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Database: PDB
Entry: 6R7I
LinkDB: 6R7I
Original site: 6R7I 
HEADER    LIGASE                                  28-MAR-19   6R7I              
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 2;                        
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: SIGNALOSOME SUBUNIT 2,ALIEN HOMOLOG,JAB1-CONTAINING         
COMPND  11 SIGNALOSOME SUBUNIT 2,THYROID RECEPTOR-INTERACTING PROTEIN 15,TRIP-  
COMPND  12 15;                                                                  
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: COP9 SIGNALOSOME COMPLEX SUBUNIT 3;                        
COMPND  16 CHAIN: C;                                                            
COMPND  17 SYNONYM: SIGNALOSOME SUBUNIT 3,JAB1-CONTAINING SIGNALOSOME SUBUNIT 3;
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: COP9 SIGNALOSOME COMPLEX SUBUNIT 4;                        
COMPND  21 CHAIN: D;                                                            
COMPND  22 SYNONYM: SIGNALOSOME SUBUNIT 4,JAB1-CONTAINING SIGNALOSOME SUBUNIT 4;
COMPND  23 ENGINEERED: YES;                                                     
COMPND  24 MOL_ID: 5;                                                           
COMPND  25 MOLECULE: COP9 SIGNALOSOME COMPLEX SUBUNIT 5;                        
COMPND  26 CHAIN: E;                                                            
COMPND  27 SYNONYM: SIGNALOSOME SUBUNIT 5,JUN ACTIVATION DOMAIN-BINDING PROTEIN 
COMPND  28 1;                                                                   
COMPND  29 EC: 3.4.-.-;                                                         
COMPND  30 ENGINEERED: YES;                                                     
COMPND  31 MOL_ID: 6;                                                           
COMPND  32 MOLECULE: COP9 SIGNALOSOME COMPLEX SUBUNIT 6;                        
COMPND  33 CHAIN: F;                                                            
COMPND  34 SYNONYM: SIGNALOSOME SUBUNIT 6,JAB1-CONTAINING SIGNALOSOME SUBUNIT 6,
COMPND  35 MOV34 HOMOLOG,VPR-INTERACTING PROTEIN,HVIP;                          
COMPND  36 ENGINEERED: YES;                                                     
COMPND  37 MOL_ID: 7;                                                           
COMPND  38 MOLECULE: COP9 SIGNALOSOME COMPLEX SUBUNIT 7B;                       
COMPND  39 CHAIN: G;                                                            
COMPND  40 SYNONYM: SIGNALOSOME SUBUNIT 7B,JAB1-CONTAINING SIGNALOSOME SUBUNIT  
COMPND  41 7B;                                                                  
COMPND  42 ENGINEERED: YES;                                                     
COMPND  43 MOL_ID: 8;                                                           
COMPND  44 MOLECULE: COP9 SIGNALOSOME COMPLEX SUBUNIT 8;                        
COMPND  45 CHAIN: H;                                                            
COMPND  46 SYNONYM: SIGNALOSOME SUBUNIT 8,COP9 HOMOLOG,HCOP9,JAB1-CONTAINING    
COMPND  47 SIGNALOSOME SUBUNIT 8;                                               
COMPND  48 ENGINEERED: YES;                                                     
COMPND  49 MOL_ID: 9;                                                           
COMPND  50 MOLECULE: NEDD8;                                                     
COMPND  51 CHAIN: N;                                                            
COMPND  52 ENGINEERED: YES;                                                     
COMPND  53 MOL_ID: 10;                                                          
COMPND  54 MOLECULE: CULLIN-2;                                                  
COMPND  55 CHAIN: O;                                                            
COMPND  56 SYNONYM: CUL-2;                                                      
COMPND  57 ENGINEERED: YES;                                                     
COMPND  58 MOL_ID: 11;                                                          
COMPND  59 MOLECULE: ELONGIN-B;                                                 
COMPND  60 CHAIN: P;                                                            
COMPND  61 SYNONYM: ELOB,ELONGIN 18 KDA SUBUNIT,RNA POLYMERASE II TRANSCRIPTION 
COMPND  62 FACTOR SIII SUBUNIT B,SIII P18,TRANSCRIPTION ELONGATION FACTOR B     
COMPND  63 POLYPEPTIDE 2;                                                       
COMPND  64 ENGINEERED: YES;                                                     
COMPND  65 MOL_ID: 12;                                                          
COMPND  66 MOLECULE: ELONGIN-C;                                                 
COMPND  67 CHAIN: Q;                                                            
COMPND  68 ENGINEERED: YES;                                                     
COMPND  69 MOL_ID: 13;                                                          
COMPND  70 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RBX1;                          
COMPND  71 CHAIN: R;                                                            
COMPND  72 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: COPS2, CSN2, TRIP15;                                           
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: COPS3, CSN3;                                                   
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: COPS4, CSN4;                                                   
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: COPS5, CSN5, JAB1;                                             
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_COMMON: HUMAN;                                              
SOURCE  39 ORGANISM_TAXID: 9606;                                                
SOURCE  40 GENE: COPS6, CSN6, HVIP;                                             
SOURCE  41 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  42 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  43 MOL_ID: 7;                                                           
SOURCE  44 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  45 ORGANISM_COMMON: HUMAN;                                              
SOURCE  46 ORGANISM_TAXID: 9606;                                                
SOURCE  47 GENE: COPS7B, CSN7B;                                                 
SOURCE  48 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  49 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  50 MOL_ID: 8;                                                           
SOURCE  51 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  52 ORGANISM_COMMON: HUMAN;                                              
SOURCE  53 ORGANISM_TAXID: 9606;                                                
SOURCE  54 GENE: COPS8, CSN8;                                                   
SOURCE  55 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  56 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  57 MOL_ID: 9;                                                           
SOURCE  58 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  59 ORGANISM_COMMON: HUMAN;                                              
SOURCE  60 ORGANISM_TAXID: 9606;                                                
SOURCE  61 GENE: NEDD8;                                                         
SOURCE  62 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  63 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  64 MOL_ID: 10;                                                          
SOURCE  65 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  66 ORGANISM_COMMON: HUMAN;                                              
SOURCE  67 ORGANISM_TAXID: 9606;                                                
SOURCE  68 GENE: CUL2;                                                          
SOURCE  69 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  70 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  71 MOL_ID: 11;                                                          
SOURCE  72 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  73 ORGANISM_COMMON: HUMAN;                                              
SOURCE  74 ORGANISM_TAXID: 9606;                                                
SOURCE  75 GENE: ELOB, TCEB2;                                                   
SOURCE  76 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  77 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  78 MOL_ID: 12;                                                          
SOURCE  79 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  80 ORGANISM_TAXID: 9606;                                                
SOURCE  81 GENE: ELC1, YPL046C;                                                 
SOURCE  82 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  83 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  84 MOL_ID: 13;                                                          
SOURCE  85 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  86 ORGANISM_TAXID: 9606;                                                
SOURCE  87 GENE: RBX1, RBX1;                                                    
SOURCE  88 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  89 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    CULLIN-RING E3 LIGASES (CRLS) COP9 SIGNALOSOME (CSN) DENEDDYLATION,   
KEYWDS   2 LIGASE                                                               
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    S.F.FAULL,A.M.C.LAU,F.BEURON,N.B.CRONIN,E.P.MORRIS,A.POLITIS          
REVDAT   2   04-SEP-19 6R7I    1       JRNL                                     
REVDAT   1   28-AUG-19 6R7I    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.    5.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : EPU, RELION, RELION                       
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          : NULL                                
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)  : 5.900                          
REMARK   3   NUMBER OF PARTICLES               : 316921                         
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 6R7I 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_1292101072.                                   
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                 : CSN-CRL2-N8                       
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)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 40.00                          
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: TRIDECAMERIC                      
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, N, O,         
REMARK 350                    AND CHAINS: P, Q, R                               
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     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     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     MET B     4                                                      
REMARK 465     THR B   181                                                      
REMARK 465     ASP B   182                                                      
REMARK 465     ASP B   183                                                      
REMARK 465     GLY B   184                                                      
REMARK 465     GLU B   185                                                      
REMARK 465     ASP B   186                                                      
REMARK 465     ASP B   187                                                      
REMARK 465     LEU B   188                                                      
REMARK 465     LYS B   189                                                      
REMARK 465     LYS B   190                                                      
REMARK 465     GLY B   191                                                      
REMARK 465     ASN C    29                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     ALA E     3                                                      
REMARK 465     SER E     4                                                      
REMARK 465     GLY E     5                                                      
REMARK 465     SER E     6                                                      
REMARK 465     GLY E     7                                                      
REMARK 465     MET E     8                                                      
REMARK 465     ALA E     9                                                      
REMARK 465     GLN E    10                                                      
REMARK 465     LYS E    11                                                      
REMARK 465     THR E    12                                                      
REMARK 465     TRP E    13                                                      
REMARK 465     GLU E    14                                                      
REMARK 465     LEU E    15                                                      
REMARK 465     ALA E    16                                                      
REMARK 465     ASN E    17                                                      
REMARK 465     ASN E    18                                                      
REMARK 465     MET E    19                                                      
REMARK 465     GLN E    20                                                      
REMARK 465     GLU E    21                                                      
REMARK 465     ALA E    22                                                      
REMARK 465     GLN E    23                                                      
REMARK 465     SER E   284                                                      
REMARK 465     PHE E   285                                                      
REMARK 465     MET E   286                                                      
REMARK 465     LEU E   287                                                      
REMARK 465     GLY E   288                                                      
REMARK 465     LEU E   289                                                      
REMARK 465     GLU E   290                                                      
REMARK 465     THR E   291                                                      
REMARK 465     HIS E   292                                                      
REMARK 465     ASP E   293                                                      
REMARK 465     ARG E   294                                                      
REMARK 465     LYS E   295                                                      
REMARK 465     SER E   334                                                      
REMARK 465     MET F     1                                                      
REMARK 465     ALA F     2                                                      
REMARK 465     ALA F     3                                                      
REMARK 465     ALA F     4                                                      
REMARK 465     ALA F     5                                                      
REMARK 465     ALA F     6                                                      
REMARK 465     ALA F     7                                                      
REMARK 465     ALA F     8                                                      
REMARK 465     ALA F     9                                                      
REMARK 465     ALA F    10                                                      
REMARK 465     THR F    11                                                      
REMARK 465     ASN F    12                                                      
REMARK 465     GLY F    13                                                      
REMARK 465     THR F    14                                                      
REMARK 465     GLY F    15                                                      
REMARK 465     GLY F    16                                                      
REMARK 465     SER F    17                                                      
REMARK 465     SER F    18                                                      
REMARK 465     GLY F    19                                                      
REMARK 465     MET F    20                                                      
REMARK 465     GLU F    21                                                      
REMARK 465     VAL F    22                                                      
REMARK 465     ASP F    23                                                      
REMARK 465     ALA F    24                                                      
REMARK 465     ALA F    25                                                      
REMARK 465     VAL F    26                                                      
REMARK 465     VAL F    27                                                      
REMARK 465     PRO F    28                                                      
REMARK 465     ALA F   208                                                      
REMARK 465     THR F   209                                                      
REMARK 465     GLY F   210                                                      
REMARK 465     SER F   211                                                      
REMARK 465     GLY F   212                                                      
REMARK 465     GLU F   213                                                      
REMARK 465     ASN F   214                                                      
REMARK 465     GLY F   317                                                      
REMARK 465     ILE F   318                                                      
REMARK 465     GLY F   319                                                      
REMARK 465     ARG F   320                                                      
REMARK 465     ARG F   321                                                      
REMARK 465     MET F   322                                                      
REMARK 465     ARG F   323                                                      
REMARK 465     GLY F   324                                                      
REMARK 465     LEU F   325                                                      
REMARK 465     PHE F   326                                                      
REMARK 465     PHE F   327                                                      
REMARK 465     MET H     1                                                      
REMARK 465     PRO H     2                                                      
REMARK 465     VAL H     3                                                      
REMARK 465     ALA H     4                                                      
REMARK 465     VAL H     5                                                      
REMARK 465     MET H     6                                                      
REMARK 465     ALA H     7                                                      
REMARK 465     GLU H     8                                                      
REMARK 465     SER H     9                                                      
REMARK 465     ALA H    10                                                      
REMARK 465     GLY H    29                                                      
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     TYR O    29                                                      
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     LYS A  70    CG   CD   CE   NZ                                   
REMARK 470     VAL A  71    CG1  CG2                                            
REMARK 470     TYR A  72    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE A  73    CG1  CG2  CD1                                       
REMARK 470     GLU A  74    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  75    CB   CG   CD   CE   NZ                              
REMARK 470     ASP A  76    CG   OD1  OD2                                       
REMARK 470     GLU B   5    CG   CD   OE1  OE2                                  
REMARK 470     ASP B   6    CG   OD1  OD2                                       
REMARK 470     ASP B   7    CG   OD1  OD2                                       
REMARK 470     PHE B   8    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     MET B   9    CG   SD   CE                                        
REMARK 470     CYS B  10    SG                                                  
REMARK 470     ASP B  11    CG   OD1  OD2                                       
REMARK 470     ASP B  12    CG   OD1  OD2                                       
REMARK 470     GLU B  13    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  14    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  15    CG   OD1  OD2                                       
REMARK 470     TYR B  16    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP B  17    CG   OD1  OD2                                       
REMARK 470     LEU B  18    CG   CD1  CD2                                       
REMARK 470     GLU B  19    CG   CD   OE1  OE2                                  
REMARK 470     TYR B  20    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER B  21    OG                                                  
REMARK 470     GLU B  22    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  23    CG   OD1  OD2                                       
REMARK 470     SER B  24    OG                                                  
REMARK 470     ASN B  25    CG   OD1  ND2                                       
REMARK 470     SER B  26    OG                                                  
REMARK 470     GLU B  27    CG   CD   OE1  OE2                                  
REMARK 470     PRO B  28    CG   CD                                             
REMARK 470     ASN B  29    CG   OD1  ND2                                       
REMARK 470     GLN D  28    CG   CD   OE1  NE2                                  
REMARK 470     GLU D  90    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 322    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 362    CG   CD   OE1  OE2                                  
REMARK 470     MET O   1    N                                                   
REMARK 470     ASP O 175    CG   OD1  OD2                                       
REMARK 470     MET P   1    CG   SD   CE                                        
REMARK 470     GLN P 106    CG   CD   OE1  NE2                                  
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  HG23  VAL Q     9     C    GLU Q    45              0.19            
REMARK 500  HG23  VAL O    25     ND1  HIS O    71              0.22            
REMARK 500  HG13  ILE O    42     CE1  TYR O   105              0.28            
REMARK 500   N    LEU O   569     CA   LYS R    19              0.33            
REMARK 500   OD2  ASP O     9     N    ALA O    48              0.35            
REMARK 500   CA   THR Q     7     O    ILE Q    44              0.35            
REMARK 500   NE1  TRP E   246     O    ALA F   227              0.37            
REMARK 500   C    GLN E   110     NE   ARG N   125              0.39            
REMARK 500   CD   GLU O   174     OD1  ASN O   177              0.39            
REMARK 500   CZ   PHE P    15     HD2  TYR Q    16              0.42            
REMARK 500  HD11  LEU Q    46     HB2  PHE Q    49              0.43            
REMARK 500   CE1  PHE P    93     OH   TYR Q    16              0.43            
REMARK 500   CE2  TYR F   261     OG   SER G   106              0.46            
REMARK 500   N    MET Q     1     C    SER Q    40              0.46            
REMARK 500   SD   MET P   103     O    THR Q    84              0.47            
REMARK 500   CB   ASP A    76     CA   VAL A    77              0.48            
REMARK 500   CA   GLY E   102     OE2  GLU N   124              0.50            
REMARK 500   CB   MET Q    86     HG   SER Q    87              0.51            
REMARK 500  HD13  LEU Q    46    HD21  LEU Q    54              0.52            
REMARK 500  HG23  ILE O    42     CD2  LEU O   108              0.52            
REMARK 500   C    VAL Q     9     HB3  LEU Q    46              0.53            
REMARK 500   CD1  LEU N   169     CB   LEU N   171              0.53            
REMARK 500   OH   TYR O   107     HB2  ASP Q    95              0.54            
REMARK 500   CD1  TRP E   246     C    ALA F   227              0.56            
REMARK 500   CA   SER P    94     OD2  ASP Q    50              0.56            
REMARK 500   O    LEU O    17     CD2  PHE O    64              0.57            
REMARK 500   HG1  THR Q     7     CA   ILE Q    44              0.58            
REMARK 500   CD   GLU Q    55     O    HOH Q   101              0.58            
REMARK 500   CG   TRP O    14     OE1  GLU O    60              0.61            
REMARK 500   O    MET E    78     OE2  GLU N   128              0.62            
REMARK 500   CZ   PHE O    10     O    ARG O    56              0.64            
REMARK 500   CE1  PHE O    10     N    LEU O    57              0.64            
REMARK 500  HG12  ILE O   286     CD2  LEU O   315              0.64            
REMARK 500   CB   ASP O   727     N    ARG R    46              0.65            
REMARK 500   C    LEU O   254     CA   HIS O   255              0.65            
REMARK 500   OH   TYR O   544     NE1  TRP R    33              0.65            
REMARK 500   C    SER Q    26     H    THR Q    28              0.66            
REMARK 500  HG12  VAL Q     6    HD13  LEU Q    29              0.67            
REMARK 500   CG2  ILE O    21     CB   HIS O    68              0.68            
REMARK 500   HG3  GLN Q     3     N    ASP Q     4              0.68            
REMARK 500   CZ   TYR O   107     CB   ASP Q    95              0.68            
REMARK 500  HG23  ILE O    21     CG   HIS O    68              0.68            
REMARK 500  HE21  GLN Q     3     HB3  ASP Q     4              0.69            
REMARK 500   CA   GLY O   504     CD   LYS R    26              0.69            
REMARK 500   CG   MET O    26     OE2  GLU O    93              0.70            
REMARK 500   HA   VAL Q     6     HZ3  LYS Q    41              0.70            
REMARK 500   CB   LEU N   108     CD   ARG O   691              0.70            
REMARK 500   CZ   TYR O   100     OE2  GLU Q    34              0.70            
REMARK 500   CA   VAL O   693     CD1  LEU O   694              0.71            
REMARK 500   CG   HIS O   283     CB   GLU O   314              0.71            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS    1749 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    MET O  26   C     LEU O  27   N       0.150                       
REMARK 500    GLU O 174   C     ASP O 175   N      -0.281                       
REMARK 500    GLN O 204   C     GLU O 205   N      -0.179                       
REMARK 500    PRO O 256   C     SER O 257   N      -0.871                       
REMARK 500    HIS O 274   C     LEU O 275   N      -0.277                       
REMARK 500    GLU O 289   C     LYS O 290   N      -0.142                       
REMARK 500    PRO O 381   C     LYS O 382   N      -0.216                       
REMARK 500    ARG O 686   NE    ARG O 686   CZ      0.079                       
REMARK 500    ARG O 691   CZ    ARG O 691   NH2     0.078                       
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    ILE A  73   CA  -  C   -  N   ANGL. DEV. = -65.3 DEGREES          
REMARK 500    ILE A  73   O   -  C   -  N   ANGL. DEV. =  44.7 DEGREES          
REMARK 500    LEU C 202   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES          
REMARK 500    LEU E 273   CA  -  CB  -  CG  ANGL. DEV. = -18.2 DEGREES          
REMARK 500    HIS F  44   C   -  N   -  CA  ANGL. DEV. =  19.0 DEGREES          
REMARK 500    SER F 271   CA  -  C   -  N   ANGL. DEV. = -46.0 DEGREES          
REMARK 500    SER F 271   O   -  C   -  N   ANGL. DEV. =  45.1 DEGREES          
REMARK 500    THR F 272   C   -  N   -  CA  ANGL. DEV. = -45.8 DEGREES          
REMARK 500    THR F 294   CA  -  C   -  N   ANGL. DEV. = -60.5 DEGREES          
REMARK 500    ILE F 295   C   -  N   -  CA  ANGL. DEV. = -48.6 DEGREES          
REMARK 500    LYS G 164   O   -  C   -  N   ANGL. DEV. = -11.6 DEGREES          
REMARK 500    MET O  26   O   -  C   -  N   ANGL. DEV. = -40.9 DEGREES          
REMARK 500    GLU O 174   CA  -  C   -  N   ANGL. DEV. = -15.1 DEGREES          
REMARK 500    GLU O 174   O   -  C   -  N   ANGL. DEV. = -15.8 DEGREES          
REMARK 500    GLN O 204   CA  -  C   -  N   ANGL. DEV. = -20.2 DEGREES          
REMARK 500    GLN O 204   O   -  C   -  N   ANGL. DEV. =  15.7 DEGREES          
REMARK 500    LEU O 254   CA  -  C   -  N   ANGL. DEV. = -81.8 DEGREES          
REMARK 500    LEU O 254   O   -  C   -  N   ANGL. DEV. = -15.4 DEGREES          
REMARK 500    HIS O 255   C   -  N   -  CA  ANGL. DEV. = -95.5 DEGREES          
REMARK 500    PRO O 256   CA  -  C   -  N   ANGL. DEV. = -37.0 DEGREES          
REMARK 500    PRO O 256   O   -  C   -  N   ANGL. DEV. = -31.4 DEGREES          
REMARK 500    SER O 257   C   -  N   -  CA  ANGL. DEV. = -20.2 DEGREES          
REMARK 500    HIS O 274   CA  -  C   -  N   ANGL. DEV. =  50.4 DEGREES          
REMARK 500    HIS O 274   O   -  C   -  N   ANGL. DEV. = -75.5 DEGREES          
REMARK 500    LEU O 275   C   -  N   -  CA  ANGL. DEV. =  41.5 DEGREES          
REMARK 500    GLU O 289   CA  -  C   -  N   ANGL. DEV. = -30.7 DEGREES          
REMARK 500    GLU O 289   O   -  C   -  N   ANGL. DEV. =  13.3 DEGREES          
REMARK 500    LYS O 290   C   -  N   -  CA  ANGL. DEV. = -27.6 DEGREES          
REMARK 500    GLY O 360   CA  -  C   -  N   ANGL. DEV. =  15.7 DEGREES          
REMARK 500    GLY O 360   O   -  C   -  N   ANGL. DEV. = -37.3 DEGREES          
REMARK 500    ASP O 361   C   -  N   -  CA  ANGL. DEV. =  34.5 DEGREES          
REMARK 500    PRO O 381   CA  -  C   -  N   ANGL. DEV. = -36.1 DEGREES          
REMARK 500    PRO O 381   O   -  C   -  N   ANGL. DEV. = -44.7 DEGREES          
REMARK 500    LEU O 391   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES          
REMARK 500    MET O 665   CG  -  SD  -  CE  ANGL. DEV. = -10.1 DEGREES          
REMARK 500    ARG O 676   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    MET O 678   CG  -  SD  -  CE  ANGL. DEV. = -11.6 DEGREES          
REMARK 500    ARG O 686   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG O 691   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG O 691   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ASP Q   4   O   -  C   -  N   ANGL. DEV. = -87.6 DEGREES          
REMARK 500    PHE Q   5   C   -  N   -  CA  ANGL. DEV. =  17.5 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    GLU A  78      147.87   -175.12                                   
REMARK 500    SER A  81       40.86    -96.47                                   
REMARK 500    THR A 109      -13.21     75.06                                   
REMARK 500    THR A 125      -11.70     74.01                                   
REMARK 500    PHE A 126       66.98     61.64                                   
REMARK 500    GLN A 249       63.03     65.35                                   
REMARK 500    SER A 263      -52.18   -120.63                                   
REMARK 500    GLU A 266       63.07     63.54                                   
REMARK 500    GLN A 270       -2.86     69.04                                   
REMARK 500    ASP A 275       70.69     53.45                                   
REMARK 500    SER A 276       69.15     62.24                                   
REMARK 500    LYS A 298       49.21    -94.64                                   
REMARK 500    TYR A 299       -5.87    -55.82                                   
REMARK 500    CYS A 314      -10.40     71.67                                   
REMARK 500    ASP A 315      113.24   -160.66                                   
REMARK 500    PHE A 316      104.71   -161.03                                   
REMARK 500    LEU A 320      146.44   -178.96                                   
REMARK 500    SER A 372       66.23     61.77                                   
REMARK 500    LYS A 373       75.97   -100.97                                   
REMARK 500    SER A 450       83.12    -69.10                                   
REMARK 500    ALA A 462     -160.81    -78.89                                   
REMARK 500    ASP A 464     -159.16    -85.00                                   
REMARK 500    GLN A 499       -0.99     71.38                                   
REMARK 500    HIS A 501     -168.39   -166.40                                   
REMARK 500    LEU B  18     -119.70    -84.70                                   
REMARK 500    GLU B  19       92.46    -54.61                                   
REMARK 500    SER B  21     -112.37   -159.36                                   
REMARK 500    GLU B  22       -3.06   -142.01                                   
REMARK 500    VAL B  30      -49.46     44.68                                   
REMARK 500    GLU B  44       -8.32     76.69                                   
REMARK 500    ALA B  49       -3.62     73.90                                   
REMARK 500    GLU B  66        3.58    -64.01                                   
REMARK 500    LEU B  82     -155.45   -149.29                                   
REMARK 500    THR B  83     -176.61    -61.49                                   
REMARK 500    LYS B 140       49.45    -94.94                                   
REMARK 500    LYS B 209       -0.18     72.82                                   
REMARK 500    ASN B 210       56.45    -90.83                                   
REMARK 500    ALA B 227       49.95    -92.37                                   
REMARK 500    ASN B 292       53.07   -147.59                                   
REMARK 500    ASP B 295       30.29    -91.02                                   
REMARK 500    SER B 296      -71.10    -61.04                                   
REMARK 500    ILE B 337      -55.70   -127.25                                   
REMARK 500    ASN B 379       63.78     60.81                                   
REMARK 500    ALA C  17       66.01     60.76                                   
REMARK 500    GLN C  18     -158.13   -148.60                                   
REMARK 500    GLU C  33       -1.45     78.73                                   
REMARK 500    ALA C  36     -168.72   -128.78                                   
REMARK 500    ASP C  50      173.00    176.34                                   
REMARK 500    GLN C  52     -160.05    -73.82                                   
REMARK 500    GLU C  53       15.86    -62.65                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     202 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 LEU A  110     ARG A  111                  149.20                    
REMARK 500 ILE A  267     ALA A  268                 -148.62                    
REMARK 500 PHE A  337     ASP A  338                  146.92                    
REMARK 500 SER A  372     LYS A  373                  149.03                    
REMARK 500 VAL A  453     ASP A  454                  147.32                    
REMARK 500 LEU A  460     TYR A  461                  146.18                    
REMARK 500 THR B   83     ASN B   84                 -147.77                    
REMARK 500 HIS C   92     ILE C   93                 -148.24                    
REMARK 500 LYS C  171     GLU C  172                  137.70                    
REMARK 500 ASN C  369     PRO C  370                  148.64                    
REMARK 500 LYS D  290     ALA D  291                  144.61                    
REMARK 500 LEU D  315     TYR D  316                 -139.07                    
REMARK 500 ILE D  352     ASP D  353                  147.92                    
REMARK 500 VAL E   77     MET E   78                 -149.82                    
REMARK 500 MET E  117     ALA E  118                  149.49                    
REMARK 500 VAL F  250     PRO F  251                 -143.02                    
REMARK 500 LEU F  267     PRO F  268                 -134.11                    
REMARK 500 LYS G  164     LYS G  165                 -116.77                    
REMARK 500 LYS G  165     ASP G  166                  143.62                    
REMARK 500 GLY O  360     ASP O  361                 -102.29                    
REMARK 500 LYS O  382     SER O  383                  149.07                    
REMARK 500 ASN O  409     GLU O  410                  149.25                    
REMARK 500 ASP O  429     VAL O  430                  149.86                    
REMARK 500 ILE O  505     SER O  506                 -148.00                    
REMARK 500 SER O  506     PHE O  507                  121.46                    
REMARK 500 ASN O  567     TYR O  568                  141.88                    
REMARK 500 ARG P    8     ARG P    9                  149.92                    
REMARK 500 ARG P   80     ALA P   81                  143.55                    
REMARK 500 ASP Q    4     PHE Q    5                  143.98                    
REMARK 500 GLU Q   34     GLY Q   35                   92.64                    
REMARK 500 PHE Q   37     ARG Q   38                 -133.66                    
REMARK 500 LYS R   20     ARG R   21                  146.29                    
REMARK 500 ARG R   46     ASN R   47                  133.95                    
REMARK 500 CYS R   56     GLN R   57                  143.58                    
REMARK 500 LEU R   96     ASP R   97                  149.62                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG O 669         0.09    SIDE CHAIN                              
REMARK 500    TYR Q  60         0.12    SIDE CHAIN                              
REMARK 500    TYR Q  63         0.08    SIDE CHAIN                              
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    THR F 294        -25.68                                           
REMARK 500    MET O  26         42.16                                           
REMARK 500    GLU O 174         30.87                                           
REMARK 500    GLN O 204        -10.17                                           
REMARK 500    LEU O 254         28.97                                           
REMARK 500    PRO O 256         61.44                                           
REMARK 500    HIS O 274       -168.42                                           
REMARK 500    GLU O 289        -16.99                                           
REMARK 500    GLY O 360         38.51                                           
REMARK 500    PRO O 381        -42.37                                           
REMARK 500    ASP Q   4        -54.14                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 607        DISTANCE = 10.01 ANGSTROMS                       
REMARK 525    HOH A 608        DISTANCE = 10.72 ANGSTROMS                       
REMARK 525    HOH A 609        DISTANCE = 41.91 ANGSTROMS                       
REMARK 525    HOH P 327        DISTANCE =  6.60 ANGSTROMS                       
REMARK 525    HOH P 328        DISTANCE =  9.39 ANGSTROMS                       
REMARK 525    HOH P 329        DISTANCE = 11.42 ANGSTROMS                       
REMARK 525    HOH P 330        DISTANCE = 11.51 ANGSTROMS                       
REMARK 525    HOH P 331        DISTANCE = 12.24 ANGSTROMS                       
REMARK 525    HOH P 332        DISTANCE = 12.73 ANGSTROMS                       
REMARK 525    HOH P 333        DISTANCE = 13.14 ANGSTROMS                       
REMARK 525    HOH P 334        DISTANCE = 13.28 ANGSTROMS                       
REMARK 525    HOH P 335        DISTANCE = 14.93 ANGSTROMS                       
REMARK 525    HOH P 336        DISTANCE = 14.98 ANGSTROMS                       
REMARK 525    HOH P 337        DISTANCE = 15.92 ANGSTROMS                       
REMARK 525    HOH P 338        DISTANCE = 16.37 ANGSTROMS                       
REMARK 525    HOH P 339        DISTANCE = 17.01 ANGSTROMS                       
REMARK 525    HOH P 340        DISTANCE = 18.25 ANGSTROMS                       
REMARK 525    HOH P 341        DISTANCE = 18.25 ANGSTROMS                       
REMARK 525    HOH P 342        DISTANCE = 25.02 ANGSTROMS                       
REMARK 525    HOH P 343        DISTANCE = 38.01 ANGSTROMS                       
REMARK 525    HOH P 344        DISTANCE = 42.22 ANGSTROMS                       
REMARK 525    HOH Q 116        DISTANCE = 19.10 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 151   OD1                                                    
REMARK 620 2 THR E 154   OG1  80.7                                              
REMARK 620 N                    1                                               
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 ASN R  47   ND2                                                    
REMARK 620 2 ASP R  51   OD2 100.0                                              
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 THR R  69   O                                                      
REMARK 620 2 ALA R  78   O   101.1                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN E 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN R 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN R 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
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-4742   RELATED DB: EMDB                              
REMARK 900 STRUCTURAL BASIS OF CULLIN-2 RING E3 LIGASE REGULATION BY THE COP9   
REMARK 900 SIGNALOSOME                                                          
DBREF  6R7I A   77   527  UNP    Q13098   CSN1_HUMAN      37    491             
DBREF  6R7I B    1   443  UNP    P61201   CSN2_HUMAN       1    443             
DBREF  6R7I C    3   403  UNP    Q9UNS2   CSN3_HUMAN       3    403             
DBREF  6R7I D    1   406  UNP    Q9BT78   CSN4_HUMAN       1    406             
DBREF  6R7I E    1   334  UNP    Q92905   CSN5_HUMAN       1    334             
DBREF  6R7I F    1   327  UNP    Q7L5N1   CSN6_HUMAN       1    327             
DBREF  6R7I G    1   215  UNP    Q9H9Q2   CSN7B_HUMAN      1    215             
DBREF  6R7I H    1   209  UNP    Q99627   CSN8_HUMAN       1    209             
DBREF  6R7I N    1   176  PDB    6R7I     6R7I             1    176             
DBREF  6R7I O    1   745  UNP    Q13617   CUL2_HUMAN      20    764             
DBREF  6R7I P    1   106  UNP    Q15370   ELOB_HUMAN       1    106             
DBREF  6R7I Q    1    99  PDB    6R7I     6R7I             1     99             
DBREF  6R7I R   18   102  PDB    6R7I     6R7I            18    102             
SEQADV 6R7I LYS A   70  UNP  Q13098              EXPRESSION TAG                 
SEQADV 6R7I VAL A   71  UNP  Q13098              EXPRESSION TAG                 
SEQADV 6R7I TYR A   72  UNP  Q13098              EXPRESSION TAG                 
SEQADV 6R7I ILE A   73  UNP  Q13098              EXPRESSION TAG                 
SEQADV 6R7I GLU A   74  UNP  Q13098              EXPRESSION TAG                 
SEQADV 6R7I LYS A   75  UNP  Q13098              EXPRESSION TAG                 
SEQADV 6R7I ASP A   76  UNP  Q13098              EXPRESSION TAG                 
SEQADV 6R7I ARG D    0  UNP  Q9BT78              EXPRESSION TAG                 
SEQADV 6R7I LEU G  167  UNP  Q9H9Q2    ILE   167 CONFLICT                       
SEQADV 6R7I SER G  168  UNP  Q9H9Q2    ASN   168 CONFLICT                       
SEQADV 6R7I ALA G  169  UNP  Q9H9Q2    ASN   169 CONFLICT                       
SEQADV 6R7I ALA G  171  UNP  Q9H9Q2    VAL   171 CONFLICT                       
SEQADV 6R7I ARG G  172  UNP  Q9H9Q2    LYS   172 CONFLICT                       
SEQADV 6R7I GLN G  175  UNP  Q9H9Q2    HIS   175 CONFLICT                       
SEQADV 6R7I VAL G  179  UNP  Q9H9Q2    ASP   179 CONFLICT                       
SEQADV 6R7I VAL G  183  UNP  Q9H9Q2    ALA   183 CONFLICT                       
SEQADV 6R7I SER G  186  UNP  Q9H9Q2    LEU   186 CONFLICT                       
SEQADV 6R7I GLU G  190  UNP  Q9H9Q2    GLN   190 CONFLICT                       
SEQADV 6R7I SER G  193  UNP  Q9H9Q2    LEU   193 CONFLICT                       
SEQADV 6R7I HIS G  198  UNP  Q9H9Q2    TYR   198 CONFLICT                       
SEQADV 6R7I GLN G  201  UNP  Q9H9Q2    ASN   201 CONFLICT                       
SEQADV 6R7I GLN G  202  UNP  Q9H9Q2    HIS   202 CONFLICT                       
SEQADV 6R7I LEU G  203  UNP  Q9H9Q2    ASN   203 CONFLICT                       
SEQADV 6R7I GLY G  204  UNP  Q9H9Q2    ARG   204 CONFLICT                       
SEQADV 6R7I LEU G  205  UNP  Q9H9Q2    THR   205 CONFLICT                       
SEQADV 6R7I LYS G  206  UNP  Q9H9Q2    GLN   206 CONFLICT                       
SEQADV 6R7I ILE G  209  UNP  Q9H9Q2    VAL   209 CONFLICT                       
SEQADV 6R7I SER G  211  UNP  Q9H9Q2    ALA   211 CONFLICT                       
SEQADV 6R7I ALA G  214  UNP  Q9H9Q2    THR   214 CONFLICT                       
SEQRES   1 A  462  LYS VAL TYR ILE GLU LYS ASP VAL GLU ASN PRO SER LEU          
SEQRES   2 A  462  ASP LEU GLU GLN TYR ALA ALA SER TYR SER GLY LEU MET          
SEQRES   3 A  462  ARG ILE GLU ARG LEU GLN PHE ILE ALA ASP HIS CYS PRO          
SEQRES   4 A  462  THR LEU ARG VAL GLU ALA LEU LYS MET ALA LEU SER PHE          
SEQRES   5 A  462  VAL GLN ARG THR PHE ASN VAL ASP MET TYR GLU GLU ILE          
SEQRES   6 A  462  HIS ARG LYS LEU SER GLU ALA THR ARG SER SER LEU ARG          
SEQRES   7 A  462  GLU LEU GLN ASN ALA PRO ASP ALA ILE PRO GLU SER GLY          
SEQRES   8 A  462  VAL GLU PRO PRO ALA LEU ASP THR ALA TRP VAL GLU ALA          
SEQRES   9 A  462  THR ARG LYS LYS ALA LEU LEU LYS LEU GLU LYS LEU ASP          
SEQRES  10 A  462  THR ASP LEU LYS ASN TYR LYS GLY ASN SER ILE LYS GLU          
SEQRES  11 A  462  SER ILE ARG ARG GLY HIS ASP ASP LEU GLY ASP HIS TYR          
SEQRES  12 A  462  LEU ASP CYS GLY ASP LEU SER ASN ALA LEU LYS CYS TYR          
SEQRES  13 A  462  SER ARG ALA ARG ASP TYR CYS THR SER ALA LYS HIS VAL          
SEQRES  14 A  462  ILE ASN MET CYS LEU ASN VAL ILE LYS VAL SER VAL TYR          
SEQRES  15 A  462  LEU GLN ASN TRP SER HIS VAL LEU SER TYR VAL SER LYS          
SEQRES  16 A  462  ALA GLU SER THR PRO GLU ILE ALA GLU GLN ARG GLY GLU          
SEQRES  17 A  462  ARG ASP SER GLN THR GLN ALA ILE LEU THR LYS LEU LYS          
SEQRES  18 A  462  CYS ALA ALA GLY LEU ALA GLU LEU ALA ALA ARG LYS TYR          
SEQRES  19 A  462  LYS GLN ALA ALA LYS CYS LEU LEU LEU ALA SER PHE ASP          
SEQRES  20 A  462  HIS CYS ASP PHE PRO GLU LEU LEU SER PRO SER ASN VAL          
SEQRES  21 A  462  ALA ILE TYR GLY GLY LEU CYS ALA LEU ALA THR PHE ASP          
SEQRES  22 A  462  ARG GLN GLU LEU GLN ARG ASN VAL ILE SER SER SER SER          
SEQRES  23 A  462  PHE LYS LEU PHE LEU GLU LEU GLU PRO GLN VAL ARG ASP          
SEQRES  24 A  462  ILE ILE PHE LYS PHE TYR GLU SER LYS TYR ALA SER CYS          
SEQRES  25 A  462  LEU LYS MET LEU ASP GLU MET LYS ASP ASN LEU LEU LEU          
SEQRES  26 A  462  ASP MET TYR LEU ALA PRO HIS VAL ARG THR LEU TYR THR          
SEQRES  27 A  462  GLN ILE ARG ASN ARG ALA LEU ILE GLN TYR PHE SER PRO          
SEQRES  28 A  462  TYR VAL SER ALA ASP MET HIS ARG MET ALA ALA ALA PHE          
SEQRES  29 A  462  ASN THR THR VAL ALA ALA LEU GLU ASP GLU LEU THR GLN          
SEQRES  30 A  462  LEU ILE LEU GLU GLY LEU ILE SER ALA ARG VAL ASP SER          
SEQRES  31 A  462  HIS SER LYS ILE LEU TYR ALA ARG ASP VAL ASP GLN ARG          
SEQRES  32 A  462  SER THR THR PHE GLU LYS SER LEU LEU MET GLY LYS GLU          
SEQRES  33 A  462  PHE GLN ARG ARG ALA LYS ALA MET MET LEU ARG ALA ALA          
SEQRES  34 A  462  VAL LEU ARG ASN GLN ILE HIS VAL LYS SER PRO PRO ARG          
SEQRES  35 A  462  GLU GLY SER GLN GLY GLU LEU THR PRO ALA ASN SER GLN          
SEQRES  36 A  462  SER ARG MET SER THR ASN MET                                  
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                                                          
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 D  407  ARG MET ALA ALA ALA VAL ARG GLN ASP LEU ALA GLN LEU          
SEQRES   2 D  407  MET ASN SER SER GLY SER HIS LYS ASP LEU ALA GLY LYS          
SEQRES   3 D  407  TYR ARG GLN ILE LEU GLU LYS ALA ILE GLN LEU SER GLY          
SEQRES   4 D  407  ALA GLU GLN LEU GLU ALA LEU LYS ALA PHE VAL GLU ALA          
SEQRES   5 D  407  MET VAL ASN GLU ASN VAL SER LEU VAL ILE SER ARG GLN          
SEQRES   6 D  407  LEU LEU THR ASP PHE CYS THR HIS LEU PRO ASN LEU PRO          
SEQRES   7 D  407  ASP SER THR ALA LYS GLU ILE TYR HIS PHE THR LEU GLU          
SEQRES   8 D  407  LYS ILE GLN PRO ARG VAL ILE SER PHE GLU GLU GLN VAL          
SEQRES   9 D  407  ALA SER ILE ARG GLN HIS LEU ALA SER ILE TYR GLU LYS          
SEQRES  10 D  407  GLU GLU ASP TRP ARG ASN ALA ALA GLN VAL LEU VAL GLY          
SEQRES  11 D  407  ILE PRO LEU GLU THR GLY GLN LYS GLN TYR ASN VAL ASP          
SEQRES  12 D  407  TYR LYS LEU GLU THR TYR LEU LYS ILE ALA ARG LEU TYR          
SEQRES  13 D  407  LEU GLU ASP ASP ASP PRO VAL GLN ALA GLU ALA TYR ILE          
SEQRES  14 D  407  ASN ARG ALA SER LEU LEU GLN ASN GLU SER THR ASN GLU          
SEQRES  15 D  407  GLN LEU GLN ILE HIS TYR LYS VAL CYS TYR ALA ARG VAL          
SEQRES  16 D  407  LEU ASP TYR ARG ARG LYS PHE ILE GLU ALA ALA GLN ARG          
SEQRES  17 D  407  TYR ASN GLU LEU SER TYR LYS THR ILE VAL HIS GLU SER          
SEQRES  18 D  407  GLU ARG LEU GLU ALA LEU LYS HIS ALA LEU HIS CYS THR          
SEQRES  19 D  407  ILE LEU ALA SER ALA GLY GLN GLN ARG SER ARG MET LEU          
SEQRES  20 D  407  ALA THR LEU PHE LYS ASP GLU ARG CYS GLN GLN LEU ALA          
SEQRES  21 D  407  ALA TYR GLY ILE LEU GLU LYS MET TYR LEU ASP ARG ILE          
SEQRES  22 D  407  ILE ARG GLY ASN GLN LEU GLN GLU PHE ALA ALA MET LEU          
SEQRES  23 D  407  MET PRO HIS GLN LYS ALA THR THR ALA ASP GLY SER SER          
SEQRES  24 D  407  ILE LEU ASP ARG ALA VAL ILE GLU HIS ASN LEU LEU SER          
SEQRES  25 D  407  ALA SER LYS LEU TYR ASN ASN ILE THR PHE GLU GLU LEU          
SEQRES  26 D  407  GLY ALA LEU LEU GLU ILE PRO ALA ALA LYS ALA GLU LYS          
SEQRES  27 D  407  ILE ALA SER GLN MET ILE THR GLU GLY ARG MET ASN GLY          
SEQRES  28 D  407  PHE ILE ASP GLN ILE ASP GLY ILE VAL HIS PHE GLU THR          
SEQRES  29 D  407  ARG GLU ALA LEU PRO THR TRP ASP LYS GLN ILE GLN SER          
SEQRES  30 D  407  LEU CYS PHE GLN VAL ASN ASN LEU LEU GLU LYS ILE SER          
SEQRES  31 D  407  GLN THR ALA PRO GLU TRP THR ALA GLN ALA MET GLU ALA          
SEQRES  32 D  407  GLN MET ALA GLN                                              
SEQRES   1 E  334  MET ALA ALA SER GLY SER GLY MET ALA GLN LYS THR TRP          
SEQRES   2 E  334  GLU LEU ALA ASN ASN MET GLN GLU ALA GLN SER ILE ASP          
SEQRES   3 E  334  GLU ILE TYR LYS TYR ASP LYS LYS GLN GLN GLN GLU ILE          
SEQRES   4 E  334  LEU ALA ALA LYS PRO TRP THR LYS ASP HIS HIS TYR PHE          
SEQRES   5 E  334  LYS TYR CYS LYS ILE SER ALA LEU ALA LEU LEU LYS MET          
SEQRES   6 E  334  VAL MET HIS ALA ARG SER GLY GLY ASN LEU GLU VAL MET          
SEQRES   7 E  334  GLY LEU MET LEU GLY LYS VAL ASP GLY GLU THR MET ILE          
SEQRES   8 E  334  ILE MET ASP SER PHE ALA LEU PRO VAL GLU GLY THR GLU          
SEQRES   9 E  334  THR ARG VAL ASN ALA GLN ALA ALA ALA TYR GLU TYR MET          
SEQRES  10 E  334  ALA ALA TYR ILE GLU ASN ALA LYS GLN VAL GLY ARG LEU          
SEQRES  11 E  334  GLU ASN ALA ILE GLY TRP TYR HIS SER HIS PRO GLY TYR          
SEQRES  12 E  334  GLY CYS TRP LEU SER GLY ILE ASP VAL SER THR GLN MET          
SEQRES  13 E  334  LEU ASN GLN GLN PHE GLN GLU PRO PHE VAL ALA VAL VAL          
SEQRES  14 E  334  ILE ASP PRO THR ARG THR ILE SER ALA GLY LYS VAL ASN          
SEQRES  15 E  334  LEU GLY ALA PHE ARG THR TYR PRO LYS GLY TYR LYS PRO          
SEQRES  16 E  334  PRO ASP GLU GLY PRO SER GLU TYR GLN THR ILE PRO LEU          
SEQRES  17 E  334  ASN LYS ILE GLU ASP PHE GLY VAL HIS CYS LYS GLN TYR          
SEQRES  18 E  334  TYR ALA LEU GLU VAL SER TYR PHE LYS SER SER LEU ASP          
SEQRES  19 E  334  ARG LYS LEU LEU GLU LEU LEU TRP ASN LYS TYR TRP VAL          
SEQRES  20 E  334  ASN THR LEU SER SER SER SER LEU LEU THR ASN ALA ASP          
SEQRES  21 E  334  TYR THR THR GLY GLN VAL PHE ASP LEU SER GLU LYS LEU          
SEQRES  22 E  334  GLU GLN SER GLU ALA GLN LEU GLY ARG GLY SER PHE MET          
SEQRES  23 E  334  LEU GLY LEU GLU THR HIS ASP ARG LYS SER GLU ASP LYS          
SEQRES  24 E  334  LEU ALA LYS ALA THR ARG ASP SER CYS LYS THR THR ILE          
SEQRES  25 E  334  GLU ALA ILE HIS GLY LEU MET SER GLN VAL ILE LYS ASP          
SEQRES  26 E  334  LYS LEU PHE ASN GLN ILE ASN ILE SER                          
SEQRES   1 F  327  MET ALA ALA ALA ALA ALA ALA ALA ALA ALA THR ASN GLY          
SEQRES   2 F  327  THR GLY GLY SER SER GLY MET GLU VAL ASP ALA ALA VAL          
SEQRES   3 F  327  VAL PRO SER VAL MET ALA CYS GLY VAL THR GLY SER VAL          
SEQRES   4 F  327  SER VAL ALA LEU HIS PRO LEU VAL ILE LEU ASN ILE SER          
SEQRES   5 F  327  ASP HIS TRP ILE ARG MET ARG SER GLN GLU GLY ARG PRO          
SEQRES   6 F  327  VAL GLN VAL ILE GLY ALA LEU ILE GLY LYS GLN GLU GLY          
SEQRES   7 F  327  ARG ASN ILE GLU VAL MET ASN SER PHE GLU LEU LEU SER          
SEQRES   8 F  327  HIS THR VAL GLU GLU LYS ILE ILE ILE ASP LYS GLU TYR          
SEQRES   9 F  327  TYR TYR THR LYS GLU GLU GLN PHE LYS GLN VAL PHE LYS          
SEQRES  10 F  327  GLU LEU GLU PHE LEU GLY TRP TYR THR THR GLY GLY PRO          
SEQRES  11 F  327  PRO ASP PRO SER ASP ILE HIS VAL HIS LYS GLN VAL CYS          
SEQRES  12 F  327  GLU ILE ILE GLU SER PRO LEU PHE LEU LYS LEU ASN PRO          
SEQRES  13 F  327  MET THR LYS HIS THR ASP LEU PRO VAL SER VAL PHE GLU          
SEQRES  14 F  327  SER VAL ILE ASP ILE ILE ASN GLY GLU ALA THR MET LEU          
SEQRES  15 F  327  PHE ALA GLU LEU THR TYR THR LEU ALA THR GLU GLU ALA          
SEQRES  16 F  327  GLU ARG ILE GLY VAL ASP HIS VAL ALA ARG MET THR ALA          
SEQRES  17 F  327  THR GLY SER GLY GLU ASN SER THR VAL ALA GLU HIS LEU          
SEQRES  18 F  327  ILE ALA GLN HIS SER ALA ILE LYS MET LEU HIS SER ARG          
SEQRES  19 F  327  VAL LYS LEU ILE LEU GLU TYR VAL LYS ALA SER GLU ALA          
SEQRES  20 F  327  GLY GLU VAL PRO PHE ASN HIS GLU ILE LEU ARG GLU ALA          
SEQRES  21 F  327  TYR ALA LEU CYS HIS CYS LEU PRO VAL LEU SER THR ASP          
SEQRES  22 F  327  LYS PHE LYS THR ASP PHE TYR ASP GLN CYS ASN ASP VAL          
SEQRES  23 F  327  GLY LEU MET ALA TYR LEU GLY THR ILE THR LYS THR CYS          
SEQRES  24 F  327  ASN THR MET ASN GLN PHE VAL ASN LYS PHE ASN VAL LEU          
SEQRES  25 F  327  TYR ASP ARG GLN GLY ILE GLY ARG ARG MET ARG GLY LEU          
SEQRES  26 F  327  PHE 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 H  209  MET PRO VAL ALA VAL MET ALA GLU SER ALA PHE SER PHE          
SEQRES   2 H  209  LYS LYS LEU LEU ASP GLN CYS GLU ASN GLN GLU LEU GLU          
SEQRES   3 H  209  ALA PRO GLY GLY ILE ALA THR PRO PRO VAL TYR GLY GLN          
SEQRES   4 H  209  LEU LEU ALA LEU TYR LEU LEU HIS ASN ASP MET ASN ASN          
SEQRES   5 H  209  ALA ARG TYR LEU TRP LYS ARG ILE PRO PRO ALA ILE LYS          
SEQRES   6 H  209  SER ALA ASN SER GLU LEU GLY GLY ILE TRP SER VAL GLY          
SEQRES   7 H  209  GLN ARG ILE TRP GLN ARG ASP PHE PRO GLY ILE TYR THR          
SEQRES   8 H  209  THR ILE ASN ALA HIS GLN TRP SER GLU THR VAL GLN PRO          
SEQRES   9 H  209  ILE MET GLU ALA LEU ARG ASP ALA THR ARG ARG ARG ALA          
SEQRES  10 H  209  PHE ALA LEU VAL SER GLN ALA TYR THR SER ILE ILE ALA          
SEQRES  11 H  209  ASP ASP PHE ALA ALA PHE VAL GLY LEU PRO VAL GLU GLU          
SEQRES  12 H  209  ALA VAL LYS GLY ILE LEU GLU GLN GLY TRP GLN ALA ASP          
SEQRES  13 H  209  SER THR THR ARG MET VAL LEU PRO ARG LYS PRO VAL ALA          
SEQRES  14 H  209  GLY ALA LEU ASP VAL SER PHE ASN LYS PHE ILE PRO LEU          
SEQRES  15 H  209  SER GLU PRO ALA PRO VAL PRO PRO ILE PRO ASN GLU GLN          
SEQRES  16 H  209  GLN LEU ALA ARG LEU THR ASP TYR VAL ALA PHE LEU GLU          
SEQRES  17 H  209  ASN                                                          
SEQRES   1 N   78  GLY SER MSE LEU ILE LYS VAL LYS THR LEU THR GLY LYS          
SEQRES   2 N   78  GLU ILE GLU ILE ASP ILE GLU PRO THR ASP LYS VAL GLU          
SEQRES   3 N   78  ARG ILE LYS GLU ARG VAL GLU GLU LYS GLU GLY ILE PRO          
SEQRES   4 N   78  PRO GLN GLN GLN ARG LEU ILE TYR SER GLY LYS GLN MSE          
SEQRES   5 N   78  ASN ASP GLU LYS THR ALA ALA ASP TYR LYS ILE MSE GLY          
SEQRES   6 N   78  GLY SER VAL LEU HIS LEU VAL LEU ALA LEU ARG GLY GLY          
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 P  106  MET ASP VAL PHE LEU MET ILE ARG ARG HIS LYS THR THR          
SEQRES   2 P  106  ILE PHE THR ASP ALA LYS GLU SER SER THR VAL PHE GLU          
SEQRES   3 P  106  LEU LYS ARG ILE VAL GLU GLY ILE LEU LYS ARG PRO PRO          
SEQRES   4 P  106  ASP GLU GLN ARG LEU TYR LYS ASP ASP GLN LEU LEU ASP          
SEQRES   5 P  106  ASP GLY LYS THR LEU GLY GLU CYS GLY PHE THR SER GLN          
SEQRES   6 P  106  THR ALA ARG PRO GLN ALA PRO ALA THR VAL GLY LEU ALA          
SEQRES   7 P  106  PHE ARG ALA ASP ASP THR PHE GLU ALA LEU CYS ILE GLU          
SEQRES   8 P  106  PRO PHE SER SER PRO PRO GLU LEU PRO ASP VAL MET LYS          
SEQRES   9 P  106  PRO GLN                                                      
SEQRES   1 Q   99  MET SER GLN ASP PHE VAL THR LEU VAL SER LYS ASP ASP          
SEQRES   2 Q   99  LYS GLU TYR GLU ILE SER ARG SER ALA ALA MET ILE SER          
SEQRES   3 Q   99  PRO THR LEU LYS ALA MET ILE GLU GLY PRO PHE ARG GLU          
SEQRES   4 Q   99  SER LYS GLY ARG ILE GLU LEU LYS GLN PHE ASP SER HIS          
SEQRES   5 Q   99  ILE LEU GLU LYS ALA VAL GLU TYR LEU ASN TYR ASN LEU          
SEQRES   6 Q   99  LYS TYR SER GLY VAL SER GLU ASP ASP ASP GLU ILE PRO          
SEQRES   7 Q   99  GLU PHE GLU ILE PRO THR GLU MET SER LEU GLU LEU LEU          
SEQRES   8 Q   99  LEU ALA ALA ASP TYR LEU SER ILE                              
SEQRES   1 R   85  LYS LYS LYS ARG PHE GLU VAL LYS LYS TRP ASN ALA VAL          
SEQRES   2 R   85  ALA LEU TRP ALA TRP ASP ILE VAL VAL ASP ASN CYS ALA          
SEQRES   3 R   85  ILE CYS ARG ASN HIS ILE MET ASP LEU CYS ILE GLU CYS          
SEQRES   4 R   85  GLN ALA ASN GLN ALA SER ALA THR SER GLU GLU CYS THR          
SEQRES   5 R   85  VAL ALA TRP GLY VAL CYS ASN HIS ALA PHE HIS PHE HIS          
SEQRES   6 R   85  CYS ILE SER ARG TRP LEU LYS THR ARG GLN VAL CYS PRO          
SEQRES   7 R   85  LEU ASP ASN ARG GLU TRP GLU                                  
MODRES 6R7I MSE N  101  MET  MODIFIED RESIDUE                                   
MODRES 6R7I MSE N  150  MET  MODIFIED RESIDUE                                   
HET    MSE  N 101       8                                                       
HET    MSE  N 150       8                                                       
HET    MSE  N 162       8                                                       
HET     ZN  E 401       1                                                       
HET     ZN  R 201       1                                                       
HET     ZN  R 202       1                                                       
HET     ZN  R 203       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      ZN ZINC ION                                                         
FORMUL   9  MSE    3(C5 H11 N O2 SE)                                            
FORMUL  14   ZN    4(ZN 2+)                                                     
FORMUL  18  HOH   *169(H2 O)                                                    
HELIX    1 AA1 ASP A   83  TYR A   91  1                                   9    
HELIX    2 AA2 SER A   92  HIS A  106  1                                  15    
HELIX    3 AA3 LEU A  110  GLN A  123  1                                  14    
HELIX    4 AA4 ASN A  127  GLN A  146  1                                  20    
HELIX    5 AA5 ASP A  163  SER A  192  1                                  30    
HELIX    6 AA6 ILE A  193  CYS A  211  1                                  19    
HELIX    7 AA7 LEU A  214  ARG A  225  1                                  12    
HELIX    8 AA8 ASP A  226  CYS A  228  5                                   3    
HELIX    9 AA9 SER A  230  GLN A  249  1                                  20    
HELIX   10 AB1 ASN A  250  THR A  264  1                                  15    
HELIX   11 AB2 ARG A  271  THR A  278  1                                   8    
HELIX   12 AB3 ILE A  281  ALA A  296  1                                  16    
HELIX   13 AB4 LYS A  298  LEU A  307  1                                  10    
HELIX   14 AB5 LEU A  308  ALA A  309  5                                   2    
HELIX   15 AB6 SER A  310  CYS A  314  5                                   5    
HELIX   16 AB7 SER A  321  PHE A  337  1                                  17    
HELIX   17 AB8 ASP A  338  ILE A  347  1                                  10    
HELIX   18 AB9 PHE A  352  GLU A  357  1                                   6    
HELIX   19 AC1 GLU A  359  GLU A  371  1                                  13    
HELIX   20 AC2 LYS A  373  ASP A  382  1                                  10    
HELIX   21 AC3 MET A  384  ASP A  391  1                                   8    
HELIX   22 AC4 LEU A  394  PRO A  396  5                                   3    
HELIX   23 AC5 HIS A  397  SER A  415  1                                  19    
HELIX   24 AC6 MET A  422  ASN A  430  1                                   9    
HELIX   25 AC7 THR A  432  GLY A  447  1                                  16    
HELIX   26 AC8 GLN A  467  ASN A  498  1                                  32    
HELIX   27 AC9 ASP B    6  ASP B   17  1                                  12    
HELIX   28 AD1 VAL B   30  LEU B   42  1                                  13    
HELIX   29 AD2 ALA B   50  LEU B   60  1                                  11    
HELIX   30 AD3 GLU B   66  LEU B   82  1                                  17    
HELIX   31 AD4 ASN B   84  THR B   97  1                                  14    
HELIX   32 AD5 THR B  104  SER B  122  1                                  19    
HELIX   33 AD6 GLN B  124  LEU B  139  1                                  16    
HELIX   34 AD7 ARG B  146  TYR B  159  1                                  14    
HELIX   35 AD8 TYR B  165  GLN B  180  1                                  16    
HELIX   36 AD9 LEU B  194  LYS B  209  1                                  16    
HELIX   37 AE1 ASN B  210  LEU B  222  1                                  13    
HELIX   38 AE2 ILE B  233  GLY B  249  1                                  17    
HELIX   39 AE3 PHE B  251  GLY B  269  1                                  19    
HELIX   40 AE4 ARG B  272  LYS B  288  1                                  17    
HELIX   41 AE5 GLU B  298  LYS B  303  1                                   6    
HELIX   42 AE6 ASP B  305  ASN B  320  1                                  16    
HELIX   43 AE7 ASP B  322  ASN B  333  1                                  12    
HELIX   44 AE8 ASP B  340  LYS B  364  1                                  25    
HELIX   45 AE9 HIS B  370  ASN B  379  1                                  10    
HELIX   46 AF1 ASP B  381  ASP B  395  1                                  15    
HELIX   47 AF2 GLY B  417  SER B  440  1                                  24    
HELIX   48 AF3 GLN C    7  GLN C   14  1                                   8    
HELIX   49 AF4 LEU C   24  ILE C   28  5                                   5    
HELIX   50 AF5 LEU C   39  THR C   44  5                                   6    
HELIX   51 AF6 LEU C   56  PHE C   63  1                                   8    
HELIX   52 AF7 GLU C   75  THR C   87  1                                  13    
HELIX   53 AF8 HIS C   92  TYR C   95  5                                   4    
HELIX   54 AF9 ALA C   96  LEU C  103  1                                   8    
HELIX   55 AG1 LEU C  103  LYS C  115  1                                  13    
HELIX   56 AG2 GLY C  120  GLN C  132  1                                  13    
HELIX   57 AG3 THR C  139  ALA C  152  1                                  14    
HELIX   58 AG4 ASP C  177  LEU C  195  1                                  19    
HELIX   59 AG5 ASN C  197  THR C  210  1                                  14    
HELIX   60 AG6 SER C  217  LEU C  234  1                                  18    
HELIX   61 AG7 ILE C  248  SER C  257  1                                  10    
HELIX   62 AG8 SER C  257  SER C  268  1                                  12    
HELIX   63 AG9 ASN C  271  HIS C  282  1                                  12    
HELIX   64 AH1 HIS C  282  THR C  287  1                                   6    
HELIX   65 AH2 GLY C  293  PHE C  314  1                                  22    
HELIX   66 AH3 SER C  318  VAL C  326  1                                   9    
HELIX   67 AH4 GLY C  330  ASP C  344  1                                  15    
HELIX   68 AH5 ASN C  369  THR C  398  1                                  30    
HELIX   69 AH6 MET D    1  MET D   13  1                                  13    
HELIX   70 AH7 SER D   18  GLN D   35  1                                  18    
HELIX   71 AH8 GLY D   38  VAL D   53  1                                  16    
HELIX   72 AH9 SER D   58  HIS D   72  1                                  15    
HELIX   73 AI1 LEU D   73  LEU D   76  5                                   4    
HELIX   74 AI2 ASP D   78  GLN D   93  1                                  16    
HELIX   75 AI3 ARG D   95  SER D   98  5                                   4    
HELIX   76 AI4 PHE D   99  GLU D  117  1                                  19    
HELIX   77 AI5 ASP D  119  GLY D  129  1                                  11    
HELIX   78 AI6 ASN D  140  ASP D  159  1                                  20    
HELIX   79 AI7 ASP D  160  ALA D  171  1                                  12    
HELIX   80 AI8 SER D  172  GLU D  177  5                                   6    
HELIX   81 AI9 ASN D  180  ARG D  198  1                                  19    
HELIX   82 AJ1 LYS D  200  TYR D  213  1                                  14    
HELIX   83 AJ2 HIS D  218  ALA D  236  1                                  19    
HELIX   84 AJ3 GLY D  239  ASP D  252  1                                  14    
HELIX   85 AJ4 GLU D  253  GLN D  257  5                                   5    
HELIX   86 AJ5 LEU D  258  MET D  267  1                                  10    
HELIX   87 AJ6 TYR D  268  ASP D  270  5                                   3    
HELIX   88 AJ7 GLU D  280  LEU D  285  1                                   6    
HELIX   89 AJ8 MET D  286  ALA D  291  1                                   6    
HELIX   90 AJ9 SER D  298  TYR D  316  1                                  19    
HELIX   91 AK1 PHE D  321  LEU D  328  1                                   8    
HELIX   92 AK2 PRO D  331  GLY D  346  1                                  16    
HELIX   93 AK3 ALA D  366  ALA D  392  1                                  27    
HELIX   94 AK4 ALA D  392  GLN D  406  1                                  15    
HELIX   95 AK5 SER E   24  ILE E   28  5                                   5    
HELIX   96 AK6 ASP E   32  ALA E   41  1                                  10    
HELIX   97 AK7 LYS E   43  ASP E   48  1                                   6    
HELIX   98 AK8 ALA E   59  SER E   71  1                                  13    
HELIX   99 AK9 ALA E  109  ALA E  113  5                                   5    
HELIX  100 AL1 TYR E  114  LYS E  125  1                                  12    
HELIX  101 AL2 GLN E  126  GLY E  128  5                                   3    
HELIX  102 AL3 SER E  148  GLU E  163  1                                  16    
HELIX  103 AL4 PRO E  207  CYS E  218  1                                  12    
HELIX  104 AL5 SER E  231  LEU E  250  1                                  20    
HELIX  105 AL6 ASN E  258  GLY E  281  1                                  24    
HELIX  106 AL7 ASP E  298  GLN E  330  1                                  33    
HELIX  107 AL8 PRO F   45  GLY F   63  1                                  19    
HELIX  108 AL9 ASP F  101  LYS F  113  1                                  13    
HELIX  109 AM1 ASP F  132  CYS F  143  1                                  12    
HELIX  110 AM2 GLU F  193  MET F  206  1                                  14    
HELIX  111 AM3 THR F  216  GLY F  248  1                                  33    
HELIX  112 AM4 LEU F  257  HIS F  265  1                                   9    
HELIX  113 AM5 THR F  272  LEU F  312  1                                  41    
HELIX  114 AM6 ASN G   10  THR G   22  1                                  13    
HELIX  115 AM7 GLY G   24  LEU G   35  1                                  12    
HELIX  116 AM8 LEU G   49  ALA G   56  1                                   8    
HELIX  117 AM9 ASN G   60  TYR G   72  1                                  13    
HELIX  118 AN1 THR G   74  ASN G   81  1                                   8    
HELIX  119 AN2 SER G   89  MET G  108  1                                  20    
HELIX  120 AN3 PRO G  112  LEU G  120  1                                   9    
HELIX  121 AN4 ASN G  124  THR G  138  1                                  15    
HELIX  122 AN5 ASP G  166  ALA G  214  1                                  49    
HELIX  123 AN6 SER H   12  ALA H   27  1                                  16    
HELIX  124 AN7 THR H   33  LEU H   46  1                                  14    
HELIX  125 AN8 MET H   50  LYS H   58  1                                   9    
HELIX  126 AN9 PRO H   61  ASN H   68  1                                   8    
HELIX  127 AO1 ASN H   68  ARG H   84  1                                  17    
HELIX  128 AO2 ASP H   85  ASN H   94  1                                  10    
HELIX  129 AO3 VAL H  102  ALA H  124  1                                  23    
HELIX  130 AO4 ILE H  129  PHE H  136  1                                   8    
HELIX  131 AO5 PRO H  140  GLN H  151  1                                  12    
HELIX  132 AO6 GLN H  196  GLU H  208  1                                  13    
HELIX  133 AO7 LYS N  122  GLU N  134  1                                  13    
HELIX  134 AO8 PRO N  137  GLN N  141  5                                   5    
HELIX  135 AO9 THR N  155  LYS N  160  5                                   6    
HELIX  136 AP1 PHE O   10  THR O   19  1                                  10    
HELIX  137 AP2 GLU O   31  ALA O   48  1                                  18    
HELIX  138 AP3 GLU O   51  HIS O   71  1                                  21    
HELIX  139 AP4 VAL O   83  PHE O  112  1                                  30    
HELIX  140 AP5 GLU O  138  MET O  151  1                                  14    
HELIX  141 AP6 VAL O  152  ARG O  165  1                                  14    
HELIX  142 AP7 LYS O  179  VAL O  191  1                                  13    
HELIX  143 AP8 LEU O  200  PHE O  207  1                                   8    
HELIX  144 AP9 GLU O  208  GLU O  229  1                                  22    
HELIX  145 AQ1 TYR O  235  CYS O  250  1                                  16    
HELIX  146 AQ2 THR O  260  LYS O  261  1                                   2    
HELIX  147 AQ3 ILE O  263  VAL O  271  1                                   9    
HELIX  148 AQ4 LEU O  275  GLN O  288  1                                  14    
HELIX  149 AQ5 LYS O  290  LEU O  301  1                                  12    
HELIX  150 AQ6 THR O  306  LEU O  330  1                                  25    
HELIX  151 AQ7 MET O  335  ASN O  355  1                                  21    
HELIX  152 AQ8 ASP O  361  ASN O  377  1                                  17    
HELIX  153 AQ9 CYS O  385  LEU O  399  1                                  15    
HELIX  154 AR1 GLU O  410  LYS O  423  1                                  14    
HELIX  155 AR2 ASP O  429  LYS O  441  1                                  13    
HELIX  156 AR3 SER O  450  CYS O  465  1                                  16    
HELIX  157 AR4 TYR O  467  PHE O  493  1                                  27    
HELIX  158 AR5 PRO O  530  PHE O  548  1                                  19    
HELIX  159 AR6 LEU O  556  CYS O  560  5                                   5    
HELIX  160 AR7 THR O  578  PHE O  588  1                                  11    
HELIX  161 AR8 SER O  595  SER O  602  1                                   8    
HELIX  162 AR9 GLU O  607  VAL O  620  1                                  14    
HELIX  163 AS1 PRO O  662  ARG O  691  1                                  30    
HELIX  164 AS2 HIS O  696  SER O  707  1                                  12    
HELIX  165 AS3 MET O  717  LYS O  728  1                                  12    
HELIX  166 AS4 THR P   23  LYS P   36  1                                  14    
HELIX  167 AS5 PRO P   38  GLN P   42  5                                   5    
HELIX  168 AS6 ARG Q   20  MET Q   24  1                                   5    
HELIX  169 AS7 SER Q   26  ILE Q   33  1                                   8    
HELIX  170 AS8 SER Q   51  SER Q   71  1                                  21    
HELIX  171 AS9 GLU Q   89  SER Q   98  1                                  10    
HELIX  172 AT1 CYS R   53  ALA R   58  1                                   6    
HELIX  173 AT2 HIS R   80  THR R   90  1                                  11    
SHEET    1 AA1 2 TYR A 417  SER A 419  0                                        
SHEET    2 AA1 2 ILE B 402  ASP B 403  1  O  ILE B 402   N  VAL A 418           
SHEET    1 AA2 2 ARG A 452  ASP A 454  0                                        
SHEET    2 AA2 2 ILE A 459  TYR A 461 -1  O  TYR A 461   N  ARG A 452           
SHEET    1 AA3 2 ARG B 368  ILE B 369  0                                        
SHEET    2 AA3 2 LEU B 409  GLU B 410 -1  O  LEU B 409   N  ILE B 369           
SHEET    1 AA4 2 ILE C 351  ASN C 352  0                                        
SHEET    2 AA4 2 TYR H 125  SER H 127  1  O  SER H 127   N  ILE C 351           
SHEET    1 AA5 3 ASN D 318  THR D 320  0                                        
SHEET    2 AA5 3 ILE D 358  HIS D 360 -1  O  VAL D 359   N  ILE D 319           
SHEET    3 AA5 3 ILE D 352  ASP D 353 -1  N  ASP D 353   O  ILE D 358           
SHEET    1 AA6 4 TYR E  54  ILE E  57  0                                        
SHEET    2 AA6 4 THR E  89  ILE E  92  1  O  MET E  90   N  TYR E  54           
SHEET    3 AA6 4 MET E  81  ASP E  86 -1  N  ASP E  86   O  THR E  89           
SHEET    4 AA6 4 ASN E 132  GLY E 135 -1  O  ILE E 134   N  MET E  81           
SHEET    1 AA7 3 VAL E 168  VAL E 169  0                                        
SHEET    2 AA7 3 GLY E 184  THR E 188 -1  O  GLY E 184   N  VAL E 169           
SHEET    3 AA7 3 TYR E 221  LEU E 224 -1  O  TYR E 222   N  ARG E 187           
SHEET    1 AA8 6 ASN F  80  ASN F  85  0                                        
SHEET    2 AA8 6 GLY F  70  GLU F  77 -1  N  GLU F  77   O  ASN F  80           
SHEET    3 AA8 6 GLY F 123  TYR F 125 -1  N  GLY F 123   O  LEU F  72           
SHEET    4 AA8 6 LEU F 150  LYS F 153  1  O  LEU F 152   N  TRP F 124           
SHEET    5 AA8 6 SER F 166  ILE F 175 -1  O  PHE F 168   N  PHE F 151           
SHEET    6 AA8 6 GLU F 178  GLU F 185 -1  O  THR F 180   N  ASP F 173           
SHEET    1 AA9 2 SER F  91  VAL F  94  0                                        
SHEET    2 AA9 2 LYS F  97  ILE F 100 -1  O  LYS F  97   N  VAL F  94           
SHEET    1 AB1 2 LEU G 145  ASP G 146  0                                        
SHEET    2 AB1 2 LEU G 151  LEU G 152 -1  O  LEU G 151   N  ASP G 146           
SHEET    1 AB2 3 GLU N 112  ILE N 117  0                                        
SHEET    2 AB2 3 MSE N 101  THR N 107 -1  N  MSE N 101   O  ILE N 117           
SHEET    3 AB2 3 VAL N 166  LEU N 169  1  O  LEU N 169   N  LYS N 106           
SHEET    1 AB3 2 ILE N 144  TYR N 145  0                                        
SHEET    2 AB3 2 LYS N 148  GLN N 149 -1  O  LYS N 148   N  TYR N 145           
SHEET    1 AB4 2 ILE O 623  HIS O 625  0                                        
SHEET    2 AB4 2 PHE O 638  LEU O 640 -1  O  SER O 639   N  ASN O 624           
SHEET    1 AB5 2 ILE O 731  GLU O 732  0                                        
SHEET    2 AB5 2 SER O 742  TYR O 743 -1  O  SER O 742   N  GLU O 732           
SHEET    1 AB6 7 LEU P  50  LEU P  51  0                                        
SHEET    2 AB6 7 ARG P  43  TYR P  45 -1  N  LEU P  44   O  LEU P  51           
SHEET    3 AB6 7 ALA P  73  ALA P  78 -1  O  ALA P  78   N  ARG P  43           
SHEET    4 AB6 7 ASP P   2  ARG P   9  1  N  MET P   6   O  VAL P  75           
SHEET    5 AB6 7 THR P  12  LYS P  19 -1  O  THR P  16   N  LEU P   5           
SHEET    6 AB6 7 LYS Q  14  SER Q  19  1  O  GLU Q  17   N  THR P  13           
SHEET    7 AB6 7 PHE Q   5  SER Q  10 -1  N  SER Q  10   O  LYS Q  14           
SSBOND   1 MET O  297    MET O  311                          1555   1555  2.07  
LINK         OD1 ASP E 151                ZN    ZN E 401     1555   1555  2.24  
LINK         OG1 THR E 154                ZN    ZN E 401     1555   1555  1.99  
LINK         ND2 ASN R  47                ZN    ZN R 201     1555   1555  2.53  
LINK         OD2 ASP R  51                ZN    ZN R 201     1555   1555  1.91  
LINK         O   THR R  69                ZN    ZN R 202     1555   1555  1.98  
LINK         O   ALA R  78                ZN    ZN R 202     1555   1555  2.06  
LINK         ND1 HIS R  82                ZN    ZN R 203     1555   1555  2.12  
CISPEP   1 GLU E  163    PRO E  164          0        11.24                     
CISPEP   2 VAL R   38    VAL R   39          0        -7.96                     
SITE     1 AC1  5 ARG E 106  ASN E 108  ILE E 150  ASP E 151                    
SITE     2 AC1  5 THR E 154                                                     
SITE     1 AC2  5 ASN R  47  ASP R  51  LEU R  52  CYS R  53                    
SITE     2 AC2  5 ILE R  54                                                     
SITE     1 AC3  4 CYS R  42  ILE R  49  THR R  69  ALA R  78                    
SITE     1 AC4  1 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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