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Database: PDB
Entry: 6R7H
LinkDB: 6R7H
Original site: 6R7H 
HEADER    LIGASE                                  28-MAR-19   6R7H              
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: ELONGIN-C;                                                 
COMPND   9 CHAIN: Q;                                                            
COMPND  10 SYNONYM: ELOC,ELONGIN 15 KDA SUBUNIT,RNA POLYMERASE II TRANSCRIPTION 
COMPND  11 FACTOR SIII SUBUNIT C,SIII P15,TRANSCRIPTION ELONGATION FACTOR B     
COMPND  12 POLYPEPTIDE 1;                                                       
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: CULLIN-2;                                                  
COMPND  16 CHAIN: O;                                                            
COMPND  17 SYNONYM: CUL-2;                                                      
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RBX1;                          
COMPND  21 CHAIN: R;                                                            
COMPND  22 ENGINEERED: YES;                                                     
COMPND  23 MOL_ID: 5;                                                           
COMPND  24 MOLECULE: COP9 SIGNALOSOME COMPLEX SUBUNIT 2;                        
COMPND  25 CHAIN: B;                                                            
COMPND  26 SYNONYM: SIGNALOSOME SUBUNIT 2,ALIEN HOMOLOG,JAB1-CONTAINING         
COMPND  27 SIGNALOSOME SUBUNIT 2,THYROID RECEPTOR-INTERACTING PROTEIN 15,TRIP-  
COMPND  28 15;                                                                  
COMPND  29 ENGINEERED: YES;                                                     
COMPND  30 MOL_ID: 6;                                                           
COMPND  31 MOLECULE: COP9 SIGNALOSOME COMPLEX SUBUNIT 3;                        
COMPND  32 CHAIN: C;                                                            
COMPND  33 SYNONYM: SIGNALOSOME SUBUNIT 3,JAB1-CONTAINING SIGNALOSOME SUBUNIT 3;
COMPND  34 ENGINEERED: YES;                                                     
COMPND  35 MOL_ID: 7;                                                           
COMPND  36 MOLECULE: COP9 SIGNALOSOME COMPLEX SUBUNIT 4;                        
COMPND  37 CHAIN: D;                                                            
COMPND  38 SYNONYM: SIGNALOSOME SUBUNIT 4,JAB1-CONTAINING SIGNALOSOME SUBUNIT 4;
COMPND  39 ENGINEERED: YES;                                                     
COMPND  40 MOL_ID: 8;                                                           
COMPND  41 MOLECULE: COP9 SIGNALOSOME COMPLEX SUBUNIT 5;                        
COMPND  42 CHAIN: E;                                                            
COMPND  43 SYNONYM: SIGNALOSOME SUBUNIT 5,JUN ACTIVATION DOMAIN-BINDING PROTEIN 
COMPND  44 1;                                                                   
COMPND  45 EC: 3.4.-.-;                                                         
COMPND  46 ENGINEERED: YES;                                                     
COMPND  47 MOL_ID: 9;                                                           
COMPND  48 MOLECULE: COP9 SIGNALOSOME COMPLEX SUBUNIT 6;                        
COMPND  49 CHAIN: F;                                                            
COMPND  50 SYNONYM: SIGNALOSOME SUBUNIT 6,JAB1-CONTAINING SIGNALOSOME SUBUNIT 6,
COMPND  51 MOV34 HOMOLOG,VPR-INTERACTING PROTEIN,HVIP;                          
COMPND  52 ENGINEERED: YES;                                                     
COMPND  53 MOL_ID: 10;                                                          
COMPND  54 MOLECULE: COP9 SIGNALOSOME COMPLEX SUBUNIT 7B;                       
COMPND  55 CHAIN: G;                                                            
COMPND  56 SYNONYM: SIGNALOSOME SUBUNIT 7B,JAB1-CONTAINING SIGNALOSOME SUBUNIT  
COMPND  57 7B;                                                                  
COMPND  58 ENGINEERED: YES;                                                     
COMPND  59 MOL_ID: 11;                                                          
COMPND  60 MOLECULE: COP9 SIGNALOSOME COMPLEX SUBUNIT 8;                        
COMPND  61 CHAIN: H;                                                            
COMPND  62 SYNONYM: SIGNALOSOME SUBUNIT 8,COP9 HOMOLOG,HCOP9,JAB1-CONTAINING    
COMPND  63 SIGNALOSOME SUBUNIT 8;                                               
COMPND  64 ENGINEERED: YES;                                                     
COMPND  65 MOL_ID: 12;                                                          
COMPND  66 MOLECULE: ELONGIN-B;                                                 
COMPND  67 CHAIN: P;                                                            
COMPND  68 SYNONYM: ELOB,ELONGIN 18 KDA SUBUNIT,RNA POLYMERASE II TRANSCRIPTION 
COMPND  69 FACTOR SIII SUBUNIT B,SIII P18,TRANSCRIPTION ELONGATION FACTOR B     
COMPND  70 POLYPEPTIDE 2;                                                       
COMPND  71 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GPS1, COPS1, CSN1;                                             
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: ELOC, TCEB1;                                                   
SOURCE  13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: CUL2;                                                          
SOURCE  20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  26 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  27 MOL_ID: 5;                                                           
SOURCE  28 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  29 ORGANISM_COMMON: HUMAN;                                              
SOURCE  30 ORGANISM_TAXID: 9606;                                                
SOURCE  31 GENE: COPS2, CSN2, TRIP15;                                           
SOURCE  32 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  33 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  34 MOL_ID: 6;                                                           
SOURCE  35 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  36 ORGANISM_COMMON: HUMAN;                                              
SOURCE  37 ORGANISM_TAXID: 9606;                                                
SOURCE  38 GENE: COPS3, CSN3;                                                   
SOURCE  39 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  40 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  41 MOL_ID: 7;                                                           
SOURCE  42 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  43 ORGANISM_COMMON: HUMAN;                                              
SOURCE  44 ORGANISM_TAXID: 9606;                                                
SOURCE  45 GENE: COPS4, CSN4;                                                   
SOURCE  46 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  47 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  48 MOL_ID: 8;                                                           
SOURCE  49 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  50 ORGANISM_COMMON: HUMAN;                                              
SOURCE  51 ORGANISM_TAXID: 9606;                                                
SOURCE  52 GENE: COPS5, CSN5, JAB1;                                             
SOURCE  53 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  54 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  55 MOL_ID: 9;                                                           
SOURCE  56 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  57 ORGANISM_COMMON: HUMAN;                                              
SOURCE  58 ORGANISM_TAXID: 9606;                                                
SOURCE  59 GENE: COPS6, CSN6, HVIP;                                             
SOURCE  60 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  61 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  62 MOL_ID: 10;                                                          
SOURCE  63 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  64 ORGANISM_COMMON: HUMAN;                                              
SOURCE  65 ORGANISM_TAXID: 9606;                                                
SOURCE  66 GENE: COPS7B, CSN7B;                                                 
SOURCE  67 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  68 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  69 MOL_ID: 11;                                                          
SOURCE  70 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  71 ORGANISM_COMMON: HUMAN;                                              
SOURCE  72 ORGANISM_TAXID: 9606;                                                
SOURCE  73 GENE: COPS8, CSN8;                                                   
SOURCE  74 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  75 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  76 MOL_ID: 12;                                                          
SOURCE  77 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  78 ORGANISM_COMMON: HUMAN;                                              
SOURCE  79 ORGANISM_TAXID: 9606;                                                
SOURCE  80 GENE: ELOB, TCEB2;                                                   
SOURCE  81 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  82 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    CULLIN-RING E3 LIGASES (CRLS) COP9 SIGNALOSOME (CSN) DENEDDYLATION,   
KEYWDS   2 LIGASE                                                               
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    S.V.FAULL,A.M.C.LAU,F.BEURON,N.B.CRONIN,E.P.MORRIS,A.POLITIS          
REVDAT   2   04-SEP-19 6R7H    1       JRNL                                     
REVDAT   1   28-AUG-19 6R7H    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.    8.80 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)  : 8.800                          
REMARK   3   NUMBER OF PARTICLES               : 17191                          
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 6R7H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-MAR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292101553.                                   
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                 : TERNARY COMPLEX OF COP9           
REMARK 245                                    SIGNALOSOME (CSN1-CSN8) WITH      
REMARK 245                                    CULLIN-RING E3 LIGASE             
REMARK 245                                    DENEDDYLATED CULLIN-2, RBX1,      
REMARK 245                                    ELONGIN-B AND ELONGINC            
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                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 83.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, Q, O, R, B, C, D, E, F, G,         
REMARK 350                    AND CHAINS: H, P                                  
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     LYS H   166                                                      
REMARK 465     PRO H   167                                                      
REMARK 465     VAL H   168                                                      
REMARK 465     ALA H   169                                                      
REMARK 465     GLY H   170                                                      
REMARK 465     ALA H   171                                                      
REMARK 465     LEU H   172                                                      
REMARK 465     ASP H   173                                                      
REMARK 465     VAL H   174                                                      
REMARK 465     SER H   175                                                      
REMARK 465     PHE H   176                                                      
REMARK 465     ASN H   177                                                      
REMARK 465     LYS H   178                                                      
REMARK 465     PHE H   179                                                      
REMARK 465     ILE H   180                                                      
REMARK 465     PRO H   181                                                      
REMARK 465     LEU H   182                                                      
REMARK 465     SER H   183                                                      
REMARK 465     GLU H   184                                                      
REMARK 465     PRO H   185                                                      
REMARK 465     ALA H   186                                                      
REMARK 465     PRO H   187                                                      
REMARK 465     VAL H   188                                                      
REMARK 465     PRO H   189                                                      
REMARK 465     PRO H   190                                                      
REMARK 465     ILE H   191                                                      
REMARK 465     PRO H   192                                                      
REMARK 465     ASN H   193                                                      
REMARK 465     GLU H   194                                                      
REMARK 465     GLN H   195                                                      
REMARK 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    TYR D 316   CG    TYR D 316   CD2     0.298                       
REMARK 500    TYR D 316   CG    TYR D 316   CD1     0.298                       
REMARK 500    TYR D 316   CD1   TYR D 316   CE1     0.598                       
REMARK 500    TYR D 316   CE1   TYR D 316   CZ      0.378                       
REMARK 500    TYR D 316   CZ    TYR D 316   CE2     0.376                       
REMARK 500    TYR D 316   CE2   TYR D 316   CD2     0.599                       
REMARK 500    ARG G 126   CG    ARG G 126   CD      1.694                       
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    ARG G 126   CB  -  CG  -  CD  ANGL. DEV. =  21.2 DEGREES          
REMARK 500    ARG G 126   CG  -  CD  -  NE  ANGL. DEV. =  13.6 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    LEU A  70       50.24    -97.02                                   
REMARK 500    THR A  85       86.24     56.10                                   
REMARK 500    GLN A 110      -38.90   -150.64                                   
REMARK 500    ASP A 127     -161.99   -128.64                                   
REMARK 500    THR A 193       -5.08   -152.94                                   
REMARK 500    ASN A 214       79.30   -107.71                                   
REMARK 500    ILE A 231       94.72     61.05                                   
REMARK 500    GLU A 233     -160.26     57.13                                   
REMARK 500    ARG A 235       -8.49   -147.25                                   
REMARK 500    ARG A 238     -140.87     59.07                                   
REMARK 500    ASP A 239      -81.21    -88.31                                   
REMARK 500    LYS A 262       73.27   -119.22                                   
REMARK 500    ASP A 276       70.59   -154.68                                   
REMARK 500    HIS A 277      -19.29   -154.65                                   
REMARK 500    CYS A 278       81.10     56.24                                   
REMARK 500    ASP A 279     -161.39     57.69                                   
REMARK 500    GLU A 282       53.45   -149.13                                   
REMARK 500    ASP A 302     -157.13    -92.17                                   
REMARK 500    ASN A 309      -67.36   -105.93                                   
REMARK 500    LYS A 337       70.18   -109.66                                   
REMARK 500    VAL A 382      -12.60   -155.72                                   
REMARK 500    THR A 395     -159.92   -121.38                                   
REMARK 500    HIS A 465     -155.84   -101.89                                   
REMARK 500    TYR Q   8       73.79   -108.28                                   
REMARK 500    PRO Q  14     -150.19    -78.48                                   
REMARK 500    ASN Q  55       15.56   -153.08                                   
REMARK 500    PRO Q  66     -135.60    -78.44                                   
REMARK 500    TYR Q  83       42.28    -89.01                                   
REMARK 500    SER Q  87       70.81   -156.05                                   
REMARK 500    ARG O   6     -152.99   -101.07                                   
REMARK 500    LEU O  27       71.33     56.12                                   
REMARK 500    TYR O  49      153.57     67.52                                   
REMARK 500    GLN O  82       25.53   -159.32                                   
REMARK 500    ILE O 113       86.13     57.93                                   
REMARK 500    ASN O 116     -150.99   -107.79                                   
REMARK 500    ALA O 121       76.03   -153.68                                   
REMARK 500    MET O 132      -83.46    -85.66                                   
REMARK 500    PRO O 154       78.88    -59.10                                   
REMARK 500    LEU O 155       -7.09   -157.21                                   
REMARK 500    ASN O 169       97.76    -69.62                                   
REMARK 500    GLN O 193     -169.79   -117.64                                   
REMARK 500    LYS O 197     -146.54   -135.51                                   
REMARK 500    PRO O 199       34.11    -88.01                                   
REMARK 500    PHE O 207      -51.93   -153.89                                   
REMARK 500    GLU O 229      -66.52   -104.31                                   
REMARK 500    MET O 270      -74.09    -74.39                                   
REMARK 500    ALA O 272      -77.13   -164.51                                   
REMARK 500    HIS O 274       34.25    -90.07                                   
REMARK 500    GLN O 288     -142.31   -107.22                                   
REMARK 500    THR O 331     -120.63     57.97                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     196 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-4741   RELATED DB: EMDB                              
REMARK 900 STRUCTURAL BASIS OF CULLIN-2 RING E3 LIGASE REGULATION BY THE COP9   
REMARK 900 SIGNALOSOME                                                          
DBREF  6R7H A   37   469  UNP    Q13098   CSN1_HUMAN      37    469             
DBREF  6R7H Q    1   112  UNP    Q15369   ELOC_HUMAN       1    112             
DBREF  6R7H O    1   654  UNP    Q13617   CUL2_HUMAN      20    673             
DBREF  6R7H R   19   108  PDB    6R7H     6R7H            19    108             
DBREF  6R7H B   30   443  UNP    P61201   CSN2_HUMAN      30    443             
DBREF  6R7H C    1   403  UNP    Q9UNS2   CSN3_HUMAN       1    403             
DBREF  6R7H D    1   406  UNP    Q9BT78   CSN4_HUMAN       1    406             
DBREF  6R7H E   24   334  UNP    Q92905   CSN5_HUMAN      24    334             
DBREF  6R7H F   29   316  UNP    Q7L5N1   CSN6_HUMAN      29    316             
DBREF  6R7H G    8   215  UNP    Q9H9Q2   CSN7B_HUMAN      8    215             
DBREF  6R7H H   11   209  UNP    Q99627   CSN8_HUMAN      11    209             
DBREF  6R7H P    1   104  UNP    Q15370   ELOB_HUMAN       1    104             
SEQRES   1 A  433  VAL GLU ASN PRO SER LEU ASP LEU GLU GLN TYR ALA ALA          
SEQRES   2 A  433  SER TYR SER GLY LEU MET ARG ILE GLU ARG LEU GLN PHE          
SEQRES   3 A  433  ILE ALA ASP HIS CYS PRO THR LEU ARG VAL GLU ALA LEU          
SEQRES   4 A  433  LYS MET ALA LEU SER PHE VAL GLN ARG THR PHE ASN VAL          
SEQRES   5 A  433  ASP MET TYR GLU GLU ILE HIS ARG LYS LEU SER GLU ALA          
SEQRES   6 A  433  THR ARG SER SER LEU ARG GLU LEU GLN ASN ALA PRO ASP          
SEQRES   7 A  433  ALA ILE PRO GLU SER GLY VAL GLU PRO PRO ALA LEU ASP          
SEQRES   8 A  433  THR ALA TRP VAL GLU ALA THR ARG LYS LYS ALA LEU LEU          
SEQRES   9 A  433  LYS LEU GLU LYS LEU ASP THR ASP LEU LYS ASN TYR LYS          
SEQRES  10 A  433  GLY ASN SER ILE LYS GLU SER ILE ARG ARG GLY HIS ASP          
SEQRES  11 A  433  ASP LEU GLY ASP HIS TYR LEU ASP CYS GLY ASP LEU SER          
SEQRES  12 A  433  ASN ALA LEU LYS CYS TYR SER ARG ALA ARG ASP TYR CYS          
SEQRES  13 A  433  THR SER ALA LYS HIS VAL ILE ASN MET CYS LEU ASN VAL          
SEQRES  14 A  433  ILE LYS VAL SER VAL TYR LEU GLN ASN TRP SER HIS VAL          
SEQRES  15 A  433  LEU SER TYR VAL SER LYS ALA GLU SER THR PRO GLU ILE          
SEQRES  16 A  433  ALA GLU GLN ARG GLY GLU ARG ASP SER GLN THR GLN ALA          
SEQRES  17 A  433  ILE LEU THR LYS LEU LYS CYS ALA ALA GLY LEU ALA GLU          
SEQRES  18 A  433  LEU ALA ALA ARG LYS TYR LYS GLN ALA ALA LYS CYS LEU          
SEQRES  19 A  433  LEU LEU ALA SER PHE ASP HIS CYS ASP PHE PRO GLU LEU          
SEQRES  20 A  433  LEU SER PRO SER ASN VAL ALA ILE TYR GLY GLY LEU CYS          
SEQRES  21 A  433  ALA LEU ALA THR PHE ASP ARG GLN GLU LEU GLN ARG ASN          
SEQRES  22 A  433  VAL ILE SER SER SER SER PHE LYS LEU PHE LEU GLU LEU          
SEQRES  23 A  433  GLU PRO GLN VAL ARG ASP ILE ILE PHE LYS PHE TYR GLU          
SEQRES  24 A  433  SER LYS TYR ALA SER CYS LEU LYS MET LEU ASP GLU MET          
SEQRES  25 A  433  LYS ASP ASN LEU LEU LEU ASP MET TYR LEU ALA PRO HIS          
SEQRES  26 A  433  VAL ARG THR LEU TYR THR GLN ILE ARG ASN ARG ALA LEU          
SEQRES  27 A  433  ILE GLN TYR PHE SER PRO TYR VAL SER ALA ASP MET HIS          
SEQRES  28 A  433  ARG MET ALA ALA ALA PHE ASN THR THR VAL ALA ALA LEU          
SEQRES  29 A  433  GLU ASP GLU LEU THR GLN LEU ILE LEU GLU GLY LEU ILE          
SEQRES  30 A  433  SER ALA ARG VAL ASP SER HIS SER LYS ILE LEU TYR ALA          
SEQRES  31 A  433  ARG ASP VAL ASP GLN ARG SER THR THR PHE GLU LYS SER          
SEQRES  32 A  433  LEU LEU MET GLY LYS GLU PHE GLN ARG ARG ALA LYS ALA          
SEQRES  33 A  433  MET MET LEU ARG ALA ALA VAL LEU ARG ASN GLN ILE HIS          
SEQRES  34 A  433  VAL LYS SER PRO                                              
SEQRES   1 Q  112  MET ASP GLY GLU GLU LYS THR TYR GLY GLY CYS GLU GLY          
SEQRES   2 Q  112  PRO ASP ALA MET TYR VAL LYS LEU ILE SER SER ASP GLY          
SEQRES   3 Q  112  HIS GLU PHE ILE VAL LYS ARG GLU HIS ALA LEU THR SER          
SEQRES   4 Q  112  GLY THR ILE LYS ALA MET LEU SER GLY PRO GLY GLN PHE          
SEQRES   5 Q  112  ALA GLU ASN GLU THR ASN GLU VAL ASN PHE ARG GLU ILE          
SEQRES   6 Q  112  PRO SER HIS VAL LEU SER LYS VAL CYS MET TYR PHE THR          
SEQRES   7 Q  112  TYR LYS VAL ARG TYR THR ASN SER SER THR GLU ILE PRO          
SEQRES   8 Q  112  GLU PHE PRO ILE ALA PRO GLU ILE ALA LEU GLU LEU LEU          
SEQRES   9 Q  112  MET ALA ALA ASN PHE LEU ASP CYS                              
SEQRES   1 O  654  MET SER LEU LYS PRO ARG VAL VAL ASP PHE ASP GLU THR          
SEQRES   2 O  654  TRP ASN LYS LEU LEU THR THR ILE LYS ALA VAL VAL MET          
SEQRES   3 O  654  LEU GLU TYR VAL GLU ARG ALA THR TRP ASN ASP ARG PHE          
SEQRES   4 O  654  SER ASP ILE TYR ALA LEU CYS VAL ALA TYR PRO GLU PRO          
SEQRES   5 O  654  LEU GLY GLU ARG LEU TYR THR GLU THR LYS ILE PHE LEU          
SEQRES   6 O  654  GLU ASN HIS VAL ARG HIS LEU HIS LYS ARG VAL LEU GLU          
SEQRES   7 O  654  SER GLU GLU GLN VAL LEU VAL MET TYR HIS ARG TYR TRP          
SEQRES   8 O  654  GLU GLU TYR SER LYS GLY ALA ASP TYR MET ASP CYS LEU          
SEQRES   9 O  654  TYR ARG TYR LEU ASN THR GLN PHE ILE LYS LYS ASN LYS          
SEQRES  10 O  654  LEU THR GLU ALA ASP LEU GLN TYR GLY TYR GLY GLY VAL          
SEQRES  11 O  654  ASP MET ASN GLU PRO LEU MET GLU ILE GLY GLU LEU ALA          
SEQRES  12 O  654  LEU ASP MET TRP ARG LYS LEU MET VAL GLU PRO LEU GLN          
SEQRES  13 O  654  ALA ILE LEU ILE ARG MET LEU LEU ARG GLU ILE LYS ASN          
SEQRES  14 O  654  ASP ARG GLY GLY GLU ASP PRO ASN GLN LYS VAL ILE HIS          
SEQRES  15 O  654  GLY VAL ILE ASN SER PHE VAL HIS VAL GLU GLN TYR LYS          
SEQRES  16 O  654  LYS LYS PHE PRO LEU LYS PHE TYR GLN GLU ILE PHE GLU          
SEQRES  17 O  654  SER PRO PHE LEU THR GLU THR GLY GLU TYR TYR LYS GLN          
SEQRES  18 O  654  GLU ALA SER ASN LEU LEU GLN GLU SER ASN CYS SER GLN          
SEQRES  19 O  654  TYR MET GLU LYS VAL LEU GLY ARG LEU LYS ASP GLU GLU          
SEQRES  20 O  654  ILE ARG CYS ARG LYS TYR LEU HIS PRO SER SER TYR THR          
SEQRES  21 O  654  LYS VAL ILE HIS GLU CYS GLN GLN ARG MET VAL ALA ASP          
SEQRES  22 O  654  HIS LEU GLN PHE LEU HIS ALA GLU CYS HIS ASN ILE ILE          
SEQRES  23 O  654  ARG GLN GLU LYS LYS ASN ASP MET ALA ASN MET TYR VAL          
SEQRES  24 O  654  LEU LEU ARG ALA VAL SER THR GLY LEU PRO HIS MET ILE          
SEQRES  25 O  654  GLN GLU LEU GLN ASN HIS ILE HIS ASP GLU GLY LEU ARG          
SEQRES  26 O  654  ALA THR SER ASN LEU THR GLN GLU ASN MET PRO THR LEU          
SEQRES  27 O  654  PHE VAL GLU SER VAL LEU GLU VAL HIS GLY LYS PHE VAL          
SEQRES  28 O  654  GLN LEU ILE ASN THR VAL LEU ASN GLY ASP GLN HIS PHE          
SEQRES  29 O  654  MET SER ALA LEU ASP LYS ALA LEU THR SER VAL VAL ASN          
SEQRES  30 O  654  TYR ARG GLU PRO LYS SER VAL CYS LYS ALA PRO GLU LEU          
SEQRES  31 O  654  LEU ALA LYS TYR CYS ASP ASN LEU LEU LYS LYS SER ALA          
SEQRES  32 O  654  LYS GLY MET THR GLU ASN GLU VAL GLU ASP ARG LEU THR          
SEQRES  33 O  654  SER PHE ILE THR VAL PHE LYS TYR ILE ASP ASP LYS ASP          
SEQRES  34 O  654  VAL PHE GLN LYS PHE TYR ALA ARG MET LEU ALA LYS ARG          
SEQRES  35 O  654  LEU ILE HIS GLY LEU SER MET SER MET ASP SER GLU GLU          
SEQRES  36 O  654  ALA MET ILE ASN LYS LEU LYS GLN ALA CYS GLY TYR GLU          
SEQRES  37 O  654  PHE THR SER LYS LEU HIS ARG MET TYR THR ASP MET SER          
SEQRES  38 O  654  VAL SER ALA ASP LEU ASN ASN LYS PHE ASN ASN PHE ILE          
SEQRES  39 O  654  LYS ASN GLN ASP THR VAL ILE ASP LEU GLY ILE SER PHE          
SEQRES  40 O  654  GLN ILE TYR VAL LEU GLN ALA GLY ALA TRP PRO LEU THR          
SEQRES  41 O  654  GLN ALA PRO SER SER THR PHE ALA ILE PRO GLN GLU LEU          
SEQRES  42 O  654  GLU LYS SER VAL GLN MET PHE GLU LEU PHE TYR SER GLN          
SEQRES  43 O  654  HIS PHE SER GLY ARG LYS LEU THR TRP LEU HIS TYR LEU          
SEQRES  44 O  654  CYS THR GLY GLU VAL LYS MET ASN TYR LEU GLY LYS PRO          
SEQRES  45 O  654  TYR VAL ALA MET VAL THR THR TYR GLN MET ALA VAL LEU          
SEQRES  46 O  654  LEU ALA PHE ASN ASN SER GLU THR VAL SER TYR LYS GLU          
SEQRES  47 O  654  LEU GLN ASP SER THR GLN MET ASN GLU LYS GLU LEU THR          
SEQRES  48 O  654  LYS THR ILE LYS SER LEU LEU ASP VAL LYS MET ILE ASN          
SEQRES  49 O  654  HIS ASP SER GLU LYS GLU ASP ILE ASP ALA GLU SER SER          
SEQRES  50 O  654  PHE SER LEU ASN MET ASN PHE SER SER LYS ARG THR LYS          
SEQRES  51 O  654  PHE LYS ILE THR                                              
SEQRES   1 R   90  LYS LYS ARG PHE GLU VAL LYS LYS TRP ASN ALA VAL ALA          
SEQRES   2 R   90  LEU TRP ALA TRP ASP ILE VAL VAL ASP ASN CYS ALA ILE          
SEQRES   3 R   90  CYS ARG ASN HIS ILE MET ASP LEU CYS ILE GLU CYS GLN          
SEQRES   4 R   90  ALA ASN GLN ALA SER ALA THR SER GLU GLU CYS THR VAL          
SEQRES   5 R   90  ALA TRP GLY VAL CYS ASN HIS ALA PHE HIS PHE HIS CYS          
SEQRES   6 R   90  ILE SER ARG TRP LEU LYS THR ARG GLN VAL CYS PRO LEU          
SEQRES   7 R   90  ASP ASN ARG GLU TRP GLU PHE GLN LYS TYR GLY HIS              
SEQRES   1 B  414  VAL ASP LEU GLU ASN GLN TYR TYR ASN SER LYS ALA LEU          
SEQRES   2 B  414  LYS GLU ASP ASP PRO LYS ALA ALA LEU SER SER PHE GLN          
SEQRES   3 B  414  LYS VAL LEU GLU LEU GLU GLY GLU LYS GLY GLU TRP GLY          
SEQRES   4 B  414  PHE LYS ALA LEU LYS GLN MET ILE LYS ILE ASN PHE LYS          
SEQRES   5 B  414  LEU THR ASN PHE PRO GLU MET MET ASN ARG TYR LYS GLN          
SEQRES   6 B  414  LEU LEU THR TYR ILE ARG SER ALA VAL THR ARG ASN TYR          
SEQRES   7 B  414  SER GLU LYS SER ILE ASN SER ILE LEU ASP TYR ILE SER          
SEQRES   8 B  414  THR SER LYS GLN MET ASP LEU LEU GLN GLU PHE TYR GLU          
SEQRES   9 B  414  THR THR LEU GLU ALA LEU LYS ASP ALA LYS ASN ASP ARG          
SEQRES  10 B  414  LEU TRP PHE LYS THR ASN THR LYS LEU GLY LYS LEU TYR          
SEQRES  11 B  414  LEU GLU ARG GLU GLU TYR GLY LYS LEU GLN LYS ILE LEU          
SEQRES  12 B  414  ARG GLN LEU HIS GLN SER CYS GLN THR ASP ASP GLY GLU          
SEQRES  13 B  414  ASP ASP LEU LYS LYS GLY THR GLN LEU LEU GLU ILE TYR          
SEQRES  14 B  414  ALA LEU GLU ILE GLN MET TYR THR ALA GLN LYS ASN ASN          
SEQRES  15 B  414  LYS LYS LEU LYS ALA LEU TYR GLU GLN SER LEU HIS ILE          
SEQRES  16 B  414  LYS SER ALA ILE PRO HIS PRO LEU ILE MET GLY VAL ILE          
SEQRES  17 B  414  ARG GLU CYS GLY GLY LYS MET HIS LEU ARG GLU GLY GLU          
SEQRES  18 B  414  PHE GLU LYS ALA HIS THR ASP PHE PHE GLU ALA PHE LYS          
SEQRES  19 B  414  ASN TYR ASP GLU SER GLY SER PRO ARG ARG THR THR CYS          
SEQRES  20 B  414  LEU LYS TYR LEU VAL LEU ALA ASN MET LEU MET LYS SER          
SEQRES  21 B  414  GLY ILE ASN PRO PHE ASP SER GLN GLU ALA LYS PRO TYR          
SEQRES  22 B  414  LYS ASN ASP PRO GLU ILE LEU ALA MET THR ASN LEU VAL          
SEQRES  23 B  414  SER ALA TYR GLN ASN ASN ASP ILE THR GLU PHE GLU LYS          
SEQRES  24 B  414  ILE LEU LYS THR ASN HIS SER ASN ILE MET ASP ASP PRO          
SEQRES  25 B  414  PHE ILE ARG GLU HIS ILE GLU GLU LEU LEU ARG ASN ILE          
SEQRES  26 B  414  ARG THR GLN VAL LEU ILE LYS LEU ILE LYS PRO TYR THR          
SEQRES  27 B  414  ARG ILE HIS ILE PRO PHE ILE SER LYS GLU LEU ASN ILE          
SEQRES  28 B  414  ASP VAL ALA ASP VAL GLU SER LEU LEU VAL GLN CYS ILE          
SEQRES  29 B  414  LEU ASP ASN THR ILE HIS GLY ARG ILE ASP GLN VAL ASN          
SEQRES  30 B  414  GLN LEU LEU GLU LEU ASP HIS GLN LYS ARG GLY GLY ALA          
SEQRES  31 B  414  ARG TYR THR ALA LEU ASP LYS TRP THR ASN GLN LEU ASN          
SEQRES  32 B  414  SER LEU ASN GLN ALA VAL VAL SER LYS LEU 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  311  SER ILE ASP GLU ILE TYR LYS TYR ASP LYS LYS GLN GLN          
SEQRES   2 E  311  GLN GLU ILE LEU ALA ALA LYS PRO TRP THR LYS ASP HIS          
SEQRES   3 E  311  HIS TYR PHE LYS TYR CYS LYS ILE SER ALA LEU ALA LEU          
SEQRES   4 E  311  LEU LYS MET VAL MET HIS ALA ARG SER GLY GLY ASN LEU          
SEQRES   5 E  311  GLU VAL MET GLY LEU MET LEU GLY LYS VAL ASP GLY GLU          
SEQRES   6 E  311  THR MET ILE ILE MET ASP SER PHE ALA LEU PRO VAL GLU          
SEQRES   7 E  311  GLY THR GLU THR ARG VAL ASN ALA GLN ALA ALA ALA TYR          
SEQRES   8 E  311  GLU TYR MET ALA ALA TYR ILE GLU ASN ALA LYS GLN VAL          
SEQRES   9 E  311  GLY ARG LEU GLU ASN ALA ILE GLY TRP TYR HIS SER HIS          
SEQRES  10 E  311  PRO GLY TYR GLY CYS TRP LEU SER GLY ILE ASP VAL SER          
SEQRES  11 E  311  THR GLN MET LEU ASN GLN GLN PHE GLN GLU PRO PHE VAL          
SEQRES  12 E  311  ALA VAL VAL ILE ASP PRO THR ARG THR ILE SER ALA GLY          
SEQRES  13 E  311  LYS VAL ASN LEU GLY ALA PHE ARG THR TYR PRO LYS GLY          
SEQRES  14 E  311  TYR LYS PRO PRO ASP GLU GLY PRO SER GLU TYR GLN THR          
SEQRES  15 E  311  ILE PRO LEU ASN LYS ILE GLU ASP PHE GLY VAL HIS CYS          
SEQRES  16 E  311  LYS GLN TYR TYR ALA LEU GLU VAL SER TYR PHE LYS SER          
SEQRES  17 E  311  SER LEU ASP ARG LYS LEU LEU GLU LEU LEU TRP ASN LYS          
SEQRES  18 E  311  TYR TRP VAL ASN THR LEU SER SER SER SER LEU LEU THR          
SEQRES  19 E  311  ASN ALA ASP TYR THR THR GLY GLN VAL PHE ASP LEU SER          
SEQRES  20 E  311  GLU LYS LEU GLU GLN SER GLU ALA GLN LEU GLY ARG GLY          
SEQRES  21 E  311  SER PHE MET LEU GLY LEU GLU THR HIS ASP ARG LYS SER          
SEQRES  22 E  311  GLU ASP LYS LEU ALA LYS ALA THR ARG ASP SER CYS LYS          
SEQRES  23 E  311  THR THR ILE GLU ALA ILE HIS GLY LEU MET SER GLN VAL          
SEQRES  24 E  311  ILE LYS ASP LYS LEU PHE ASN GLN ILE ASN ILE SER              
SEQRES   1 F  288  SER VAL MET ALA CYS GLY VAL THR GLY SER VAL SER VAL          
SEQRES   2 F  288  ALA LEU HIS PRO LEU VAL ILE LEU ASN ILE SER ASP HIS          
SEQRES   3 F  288  TRP ILE ARG MET ARG SER GLN GLU GLY ARG PRO VAL GLN          
SEQRES   4 F  288  VAL ILE GLY ALA LEU ILE GLY LYS GLN GLU GLY ARG ASN          
SEQRES   5 F  288  ILE GLU VAL MET ASN SER PHE GLU LEU LEU SER HIS THR          
SEQRES   6 F  288  VAL GLU GLU LYS ILE ILE ILE ASP LYS GLU TYR TYR TYR          
SEQRES   7 F  288  THR LYS GLU GLU GLN PHE LYS GLN VAL PHE LYS GLU LEU          
SEQRES   8 F  288  GLU PHE LEU GLY TRP TYR THR THR GLY GLY PRO PRO ASP          
SEQRES   9 F  288  PRO SER ASP ILE HIS VAL HIS LYS GLN VAL CYS GLU ILE          
SEQRES  10 F  288  ILE GLU SER PRO LEU PHE LEU LYS LEU ASN PRO MET THR          
SEQRES  11 F  288  LYS HIS THR ASP LEU PRO VAL SER VAL PHE GLU SER VAL          
SEQRES  12 F  288  ILE ASP ILE ILE ASN GLY GLU ALA THR MET LEU PHE ALA          
SEQRES  13 F  288  GLU LEU THR TYR THR LEU ALA THR GLU GLU ALA GLU ARG          
SEQRES  14 F  288  ILE GLY VAL ASP HIS VAL ALA ARG MET THR ALA THR GLY          
SEQRES  15 F  288  SER GLY GLU ASN SER THR VAL ALA GLU HIS LEU ILE ALA          
SEQRES  16 F  288  GLN HIS SER ALA ILE LYS MET LEU HIS SER ARG VAL LYS          
SEQRES  17 F  288  LEU ILE LEU GLU TYR VAL LYS ALA SER GLU ALA GLY GLU          
SEQRES  18 F  288  VAL PRO PHE ASN HIS GLU ILE LEU ARG GLU ALA TYR ALA          
SEQRES  19 F  288  LEU CYS HIS CYS LEU PRO VAL LEU SER THR ASP LYS PHE          
SEQRES  20 F  288  LYS THR ASP PHE TYR ASP GLN CYS ASN ASP VAL GLY LEU          
SEQRES  21 F  288  MET ALA TYR LEU GLY THR ILE THR LYS THR CYS ASN THR          
SEQRES  22 F  288  MET ASN GLN PHE VAL ASN LYS PHE ASN VAL LEU TYR ASP          
SEQRES  23 F  288  ARG GLN                                                      
SEQRES   1 G  208  SER SER ASN LEU LEU GLU GLN PHE ILE LEU LEU ALA LYS          
SEQRES   2 G  208  GLY THR SER GLY SER ALA LEU THR ALA LEU ILE SER GLN          
SEQRES   3 G  208  VAL LEU GLU ALA PRO GLY VAL TYR VAL PHE GLY GLU LEU          
SEQRES   4 G  208  LEU GLU LEU ALA ASN VAL GLN GLU LEU ALA GLU GLY ALA          
SEQRES   5 G  208  ASN ALA ALA TYR LEU GLN LEU LEU ASN LEU PHE ALA TYR          
SEQRES   6 G  208  GLY THR TYR PRO ASP TYR ILE ALA ASN LYS GLU SER LEU          
SEQRES   7 G  208  PRO GLU LEU SER THR ALA GLN GLN ASN LYS LEU LYS HIS          
SEQRES   8 G  208  LEU THR ILE VAL SER LEU ALA SER ARG MET LYS CYS ILE          
SEQRES   9 G  208  PRO TYR SER VAL LEU LEU LYS ASP LEU GLU MET ARG ASN          
SEQRES  10 G  208  LEU ARG GLU LEU GLU ASP LEU ILE ILE GLU ALA VAL TYR          
SEQRES  11 G  208  THR ASP ILE ILE GLN GLY LYS LEU ASP GLN ARG ASN GLN          
SEQRES  12 G  208  LEU LEU GLU VAL ASP PHE CYS ILE GLY ARG ASP ILE ARG          
SEQRES  13 G  208  LYS LYS ASP ILE ASN ASN ILE VAL LYS THR LEU HIS GLU          
SEQRES  14 G  208  TRP CYS ASP GLY CYS GLU ALA VAL LEU LEU GLY ILE GLU          
SEQRES  15 G  208  GLN GLN VAL LEU ARG ALA ASN GLN TYR LYS GLU ASN HIS          
SEQRES  16 G  208  ASN ARG THR GLN GLN GLN VAL GLU ALA GLU VAL THR ASN          
SEQRES   1 H  199  PHE SER PHE LYS LYS LEU LEU ASP GLN CYS GLU ASN GLN          
SEQRES   2 H  199  GLU LEU GLU ALA PRO GLY GLY ILE ALA THR PRO PRO VAL          
SEQRES   3 H  199  TYR GLY GLN LEU LEU ALA LEU TYR LEU LEU HIS ASN ASP          
SEQRES   4 H  199  MET ASN ASN ALA ARG TYR LEU TRP LYS ARG ILE PRO PRO          
SEQRES   5 H  199  ALA ILE LYS SER ALA ASN SER GLU LEU GLY GLY ILE TRP          
SEQRES   6 H  199  SER VAL GLY GLN ARG ILE TRP GLN ARG ASP PHE PRO GLY          
SEQRES   7 H  199  ILE TYR THR THR ILE ASN ALA HIS GLN TRP SER GLU THR          
SEQRES   8 H  199  VAL GLN PRO ILE MET GLU ALA LEU ARG ASP ALA THR ARG          
SEQRES   9 H  199  ARG ARG ALA PHE ALA LEU VAL SER GLN ALA TYR THR SER          
SEQRES  10 H  199  ILE ILE ALA ASP ASP PHE ALA ALA PHE VAL GLY LEU PRO          
SEQRES  11 H  199  VAL GLU GLU ALA VAL LYS GLY ILE LEU GLU GLN GLY TRP          
SEQRES  12 H  199  GLN ALA ASP SER THR THR ARG MET VAL LEU PRO ARG LYS          
SEQRES  13 H  199  PRO VAL ALA GLY ALA LEU ASP VAL SER PHE ASN LYS PHE          
SEQRES  14 H  199  ILE PRO LEU SER GLU PRO ALA PRO VAL PRO PRO ILE PRO          
SEQRES  15 H  199  ASN GLU GLN GLN LEU ALA ARG LEU THR ASP TYR VAL ALA          
SEQRES  16 H  199  PHE LEU GLU ASN                                              
SEQRES   1 P  104  MET ASP VAL PHE LEU MET ILE ARG ARG HIS LYS THR THR          
SEQRES   2 P  104  ILE PHE THR ASP ALA LYS GLU SER SER THR VAL PHE GLU          
SEQRES   3 P  104  LEU LYS ARG ILE VAL GLU GLY ILE LEU LYS ARG PRO PRO          
SEQRES   4 P  104  ASP GLU GLN ARG LEU TYR LYS ASP ASP GLN LEU LEU ASP          
SEQRES   5 P  104  ASP GLY LYS THR LEU GLY GLU CYS GLY PHE THR SER GLN          
SEQRES   6 P  104  THR ALA ARG PRO GLN ALA PRO ALA THR VAL GLY LEU ALA          
SEQRES   7 P  104  PHE ARG ALA ASP ASP THR PHE GLU ALA LEU CYS ILE GLU          
SEQRES   8 P  104  PRO PHE SER SER PRO PRO GLU LEU PRO ASP VAL MET LYS          
HELIX    1 AA1 ASP A   43  ALA A   49  1                                   7    
HELIX    2 AA2 GLY A   53  CYS A   67  1                                  15    
HELIX    3 AA3 ARG A   71  VAL A   82  1                                  12    
HELIX    4 AA4 GLU A   93  ARG A  103  1                                  11    
HELIX    5 AA5 ASP A  127  GLU A  132  1                                   6    
HELIX    6 AA6 GLU A  132  ASN A  155  1                                  24    
HELIX    7 AA7 ILE A  157  GLY A  176  1                                  20    
HELIX    8 AA8 SER A  179  ARG A  187  1                                   9    
HELIX    9 AA9 ALA A  188  CYS A  192  5                                   5    
HELIX   10 AB1 SER A  194  LEU A  212  1                                  19    
HELIX   11 AB2 ASN A  214  SER A  223  1                                  10    
HELIX   12 AB3 SER A  223  THR A  228  1                                   6    
HELIX   13 AB4 ALA A  244  ALA A  260  1                                  17    
HELIX   14 AB5 LYS A  262  ALA A  267  1                                   6    
HELIX   15 AB6 ASN A  288  PHE A  301  1                                  14    
HELIX   16 AB7 ASP A  302  VAL A  310  1                                   9    
HELIX   17 AB8 PHE A  316  GLU A  323  1                                   8    
HELIX   18 AB9 GLU A  323  GLU A  335  1                                  13    
HELIX   19 AC1 LYS A  337  MET A  348  1                                  12    
HELIX   20 AC2 MET A  348  LEU A  353  1                                   6    
HELIX   21 AC3 LEU A  365  SER A  379  1                                  15    
HELIX   22 AC4 ASP A  385  PHE A  393  1                                   9    
HELIX   23 AC5 THR A  396  LEU A  409  1                                  14    
HELIX   24 AC6 ARG A  432  LEU A  460  1                                  29    
HELIX   25 AC7 GLY Q   40  GLY Q   48  1                                   9    
HELIX   26 AC8 SER Q   67  TYR Q   83  1                                  17    
HELIX   27 AC9 ALA Q   96  ASP Q  111  1                                  16    
HELIX   28 AD1 PHE O   10  ALA O   23  1                                  14    
HELIX   29 AD2 GLU O   31  VAL O   47  1                                  17    
HELIX   30 AD3 LEU O   53  SER O   79  1                                  27    
HELIX   31 AD4 GLN O   82  TYR O  105  1                                  24    
HELIX   32 AD5 TYR O  105  THR O  110  1                                   6    
HELIX   33 AD6 GLU O  138  MET O  146  1                                   9    
HELIX   34 AD7 TRP O  147  MET O  151  5                                   5    
HELIX   35 AD8 LEU O  155  ASN O  169  1                                  15    
HELIX   36 AD9 ASN O  177  VAL O  191  1                                  15    
HELIX   37 AE1 PHE O  202  PHE O  207  1                                   6    
HELIX   38 AE2 PHE O  207  SER O  230  1                                  24    
HELIX   39 AE3 ASN O  231  TYR O  253  1                                  23    
HELIX   40 AE4 HIS O  255  SER O  257  5                                   3    
HELIX   41 AE5 SER O  258  VAL O  271  1                                  14    
HELIX   42 AE6 HIS O  274  ILE O  286  1                                  13    
HELIX   43 AE7 LYS O  290  VAL O  304  1                                  15    
HELIX   44 AE8 GLY O  307  SER O  328  1                                  22    
HELIX   45 AE9 THR O  337  VAL O  357  1                                  21    
HELIX   46 AF1 ASP O  361  TYR O  378  1                                  18    
HELIX   47 AF2 CYS O  385  LEU O  399  1                                  15    
HELIX   48 AF3 ASN O  409  SER O  417  1                                   9    
HELIX   49 AF4 SER O  417  LYS O  423  1                                   7    
HELIX   50 AF5 ASP O  427  HIS O  445  1                                  19    
HELIX   51 AF6 MET O  451  CYS O  465  1                                  15    
HELIX   52 AF7 THR O  470  ASN O  492  1                                  23    
HELIX   53 AF8 PHE O  493  ASN O  496  5                                   4    
HELIX   54 AF9 SER O  536  PHE O  548  1                                  13    
HELIX   55 AG1 THR O  578  ALA O  587  1                                  10    
HELIX   56 AG2 PHE O  588  ASN O  590  5                                   3    
HELIX   57 AG3 TYR O  596  GLN O  604  1                                   9    
HELIX   58 AG4 ASN O  606  VAL O  620  1                                  15    
HELIX   59 AG5 HIS R   80  LEU R   88  1                                   9    
HELIX   60 AG6 LEU B   32  LEU B   42  1                                  11    
HELIX   61 AG7 LYS B   48  SER B   52  5                                   5    
HELIX   62 AG8 GLN B   55  GLU B   59  5                                   5    
HELIX   63 AG9 GLY B   65  PHE B   80  1                                  16    
HELIX   64 AH1 PHE B   85  LEU B   96  1                                  12    
HELIX   65 AH2 THR B  104  LEU B  116  1                                  13    
HELIX   66 AH3 TYR B  118  LYS B  123  1                                   6    
HELIX   67 AH4 GLN B  124  GLU B  137  1                                  14    
HELIX   68 AH5 ASP B  145  GLU B  163  1                                  19    
HELIX   69 AH6 TYR B  165  HIS B  176  1                                  12    
HELIX   70 AH7 GLN B  193  LYS B  209  1                                  17    
HELIX   71 AH8 ASN B  210  SER B  226  1                                  17    
HELIX   72 AH9 ILE B  233  GLY B  249  1                                  17    
HELIX   73 AI1 GLU B  250  GLY B  269  1                                  20    
HELIX   74 AI2 ARG B  273  MET B  285  1                                  13    
HELIX   75 AI3 LEU B  286  LYS B  288  5                                   3    
HELIX   76 AI4 ASP B  305  ASN B  320  1                                  16    
HELIX   77 AI5 ASP B  322  ASN B  333  1                                  12    
HELIX   78 AI6 ASP B  340  GLU B  345  1                                   6    
HELIX   79 AI7 HIS B  346  LYS B  364  1                                  19    
HELIX   80 AI8 HIS B  370  LEU B  378  1                                   9    
HELIX   81 AI9 ASP B  384  ASP B  395  1                                  12    
HELIX   82 AJ1 ARG B  420  VAL B  439  1                                  20    
HELIX   83 AJ2 MET C   21  SER C   31  1                                  11    
HELIX   84 AJ3 ASN C   38  ASP C   43  1                                   6    
HELIX   85 AJ4 HIS C   54  PHE C   63  1                                  10    
HELIX   86 AJ5 PHE C   74  SER C   79  1                                   6    
HELIX   87 AJ6 SER C   79  THR C   87  1                                   9    
HELIX   88 AJ7 ALA C   96  GLU C  113  1                                  18    
HELIX   89 AJ8 LEU C  118  GLN C  132  1                                  15    
HELIX   90 AJ9 THR C  139  ALA C  152  1                                  14    
HELIX   91 AK1 ASP C  177  LEU C  195  1                                  19    
HELIX   92 AK2 ASN C  197  THR C  211  1                                  15    
HELIX   93 AK3 SER C  217  LEU C  235  1                                  19    
HELIX   94 AK4 PHE C  252  SER C  257  1                                   6    
HELIX   95 AK5 SER C  257  ASN C  270  1                                  14    
HELIX   96 AK6 ASN C  271  HIS C  282  1                                  12    
HELIX   97 AK7 HIS C  282  ASP C  289  1                                   8    
HELIX   98 AK8 VAL C  295  THR C  313  1                                  19    
HELIX   99 AK9 ASP C  321  VAL C  326  1                                   6    
HELIX  100 AL1 PRO C  331  GLY C  345  1                                  15    
HELIX  101 AL2 ASN C  369  ASN C  400  1                                  32    
HELIX  102 AL3 ALA D    2  LEU D   12  1                                  11    
HELIX  103 AL4 SER D   18  LEU D   36  1                                  19    
HELIX  104 AL5 GLY D   38  VAL D   53  1                                  16    
HELIX  105 AL6 SER D   58  LEU D   73  1                                  16    
HELIX  106 AL7 PRO D   77  ILE D   92  1                                  16    
HELIX  107 AL8 PHE D   99  GLU D  117  1                                  19    
HELIX  108 AL9 ASP D  119  GLY D  129  1                                  11    
HELIX  109 AM1 ASN D  140  ASP D  158  1                                  19    
HELIX  110 AM2 ASP D  160  GLU D  165  1                                   6    
HELIX  111 AM3 TYR D  167  ASN D  176  1                                  10    
HELIX  112 AM4 ASN D  180  TYR D  197  1                                  18    
HELIX  113 AM5 LYS D  200  LEU D  211  1                                  12    
HELIX  114 AM6 SER D  212  LYS D  214  5                                   3    
HELIX  115 AM7 HIS D  218  ALA D  236  1                                  19    
HELIX  116 AM8 GLY D  239  ASP D  252  1                                  14    
HELIX  117 AM9 GLU D  253  GLN D  257  5                                   5    
HELIX  118 AN1 ALA D  260  LEU D  269  1                                  10    
HELIX  119 AN2 ASN D  276  MET D  284  1                                   9    
HELIX  120 AN3 MET D  286  LYS D  290  5                                   5    
HELIX  121 AN4 ILE D  299  TYR D  316  1                                  18    
HELIX  122 AN5 PHE D  321  LEU D  327  1                                   7    
HELIX  123 AN6 PRO D  331  GLU D  345  1                                  15    
HELIX  124 AN7 LEU D  367  ALA D  392  1                                  26    
HELIX  125 AN8 ALA D  392  GLN D  406  1                                  15    
HELIX  126 AN9 ASP E   32  GLU E   38  1                                   7    
HELIX  127 AO1 LYS E   43  LYS E   47  5                                   5    
HELIX  128 AO2 ALA E   59  GLY E   72  1                                  14    
HELIX  129 AO3 ASN E  108  ALA E  112  5                                   5    
HELIX  130 AO4 ALA E  113  GLN E  126  1                                  14    
HELIX  131 AO5 ILE E  150  GLN E  159  1                                  10    
HELIX  132 AO6 ASP E  213  CYS E  218  1                                   6    
HELIX  133 AO7 LEU E  233  LYS E  236  5                                   4    
HELIX  134 AO8 LEU E  237  LEU E  250  1                                  14    
HELIX  135 AO9 SER E  253  ASN E  258  1                                   6    
HELIX  136 AP1 ASN E  258  GLY E  283  1                                  26    
HELIX  137 AP2 ASP E  298  ILE E  323  1                                  26    
HELIX  138 AP3 LEU F   46  GLY F   63  1                                  18    
HELIX  139 AP4 ASP F  101  LYS F  108  1                                   8    
HELIX  140 AP5 PRO F  133  GLN F  141  1                                   9    
HELIX  141 AP6 GLU F  193  ARG F  205  1                                  13    
HELIX  142 AP7 SER F  215  ALA F  247  1                                  33    
HELIX  143 AP8 ASN F  253  TYR F  261  1                                   9    
HELIX  144 AP9 THR F  272  ASN F  310  1                                  39    
HELIX  145 AQ1 LEU G   11  ALA G   19  1                                   9    
HELIX  146 AQ2 GLY G   24  ALA G   37  1                                  14    
HELIX  147 AQ3 PHE G   43  GLU G   48  1                                   6    
HELIX  148 AQ4 ALA G   59  PHE G   70  1                                  12    
HELIX  149 AQ5 TYR G   75  ALA G   80  1                                   6    
HELIX  150 AQ6 ALA G   91  SER G  106  1                                  16    
HELIX  151 AQ7 TYR G  113  LEU G  120  1                                   8    
HELIX  152 AQ8 ASN G  124  GLU G  134  1                                  11    
HELIX  153 AQ9 ILE G  167  GLN G  208  1                                  42    
HELIX  154 AR1 PHE H   13  LEU H   25  1                                  13    
HELIX  155 AR2 THR H   33  HIS H   47  1                                  15    
HELIX  156 AR3 ASP H   49  ILE H   60  1                                  12    
HELIX  157 AR4 PRO H   61  SER H   66  1                                   6    
HELIX  158 AR5 SER H   69  ARG H   84  1                                  16    
HELIX  159 AR6 ILE H   89  ASN H   94  1                                   6    
HELIX  160 AR7 VAL H  102  SER H  122  1                                  21    
HELIX  161 AR8 ALA H  130  GLY H  138  1                                   9    
HELIX  162 AR9 PRO H  140  ILE H  148  1                                   9    
HELIX  163 AS1 LEU H  197  ASN H  209  1                                  13    
HELIX  164 AS2 THR P   23  LYS P   36  1                                  14    
HELIX  165 AS3 THR P   56  GLY P   61  1                                   6    
SHEET    1 AA1 3 ILE A 423  TYR A 425  0                                        
SHEET    2 AA1 3 ARG A 416  ASP A 418 -1  N  ARG A 416   O  TYR A 425           
SHEET    3 AA1 3 PHE C 314  THR C 316  1  O  LEU C 315   N  VAL A 417           
SHEET    1 AA2 7 VAL Q  60  ASN Q  61  0                                        
SHEET    2 AA2 7 TYR Q  18  ILE Q  22  1  N  ILE Q  22   O  VAL Q  60           
SHEET    3 AA2 7 GLU Q  28  LYS Q  32 -1  O  PHE Q  29   N  LEU Q  21           
SHEET    4 AA2 7 THR P  12  ALA P  18  1  O  PHE P  15   N  ILE Q  30           
SHEET    5 AA2 7 VAL P   3  ARG P   8 -1  N  ILE P   7   O  ILE P  14           
SHEET    6 AA2 7 ALA P  73  ALA P  78  1  O  VAL P  75   N  MET P   6           
SHEET    7 AA2 7 ARG P  43  TYR P  45 -1  N  TYR P  45   O  GLY P  76           
SHEET    1 AA3 2 TYR O 510  VAL O 511  0                                        
SHEET    2 AA3 2 VAL R  30  ALA R  31  1  O  ALA R  31   N  TYR O 510           
SHEET    1 AA4 2 VAL O 564  MET O 566  0                                        
SHEET    2 AA4 2 TYR O 573  ALA O 575 -1  O  TYR O 573   N  MET O 566           
SHEET    1 AA5 2 THR O 593  SER O 595  0                                        
SHEET    2 AA5 2 SER O 637  SER O 639 -1  O  PHE O 638   N  VAL O 594           
SHEET    1 AA6 2 ARG B 401  ASP B 403  0                                        
SHEET    2 AA6 2 LEU B 408  GLU B 410 -1  O  GLU B 410   N  ARG B 401           
SHEET    1 AA7 2 ALA C 349  ASN C 352  0                                        
SHEET    2 AA7 2 MET C 357  PHE C 360 -1  O  SER C 359   N  SER C 350           
SHEET    1 AA8 3 ASN D 318  THR D 320  0                                        
SHEET    2 AA8 3 ILE D 358  HIS D 360 -1  O  VAL D 359   N  ILE D 319           
SHEET    3 AA8 3 PHE D 351  ASP D 353 -1  N  PHE D 351   O  HIS D 360           
SHEET    1 AA9 8 THR E  89  ILE E  92  0                                        
SHEET    2 AA9 8 TYR E  54  SER E  58  1  N  LYS E  56   O  MET E  90           
SHEET    3 AA9 8 ALA E 223  PHE E 229  1  O  SER E 227   N  CYS E  55           
SHEET    4 AA9 8 LEU E 183  PHE E 186 -1  N  ALA E 185   O  LEU E 224           
SHEET    5 AA9 8 ALA E 167  ILE E 170 -1  N  ALA E 167   O  PHE E 186           
SHEET    6 AA9 8 ASN E 132  SER E 139  1  N  HIS E 138   O  VAL E 168           
SHEET    7 AA9 8 GLY E  79  GLY E  83 -1  N  MET E  81   O  GLY E 135           
SHEET    8 AA9 8 SER E  95  ALA E  97 -1  O  PHE E  96   N  LEU E  80           
SHEET    1 AB1 3 SER F  40  LEU F  43  0                                        
SHEET    2 AB1 3 ASN F  80  VAL F  83  1  O  ILE F  81   N  ALA F  42           
SHEET    3 AB1 3 LYS F  75  GLN F  76 -1  N  LYS F  75   O  GLU F  82           
SHEET    1 AB2 2 GLY F  70  LEU F  72  0                                        
SHEET    2 AB2 2 SER F  86  GLU F  88 -1  O  PHE F  87   N  ALA F  71           
SHEET    1 AB3 2 SER F  91  VAL F  94  0                                        
SHEET    2 AB3 2 LYS F  97  ILE F 100 -1  O  LYS F  97   N  VAL F  94           
SHEET    1 AB4 4 TRP F 124  THR F 127  0                                        
SHEET    2 AB4 4 LEU F 150  LEU F 154  1  O  LEU F 154   N  THR F 126           
SHEET    3 AB4 4 VAL F 165  ILE F 175 -1  O  PHE F 168   N  PHE F 151           
SHEET    4 AB4 4 GLU F 178  GLU F 185 -1  O  GLU F 178   N  ILE F 175           
SHEET    1 AB5 3 CYS G 110  PRO G 112  0                                        
SHEET    2 AB5 3 LEU G 151  PHE G 156 -1  O  LEU G 152   N  ILE G 111           
SHEET    3 AB5 3 GLN G 142  LEU G 145 -1  N  GLN G 142   O  PHE G 156           
SHEET    1 AB6 3 ILE H 128  ILE H 129  0                                        
SHEET    2 AB6 3 MET H 161  LEU H 163 -1  O  VAL H 162   N  ILE H 128           
SHEET    3 AB6 3 GLN H 154  ALA H 155 -1  N  GLN H 154   O  LEU H 163           
CISPEP   1 GLY Q   48    PRO Q   49          0        -3.15                     
CISPEP   2 PRO Q   49    GLY Q   50          0         0.02                     
CISPEP   3 GLU O  174    ASP O  175          0         0.03                     
CISPEP   4 LYS B   64    GLY B   65          0        -0.76                     
CISPEP   5 SER B  270    PRO B  271          0        -1.15                     
CISPEP   6 LYS B  288    SER B  289          0         0.60                     
CISPEP   7 GLU E  163    PRO E  164          0        -0.96                     
CISPEP   8 LEU F  267    PRO F  268          0        -0.68                     
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                                                                             
DBGET integrated database retrieval system