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Database: PDB
Entry: 6R6H
LinkDB: 6R6H
Original site: 6R6H 
HEADER    LIGASE                                  27-MAR-19   6R6H              
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 8;                        
COMPND  39 CHAIN: H;                                                            
COMPND  40 SYNONYM: SIGNALOSOME SUBUNIT 8,COP9 HOMOLOG,HCOP9,JAB1-CONTAINING    
COMPND  41 SIGNALOSOME SUBUNIT 8;                                               
COMPND  42 ENGINEERED: YES;                                                     
COMPND  43 MOL_ID: 8;                                                           
COMPND  44 MOLECULE: CULLIN-2;                                                  
COMPND  45 CHAIN: O;                                                            
COMPND  46 SYNONYM: CUL-2;                                                      
COMPND  47 ENGINEERED: YES;                                                     
COMPND  48 MOL_ID: 9;                                                           
COMPND  49 MOLECULE: ELONGIN-B;                                                 
COMPND  50 CHAIN: P;                                                            
COMPND  51 SYNONYM: ELOB,ELONGIN 18 KDA SUBUNIT,RNA POLYMERASE II TRANSCRIPTION 
COMPND  52 FACTOR SIII SUBUNIT B,SIII P18,TRANSCRIPTION ELONGATION FACTOR B     
COMPND  53 POLYPEPTIDE 2;                                                       
COMPND  54 ENGINEERED: YES;                                                     
COMPND  55 MOL_ID: 10;                                                          
COMPND  56 MOLECULE: ELOC_HUMAN;                                                
COMPND  57 CHAIN: Q;                                                            
COMPND  58 ENGINEERED: YES;                                                     
COMPND  59 MOL_ID: 11;                                                          
COMPND  60 MOLECULE: RBX1_HUMAN;                                                
COMPND  61 CHAIN: R;                                                            
COMPND  62 ENGINEERED: YES;                                                     
COMPND  63 MOL_ID: 12;                                                          
COMPND  64 MOLECULE: VON HIPPEL-LINDAU DISEASE TUMOR SUPPRESSOR;                
COMPND  65 CHAIN: V;                                                            
COMPND  66 SYNONYM: PROTEIN G7,PVHL;                                            
COMPND  67 ENGINEERED: YES;                                                     
COMPND  68 MOL_ID: 13;                                                          
COMPND  69 MOLECULE: COP9 SIGNALOSOME COMPLEX SUBUNIT 7B;                       
COMPND  70 CHAIN: G;                                                            
COMPND  71 SYNONYM: SIGNALOSOME SUBUNIT 7B,JAB1-CONTAINING SIGNALOSOME SUBUNIT  
COMPND  72 7B;                                                                  
COMPND  73 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_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: COPS2, CSN2, TRIP15;                                           
SOURCE  16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  17 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  19 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 GENE: COPS3, CSN3;                                                   
SOURCE  26 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  27 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  29 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  30 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  31 MOL_ID: 4;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  33 ORGANISM_COMMON: HUMAN;                                              
SOURCE  34 ORGANISM_TAXID: 9606;                                                
SOURCE  35 GENE: COPS4, CSN4;                                                   
SOURCE  36 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  37 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  38 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  39 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  40 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  41 MOL_ID: 5;                                                           
SOURCE  42 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  43 ORGANISM_COMMON: HUMAN;                                              
SOURCE  44 ORGANISM_TAXID: 9606;                                                
SOURCE  45 GENE: COPS5, CSN5, JAB1;                                             
SOURCE  46 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  47 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  48 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  49 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  50 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  51 MOL_ID: 6;                                                           
SOURCE  52 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  53 ORGANISM_COMMON: HUMAN;                                              
SOURCE  54 ORGANISM_TAXID: 9606;                                                
SOURCE  55 GENE: COPS6, CSN6, HVIP;                                             
SOURCE  56 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  57 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  58 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  59 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  60 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  61 MOL_ID: 7;                                                           
SOURCE  62 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  63 ORGANISM_COMMON: HUMAN;                                              
SOURCE  64 ORGANISM_TAXID: 9606;                                                
SOURCE  65 GENE: COPS8, CSN8;                                                   
SOURCE  66 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  67 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  68 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  69 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  70 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  71 MOL_ID: 8;                                                           
SOURCE  72 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  73 ORGANISM_COMMON: HUMAN;                                              
SOURCE  74 ORGANISM_TAXID: 9606;                                                
SOURCE  75 GENE: CUL2;                                                          
SOURCE  76 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  77 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  78 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  79 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  80 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  81 MOL_ID: 9;                                                           
SOURCE  82 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  83 ORGANISM_COMMON: HUMAN;                                              
SOURCE  84 ORGANISM_TAXID: 9606;                                                
SOURCE  85 GENE: ELOB, TCEB2;                                                   
SOURCE  86 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  87 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  88 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  89 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  90 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  91 MOL_ID: 10;                                                          
SOURCE  92 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  93 ORGANISM_COMMON: HUMAN;                                              
SOURCE  94 ORGANISM_TAXID: 9606;                                                
SOURCE  95 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  96 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  97 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  98 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  99 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE 100 MOL_ID: 11;                                                          
SOURCE 101 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 102 ORGANISM_COMMON: HUMAN;                                              
SOURCE 103 ORGANISM_TAXID: 9606;                                                
SOURCE 104 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE 105 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE 106 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE 107 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE 108 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE 109 MOL_ID: 12;                                                          
SOURCE 110 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 111 ORGANISM_COMMON: HUMAN;                                              
SOURCE 112 ORGANISM_TAXID: 9606;                                                
SOURCE 113 GENE: VHL;                                                           
SOURCE 114 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE 115 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE 116 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE 117 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE 118 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE 119 MOL_ID: 13;                                                          
SOURCE 120 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 121 ORGANISM_COMMON: HUMAN;                                              
SOURCE 122 ORGANISM_TAXID: 9606;                                                
SOURCE 123 GENE: COPS7B, CSN7B;                                                 
SOURCE 124 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE 125 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE 126 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE 127 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE 128 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    CULLIN-RING E3 LIGASE COP9 SIGNALOSOME NEDDYLATION, LIGASE            
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    E.P.MORRIS,S.V.FAULL,A.M.C.LAU,A.POLITIS,F.BEURON,N.CRONIN            
REVDAT   2   04-SEP-19 6R6H    1       JRNL                                     
REVDAT   1   28-AUG-19 6R6H    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.    8.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NULL                                      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : 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)  : 8.400                          
REMARK   3   NUMBER OF PARTICLES               : 24040                          
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 6R6H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-MAR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292101371.                                   
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                 : CULLIN-RING E3 LIGASES (CRLS)     
REMARK 245                                    COMPLEXES WITH NEDDYLATED COP9    
REMARK 245                                    SIGNALOSOME (CSN)                 
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 QUANTUM (4K X 4K)     
REMARK 245   MINIMUM DEFOCUS (NM)              : 1800.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 3000.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 45.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 47170                          
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, H, O, P, Q,         
REMARK 350                    AND CHAINS: R, V, G                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    41                                                      
REMARK 465     PRO A    42                                                      
REMARK 465     LEU A    43                                                      
REMARK 465     PRO A    44                                                      
REMARK 465     VAL A    45                                                      
REMARK 465     GLN A    46                                                      
REMARK 465     VAL A    47                                                      
REMARK 465     PHE A    48                                                      
REMARK 465     ASN A    49                                                      
REMARK 465     LEU A    50                                                      
REMARK 465     GLN A    51                                                      
REMARK 465     GLY A    52                                                      
REMARK 465     ALA A    53                                                      
REMARK 465     VAL A    54                                                      
REMARK 465     GLU A    55                                                      
REMARK 465     PRO A    56                                                      
REMARK 465     MET A    57                                                      
REMARK 465     GLN A    58                                                      
REMARK 465     ILE A    59                                                      
REMARK 465     ASP A    60                                                      
REMARK 465     VAL A    61                                                      
REMARK 465     ASP A    62                                                      
REMARK 465     PRO A    63                                                      
REMARK 465     GLN A    64                                                      
REMARK 465     GLU A    65                                                      
REMARK 465     ASP A    66                                                      
REMARK 465     PRO A    67                                                      
REMARK 465     GLN A    68                                                      
REMARK 465     ASN A    69                                                      
REMARK 465     ALA A    70                                                      
REMARK 465     PRO A    71                                                      
REMARK 465     ASP A    72                                                      
REMARK 465     VAL A    73                                                      
REMARK 465     ASN A    74                                                      
REMARK 465     TYR A    75                                                      
REMARK 465     VAL A    76                                                      
REMARK 465     ARG A   142A                                                     
REMARK 465     SER A   142B                                                     
REMARK 465     SER A   142C                                                     
REMARK 465     LEU A   142D                                                     
REMARK 465     ASP A   150                                                      
REMARK 465     ALA A   151                                                      
REMARK 465     ILE A   152                                                      
REMARK 465     PRO A   153                                                      
REMARK 465     GLU A   154                                                      
REMARK 465     SER A   155                                                      
REMARK 465     GLY A   156                                                      
REMARK 465     VAL A   157                                                      
REMARK 465     GLU A   158                                                      
REMARK 465     PRO A   159                                                      
REMARK 465     PRO A   506                                                      
REMARK 465     ARG A   507                                                      
REMARK 465     GLU A   508                                                      
REMARK 465     GLY A   509                                                      
REMARK 465     SER A   510                                                      
REMARK 465     GLN A   511                                                      
REMARK 465     GLY A   512                                                      
REMARK 465     GLU A   513                                                      
REMARK 465     LEU A   514                                                      
REMARK 465     THR A   515                                                      
REMARK 465     PRO A   516                                                      
REMARK 465     ALA A   517                                                      
REMARK 465     ASN A   518                                                      
REMARK 465     SER A   519                                                      
REMARK 465     GLN A   520                                                      
REMARK 465     SER A   521                                                      
REMARK 465     ARG A   522                                                      
REMARK 465     MET A   523                                                      
REMARK 465     SER A   524                                                      
REMARK 465     THR A   525                                                      
REMARK 465     ASN A   526                                                      
REMARK 465     MET A   527                                                      
REMARK 465     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     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     ASN C    29                                                      
REMARK 465     ILE D    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   334                                                      
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 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     MET E 286    CG   SD   CE                                        
REMARK 470     LEU E 287    CG   CD1  CD2                                       
REMARK 470     LEU E 289    CG   CD1  CD2                                       
REMARK 470     GLU E 297    CG   CD   OE1  OE2                                  
REMARK 470     MET O   1    N                                                   
REMARK 470     TYR O  29    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG P  29    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ALA R  17    CB                                                  
REMARK 470     GLN R  57    CG   CD   OE1  NE2                                  
REMARK 470     TRP R 101    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP R 101    CZ3  CH2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    PHE P    15     HA   ILE Q    18              0.14            
REMARK 500   CE3  TRP O    35     CB   ARG Q    38              0.24            
REMARK 500   C    PHE O   490     CD1  ILE O   494              0.25            
REMARK 500   C    VAL O   564     CD   LYS R    19              0.28            
REMARK 500   O    PRO P    69     OE2  GLU Q    59              0.34            
REMARK 500   NZ   LYS P    28     OE1  GLN P    42              0.38            
REMARK 500   CG   TYR O   107     HE3  MET Q    32              0.38            
REMARK 500   CA   SER D   389     CD   PRO D   393              0.39            
REMARK 500   C    GLN E   279     NH2  ARG E   294              0.45            
REMARK 500   CG   PRO B    28     CG   ARG O   648              0.48            
REMARK 500   CB   ASN B    25     CB   LYS O   647              0.48            
REMARK 500   CE1  PHE O    39     OG   SER Q    40              0.48            
REMARK 500   N    ASN O    36     OE2  GLU Q    39              0.50            
REMARK 500   OG   SER O   524     ND1  HIS O   557              0.51            
REMARK 500   O    THR E   249     N    LEU F   221              0.51            
REMARK 500   CG   ASP F   201     OG   SER F   215              0.52            
REMARK 500   CD2  HIS B   370     CD   GLN D   354              0.53            
REMARK 500   O    PRO O   523     OH   TYR O   580              0.54            
REMARK 500   CA   THR P    13     O    GLU Q    15              0.54            
REMARK 500   C    TRP O    35     OE1  GLU Q    39              0.59            
REMARK 500   CA   PRO V   138     N    SER V   139              0.60            
REMARK 500   CB   SER O   506     CB   ASN R    28              0.61            
REMARK 500   CZ3  TRP O    35     HG3  ARG Q    38              0.62            
REMARK 500   OE1  GLN O   521     O    TRP O   555              0.62            
REMARK 500   OD2  ASP B   295     CZ3  TRP R    72              0.63            
REMARK 500   NE2  GLN P    70     HG2  PRO Q    78              0.63            
REMARK 500   CG   ARG O   106     HB1  ALA Q    31              0.64            
REMARK 500   C    SER E   252     CA   SER E   253              0.64            
REMARK 500   N    LYS O   565     CG   LYS R    19              0.65            
REMARK 500   N    ASP P    17     HG   SER Q    19              0.65            
REMARK 500   N    GLN O   521     CD2  LEU O   556              0.65            
REMARK 500   CB   TYR O   107     HE2  MET Q    32              0.66            
REMARK 500   NE1  TRP O    35     HE   ARG Q    38              0.67            
REMARK 500   N    ARG P    29    HG21  ILE P    30              0.67            
REMARK 500   O    TRP E   246     ND1  HIS F   225              0.67            
REMARK 500   O    TYR O   568     O    LYS R    20              0.67            
REMARK 500   C    GLN V    73     CB   LEU V   140              0.68            
REMARK 500   O    TRP E   246     CE1  HIS F   225              0.69            
REMARK 500   O    GLU D   386     N    ILE D   388              0.69            
REMARK 500   O    ASP E   293     CG   LYS E   295              0.69            
REMARK 500   OG1  THR P    16     HE1  PHE Q     5              0.70            
REMARK 500   CA   VAL O   693     CD1  LEU O   694              0.71            
REMARK 500   N    ARG O   551     C    ALA R    34              0.71            
REMARK 500   CZ2  TRP O    35     HD2  ARG Q    38              0.71            
REMARK 500  HG23  ILE P    14     CG   GLU Q    17              0.71            
REMARK 500   O    GLN V    73     CB   LEU V   140              0.71            
REMARK 500   C    ARG O   551     N    ALA R    34              0.72            
REMARK 500   O    ASP B    17     OE1  GLU B    27              0.74            
REMARK 500   C    PRO O   523     OH   TYR O   580              0.74            
REMARK 500   CD   GLU B    19     CA   PHE O   651              0.74            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS    1425 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    SER E 252   C     SER E 253   N       0.253                       
REMARK 500    LEU E 289   C     GLU E 290   N      -0.170                       
REMARK 500    THR O 499   C     VAL O 500   N      -0.855                       
REMARK 500    ARG O 686   NE    ARG O 686   CZ      0.079                       
REMARK 500    ARG O 691   CZ    ARG O 691   NH2     0.079                       
REMARK 500    GLU P  26   C     LEU P  27   N       0.205                       
REMARK 500    LEU P  99   C     PRO P 100   N       0.269                       
REMARK 500    VAL P 102   C     MET P 103   N      -0.502                       
REMARK 500    ILE V 206   C     ALA V 207   N      -0.232                       
REMARK 500    LYS G 172   C     THR G 173   N      -0.240                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 410   CA  -  CB  -  CG  ANGL. DEV. = -14.4 DEGREES          
REMARK 500    PRO B  28   CA  -  N   -  CD  ANGL. DEV. = -12.1 DEGREES          
REMARK 500    SER E 252   CA  -  C   -  N   ANGL. DEV. = -61.7 DEGREES          
REMARK 500    SER E 252   O   -  C   -  N   ANGL. DEV. =  45.2 DEGREES          
REMARK 500    SER E 253   C   -  N   -  CA  ANGL. DEV. = -97.9 DEGREES          
REMARK 500    PHE E 285   CA  -  C   -  N   ANGL. DEV. = -13.5 DEGREES          
REMARK 500    MET E 286   C   -  N   -  CA  ANGL. DEV. = -41.1 DEGREES          
REMARK 500    LEU E 289   CA  -  C   -  N   ANGL. DEV. = -25.9 DEGREES          
REMARK 500    LEU E 289   O   -  C   -  N   ANGL. DEV. =  21.5 DEGREES          
REMARK 500    GLU E 290   C   -  N   -  CA  ANGL. DEV. =  17.0 DEGREES          
REMARK 500    HIS F  44   C   -  N   -  CA  ANGL. DEV. =  19.0 DEGREES          
REMARK 500    THR O 499   CA  -  C   -  N   ANGL. DEV. =  41.0 DEGREES          
REMARK 500    THR O 499   O   -  C   -  N   ANGL. DEV. = -84.8 DEGREES          
REMARK 500    VAL O 500   C   -  N   -  CA  ANGL. DEV. =  17.8 DEGREES          
REMARK 500    MET O 665   CG  -  SD  -  CE  ANGL. DEV. = -10.1 DEGREES          
REMARK 500    ARG O 676   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    MET O 678   CG  -  SD  -  CE  ANGL. DEV. = -11.6 DEGREES          
REMARK 500    ARG O 686   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG O 691   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG O 691   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    LEU P  99   O   -  C   -  N   ANGL. DEV. = -25.0 DEGREES          
REMARK 500    PRO P 100   C   -  N   -  CA  ANGL. DEV. = -15.3 DEGREES          
REMARK 500    PRO P 100   C   -  N   -  CD  ANGL. DEV. = -34.3 DEGREES          
REMARK 500    VAL P 102   CA  -  C   -  N   ANGL. DEV. = -68.8 DEGREES          
REMARK 500    VAL P 102   O   -  C   -  N   ANGL. DEV. =  20.4 DEGREES          
REMARK 500    MET P 103   C   -  N   -  CA  ANGL. DEV. = -67.0 DEGREES          
REMARK 500    LYS P 104   O   -  C   -  N   ANGL. DEV. = -56.8 DEGREES          
REMARK 500    PRO V 138   CA  -  C   -  N   ANGL. DEV. = -93.8 DEGREES          
REMARK 500    PRO V 138   O   -  C   -  N   ANGL. DEV. =  13.8 DEGREES          
REMARK 500    SER V 139   C   -  N   -  CA  ANGL. DEV. = -24.3 DEGREES          
REMARK 500    ILE V 206   O   -  C   -  N   ANGL. DEV. = -34.5 DEGREES          
REMARK 500    ALA V 207   C   -  N   -  CA  ANGL. DEV. = -18.9 DEGREES          
REMARK 500    LYS G 172   CA  -  C   -  N   ANGL. DEV. =  35.9 DEGREES          
REMARK 500    LYS G 172   O   -  C   -  N   ANGL. DEV. = -42.6 DEGREES          
REMARK 500    THR G 173   C   -  N   -  CA  ANGL. DEV. =  19.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  81       31.83    -94.58                                   
REMARK 500    CYS A 107       82.64   -162.71                                   
REMARK 500    THR A 109      -10.34     73.60                                   
REMARK 500    THR A 125      -13.04     72.64                                   
REMARK 500    LEU A 162       98.62    -69.50                                   
REMARK 500    CYS A 211       11.62   -141.79                                   
REMARK 500    LEU A 214      -61.94    -91.62                                   
REMARK 500    ASP A 226       30.83    -93.64                                   
REMARK 500    TYR A 227       41.34   -109.45                                   
REMARK 500    PRO A 265       39.85    -88.84                                   
REMARK 500    ALA A 268       -4.08     79.79                                   
REMARK 500    GLN A 270       -1.06     69.65                                   
REMARK 500    GLU A 273       57.40     36.42                                   
REMARK 500    ARG A 274       71.83     60.12                                   
REMARK 500    ASP A 275       82.07     68.33                                   
REMARK 500    SER A 276       68.36     73.91                                   
REMARK 500    GLN A 277      107.08    -49.67                                   
REMARK 500    ALA A 280       94.39    -68.82                                   
REMARK 500    ARG A 297       63.39     61.10                                   
REMARK 500    CYS A 314       -0.47     69.77                                   
REMARK 500    PHE A 316       78.65   -161.08                                   
REMARK 500    LEU A 319      -28.88   -140.22                                   
REMARK 500    ASN A 345      -40.50   -131.81                                   
REMARK 500    GLU A 446      -53.49   -121.56                                   
REMARK 500    SER A 450       75.91   -100.55                                   
REMARK 500    ASP A 454       97.60    -68.78                                   
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    LEU C   5       31.68    -93.15                                   
REMARK 500    GLN C  18     -155.22   -151.67                                   
REMARK 500    SER C  31       -4.56     71.76                                   
REMARK 500    GLU C  33       -4.92     73.54                                   
REMARK 500    LEU C  46      -13.86   -141.48                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     227 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 TYR A   91     SER A   92                 -146.89                    
REMARK 500 LEU A  110     ARG A  111                  142.11                    
REMARK 500 THR B   83     ASN B   84                 -147.77                    
REMARK 500 ARG C  114     LYS C  115                 -145.98                    
REMARK 500 LEU D  309     LEU D  310                  148.46                    
REMARK 500 VAL E   77     MET E   78                 -149.82                    
REMARK 500 MET E  117     ALA E  118                  149.49                    
REMARK 500 LEU E  289     GLU E  290                  138.85                    
REMARK 500 LEU F  221     ILE F  222                 -142.39                    
REMARK 500 VAL O  191     GLU O  192                  145.46                    
REMARK 500 GLN O  193     TYR O  194                 -149.21                    
REMARK 500 LYS O  291     ASN O  292                  149.72                    
REMARK 500 THR O  499     VAL O  500                  -86.96                    
REMARK 500 GLN O  508     ILE O  509                 -149.51                    
REMARK 500 GLN O  513     ALA O  514                 -149.32                    
REMARK 500 ASN O  567     TYR O  568                  141.90                    
REMARK 500 LEU P   99     PRO P  100                  139.93                    
REMARK 500 ASP R   40     ASN R   41                  146.62                    
REMARK 500 ASN R   41     CYS R   42                  142.83                    
REMARK 500 MET R   50     ASP R   51                  148.17                    
REMARK 500 ASP R   51     LEU R   52                 -143.92                    
REMARK 500 THR R   64     SER R   65                 -138.39                    
REMARK 500 PHE R   79     HIS R   80                  144.55                    
REMARK 500 PRO V  138     SER V  139                   90.74                    
REMARK 500 ILE V  206     ALA V  207                 -110.07                    
REMARK 500 LYS G  172     THR G  173                 -103.94                    
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    PHE E 285        -13.49                                           
REMARK 500    THR O 499        166.03                                           
REMARK 500    LEU P  99         27.36                                           
REMARK 500    VAL P 102         22.32                                           
REMARK 500    LYS P 104         49.94                                           
REMARK 500    PRO V 138        -16.97                                           
REMARK 500    ILE V 206        -40.27                                           
REMARK 500    LYS G 172        -34.02                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN E 401                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-4736   RELATED DB: EMDB                              
REMARK 900 STRUCTURAL BASIS OF CULLIN-2 RING E3 LIGASE REGULATION BY THE COP9   
REMARK 900 SIGNALOSOME                                                          
DBREF  6R6H A   41   527  UNP    Q13098   CSN1_HUMAN       1    491             
DBREF  6R6H B    1   443  UNP    P61201   CSN2_HUMAN       1    443             
DBREF  6R6H C    1   383  UNP    Q9UNS2   CSN3_HUMAN       1    383             
DBREF  6R6H D    1   406  UNP    Q9BT78   CSN4_HUMAN       1    406             
DBREF  6R6H E    1   334  UNP    Q92905   CSN5_HUMAN       1    334             
DBREF  6R6H F   20   327  UNP    Q7L5N1   CSN6_HUMAN      20    327             
DBREF  6R6H H    1   209  UNP    Q99627   CSN8_HUMAN       1    209             
DBREF  6R6H O    1   745  UNP    Q13617   CUL2_HUMAN      20    764             
DBREF  6R6H P    1   104  UNP    Q15370   ELOB_HUMAN       1    104             
DBREF  6R6H Q    1    99  PDB    6R6H     6R6H             1     99             
DBREF  6R6H R   17   102  PDB    6R6H     6R6H            17    102             
DBREF  6R6H V   60   207  UNP    P40337   VHL_HUMAN        7    154             
DBREF  6R6H G    9   214  UNP    Q9H9Q2   CSN7B_HUMAN      9    214             
SEQADV 6R6H ILE C  384  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H GLU C  385  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H LEU C  386  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H ASP C  387  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H GLU C  388  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H ARG C  389  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H LEU C  390  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H LYS C  391  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H ALA C  392  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H MET C  393  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H ASP C  394  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H GLN C  395  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H GLU C  396  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H ILE C  397  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H THR C  398  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H VAL C  399  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H ASN C  400  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H PRO C  401  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H GLN C  402  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H PHE C  403  UNP  Q9UNS2              EXPRESSION TAG                 
SEQADV 6R6H ALA P  105  UNP  Q15370              EXPRESSION TAG                 
SEQADV 6R6H ALA V  208  UNP  P40337              EXPRESSION TAG                 
SEQADV 6R6H ALA V  209  UNP  P40337              EXPRESSION TAG                 
SEQRES   1 A  491  MET PRO LEU PRO VAL GLN VAL PHE ASN LEU GLN GLY ALA          
SEQRES   2 A  491  VAL GLU PRO MET GLN ILE ASP VAL ASP PRO GLN GLU ASP          
SEQRES   3 A  491  PRO GLN ASN ALA PRO ASP VAL ASN TYR VAL VAL GLU ASN          
SEQRES   4 A  491  PRO SER LEU ASP LEU GLU GLN TYR ALA ALA SER TYR SER          
SEQRES   5 A  491  GLY LEU MET ARG ILE GLU ARG LEU GLN PHE ILE ALA ASP          
SEQRES   6 A  491  HIS CYS PRO THR LEU ARG VAL GLU ALA LEU LYS MET ALA          
SEQRES   7 A  491  LEU SER PHE VAL GLN ARG THR PHE ASN VAL ASP MET TYR          
SEQRES   8 A  491  GLU GLU ILE HIS ARG LYS LEU SER GLU ALA THR ARG SER          
SEQRES   9 A  491  SER LEU ARG GLU LEU GLN ASN ALA PRO ASP ALA ILE PRO          
SEQRES  10 A  491  GLU SER GLY VAL GLU PRO PRO ALA LEU ASP THR ALA TRP          
SEQRES  11 A  491  VAL GLU ALA THR ARG LYS LYS ALA LEU LEU LYS LEU GLU          
SEQRES  12 A  491  LYS LEU ASP THR ASP LEU LYS ASN TYR LYS GLY ASN SER          
SEQRES  13 A  491  ILE LYS GLU SER ILE ARG ARG GLY HIS ASP ASP LEU GLY          
SEQRES  14 A  491  ASP HIS TYR LEU ASP CYS GLY ASP LEU SER ASN ALA LEU          
SEQRES  15 A  491  LYS CYS TYR SER ARG ALA ARG ASP TYR CYS THR SER ALA          
SEQRES  16 A  491  LYS HIS VAL ILE ASN MET CYS LEU ASN VAL ILE LYS VAL          
SEQRES  17 A  491  SER VAL TYR LEU GLN ASN TRP SER HIS VAL LEU SER TYR          
SEQRES  18 A  491  VAL SER LYS ALA GLU SER THR PRO GLU ILE ALA GLU GLN          
SEQRES  19 A  491  ARG GLY GLU ARG ASP SER GLN THR GLN ALA ILE LEU THR          
SEQRES  20 A  491  LYS LEU LYS CYS ALA ALA GLY LEU ALA GLU LEU ALA ALA          
SEQRES  21 A  491  ARG LYS TYR LYS GLN ALA ALA LYS CYS LEU LEU LEU ALA          
SEQRES  22 A  491  SER PHE ASP HIS CYS ASP PHE PRO GLU LEU LEU SER PRO          
SEQRES  23 A  491  SER ASN VAL ALA ILE TYR GLY GLY LEU CYS ALA LEU ALA          
SEQRES  24 A  491  THR PHE ASP ARG GLN GLU LEU GLN ARG ASN VAL ILE SER          
SEQRES  25 A  491  SER SER SER PHE LYS LEU PHE LEU GLU LEU GLU PRO GLN          
SEQRES  26 A  491  VAL ARG ASP ILE ILE PHE LYS PHE TYR GLU SER LYS TYR          
SEQRES  27 A  491  ALA SER CYS LEU LYS MET LEU ASP GLU MET LYS ASP ASN          
SEQRES  28 A  491  LEU LEU LEU ASP MET TYR LEU ALA PRO HIS VAL ARG THR          
SEQRES  29 A  491  LEU TYR THR GLN ILE ARG ASN ARG ALA LEU ILE GLN TYR          
SEQRES  30 A  491  PHE SER PRO TYR VAL SER ALA ASP MET HIS ARG MET ALA          
SEQRES  31 A  491  ALA ALA PHE ASN THR THR VAL ALA ALA LEU GLU ASP GLU          
SEQRES  32 A  491  LEU THR GLN LEU ILE LEU GLU GLY LEU ILE SER ALA ARG          
SEQRES  33 A  491  VAL ASP SER HIS SER LYS ILE LEU TYR ALA ARG ASP VAL          
SEQRES  34 A  491  ASP GLN ARG SER THR THR PHE GLU LYS SER LEU LEU MET          
SEQRES  35 A  491  GLY LYS GLU PHE GLN ARG ARG ALA LYS ALA MET MET LEU          
SEQRES  36 A  491  ARG ALA ALA VAL LEU ARG ASN GLN ILE HIS VAL LYS SER          
SEQRES  37 A  491  PRO PRO ARG GLU GLY SER GLN GLY GLU LEU THR PRO ALA          
SEQRES  38 A  491  ASN SER GLN SER ARG MET SER THR ASN MET                      
SEQRES   1 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  403  MET ALA SER ALA LEU GLU GLN PHE VAL ASN SER VAL ARG          
SEQRES   2 C  403  GLN LEU SER ALA GLN GLY GLN MET THR GLN LEU CYS GLU          
SEQRES   3 C  403  LEU ILE ASN LYS SER GLY GLU LEU LEU ALA LYS ASN LEU          
SEQRES   4 C  403  SER HIS LEU ASP THR VAL LEU GLY ALA LEU ASP VAL GLN          
SEQRES   5 C  403  GLU HIS SER LEU GLY VAL LEU ALA VAL LEU PHE VAL LYS          
SEQRES   6 C  403  PHE SER MET PRO SER VAL PRO ASP PHE GLU THR LEU PHE          
SEQRES   7 C  403  SER GLN VAL GLN LEU PHE ILE SER THR CYS ASN GLY GLU          
SEQRES   8 C  403  HIS ILE ARG TYR ALA THR ASP THR PHE ALA GLY LEU CYS          
SEQRES   9 C  403  HIS GLN LEU THR ASN ALA LEU VAL GLU ARG LYS GLN PRO          
SEQRES  10 C  403  LEU ARG GLY ILE GLY ILE LEU LYS GLN ALA ILE ASP LYS          
SEQRES  11 C  403  MET GLN MET ASN THR ASN GLN LEU THR SER ILE HIS ALA          
SEQRES  12 C  403  ASP LEU CYS GLN LEU CYS LEU LEU ALA LYS CYS PHE LYS          
SEQRES  13 C  403  PRO ALA LEU PRO TYR LEU ASP VAL ASP MET MET ASP ILE          
SEQRES  14 C  403  CYS LYS GLU ASN GLY ALA TYR ASP ALA LYS HIS PHE LEU          
SEQRES  15 C  403  CYS TYR TYR TYR TYR GLY GLY MET ILE TYR THR GLY LEU          
SEQRES  16 C  403  LYS ASN PHE GLU ARG ALA LEU TYR PHE TYR GLU GLN ALA          
SEQRES  17 C  403  ILE THR THR PRO ALA MET ALA VAL SER HIS ILE MET LEU          
SEQRES  18 C  403  GLU SER TYR LYS LYS TYR ILE LEU VAL SER LEU ILE LEU          
SEQRES  19 C  403  LEU GLY LYS VAL GLN GLN LEU PRO LYS TYR THR SER GLN          
SEQRES  20 C  403  ILE VAL GLY ARG PHE ILE LYS PRO LEU SER ASN ALA TYR          
SEQRES  21 C  403  HIS GLU LEU ALA GLN VAL TYR SER THR ASN ASN PRO SER          
SEQRES  22 C  403  GLU LEU ARG ASN LEU VAL ASN LYS HIS SER GLU THR PHE          
SEQRES  23 C  403  THR ARG ASP ASN ASN MET GLY LEU VAL LYS GLN CYS LEU          
SEQRES  24 C  403  SER SER LEU TYR LYS LYS ASN ILE GLN ARG LEU THR LYS          
SEQRES  25 C  403  THR PHE LEU THR LEU SER LEU GLN ASP MET ALA SER ARG          
SEQRES  26 C  403  VAL GLN LEU SER GLY PRO GLN GLU ALA GLU LYS TYR VAL          
SEQRES  27 C  403  LEU HIS MET ILE GLU ASP GLY GLU ILE PHE ALA SER ILE          
SEQRES  28 C  403  ASN GLN LYS ASP GLY MET VAL SER PHE HIS ASP ASN PRO          
SEQRES  29 C  403  GLU LYS TYR ASN ASN PRO ALA MET LEU HIS ASN ILE ASP          
SEQRES  30 C  403  GLN GLU MET LEU LYS CYS ILE GLU LEU ASP GLU ARG LEU          
SEQRES  31 C  403  LYS ALA MET ASP GLN GLU ILE THR VAL ASN PRO GLN PHE          
SEQRES   1 D  406  MET ALA ALA ALA VAL ARG GLN ASP LEU ALA GLN LEU MET          
SEQRES   2 D  406  ASN SER SER GLY SER HIS LYS ASP LEU ALA GLY LYS TYR          
SEQRES   3 D  406  ARG GLN ILE LEU GLU LYS ALA ILE GLN LEU SER GLY ALA          
SEQRES   4 D  406  GLU GLN LEU GLU ALA LEU LYS ALA PHE VAL GLU ALA MET          
SEQRES   5 D  406  VAL ASN GLU ASN VAL SER LEU VAL ILE SER ARG GLN LEU          
SEQRES   6 D  406  LEU THR ASP PHE CYS THR HIS LEU PRO ASN LEU PRO ASP          
SEQRES   7 D  406  SER THR ALA LYS GLU ILE TYR HIS PHE THR LEU GLU LYS          
SEQRES   8 D  406  ILE GLN PRO ARG VAL ILE SER PHE GLU GLU GLN VAL ALA          
SEQRES   9 D  406  SER ILE ARG GLN HIS LEU ALA SER ILE TYR GLU LYS GLU          
SEQRES  10 D  406  GLU ASP TRP ARG ASN ALA ALA GLN VAL LEU VAL GLY ILE          
SEQRES  11 D  406  PRO LEU GLU THR GLY GLN LYS GLN TYR ASN VAL ASP TYR          
SEQRES  12 D  406  LYS LEU GLU THR TYR LEU LYS ILE ALA ARG LEU TYR LEU          
SEQRES  13 D  406  GLU ASP ASP ASP PRO VAL GLN ALA GLU ALA TYR ILE ASN          
SEQRES  14 D  406  ARG ALA SER LEU LEU GLN ASN GLU SER THR ASN GLU GLN          
SEQRES  15 D  406  LEU GLN ILE HIS TYR LYS VAL CYS TYR ALA ARG VAL LEU          
SEQRES  16 D  406  ASP TYR ARG ARG LYS PHE ILE GLU ALA ALA GLN ARG TYR          
SEQRES  17 D  406  ASN GLU LEU SER TYR LYS THR ILE VAL HIS GLU SER GLU          
SEQRES  18 D  406  ARG LEU GLU ALA LEU LYS HIS ALA LEU HIS CYS THR ILE          
SEQRES  19 D  406  LEU ALA SER ALA GLY GLN GLN ARG SER ARG MET LEU ALA          
SEQRES  20 D  406  THR LEU PHE LYS ASP GLU ARG CYS GLN GLN LEU ALA ALA          
SEQRES  21 D  406  TYR GLY ILE LEU GLU LYS MET TYR LEU ASP ARG ILE ILE          
SEQRES  22 D  406  ARG GLY ASN GLN LEU GLN GLU PHE ALA ALA MET LEU MET          
SEQRES  23 D  406  PRO HIS GLN LYS ALA THR THR ALA ASP GLY SER SER ILE          
SEQRES  24 D  406  LEU ASP ARG ALA VAL ILE GLU HIS ASN LEU LEU SER ALA          
SEQRES  25 D  406  SER LYS LEU TYR ASN ASN ILE THR PHE GLU GLU LEU GLY          
SEQRES  26 D  406  ALA LEU LEU GLU ILE PRO ALA ALA LYS ALA GLU LYS ILE          
SEQRES  27 D  406  ALA SER GLN MET ILE THR GLU GLY ARG MET ASN GLY PHE          
SEQRES  28 D  406  ILE ASP GLN ILE ASP GLY ILE VAL HIS PHE GLU THR ARG          
SEQRES  29 D  406  GLU ALA LEU PRO THR TRP ASP LYS GLN ILE GLN SER LEU          
SEQRES  30 D  406  CYS PHE GLN VAL ASN ASN LEU LEU GLU LYS ILE SER GLN          
SEQRES  31 D  406  THR ALA PRO GLU TRP THR ALA GLN ALA MET GLU ALA GLN          
SEQRES  32 D  406  MET ALA GLN                                                  
SEQRES   1 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  308  MET GLU VAL ASP ALA ALA VAL VAL PRO SER VAL MET ALA          
SEQRES   2 F  308  CYS GLY VAL THR GLY SER VAL SER VAL ALA LEU HIS PRO          
SEQRES   3 F  308  LEU VAL ILE LEU ASN ILE SER ASP HIS TRP ILE ARG MET          
SEQRES   4 F  308  ARG SER GLN GLU GLY ARG PRO VAL GLN VAL ILE GLY ALA          
SEQRES   5 F  308  LEU ILE GLY LYS GLN GLU GLY ARG ASN ILE GLU VAL MET          
SEQRES   6 F  308  ASN SER PHE GLU LEU LEU SER HIS THR VAL GLU GLU LYS          
SEQRES   7 F  308  ILE ILE ILE ASP LYS GLU TYR TYR TYR THR LYS GLU GLU          
SEQRES   8 F  308  GLN PHE LYS GLN VAL PHE LYS GLU LEU GLU PHE LEU GLY          
SEQRES   9 F  308  TRP TYR THR THR GLY GLY PRO PRO ASP PRO SER ASP ILE          
SEQRES  10 F  308  HIS VAL HIS LYS GLN VAL CYS GLU ILE ILE GLU SER PRO          
SEQRES  11 F  308  LEU PHE LEU LYS LEU ASN PRO MET THR LYS HIS THR ASP          
SEQRES  12 F  308  LEU PRO VAL SER VAL PHE GLU SER VAL ILE ASP ILE ILE          
SEQRES  13 F  308  ASN GLY GLU ALA THR MET LEU PHE ALA GLU LEU THR TYR          
SEQRES  14 F  308  THR LEU ALA THR GLU GLU ALA GLU ARG ILE GLY VAL ASP          
SEQRES  15 F  308  HIS VAL ALA ARG MET THR ALA THR GLY SER GLY GLU ASN          
SEQRES  16 F  308  SER THR VAL ALA GLU HIS LEU ILE ALA GLN HIS SER ALA          
SEQRES  17 F  308  ILE LYS MET LEU HIS SER ARG VAL LYS LEU ILE LEU GLU          
SEQRES  18 F  308  TYR VAL LYS ALA SER GLU ALA GLY GLU VAL PRO PHE ASN          
SEQRES  19 F  308  HIS GLU ILE LEU ARG GLU ALA TYR ALA LEU CYS HIS CYS          
SEQRES  20 F  308  LEU PRO VAL LEU SER THR ASP LYS PHE LYS THR ASP PHE          
SEQRES  21 F  308  TYR ASP GLN CYS ASN ASP VAL GLY LEU MET ALA TYR LEU          
SEQRES  22 F  308  GLY THR ILE THR LYS THR CYS ASN THR MET ASN GLN PHE          
SEQRES  23 F  308  VAL ASN LYS PHE ASN VAL LEU TYR ASP ARG GLN GLY ILE          
SEQRES  24 F  308  GLY ARG ARG MET ARG GLY LEU PHE PHE                          
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 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  105  MET ASP VAL PHE LEU MET ILE ARG ARG HIS LYS THR THR          
SEQRES   2 P  105  ILE PHE THR ASP ALA LYS GLU SER SER THR VAL PHE GLU          
SEQRES   3 P  105  LEU LYS ARG ILE VAL GLU GLY ILE LEU LYS ARG PRO PRO          
SEQRES   4 P  105  ASP GLU GLN ARG LEU TYR LYS ASP ASP GLN LEU LEU ASP          
SEQRES   5 P  105  ASP GLY LYS THR LEU GLY GLU CYS GLY PHE THR SER GLN          
SEQRES   6 P  105  THR ALA ARG PRO GLN ALA PRO ALA THR VAL GLY LEU ALA          
SEQRES   7 P  105  PHE ARG ALA ASP ASP THR PHE GLU ALA LEU CYS ILE GLU          
SEQRES   8 P  105  PRO PHE SER SER PRO PRO GLU LEU PRO ASP VAL MET LYS          
SEQRES   9 P  105  ALA                                                          
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   86  ALA LYS LYS LYS ARG PHE GLU VAL LYS LYS TRP ASN ALA          
SEQRES   2 R   86  VAL ALA LEU TRP ALA TRP ASP ILE VAL VAL ASP ASN CYS          
SEQRES   3 R   86  ALA ILE CYS ARG ASN HIS ILE MET ASP LEU CYS ILE GLU          
SEQRES   4 R   86  CYS GLN ALA ASN GLN ALA SER ALA THR SER GLU GLU CYS          
SEQRES   5 R   86  THR VAL ALA TRP GLY VAL CYS ASN HIS ALA PHE HIS PHE          
SEQRES   6 R   86  HIS CYS ILE SER ARG TRP LEU LYS THR ARG GLN VAL CYS          
SEQRES   7 R   86  PRO LEU ASP ASN ARG GLU TRP GLU                              
SEQRES   1 V  150  ARG PRO VAL LEU ARG SER VAL ASN SER ARG GLU PRO SER          
SEQRES   2 V  150  GLN VAL ILE PHE CYS ASN ARG SER PRO ARG VAL VAL LEU          
SEQRES   3 V  150  PRO VAL TRP LEU ASN PHE ASP GLY GLU PRO GLN PRO TYR          
SEQRES   4 V  150  PRO THR LEU PRO PRO GLY THR GLY ARG ARG ILE HIS SER          
SEQRES   5 V  150  TYR ARG GLY HIS LEU TRP LEU PHE ARG ASP ALA GLY THR          
SEQRES   6 V  150  HIS ASP GLY LEU LEU VAL ASN GLN THR GLU LEU PHE VAL          
SEQRES   7 V  150  PRO SER LEU ASN VAL ASP GLY GLN PRO ILE PHE ALA ASN          
SEQRES   8 V  150  ILE THR LEU PRO VAL TYR THR LEU LYS GLU ARG CYS LEU          
SEQRES   9 V  150  GLN VAL VAL ARG SER LEU VAL LYS PRO GLU ASN TYR ARG          
SEQRES  10 V  150  ARG LEU ASP ILE VAL ARG SER LEU TYR GLU ASP LEU GLU          
SEQRES  11 V  150  ASP HIS PRO ASN VAL GLN LYS ASP LEU GLU ARG LEU THR          
SEQRES  12 V  150  GLN GLU ARG ILE ALA ALA ALA                                  
SEQRES   1 G  206  SER ASN LEU LEU GLU GLN PHE ILE LEU LEU ALA LYS GLY          
SEQRES   2 G  206  THR SER GLY SER ALA LEU THR ALA LEU ILE SER GLN VAL          
SEQRES   3 G  206  LEU GLU ALA PRO GLY VAL TYR VAL PHE GLY GLU LEU LEU          
SEQRES   4 G  206  GLU LEU ALA ASN VAL GLN GLU LEU ALA GLU GLY ALA ASN          
SEQRES   5 G  206  ALA ALA TYR LEU GLN LEU LEU ASN LEU PHE ALA TYR GLY          
SEQRES   6 G  206  THR TYR PRO ASP TYR ILE ALA ASN LYS GLU SER LEU PRO          
SEQRES   7 G  206  GLU LEU SER THR ALA GLN GLN ASN LYS LEU LYS HIS LEU          
SEQRES   8 G  206  THR ILE VAL SER LEU ALA SER ARG MET LYS CYS ILE PRO          
SEQRES   9 G  206  TYR SER VAL LEU LEU LYS ASP LEU GLU MET ARG ASN LEU          
SEQRES  10 G  206  ARG GLU LEU GLU ASP LEU ILE ILE GLU ALA VAL TYR THR          
SEQRES  11 G  206  ASP ILE ILE GLN GLY LYS LEU ASP GLN ARG ASN GLN LEU          
SEQRES  12 G  206  LEU GLU VAL ASP PHE CYS ILE GLY ARG ASP ILE ARG LYS          
SEQRES  13 G  206  LYS ASP ILE ASN ASN ILE VAL LYS THR LEU HIS GLU TRP          
SEQRES  14 G  206  CYS ASP GLY CYS GLU ALA VAL LEU LEU GLY ILE GLU GLN          
SEQRES  15 G  206  GLN VAL LEU ARG ALA ASN GLN TYR LYS GLU ASN HIS ASN          
SEQRES  16 G  206  ARG THR GLN GLN GLN VAL GLU ALA GLU VAL THR                  
HET     ZN  E 401       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL  14   ZN    ZN 2+                                                        
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 VAL A  128  GLN A  146  1                                  19    
HELIX    5 AA5 THR A  164  SER A  192  1                                  29    
HELIX    6 AA6 ILE A  193  ASP A  210  1                                  18    
HELIX    7 AA7 ASP A  213  ARG A  225  1                                  13    
HELIX    8 AA8 SER A  230  GLN A  249  1                                  20    
HELIX    9 AA9 TRP A  251  THR A  264  1                                  14    
HELIX   10 AB1 ALA A  280  ARG A  297  1                                  18    
HELIX   11 AB2 LYS A  298  ALA A  309  1                                  12    
HELIX   12 AB3 SER A  321  PHE A  337  1                                  17    
HELIX   13 AB4 ASP A  338  ASN A  345  1                                   8    
HELIX   14 AB5 PHE A  352  GLU A  359  1                                   8    
HELIX   15 AB6 GLU A  359  SER A  372  1                                  14    
HELIX   16 AB7 LYS A  373  ASP A  391  1                                  19    
HELIX   17 AB8 HIS A  397  SER A  415  1                                  19    
HELIX   18 AB9 ASP A  421  ASN A  430  1                                  10    
HELIX   19 AC1 THR A  432  GLU A  446  1                                  15    
HELIX   20 AC2 GLN A  467  ASN A  498  1                                  32    
HELIX   21 AC3 ASP B    6  ASP B   17  1                                  12    
HELIX   22 AC4 VAL B   30  LEU B   42  1                                  13    
HELIX   23 AC5 ALA B   50  LEU B   60  1                                  11    
HELIX   24 AC6 GLU B   66  LEU B   82  1                                  17    
HELIX   25 AC7 ASN B   84  THR B   97  1                                  14    
HELIX   26 AC8 THR B  104  SER B  122  1                                  19    
HELIX   27 AC9 GLN B  124  LEU B  139  1                                  16    
HELIX   28 AD1 ARG B  146  TYR B  159  1                                  14    
HELIX   29 AD2 TYR B  165  GLN B  180  1                                  16    
HELIX   30 AD3 LEU B  194  LYS B  209  1                                  16    
HELIX   31 AD4 ASN B  210  LEU B  222  1                                  13    
HELIX   32 AD5 ILE B  233  GLY B  249  1                                  17    
HELIX   33 AD6 PHE B  251  GLY B  269  1                                  19    
HELIX   34 AD7 ARG B  272  LYS B  288  1                                  17    
HELIX   35 AD8 GLU B  298  LYS B  303  1                                   6    
HELIX   36 AD9 ASP B  305  ASN B  320  1                                  16    
HELIX   37 AE1 ASP B  322  ASN B  333  1                                  12    
HELIX   38 AE2 ASP B  340  LYS B  364  1                                  25    
HELIX   39 AE3 HIS B  370  ASN B  379  1                                  10    
HELIX   40 AE4 ASP B  381  ASP B  395  1                                  15    
HELIX   41 AE5 GLY B  417  SER B  440  1                                  24    
HELIX   42 AE6 GLN C    7  GLN C   14  1                                   8    
HELIX   43 AE7 MET C   21  LEU C   27  1                                   7    
HELIX   44 AE8 LYS C   37  VAL C   45  1                                   9    
HELIX   45 AE9 HIS C   54  PHE C   66  1                                  13    
HELIX   46 AF1 VAL C   71  PHE C   74  5                                   4    
HELIX   47 AF2 GLU C   75  THR C   87  1                                  13    
HELIX   48 AF3 ALA C   96  ARG C  114  1                                  19    
HELIX   49 AF4 ARG C  119  LYS C  130  1                                  12    
HELIX   50 AF5 SER C  140  ALA C  152  1                                  13    
HELIX   51 AF6 PHE C  155  PRO C  157  5                                   3    
HELIX   52 AF7 ALA C  158  VAL C  164  1                                   7    
HELIX   53 AF8 ASP C  177  LEU C  195  1                                  19    
HELIX   54 AF9 ASN C  197  THR C  211  1                                  15    
HELIX   55 AG1 SER C  217  ILE C  233  1                                  17    
HELIX   56 AG2 SER C  246  PHE C  252  1                                   7    
HELIX   57 AG3 SER C  257  ASN C  270  1                                  14    
HELIX   58 AG4 ASN C  271  HIS C  282  1                                  12    
HELIX   59 AG5 HIS C  282  ASP C  289  1                                   8    
HELIX   60 AG6 GLY C  293  PHE C  314  1                                  22    
HELIX   61 AG7 GLN C  320  VAL C  326  1                                   7    
HELIX   62 AG8 SER C  329  ASP C  344  1                                  16    
HELIX   63 AG9 ASN C  369  ASN C  400  1                                  32    
HELIX   64 AH1 ALA D    2  SER D   15  1                                  14    
HELIX   65 AH2 SER D   18  GLN D   28  1                                  11    
HELIX   66 AH3 GLU D   31  GLN D   35  1                                   5    
HELIX   67 AH4 GLY D   38  VAL D   53  1                                  16    
HELIX   68 AH5 SER D   58  LEU D   76  1                                  19    
HELIX   69 AH6 PRO D   77  ILE D   92  1                                  16    
HELIX   70 AH7 VAL D   96  SER D   98  5                                   3    
HELIX   71 AH8 PHE D   99  GLU D  118  1                                  20    
HELIX   72 AH9 ASP D  119  GLY D  129  1                                  11    
HELIX   73 AI1 ASN D  140  ASP D  159  1                                  20    
HELIX   74 AI2 ASP D  160  SER D  172  1                                  13    
HELIX   75 AI3 LEU D  173  GLN D  175  5                                   3    
HELIX   76 AI4 ASN D  180  ARG D  198  1                                  19    
HELIX   77 AI5 LYS D  200  LYS D  214  1                                  15    
HELIX   78 AI6 HIS D  218  ALA D  236  1                                  19    
HELIX   79 AI7 GLY D  239  ASP D  252  1                                  14    
HELIX   80 AI8 GLU D  253  LEU D  258  1                                   6    
HELIX   81 AI9 ALA D  260  LEU D  269  1                                  10    
HELIX   82 AJ1 ARG D  274  MET D  284  1                                  11    
HELIX   83 AJ2 ILE D  299  SER D  311  1                                  13    
HELIX   84 AJ3 PHE D  321  LEU D  328  1                                   8    
HELIX   85 AJ4 ALA D  332  GLU D  345  1                                  14    
HELIX   86 AJ5 ASP D  353  ASP D  356  5                                   4    
HELIX   87 AJ6 ALA D  366  GLU D  386  1                                  21    
HELIX   88 AJ7 ALA D  392  MET D  404  1                                  13    
HELIX   89 AJ8 ALA D  405  GLN D  406  5                                   2    
HELIX   90 AJ9 SER E   24  ILE E   28  5                                   5    
HELIX   91 AK1 ASP E   32  ALA E   41  1                                  10    
HELIX   92 AK2 LYS E   43  ASP E   48  1                                   6    
HELIX   93 AK3 ALA E   59  SER E   71  1                                  13    
HELIX   94 AK4 ALA E  109  ALA E  113  5                                   5    
HELIX   95 AK5 TYR E  114  LYS E  125  1                                  12    
HELIX   96 AK6 GLN E  126  GLY E  128  5                                   3    
HELIX   97 AK7 SER E  148  GLU E  163  1                                  16    
HELIX   98 AK8 PRO E  207  CYS E  218  1                                  12    
HELIX   99 AK9 SER E  231  LEU E  250  1                                  20    
HELIX  100 AL1 LEU E  255  ALA E  259  5                                   5    
HELIX  101 AL2 ASP E  260  GLN E  279  1                                  20    
HELIX  102 AL3 LYS E  299  PHE E  328  1                                  30    
HELIX  103 AL4 PRO F   45  GLY F   63  1                                  19    
HELIX  104 AL5 ASP F  101  LYS F  113  1                                  13    
HELIX  105 AL6 ASP F  132  CYS F  143  1                                  12    
HELIX  106 AL7 GLU F  193  MET F  206  1                                  14    
HELIX  107 AL8 LEU F  221  GLU F  246  1                                  26    
HELIX  108 AL9 ASN F  253  LEU F  267  1                                  15    
HELIX  109 AM1 ASP F  273  ASP F  273  1                                   1    
HELIX  110 AM2 PHE F  275  TYR F  313  1                                  39    
HELIX  111 AM3 SER H   12  ALA H   27  1                                  16    
HELIX  112 AM4 THR H   33  HIS H   47  1                                  15    
HELIX  113 AM5 ASN H   51  LYS H   58  1                                   8    
HELIX  114 AM6 PRO H   61  ASN H   68  1                                   8    
HELIX  115 AM7 ASN H   68  ARG H   84  1                                  17    
HELIX  116 AM8 ASP H   85  ASN H   94  1                                  10    
HELIX  117 AM9 VAL H  102  GLN H  123  1                                  22    
HELIX  118 AN1 ILE H  129  VAL H  137  1                                   9    
HELIX  119 AN2 PRO H  140  GLN H  151  1                                  12    
HELIX  120 AN3 GLN H  195  GLU H  208  1                                  14    
HELIX  121 AN4 VAL O    8  VAL O   24  1                                  17    
HELIX  122 AN5 GLU O   31  VAL O   47  1                                  17    
HELIX  123 AN6 PRO O   52  LYS O   74  1                                  23    
HELIX  124 AN7 GLU O   80  ILE O  113  1                                  34    
HELIX  125 AN8 GLU O  138  ASN O  169  1                                  32    
HELIX  126 AN9 ASP O  170  GLY O  172  5                                   3    
HELIX  127 AO1 LYS O  179  HIS O  190  1                                  12    
HELIX  128 AO2 LEU O  200  PHE O  207  1                                   8    
HELIX  129 AO3 PHE O  207  SER O  230  1                                  24    
HELIX  130 AO4 CYS O  232  TYR O  253  1                                  22    
HELIX  131 AO5 SER O  257  ALA O  272  1                                  16    
HELIX  132 AO6 LEU O  275  GLN O  288  1                                  14    
HELIX  133 AO7 ASN O  292  VAL O  304  1                                  13    
HELIX  134 AO8 GLY O  307  THR O  327  1                                  21    
HELIX  135 AO9 MET O  335  THR O  356  1                                  22    
HELIX  136 AP1 ASP O  361  TYR O  378  1                                  18    
HELIX  137 AP2 CYS O  385  LYS O  400  1                                  16    
HELIX  138 AP3 ASN O  409  LYS O  423  1                                  15    
HELIX  139 AP4 ASP O  427  GLY O  446  1                                  20    
HELIX  140 AP5 SER O  450  CYS O  465  1                                  16    
HELIX  141 AP6 TYR O  467  LYS O  495  1                                  29    
HELIX  142 AP7 PRO O  530  PHE O  548  1                                  19    
HELIX  143 AP8 LEU O  556  CYS O  560  5                                   5    
HELIX  144 AP9 THR O  578  PHE O  588  1                                  11    
HELIX  145 AQ1 SER O  595  SER O  602  1                                   8    
HELIX  146 AQ2 GLU O  607  VAL O  620  1                                  14    
HELIX  147 AQ3 PRO O  662  ARG O  691  1                                  30    
HELIX  148 AQ4 HIS O  696  SER O  707  1                                  12    
HELIX  149 AQ5 MET O  717  LYS O  728  1                                  12    
HELIX  150 AQ6 VAL P   31  LEU P   35  1                                   5    
HELIX  151 AQ7 ARG Q   20  MET Q   24  1                                   5    
HELIX  152 AQ8 SER Q   26  GLY Q   35  1                                  10    
HELIX  153 AQ9 ASP Q   50  SER Q   71  1                                  22    
HELIX  154 AR1 PRO Q   83  SER Q   98  1                                  16    
HELIX  155 AR2 CYS R   53  GLN R   60  1                                   8    
HELIX  156 AR3 HIS R   80  ARG R   91  1                                  12    
HELIX  157 AR4 LEU V  129  THR V  133  5                                   5    
HELIX  158 AR5 THR V  157  LEU V  169  1                                  13    
HELIX  159 AR6 LYS V  171  ARG V  176  1                                   6    
HELIX  160 AR7 VAL V  181  GLU V  189  1                                   9    
HELIX  161 AR8 ASN V  193  ALA V  207  1                                  15    
HELIX  162 AR9 ASN G   10  THR G   22  1                                  13    
HELIX  163 AS1 SER G   23  GLU G   36  1                                  14    
HELIX  164 AS2 GLU G   45  GLU G   48  5                                   4    
HELIX  165 AS3 LEU G   49  ALA G   56  1                                   8    
HELIX  166 AS4 ASN G   60  TYR G   72  1                                  13    
HELIX  167 AS5 THR G   74  ASN G   81  1                                   8    
HELIX  168 AS6 SER G   89  MET G  108  1                                  20    
HELIX  169 AS7 PRO G  112  LEU G  120  1                                   9    
HELIX  170 AS8 ASN G  124  THR G  138  1                                  15    
HELIX  171 AS9 ASP G  166  THR G  214  1                                  49    
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 B 368  ILE B 369  0                                        
SHEET    2 AA2 2 LEU B 409  GLU B 410 -1  O  LEU B 409   N  ILE B 369           
SHEET    1 AA3 2 ASN D 318  THR D 320  0                                        
SHEET    2 AA3 2 ILE D 358  HIS D 360 -1  O  VAL D 359   N  ILE D 319           
SHEET    1 AA4 4 TYR E  54  ILE E  57  0                                        
SHEET    2 AA4 4 THR E  89  ILE E  92  1  O  MET E  90   N  TYR E  54           
SHEET    3 AA4 4 MET E  81  ASP E  86 -1  N  ASP E  86   O  THR E  89           
SHEET    4 AA4 4 ASN E 132  GLY E 135 -1  O  ILE E 134   N  MET E  81           
SHEET    1 AA5 3 VAL E 168  VAL E 169  0                                        
SHEET    2 AA5 3 GLY E 184  THR E 188 -1  O  GLY E 184   N  VAL E 169           
SHEET    3 AA5 3 TYR E 221  LEU E 224 -1  O  TYR E 222   N  ARG E 187           
SHEET    1 AA6 6 ASN F  80  ASN F  85  0                                        
SHEET    2 AA6 6 GLY F  70  GLU F  77 -1  N  GLU F  77   O  ASN F  80           
SHEET    3 AA6 6 GLY F 123  TYR F 125 -1  N  GLY F 123   O  LEU F  72           
SHEET    4 AA6 6 LEU F 150  LYS F 153  1  O  LEU F 152   N  TRP F 124           
SHEET    5 AA6 6 SER F 166  ILE F 175 -1  O  PHE F 168   N  PHE F 151           
SHEET    6 AA6 6 GLU F 178  GLU F 185 -1  O  THR F 180   N  ASP F 173           
SHEET    1 AA7 2 SER F  91  VAL F  94  0                                        
SHEET    2 AA7 2 LYS F  97  ILE F 100 -1  O  LYS F  97   N  VAL F  94           
SHEET    1 AA8 2 GLN O 508  ILE O 509  0                                        
SHEET    2 AA8 2 VAL R  30  ALA R  31  1  O  ALA R  31   N  GLN O 508           
SHEET    1 AA9 2 ILE O 623  HIS O 625  0                                        
SHEET    2 AA9 2 PHE O 638  LEU O 640 -1  O  SER O 639   N  ASN O 624           
SHEET    1 AB1 2 ILE O 731  GLU O 732  0                                        
SHEET    2 AB1 2 SER O 742  TYR O 743 -1  O  SER O 742   N  GLU O 732           
SHEET    1 AB2 3 PHE P  15  ASP P  17  0                                        
SHEET    2 AB2 3 PHE P   4  ILE P   7 -1  N  LEU P   5   O  THR P  16           
SHEET    3 AB2 3 ALA P  73  VAL P  75  1  O  ALA P  73   N  PHE P   4           
SHEET    1 AB3 3 LYS Q  14  SER Q  19  0                                        
SHEET    2 AB3 3 PHE Q   5  SER Q  10 -1  N  SER Q  10   O  LYS Q  14           
SHEET    3 AB3 3 ARG Q  43  GLU Q  45  1  O  ILE Q  44   N  VAL Q   9           
SHEET    1 AB4 2 PRO V  71  ASN V  78  0                                        
SHEET    2 AB4 2 THR V 105  TYR V 112 -1  O  THR V 105   N  ASN V  78           
SHEET    1 AB5 3 PRO V  95  PRO V  97  0                                        
SHEET    2 AB5 3 LEU V  85  LEU V  89 -1  N  TRP V  88   O  GLN V  96           
SHEET    3 AB5 3 LEU V 118  ARG V 120 -1  O  ARG V 120   N  LEU V  85           
SHEET    1 AB6 2 LEU G 145  ASP G 146  0                                        
SHEET    2 AB6 2 LEU G 151  LEU G 152 -1  O  LEU G 151   N  ASP G 146           
CISPEP   1 GLU E  163    PRO E  164          0        11.24                     
CISPEP   2 LEU F  267    PRO F  268          0        -4.65                     
CISPEP   3 LEU O   27    GLU O   28          0        -1.96                     
CISPEP   4 VAL R   38    VAL R   39          0        11.55                     
SITE     1 AC1  5 ARG E 106  ASN E 108  ILE E 150  ASP E 151                    
SITE     2 AC1  5 THR E 154                                                     
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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