LYS ASP GLU GLU          
SEQRES  20 O  745  ILE ARG CYS ARG LYS TYR LEU HIS PRO SER SER TYR THR          
SEQRES  21 O  745  LYS VAL ILE HIS GLU CYS GLN GLN ARG MET VAL ALA ASP          
SEQRES  22 O  745  HIS LEU GLN PHE LEU HIS ALA GLU CYS HIS ASN ILE ILE          
SEQRES  23 O  745  ARG GLN GLU LYS LYS ASN ASP MET ALA ASN MET TYR VAL          
SEQRES  24 O  745  LEU LEU ARG ALA VAL SER THR GLY LEU PRO HIS MET ILE          
SEQRES  25 O  745  GLN GLU LEU GLN ASN HIS ILE HIS ASP GLU GLY LEU ARG          
SEQRES  26 O  745  ALA THR SER ASN LEU THR GLN GLU ASN MET PRO THR LEU          
SEQRES  27 O  745  PHE VAL GLU SER VAL LEU GLU VAL HIS GLY LYS PHE VAL          
SEQRES  28 O  745  GLN LEU ILE ASN THR VAL LEU ASN GLY ASP GLN HIS PHE          
SEQRES  29 O  745  MET SER ALA LEU ASP LYS ALA LEU THR SER VAL VAL ASN          
SEQRES  30 O  745  TYR ARG GLU PRO LYS SER VAL CYS LYS ALA PRO GLU LEU          
SEQRES  31 O  745  LEU ALA LYS TYR CYS ASP ASN LEU LEU LYS LYS SER ALA          
SEQRES  32 O  745  LYS GLY MET THR GLU ASN GLU VAL GLU ASP ARG LEU THR          
SEQRES  33 O  745  SER PHE ILE THR VAL PHE LYS TYR ILE ASP ASP LYS ASP          
SEQRES  34 O  745  VAL PHE GLN LYS PHE TYR ALA ARG MET LEU ALA LYS ARG          
SEQRES  35 O  745  LEU ILE HIS GLY LEU SER MET SER MET ASP SER GLU GLU          
SEQRES  36 O  745  ALA MET ILE ASN LYS LEU LYS GLN ALA CYS GLY TYR GLU          
SEQRES  37 O  745  PHE THR SER LYS LEU HIS ARG MET TYR THR ASP MET SER          
SEQRES  38 O  745  VAL SER ALA ASP LEU ASN ASN LYS PHE ASN ASN PHE ILE          
SEQRES  39 O  745  LYS ASN GLN ASP THR VAL ILE ASP LEU GLY ILE SER PHE          
SEQRES  40 O  745  GLN ILE TYR VAL LEU GLN ALA GLY ALA TRP PRO LEU THR          
SEQRES  41 O  745  GLN ALA PRO SER SER THR PHE ALA ILE PRO GLN GLU LEU          
SEQRES  42 O  745  GLU LYS SER VAL GLN MET PHE GLU LEU PHE TYR SER GLN          
SEQRES  43 O  745  HIS PHE SER GLY ARG LYS LEU THR TRP LEU HIS TYR LEU          
SEQRES  44 O  745  CYS THR GLY GLU VAL LYS MET ASN TYR LEU GLY LYS PRO          
SEQRES  45 O  745  TYR VAL ALA MET VAL THR THR TYR GLN MET ALA VAL LEU          
SEQRES  46 O  745  LEU ALA PHE ASN ASN SER GLU THR VAL SER TYR LYS GLU          
SEQRES  47 O  745  LEU GLN ASP SER THR GLN MET ASN GLU LYS GLU LEU THR          
SEQRES  48 O  745  LYS THR ILE LYS SER LEU LEU ASP VAL LYS MET ILE ASN          
SEQRES  49 O  745  HIS ASP SER GLU LYS GLU ASP ILE ASP ALA GLU SER SER          
SEQRES  50 O  745  PHE SER LEU ASN MET ASN PHE SER SER LYS ARG THR LYS          
SEQRES  51 O  745  PHE LYS ILE THR THR SER MET GLN LYS ASP THR PRO GLN          
SEQRES  52 O  745  GLU MET GLU GLN THR ARG SER ALA VAL ASP GLU ASP ARG          
SEQRES  53 O  745  LYS MET TYR LEU GLN ALA ALA ILE VAL ARG ILE MET LYS          
SEQRES  54 O  745  ALA ARG LYS VAL LEU ARG HIS ASN ALA LEU ILE GLN GLU          
SEQRES  55 O  745  VAL ILE SER GLN SER ARG ALA ARG PHE ASN PRO SER ILE          
SEQRES  56 O  745  SER MET ILE LYS LYS CYS ILE GLU VAL LEU ILE ASP LYS          
SEQRES  57 O  745  GLN TYR ILE GLU ARG SER GLN ALA SER ALA ASP GLU TYR          
SEQRES  58 O  745  SER TYR VAL ALA                                              
SEQRES   1 B  443  MET SER ASP MET GLU ASP ASP PHE MET CYS ASP ASP GLU          
SEQRES   2 B  443  GLU ASP TYR ASP LEU GLU TYR SER GLU ASP SER ASN SER          
SEQRES   3 B  443  GLU PRO ASN VAL ASP LEU GLU ASN GLN TYR TYR ASN SER          
SEQRES   4 B  443  LYS ALA LEU LYS GLU ASP ASP PRO LYS ALA ALA LEU SER          
SEQRES   5 B  443  SER PHE GLN LYS VAL LEU GLU LEU GLU GLY GLU LYS GLY          
SEQRES   6 B  443  GLU TRP GLY PHE LYS ALA LEU LYS GLN MET ILE LYS ILE          
SEQRES   7 B  443  ASN PHE LYS LEU THR ASN PHE PRO GLU MET MET ASN ARG          
SEQRES   8 B  443  TYR LYS GLN LEU LEU THR TYR ILE ARG SER ALA VAL THR          
SEQRES   9 B  443  ARG ASN TYR SER GLU LYS SER ILE ASN SER ILE LEU ASP          
SEQRES  10 B  443  TYR ILE SER THR SER LYS GLN MET ASP LEU LEU GLN GLU          
SEQRES  11 B  443  PHE TYR GLU THR THR LEU GLU ALA LEU LYS ASP ALA LYS          
SEQRES  12 B  443  ASN ASP ARG LEU TRP PHE LYS THR ASN THR LYS LEU GLY          
SEQRES  13 B  443  LYS LEU TYR LEU GLU ARG GLU GLU TYR GLY LYS LEU GLN          
SEQRES  14 B  443  LYS ILE LEU ARG GLN LEU HIS GLN SER CYS GLN THR ASP          
SEQRES  15 B  443  ASP GLY GLU ASP ASP LEU LYS LYS GLY THR GLN LEU LEU          
SEQRES  16 B  443  GLU ILE TYR ALA LEU GLU ILE GLN MET TYR THR ALA GLN          
SEQRES  17 B  443  LYS ASN ASN LYS LYS LEU LYS ALA LEU TYR GLU GLN SER          
SEQRES  18 B  443  LEU HIS ILE LYS SER ALA ILE PRO HIS PRO LEU ILE MET          
SEQRES  19 B  443  GLY VAL ILE ARG GLU CYS GLY GLY LYS MET HIS LEU ARG          
SEQRES  20 B  443  GLU GLY GLU PHE GLU LYS ALA HIS THR ASP PHE PHE GLU          
SEQRES  21 B  443  ALA PHE LYS ASN TYR ASP GLU SER GLY SER PRO ARG ARG          
SEQRES  22 B  443  THR THR CYS LEU LYS TYR LEU VAL LEU ALA ASN MET LEU          
SEQRES  23 B  443  MET LYS SER GLY ILE ASN PRO PHE ASP SER GLN GLU ALA          
SEQRES  24 B  443  LYS PRO TYR LYS ASN ASP PRO GLU ILE LEU ALA MET THR          
SEQRES  25 B  443  ASN LEU VAL SER ALA TYR GLN ASN ASN ASP ILE THR GLU          
SEQRES  26 B  443  PHE GLU LYS ILE LEU LYS THR ASN HIS SER ASN ILE MET          
SEQRES  27 B  443  ASP ASP PRO PHE ILE ARG GLU HIS ILE GLU GLU LEU LEU          
SEQRES  28 B  443  ARG ASN ILE ARG THR GLN VAL LEU ILE LYS LEU ILE LYS          
SEQRES  29 B  443  PRO TYR THR ARG ILE HIS ILE PRO PHE ILE SER LYS GLU          
SEQRES  30 B  443  LEU ASN ILE ASP VAL ALA ASP VAL GLU SER LEU LEU VAL          
SEQRES  31 B  443  GLN CYS ILE LEU ASP ASN THR ILE HIS GLY ARG ILE ASP          
SEQRES  32 B  443  GLN VAL ASN GLN LEU LEU GLU LEU ASP HIS GLN LYS ARG          
SEQRES  33 B  443  GLY GLY ALA ARG TYR THR ALA LEU ASP LYS TRP THR ASN          
SEQRES  34 B  443  GLN LEU ASN SER LEU ASN GLN ALA VAL VAL SER LYS LEU          
SEQRES  35 B  443  ALA                                                          
HET     ZN  R 201       1                                                       
HET     ZN  R 202       1                                                       
HET     ZN  R 203       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL  11   ZN    3(ZN 2+)                                                     
HELIX    1 AA1 ASP A   83  SER A   90  1                                   8    
HELIX    2 AA2 GLY A   93  HIS A  106  1                                  14    
HELIX    3 AA3 ARG A  111  GLN A  123  1                                  13    
HELIX    4 AA4 VAL A  128  LEU A  145  1                                  18    
HELIX    5 AA5 ASP A  163  SER A  192  1                                  30    
HELIX    6 AA6 ILE A  193  GLY A  212  1                                  20    
HELIX    7 AA7 ASP A  213  ARG A  223  1                                  11    
HELIX    8 AA8 SER A  230  GLN A  249  1                                  20    
HELIX    9 AA9 HIS A  253  SER A  263  1                                  11    
HELIX   10 AB1 PRO A  265  ARG A  271  1                                   7    
HELIX   11 AB2 ILE A  281  ALA A  296  1                                  16    
HELIX   12 AB3 LYS A  298  LEU A  307  1                                  10    
HELIX   13 AB4 SER A  321  PHE A  337  1                                  17    
HELIX   14 AB5 ASP A  338  ASN A  345  1                                   8    
HELIX   15 AB6 PHE A  352  LEU A  358  1                                   7    
HELIX   16 AB7 GLU A  359  GLU A  371  1                                  13    
HELIX   17 AB8 LYS A  373  LEU A  390  1                                  18    
HELIX   18 AB9 LEU A  394  SER A  415  1                                  22    
HELIX   19 AC1 ASP A  421  PHE A  429  1                                   9    
HELIX   20 AC2 VAL A  433  GLY A  447  1                                  15    
HELIX   21 AC3 ASP A  466  ARG A  497  1                                  32    
HELIX   22 AC4 ALA D    3  ASN D   14  1                                  12    
HELIX   23 AC5 SER D   18  GLN D   35  1                                  18    
HELIX   24 AC6 GLY D   38  MET D   52  1                                  15    
HELIX   25 AC7 SER D   58  LEU D   73  1                                  16    
HELIX   26 AC8 PRO D   74  LEU D   76  5                                   3    
HELIX   27 AC9 PRO D   77  GLN D   93  1                                  17    
HELIX   28 AD1 PHE D   99  GLU D  117  1                                  19    
HELIX   29 AD2 ASP D  119  LEU D  127  1                                   9    
HELIX   30 AD3 ASN D  140  ASP D  158  1                                  19    
HELIX   31 AD4 ASP D  160  GLN D  175  1                                  16    
HELIX   32 AD5 ASN D  180  ARG D  199  1                                  20    
HELIX   33 AD6 LYS D  200  TYR D  213  1                                  14    
HELIX   34 AD7 HIS D  218  LEU D  235  1                                  18    
HELIX   35 AD8 GLY D  239  LYS D  251  1                                  13    
HELIX   36 AD9 ASP D  252  GLN D  257  1                                   6    
HELIX   37 AE1 ALA D  260  LEU D  269  1                                  10    
HELIX   38 AE2 ARG D  274  MET D  284  1                                  11    
HELIX   39 AE3 MET D  286  ALA D  291  5                                   6    
HELIX   40 AE4 SER D  298  LEU D  315  1                                  18    
HELIX   41 AE5 PHE D  321  LEU D  328  1                                   8    
HELIX   42 AE6 PRO D  331  GLU D  345  1                                  15    
HELIX   43 AE7 ALA D  366  THR D  391  1                                  26    
HELIX   44 AE8 ALA D  392  GLN D  406  1                                  15    
HELIX   45 AE9 SER H   12  LEU H   25  1                                  14    
HELIX   46 AF1 THR H   33  LEU H   46  1                                  14    
HELIX   47 AF2 ASP H   49  ILE H   60  1                                  12    
HELIX   48 AF3 PRO H   61  ASN H   68  1                                   8    
HELIX   49 AF4 SER H   69  GLN H   83  1                                  15    
HELIX   50 AF5 ASP H   85  THR H   92  1                                   8    
HELIX   51 AF6 VAL H  102  TYR H  125  1                                  24    
HELIX   52 AF7 ALA H  130  GLY H  138  1                                   9    
HELIX   53 AF8 PRO H  140  GLY H  152  1                                  13    
HELIX   54 AF9 ALA H  198  LEU H  207  1                                  10    
HELIX   55 AG1 VAL P   24  LYS P   36  1                                  13    
HELIX   56 AG2 THR P   56  GLY P   61  1                                   6    
HELIX   57 AG3 HIS Q   35  SER Q   39  5                                   5    
HELIX   58 AG4 GLY Q   40  MET Q   45  1                                   6    
HELIX   59 AG5 PRO Q   66  TYR Q   83  1                                  18    
HELIX   60 AG6 ALA Q   96  ALA Q  100  5                                   5    
HELIX   61 AG7 LEU Q  101  LEU Q  110  1                                  10    
HELIX   62 AG8 HIS R   80  THR R   90  1                                  11    
HELIX   63 AG9 ALA C    4  SER C   16  1                                  13    
HELIX   64 AH1 MET C   21  SER C   31  1                                  11    
HELIX   65 AH2 LYS C   37  ASP C   43  1                                   7    
HELIX   66 AH3 GLU C   53  LYS C   65  1                                  13    
HELIX   67 AH4 ASP C   73  SER C   86  1                                  14    
HELIX   68 AH5 ALA C   96  ARG C  114  1                                  19    
HELIX   69 AH6 LEU C  118  GLN C  132  1                                  15    
HELIX   70 AH7 SER C  140  ALA C  152  1                                  13    
HELIX   71 AH8 PHE C  155  LEU C  162  5                                   8    
HELIX   72 AH9 ASP C  177  LEU C  195  1                                  19    
HELIX   73 AI1 ASN C  197  THR C  210  1                                  14    
HELIX   74 AI2 SER C  217  LEU C  235  1                                  19    
HELIX   75 AI3 SER C  246  PHE C  252  1                                   7    
HELIX   76 AI4 PHE C  252  SER C  257  1                                   6    
HELIX   77 AI5 SER C  257  SER C  268  1                                  12    
HELIX   78 AI6 ASN C  271  HIS C  282  1                                  12    
HELIX   79 AI7 HIS C  282  ASP C  289  1                                   8    
HELIX   80 AI8 GLY C  293  ARG C  309  1                                  17    
HELIX   81 AI9 LEU C  319  VAL C  326  1                                   8    
HELIX   82 AJ1 GLY C  330  ASP C  344  1                                  15    
HELIX   83 AJ2 ASN C  369  VAL C  399  1                                  31    
HELIX   84 AJ3 ASN G   10  THR G   22  1                                  13    
HELIX   85 AJ4 GLY G   24  LEU G   35  1                                  12    
HELIX   86 AJ5 LEU G   49  ALA G   56  1                                   8    
HELIX   87 AJ6 ASN G   60  TYR G   72  1                                  13    
HELIX   88 AJ7 THR G   74  ASN G   81  1                                   8    
HELIX   89 AJ8 SER G   89  MET G  108  1                                  20    
HELIX   90 AJ9 PRO G  112  LEU G  120  1                                   9    
HELIX   91 AK1 ASN G  124  THR G  138  1                                  15    
HELIX   92 AK2 ASP G  166  ALA G  214  1                                  49    
HELIX   93 AK3 PHE O   10  ALA O   23  1                                  14    
HELIX   94 AK4 GLU O   31  ALA O   48  1                                  18    
HELIX   95 AK5 TYR O   49  VAL O   76  1                                  28    
HELIX   96 AK6 GLU O   81  ILE O  113  1                                  33    
HELIX   97 AK7 GLU O  138  LYS O  149  1                                  12    
HELIX   98 AK8 VAL O  152  ILE O  158  1                                   7    
HELIX   99 AK9 ILE O  158  GLY O  172  1                                  15    
HELIX  100 AL1 ASN O  177  VAL O  191  1                                  15    
HELIX  101 AL2 LEU O  200  PHE O  207  1                                   8    
HELIX  102 AL3 PHE O  207  SER O  230  1                                  24    
HELIX  103 AL4 ASN O  231  TYR O  253  1                                  23    
HELIX  104 AL5 SER O  257  ALA O  272  1                                  16    
HELIX  105 AL6 LEU O  275  GLN O  288  1                                  14    
HELIX  106 AL7 LYS O  290  VAL O  304  1                                  15    
HELIX  107 AL8 GLY O  307  ALA O  326  1                                  20    
HELIX  108 AL9 MET O  335  THR O  356  1                                  22    
HELIX  109 AM1 ASP O  361  ASN O  377  1                                  17    
HELIX  110 AM2 CYS O  385  LEU O  399  1                                  15    
HELIX  111 AM3 ASN O  409  LYS O  423  1                                  15    
HELIX  112 AM4 ASP O  427  GLY O  446  1                                  20    
HELIX  113 AM5 MET O  451  CYS O  465  1                                  15    
HELIX  114 AM6 GLY O  466  PHE O  493  1                                  28    
HELIX  115 AM7 PRO O  530  PHE O  548  1                                  19    
HELIX  116 AM8 THR O  579  SER O  591  1                                  13    
HELIX  117 AM9 SER O  595  GLN O  604  1                                  10    
HELIX  118 AN1 GLU O  609  LYS O  621  1                                  13    
HELIX  119 AN2 LYS O  659  LYS O  689  1                                  31    
HELIX  120 AN3 ARG O  695  ILE O  700  5                                   6    
HELIX  121 AN4 GLU O  702  ARG O  708  1                                   7    
HELIX  122 AN5 MET O  717  ILE O  726  1                                  10    
HELIX  123 AN6 MET B    4  ASN B   25  1                                  22    
HELIX  124 AN7 GLU B   33  LEU B   42  1                                  10    
HELIX  125 AN8 ALA B   50  LEU B   58  1                                   9    
HELIX  126 AN9 TRP B   67  LEU B   82  1                                  16    
HELIX  127 AO1 PHE B   85  THR B   97  1                                  13    
HELIX  128 AO2 THR B  104  LYS B  123  1                                  20    
HELIX  129 AO3 LEU B  127  LEU B  139  1                                  13    
HELIX  130 AO4 ARG B  146  GLU B  163  1                                  18    
HELIX  131 AO5 GLU B  164  GLN B  177  1                                  14    
HELIX  132 AO6 CYS B  179  ASP B  183  5                                   5    
HELIX  133 AO7 LEU B  195  LYS B  209  1                                  15    
HELIX  134 AO8 ASN B  210  SER B  221  1                                  12    
HELIX  135 AO9 LEU B  222  SER B  226  5                                   5    
HELIX  136 AP1 ILE B  233  GLY B  249  1                                  17    
HELIX  137 AP2 GLU B  250  GLY B  269  1                                  20    
HELIX  138 AP3 ARG B  272  LYS B  288  1                                  17    
HELIX  139 AP4 GLU B  298  LYS B  303  1                                   6    
HELIX  140 AP5 ILE B  308  ASN B  320  1                                  13    
HELIX  141 AP6 ASP B  322  ASN B  333  1                                  12    
HELIX  142 AP7 ASP B  340  LYS B  364  1                                  25    
HELIX  143 AP8 ILE B  371  ASN B  379  1                                   9    
HELIX  144 AP9 ASP B  381  ASN B  396  1                                  16    
HELIX  145 AQ1 ALA B  419  LEU B  442  1                                  24    
SHEET    1 AA1 2 ALA A 451  ASP A 454  0                                        
SHEET    2 AA1 2 ILE A 459  ALA A 462 -1  O  TYR A 461   N  ARG A 452           
SHEET    1 AA2 3 ASN D 318  THR D 320  0                                        
SHEET    2 AA2 3 ILE D 358  PHE D 361 -1  O  VAL D 359   N  ILE D 319           
SHEET    3 AA2 3 GLY D 350  ASP D 353 -1  N  PHE D 351   O  HIS D 360           
SHEET    1 AA3 2 ILE H 128  ILE H 129  0                                        
SHEET    2 AA3 2 MET H 161  VAL H 162 -1  O  VAL H 162   N  ILE H 128           
SHEET    1 AA4 2 VAL P   3  PHE P   4  0                                        
SHEET    2 AA4 2 ASP P  17  ALA P  18 -1  O  ALA P  18   N  VAL P   3           
SHEET    1 AA5 2 ILE P   7  ARG P   8  0                                        
SHEET    2 AA5 2 THR P  13  ILE P  14 -1  O  ILE P  14   N  ILE P   7           
SHEET    1 AA6 3 ILE Q  30  VAL Q  31  0                                        
SHEET    2 AA6 3 VAL Q  19  ILE Q  22 -1  N  VAL Q  19   O  VAL Q  31           
SHEET    3 AA6 3 GLU Q  59  ASN Q  61  1  O  VAL Q  60   N  LYS Q  20           
SHEET    1 AA7 3 THR C 316  SER C 318  0                                        
SHEET    2 AA7 3 MET C 357  PHE C 360 -1  O  VAL C 358   N  LEU C 317           
SHEET    3 AA7 3 ALA C 349  ASN C 352 -1  N  SER C 350   O  SER C 359           
SHEET    1 AA8 2 LEU G 145  ASP G 146  0                                        
SHEET    2 AA8 2 LEU G 151  LEU G 152 -1  O  LEU G 151   N  ASP G 146           
SHEET    1 AA9 2 VAL O 564  MET O 566  0                                        
SHEET    2 AA9 2 TYR O 573  ALA O 575 -1  O  ALA O 575   N  VAL O 564           
SHEET    1 AB1 3 ARG B 368  HIS B 370  0                                        
SHEET    2 AB1 3 LEU B 408  LEU B 411 -1  O  LEU B 409   N  ILE B 369           
SHEET    3 AB1 3 GLY B 400  ASP B 403 -1  N  ARG B 401   O  GLU B 410           
CISPEP   1 GLY Q   48    PRO Q   49          0        -2.77                     
CISPEP   2 VAL R   38    VAL R   39          0        -6.83                     
CISPEP   3 THR O  655    SER O  656          0         7.36                     
SITE     1 AC1  2 ASP R  51  LEU R  52                                          
SITE     1 AC2  6 ILE R  49  GLU R  66  GLU R  67  CYS R  68                    
SITE     2 AC2  6 THR R  69  VAL R  70                                          
SITE     1 AC3  3 GLU R  55  PHE R  81  HIS R  82                               
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1                      
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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