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Database: PDB
Entry: 6R7F
LinkDB: 6R7F
Original site: 6R7F 
HEADER    LIGASE                                  28-MAR-19   6R7F              
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: COP9 SIGNALOSOME COMPLEX SUBUNIT 7B;                       
COMPND  45 CHAIN: G;                                                            
COMPND  46 SYNONYM: SIGNALOSOME SUBUNIT 7B,JAB1-CONTAINING SIGNALOSOME SUBUNIT  
COMPND  47 7B;                                                                  
COMPND  48 ENGINEERED: YES;                                                     
COMPND  49 MOL_ID: 9;                                                           
COMPND  50 MOLECULE: VON HIPPEL-LINDAU DISEASE TUMOR SUPPRESSOR;                
COMPND  51 CHAIN: V;                                                            
COMPND  52 SYNONYM: PROTEIN G7,PVHL;                                            
COMPND  53 ENGINEERED: YES;                                                     
COMPND  54 MOL_ID: 10;                                                          
COMPND  55 MOLECULE: ELONGIN-B;                                                 
COMPND  56 CHAIN: P;                                                            
COMPND  57 SYNONYM: ELOB,ELONGIN 18 KDA SUBUNIT,RNA POLYMERASE II TRANSCRIPTION 
COMPND  58 FACTOR SIII SUBUNIT B,SIII P18,TRANSCRIPTION ELONGATION FACTOR B     
COMPND  59 POLYPEPTIDE 2;                                                       
COMPND  60 ENGINEERED: YES;                                                     
COMPND  61 MOL_ID: 11;                                                          
COMPND  62 MOLECULE: ELONGIN-C;                                                 
COMPND  63 CHAIN: Q;                                                            
COMPND  64 SYNONYM: ELOC,ELONGIN 15 KDA SUBUNIT,RNA POLYMERASE II TRANSCRIPTION 
COMPND  65 FACTOR SIII SUBUNIT C,SIII P15,TRANSCRIPTION ELONGATION FACTOR B     
COMPND  66 POLYPEPTIDE 1;                                                       
COMPND  67 ENGINEERED: YES;                                                     
COMPND  68 MOL_ID: 12;                                                          
COMPND  69 MOLECULE: CULLIN-2;                                                  
COMPND  70 CHAIN: O;                                                            
COMPND  71 SYNONYM: CUL-2;                                                      
COMPND  72 ENGINEERED: YES;                                                     
COMPND  73 MOL_ID: 13;                                                          
COMPND  74 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RBX1;                          
COMPND  75 CHAIN: R;                                                            
COMPND  76 ENGINEERED: YES;                                                     
COMPND  77 MOL_ID: 14;                                                          
COMPND  78 MOLECULE: NEDD8;                                                     
COMPND  79 CHAIN: N;                                                            
COMPND  80 SYNONYM: NEDDYLIN,NEURAL PRECURSOR CELL EXPRESSED DEVELOPMENTALLY    
COMPND  81 DOWN-REGULATED PROTEIN 8,NEDD-8,UBIQUITIN-LIKE PROTEIN NEDD8;        
COMPND  82 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GPS1, COPS1, CSN1;                                             
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: COPS2, CSN2, TRIP15;                                           
SOURCE  13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: COPS3, CSN3;                                                   
SOURCE  20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  24 ORGANISM_COMMON: HUMAN;                                              
SOURCE  25 ORGANISM_TAXID: 9606;                                                
SOURCE  26 GENE: COPS4, CSN4;                                                   
SOURCE  27 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  29 MOL_ID: 5;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  31 ORGANISM_COMMON: HUMAN;                                              
SOURCE  32 ORGANISM_TAXID: 9606;                                                
SOURCE  33 GENE: COPS5, CSN5, JAB1;                                             
SOURCE  34 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  35 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  36 MOL_ID: 6;                                                           
SOURCE  37 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  38 ORGANISM_COMMON: HUMAN;                                              
SOURCE  39 ORGANISM_TAXID: 9606;                                                
SOURCE  40 GENE: COPS6, CSN6, HVIP;                                             
SOURCE  41 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  42 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  43 MOL_ID: 7;                                                           
SOURCE  44 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  45 ORGANISM_COMMON: HUMAN;                                              
SOURCE  46 ORGANISM_TAXID: 9606;                                                
SOURCE  47 GENE: COPS8, CSN8;                                                   
SOURCE  48 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  49 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  50 MOL_ID: 8;                                                           
SOURCE  51 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  52 ORGANISM_COMMON: HUMAN;                                              
SOURCE  53 ORGANISM_TAXID: 9606;                                                
SOURCE  54 GENE: COPS7B, CSN7B;                                                 
SOURCE  55 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  56 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  57 MOL_ID: 9;                                                           
SOURCE  58 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  59 ORGANISM_COMMON: HUMAN;                                              
SOURCE  60 ORGANISM_TAXID: 9606;                                                
SOURCE  61 GENE: VHL;                                                           
SOURCE  62 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  63 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  64 MOL_ID: 10;                                                          
SOURCE  65 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  66 ORGANISM_COMMON: HUMAN;                                              
SOURCE  67 ORGANISM_TAXID: 9606;                                                
SOURCE  68 GENE: ELOB, TCEB2;                                                   
SOURCE  69 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  70 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  71 MOL_ID: 11;                                                          
SOURCE  72 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  73 ORGANISM_COMMON: HUMAN;                                              
SOURCE  74 ORGANISM_TAXID: 9606;                                                
SOURCE  75 GENE: ELOC, TCEB1;                                                   
SOURCE  76 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  77 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  78 MOL_ID: 12;                                                          
SOURCE  79 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  80 ORGANISM_COMMON: HUMAN;                                              
SOURCE  81 ORGANISM_TAXID: 9606;                                                
SOURCE  82 GENE: CUL2;                                                          
SOURCE  83 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  84 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  85 MOL_ID: 13;                                                          
SOURCE  86 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  87 ORGANISM_TAXID: 9606;                                                
SOURCE  88 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  89 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  90 MOL_ID: 14;                                                          
SOURCE  91 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  92 ORGANISM_COMMON: HUMAN;                                              
SOURCE  93 ORGANISM_TAXID: 9606;                                                
SOURCE  94 GENE: NEDD8;                                                         
SOURCE  95 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  96 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    CULLIN-RING E3 LIGASE COP9 SIGNALOSOME NEDDYLATION, LIGASE            
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    S.V.FAULL,A.M.C.LAU,C.MARTENS,Z.AHDASH,H.YEBENES,C.SCHMIDT,F.BEURON,  
AUTHOR   2 N.B.CRONIN,E.P.MORRIS,A.POLITIS                                      
REVDAT   3   09-OCT-19 6R7F    1       REMARK LINK                              
REVDAT   2   04-SEP-19 6R7F    1       JRNL                                     
REVDAT   1   28-AUG-19 6R7F    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.    8.20 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)  : 8.200                          
REMARK   3   NUMBER OF PARTICLES               : 20055                          
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 6R7F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292101543.                                   
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 (CSN) AND             
REMARK 245                                    NEDDYLATED CULLIN-RING E3         
REMARK 245                                    LIGASE CRL (CULLIN-2 WITH RBX1,   
REMARK 245                                    ELONGIN-B, ELONGIN-C AND VHL)     
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)  : 45.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRADECAMERIC                    
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, G, V, P,         
REMARK 350                    AND CHAINS: Q, O, R, N                            
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 B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     MET B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     ASP B     7                                                      
REMARK 465     PHE B     8                                                      
REMARK 465     MET B     9                                                      
REMARK 465     CYS B    10                                                      
REMARK 465     ASP B    11                                                      
REMARK 465     ASP B    12                                                      
REMARK 465     GLU B    13                                                      
REMARK 465     GLU B    14                                                      
REMARK 465     ASP B    15                                                      
REMARK 465     TYR B    16                                                      
REMARK 465     ASP B    17                                                      
REMARK 465     LEU B    18                                                      
REMARK 465     GLU B    19                                                      
REMARK 465     TYR B    20                                                      
REMARK 465     SER B    21                                                      
REMARK 465     GLU B    22                                                      
REMARK 465     ASP B    23                                                      
REMARK 465     SER B    24                                                      
REMARK 465     ASN B    25                                                      
REMARK 465     SER B    26                                                      
REMARK 465     GLU B    27                                                      
REMARK 465     PRO B    28                                                      
REMARK 465     ASN B    29                                                      
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     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 465     GLN H   196                                                      
REMARK 465     ARG O   691                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS N   4    CG   CD   CE   NZ                                   
REMARK 470     LYS N  60    CG   CD   CE   NZ                                   
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   CE   LYS O   393     CE   MET O   665              0.71            
REMARK 500   NH2  ARG V   177     CB   ASP P   101              0.81            
REMARK 500   CG2  ILE V   180     CB   LEU Q   101              0.83            
REMARK 500   CZ   ARG V   177     CB   ASP P   101              0.84            
REMARK 500   O    ASN V   174     CG1  VAL P   102              0.86            
REMARK 500   CE   LYS O   370     O    LYS N    33              0.88            
REMARK 500   CB   ARG V   177     CG2  VAL P   102              0.90            
REMARK 500   CB   VAL V   181     SD   MET Q   105              1.00            
REMARK 500   CE   LYS O   370     C    LYS N    33              1.10            
REMARK 500   NZ   LYS O   393     CE   MET O   665              1.14            
REMARK 500   CG2  ILE V   180     CG   LEU Q   101              1.15            
REMARK 500   CA   ARG V   177     CG2  VAL P   102              1.18            
REMARK 500   C    ASN V   174     CG1  VAL P   102              1.20            
REMARK 500   CD1  LEU V   184     CG   MET Q   105              1.26            
REMARK 500   NH2  ARG V   177     CG   ASP P   101              1.30            
REMARK 500   OH   TYR O   679     NH1  ARG R    46              1.41            
REMARK 500   CB   ARG V   182     CG   PRO O     5              1.54            
REMARK 500   CB   ILE V   180     CB   LEU Q   101              1.55            
REMARK 500   NE   ARG V   177     CB   ASP P   101              1.56            
REMARK 500   CD   ARG O   708     OE1  GLN N    40              1.59            
REMARK 500   N    VAL V   181     CE   MET Q   105              1.60            
REMARK 500   CD   LYS O   370     O    LYS N    33              1.61            
REMARK 500   NZ   LYS O   370     C    LYS N    33              1.61            
REMARK 500   CG   ARG V   182     CG   PRO O     5              1.66            
REMARK 500   NZ   LYS O   370     N    GLU N    34              1.67            
REMARK 500   NZ   LYS V   171     CB   GLN P   106              1.70            
REMARK 500   O    ASN V   174     CB   VAL P   102              1.75            
REMARK 500   CD2  LEU V   178     CG   MET P   103              1.75            
REMARK 500   OG1  THR O   654     N    THR O   655              1.77            
REMARK 500   N    ARG V   177     CG2  VAL P   102              1.79            
REMARK 500   NH2  ARG V   177     OD1  ASP P   101              1.81            
REMARK 500   CE   LYS O   393     SD   MET O   665              1.82            
REMARK 500   CD   LYS O   393     CE   MET O   665              1.82            
REMARK 500   NH2  ARG V   177     CA   ASP P   101              1.83            
REMARK 500   CG2  VAL V   181     CE   MET Q   105              1.85            
REMARK 500   CE   LYS O   370     N    GLU N    34              1.86            
REMARK 500   CB   ASN V   174     O    VAL P   102              1.87            
REMARK 500   CG1  ILE V   180     CD2  LEU Q   101              1.87            
REMARK 500   CG2  VAL V   181     SD   MET Q   105              1.89            
REMARK 500   CG   LYS O   370     O    GLU N    32              1.96            
REMARK 500   OE2  GLU O   389     CB   MET O   665              1.97            
REMARK 500   CD   GLN O   316     OE1  GLU N    32              2.00            
REMARK 500   CD   ARG V   182     CG   PRO O     5              2.00            
REMARK 500   CG2  ILE V   180     CD1  LEU Q   101              2.01            
REMARK 500   CB   VAL V   181     CE   MET Q   105              2.05            
REMARK 500   CA   ASN V   174     CG1  VAL P   102              2.05            
REMARK 500   CA   VAL V   181     SD   MET Q   105              2.07            
REMARK 500   CB   ARG V   177     CB   VAL P   102              2.07            
REMARK 500   C    ARG V   177     CG2  VAL P   102              2.07            
REMARK 500   CD1  LEU V   184     SD   MET Q   105              2.07            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      65 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    ARG A  56   CZ    ARG A  56   NH1     0.080                       
REMARK 500    ARG A  96   CD    ARG A  96   NE      0.131                       
REMARK 500    ARG A 103   CD    ARG A 103   NE      0.137                       
REMARK 500    SER A 119   CA    SER A 119   CB      0.103                       
REMARK 500    ARG A 135   CZ    ARG A 135   NH1     0.078                       
REMARK 500    SER A 156   CA    SER A 156   CB      0.109                       
REMARK 500    HIS A 165   CE1   HIS A 165   NE2    -0.079                       
REMARK 500    CYS A 269   CB    CYS A 269   SG      0.138                       
REMARK 500    PHE A 319   CG    PHE A 319   CD1     0.109                       
REMARK 500    PHE A 333   CG    PHE A 333   CD2     0.091                       
REMARK 500    ARG A 363   CD    ARG A 363   NE      0.107                       
REMARK 500    GLU A 410   CD    GLU A 410   OE2     0.074                       
REMARK 500    SER A 433   CA    SER A 433   CB      0.100                       
REMARK 500    ARG A 449   NE    ARG A 449   CZ      0.091                       
REMARK 500    ARG A 461   CZ    ARG A 461   NH1     0.092                       
REMARK 500    TYR B  37   CG    TYR B  37   CD1     0.104                       
REMARK 500    TYR B  92   CG    TYR B  92   CD2     0.092                       
REMARK 500    TYR B  92   CZ    TYR B  92   CE2     0.080                       
REMARK 500    SER B 114   CA    SER B 114   CB      0.106                       
REMARK 500    TYR B 159   CZ    TYR B 159   CE2     0.097                       
REMARK 500    GLU B 164   CG    GLU B 164   CD      0.111                       
REMARK 500    TYR B 218   CE1   TYR B 218   CZ      0.082                       
REMARK 500    GLU B 252   CB    GLU B 252   CG      0.130                       
REMARK 500    ARG B 273   NE    ARG B 273   CZ      0.091                       
REMARK 500    PHE B 294   CA    PHE B 294   CB      0.147                       
REMARK 500    PHE B 294   CA    PHE B 294   C       1.831                       
REMARK 500    TYR B 302   CG    TYR B 302   CD2     0.092                       
REMARK 500    TYR B 318   CG    TYR B 318   CD2     0.078                       
REMARK 500    ARG B 401   CZ    ARG B 401   NH2     0.101                       
REMARK 500    TYR C  95   CE1   TYR C  95   CZ      0.085                       
REMARK 500    ARG C 114   CZ    ARG C 114   NH2     0.080                       
REMARK 500    TYR C 187   CG    TYR C 187   CD1     0.079                       
REMARK 500    TYR C 205   CG    TYR C 205   CD1     0.085                       
REMARK 500    SER C 223   CA    SER C 223   CB      0.126                       
REMARK 500    SER C 231   CA    SER C 231   CB      0.092                       
REMARK 500    PRO C 331   CD    PRO C 331   N       0.091                       
REMARK 500    VAL C 338   CB    VAL C 338   CG1     0.148                       
REMARK 500    ARG D 121   NE    ARG D 121   CZ      0.095                       
REMARK 500    ARG D 170   NE    ARG D 170   CZ      0.088                       
REMARK 500    TYR D 187   CG    TYR D 187   CD2     0.078                       
REMARK 500    ARG D 222   CZ    ARG D 222   NH1     0.079                       
REMARK 500    ARG D 274   NE    ARG D 274   CZ      0.093                       
REMARK 500    ARG D 302   NE    ARG D 302   CZ      0.088                       
REMARK 500    ARG D 364   CD    ARG D 364   NE      0.113                       
REMARK 500    GLU E 115   CG    GLU E 115   CD      0.098                       
REMARK 500    HIS E 140   CG    HIS E 140   CD2     0.073                       
REMARK 500    ARG E 187   CD    ARG E 187   NE      0.116                       
REMARK 500    TYR E 203   CG    TYR E 203   CD2     0.345                       
REMARK 500    TYR E 203   CG    TYR E 203   CD1     0.300                       
REMARK 500    TYR E 203   CD1   TYR E 203   CE1     0.308                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     104 BOND DEVIATIONS.                              
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    VAL A  37   CG1 -  CB  -  CG2 ANGL. DEV. =   9.6 DEGREES          
REMARK 500    ARG A  59   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A  59   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    PHE A  62   CB  -  CG  -  CD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG A  71   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    PHE A  81   CB  -  CG  -  CD2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    PHE A  81   CB  -  CG  -  CD1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    MET A  90   CG  -  SD  -  CE  ANGL. DEV. =  11.6 DEGREES          
REMARK 500    ARG A  96   NE  -  CZ  -  NH1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG A  96   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ALA A 115   N   -  CA  -  CB  ANGL. DEV. =  13.3 DEGREES          
REMARK 500    ARG A 162   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    ARG A 162   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ASP A 170   CB  -  CG  -  OD1 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    TYR A 172   CB  -  CG  -  CD1 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    CYS A 175   CA  -  CB  -  SG  ANGL. DEV. =   7.8 DEGREES          
REMARK 500    ASP A 177   CB  -  CG  -  OD1 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    TYR A 221   CB  -  CG  -  CD1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 261   NE  -  CZ  -  NH2 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ASP A 276   CB  -  CG  -  OD1 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    TYR A 292   CG  -  CD2 -  CE2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    TYR A 292   CD1 -  CE1 -  CZ  ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    PHE A 301   CB  -  CG  -  CD2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    PHE A 301   CB  -  CG  -  CD1 ANGL. DEV. =   7.7 DEGREES          
REMARK 500    PHE A 319   CB  -  CG  -  CD2 ANGL. DEV. =   5.3 DEGREES          
REMARK 500    PHE A 319   CB  -  CG  -  CD1 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A 327   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    PHE A 333   CB  -  CG  -  CD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    PHE A 333   CB  -  CG  -  CD1 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    TYR A 338   CB  -  CG  -  CD1 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A 363   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A 388   NE  -  CZ  -  NH2 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ALA A 426   N   -  CA  -  CB  ANGL. DEV. =   8.6 DEGREES          
REMARK 500    MET A 453   CG  -  SD  -  CE  ANGL. DEV. = -10.0 DEGREES          
REMARK 500    TYR B  36   CB  -  CG  -  CD1 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    SER B  53   N   -  CA  -  CB  ANGL. DEV. =  10.6 DEGREES          
REMARK 500    PHE B  54   CB  -  CG  -  CD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    GLY B  62   N   -  CA  -  C   ANGL. DEV. = -16.2 DEGREES          
REMARK 500    PHE B  85   CB  -  CG  -  CD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    PHE B  85   CB  -  CG  -  CD1 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500    ASN B  90   N   -  CA  -  CB  ANGL. DEV. =  12.2 DEGREES          
REMARK 500    TYR B  92   CB  -  CG  -  CD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    TYR B  92   CB  -  CG  -  CD1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    TYR B  98   CB  -  CG  -  CD2 ANGL. DEV. = -11.3 DEGREES          
REMARK 500    TYR B  98   CB  -  CG  -  CD1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG B 105   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG B 105   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ASP B 126   CB  -  CG  -  OD1 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500    PHE B 131   CG  -  CD1 -  CE1 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG B 146   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     352 ANGLE DEVIATIONS.                             
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    ASN A  39      109.25   -178.78                                   
REMARK 500    SER A  41       47.41   -101.98                                   
REMARK 500    THR A  85      -36.04     71.30                                   
REMARK 500    PHE A  86       74.11     80.85                                   
REMARK 500    ALA A 115      145.17    137.22                                   
REMARK 500    SER A 119      -84.29   -156.96                                   
REMARK 500    TYR A 191        8.28   -158.94                                   
REMARK 500    THR A 193       20.84   -151.62                                   
REMARK 500    GLN A 213       38.95     74.53                                   
REMARK 500    GLU A 230       37.63     75.30                                   
REMARK 500    GLU A 233     -176.07     61.41                                   
REMARK 500    GLN A 234        7.30   -152.25                                   
REMARK 500    ARG A 235       -0.06   -150.28                                   
REMARK 500    ARG A 238     -129.67     76.12                                   
REMARK 500    LYS A 262       35.89    -88.82                                   
REMARK 500    CYS A 278      -51.28     97.40                                   
REMARK 500    LEU A 283      -56.77   -149.08                                   
REMARK 500    SER A 336       24.95     85.89                                   
REMARK 500    LYS A 337       30.58    -83.30                                   
REMARK 500    ALA A 426       30.76    169.98                                   
REMARK 500    LYS B  43     -155.90    -80.27                                   
REMARK 500    GLU B  44      -51.11     84.95                                   
REMARK 500    ALA B  49      -21.60     82.75                                   
REMARK 500    GLU B  61      148.81    131.56                                   
REMARK 500    LEU B  82     -145.78   -107.36                                   
REMARK 500    THR B  83     -114.82     57.10                                   
REMARK 500    ASN B  84      141.17    174.74                                   
REMARK 500    SER B 101     -155.60    -87.20                                   
REMARK 500    ASP B 141      142.06    139.95                                   
REMARK 500    ASN B 144       59.28   -141.02                                   
REMARK 500    ASP B 145      -73.41    -63.68                                   
REMARK 500    GLU B 163       29.79     87.35                                   
REMARK 500    ASP B 182       -6.84   -170.28                                   
REMARK 500    GLU B 185       -6.12   -164.52                                   
REMARK 500    ASP B 186      177.50    -46.89                                   
REMARK 500    ASP B 187      -83.68    -79.09                                   
REMARK 500    LYS B 189       56.98   -157.54                                   
REMARK 500    LYS B 209       52.55     74.39                                   
REMARK 500    PRO B 229     -126.73    -89.03                                   
REMARK 500    GLU B 250       62.31   -106.68                                   
REMARK 500    SER B 270      166.22    -36.41                                   
REMARK 500    ASN B 292       55.28   -159.21                                   
REMARK 500    SER B 296     -147.37   -110.21                                   
REMARK 500    GLU B 298      107.75   -174.04                                   
REMARK 500    ALA B 299      123.44     60.62                                   
REMARK 500    ASN B 333       52.07   -115.64                                   
REMARK 500    ASN B 379       50.55     90.70                                   
REMARK 500    ASN B 406       -6.68   -160.64                                   
REMARK 500    LEU B 411      151.34    -31.45                                   
REMARK 500    HIS B 413       33.25   -149.44                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     187 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  425     ALA A  426                  -42.30                    
REMARK 500 GLN B  180     THR B  181                 -133.91                    
REMARK 500 GLU B  410     LEU B  411                  147.75                    
REMARK 500 ILE D  299     LEU D  300                  139.72                    
REMARK 500 HIS F   44     PRO F   45                 -142.73                    
REMARK 500 GLY F  212     GLU F  213                   94.42                    
REMARK 500 ARG G  160     ASP G  161                  129.29                    
REMARK 500 VAL O  152     GLU O  153                 -144.50                    
REMARK 500 LYS O  382     SER O  383                 -130.31                    
REMARK 500 LYS R   25     LYS R   26                 -145.36                    
REMARK 500 TRP R   35     ASP R   36                  -34.00                    
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    HIS A  66         0.08    SIDE CHAIN                              
REMARK 500    ARG A 135         0.10    SIDE CHAIN                              
REMARK 500    TYR A 152         0.06    SIDE CHAIN                              
REMARK 500    ARG A 187         0.09    SIDE CHAIN                              
REMARK 500    TYR A 221         0.08    SIDE CHAIN                              
REMARK 500    ARG A 238         0.08    SIDE CHAIN                              
REMARK 500    TYR A 263         0.11    SIDE CHAIN                              
REMARK 500    ARG A 363         0.09    SIDE CHAIN                              
REMARK 500    ARG A 370         0.11    SIDE CHAIN                              
REMARK 500    ARG A 432         0.09    SIDE CHAIN                              
REMARK 500    ARG A 449         0.11    SIDE CHAIN                              
REMARK 500    TYR B  36         0.08    SIDE CHAIN                              
REMARK 500    TYR B 118         0.08    SIDE CHAIN                              
REMARK 500    ARG B 146         0.09    SIDE CHAIN                              
REMARK 500    ARG B 162         0.08    SIDE CHAIN                              
REMARK 500    TYR B 165         0.10    SIDE CHAIN                              
REMARK 500    TYR B 218         0.08    SIDE CHAIN                              
REMARK 500    PHE B 259         0.12    SIDE CHAIN                              
REMARK 500    TYR B 279         0.07    SIDE CHAIN                              
REMARK 500    PHE B 342         0.08    SIDE CHAIN                              
REMARK 500    ARG B 352         0.10    SIDE CHAIN                              
REMARK 500    ARG B 416         0.13    SIDE CHAIN                              
REMARK 500    ARG C 114         0.10    SIDE CHAIN                              
REMARK 500    ARG C 119         0.08    SIDE CHAIN                              
REMARK 500    TYR C 185         0.10    SIDE CHAIN                              
REMARK 500    TYR C 224         0.16    SIDE CHAIN                              
REMARK 500    ARG C 276         0.09    SIDE CHAIN                              
REMARK 500    TYR C 337         0.08    SIDE CHAIN                              
REMARK 500    TYR D  85         0.08    SIDE CHAIN                              
REMARK 500    ARG D  95         0.11    SIDE CHAIN                              
REMARK 500    TYR D 114         0.08    SIDE CHAIN                              
REMARK 500    TYR D 155         0.08    SIDE CHAIN                              
REMARK 500    TYR D 187         0.16    SIDE CHAIN                              
REMARK 500    ARG D 198         0.09    SIDE CHAIN                              
REMARK 500    ARG D 242         0.08    SIDE CHAIN                              
REMARK 500    PHE D 250         0.08    SIDE CHAIN                              
REMARK 500    TYR E  54         0.09    SIDE CHAIN                              
REMARK 500    TYR E 114         0.09    SIDE CHAIN                              
REMARK 500    TYR E 116         0.11    SIDE CHAIN                              
REMARK 500    TYR E 143         0.07    SIDE CHAIN                              
REMARK 500    TYR E 189         0.10    SIDE CHAIN                              
REMARK 500    TYR E 193         0.11    SIDE CHAIN                              
REMARK 500    TYR E 222         0.09    SIDE CHAIN                              
REMARK 500    PHE E 229         0.10    SIDE CHAIN                              
REMARK 500    TYR E 261         0.11    SIDE CHAIN                              
REMARK 500    ARG E 282         0.08    SIDE CHAIN                              
REMARK 500    ARG F  59         0.10    SIDE CHAIN                              
REMARK 500    TYR F 104         0.08    SIDE CHAIN                              
REMARK 500    ARG F 205         0.10    SIDE CHAIN                              
REMARK 500    TYR F 313         0.09    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      87 PLANE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    THR B  83        -12.12                                           
REMARK 500    GLU B 410         13.52                                           
REMARK 500    LEU D 300         11.13                                           
REMARK 500    LEU F  43         15.44                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-4739   RELATED DB: EMDB                              
REMARK 900 STRUCTURAL BASIS OF CULLIN-2 RING E3 LIGASE REGULATION BY THE COP9   
REMARK 900 SIGNALOSOME                                                          
DBREF  6R7F A   37   469  UNP    Q13098   CSN1_HUMAN      37    469             
DBREF  6R7F B    1   443  UNP    P61201   CSN2_HUMAN       1    443             
DBREF  6R7F C    1   403  UNP    Q9UNS2   CSN3_HUMAN       1    403             
DBREF  6R7F D    1   406  UNP    Q9BT78   CSN4_HUMAN       1    406             
DBREF  6R7F E   24   334  UNP    Q92905   CSN5_HUMAN      24    334             
DBREF  6R7F F   29   316  UNP    Q7L5N1   CSN6_HUMAN      29    316             
DBREF  6R7F H    1   209  UNP    Q99627   CSN8_HUMAN       1    209             
DBREF  6R7F G    8   215  UNP    Q9H9Q2   CSN7B_HUMAN      8    215             
DBREF  6R7F V   54   213  UNP    P40337   VHL_HUMAN        1    160             
DBREF  6R7F P    1   118  UNP    Q15370   ELOB_HUMAN       1    118             
DBREF  6R7F Q    1   112  UNP    Q15369   ELOC_HUMAN       1    112             
DBREF  6R7F O    1   745  UNP    Q13617   CUL2_HUMAN      20    764             
DBREF  6R7F R   19   108  PDB    6R7F     6R7F            19    108             
DBREF  6R7F N    1    76  UNP    Q15843   NEDD8_HUMAN      1     76             
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 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  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 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 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 V  160  MET GLU ALA GLY ARG PRO ARG PRO VAL LEU ARG SER VAL          
SEQRES   2 V  160  ASN SER ARG GLU PRO SER GLN VAL ILE PHE CYS ASN ARG          
SEQRES   3 V  160  SER PRO ARG VAL VAL LEU PRO VAL TRP LEU ASN PHE ASP          
SEQRES   4 V  160  GLY GLU PRO GLN PRO TYR PRO THR LEU PRO PRO GLY THR          
SEQRES   5 V  160  GLY ARG ARG ILE HIS SER TYR ARG GLY HIS LEU TRP LEU          
SEQRES   6 V  160  PHE ARG ASP ALA GLY THR HIS ASP GLY LEU LEU VAL ASN          
SEQRES   7 V  160  GLN THR GLU LEU PHE VAL PRO SER LEU ASN VAL ASP GLY          
SEQRES   8 V  160  GLN PRO ILE PHE ALA ASN ILE THR LEU PRO VAL TYR THR          
SEQRES   9 V  160  LEU LYS GLU ARG CYS LEU GLN VAL VAL ARG SER LEU VAL          
SEQRES  10 V  160  LYS PRO GLU ASN TYR ARG ARG LEU ASP ILE VAL ARG SER          
SEQRES  11 V  160  LEU TYR GLU ASP LEU GLU ASP HIS PRO ASN VAL GLN LYS          
SEQRES  12 V  160  ASP LEU GLU ARG LEU THR GLN GLU ARG ILE ALA HIS GLN          
SEQRES  13 V  160  ARG MET GLY ASP                                              
SEQRES   1 P  118  MET ASP VAL PHE LEU MET ILE ARG ARG HIS LYS THR THR          
SEQRES   2 P  118  ILE PHE THR ASP ALA LYS GLU SER SER THR VAL PHE GLU          
SEQRES   3 P  118  LEU LYS ARG ILE VAL GLU GLY ILE LEU LYS ARG PRO PRO          
SEQRES   4 P  118  ASP GLU GLN ARG LEU TYR LYS ASP ASP GLN LEU LEU ASP          
SEQRES   5 P  118  ASP GLY LYS THR LEU GLY GLU CYS GLY PHE THR SER GLN          
SEQRES   6 P  118  THR ALA ARG PRO GLN ALA PRO ALA THR VAL GLY LEU ALA          
SEQRES   7 P  118  PHE ARG ALA ASP ASP THR PHE GLU ALA LEU CYS ILE GLU          
SEQRES   8 P  118  PRO PHE SER SER PRO PRO GLU LEU PRO ASP VAL MET LYS          
SEQRES   9 P  118  PRO GLN ASP SER GLY SER SER ALA ASN GLU GLN ALA VAL          
SEQRES  10 P  118  GLN                                                          
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  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 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 N   76  MET LEU ILE LYS VAL LYS THR LEU THR GLY LYS GLU ILE          
SEQRES   2 N   76  GLU ILE ASP ILE GLU PRO THR ASP LYS VAL GLU ARG ILE          
SEQRES   3 N   76  LYS GLU ARG VAL GLU GLU LYS GLU GLY ILE PRO PRO GLN          
SEQRES   4 N   76  GLN GLN ARG LEU ILE TYR SER GLY LYS GLN MET ASN ASP          
SEQRES   5 N   76  GLU LYS THR ALA ALA ASP TYR LYS ILE LEU GLY GLY SER          
SEQRES   6 N   76  VAL LEU HIS LEU VAL LEU ALA LEU ARG GLY GLY                  
HELIX    1 AA1 ASP A   43  SER A   50  1                                   8    
HELIX    2 AA2 SER A   52  CYS A   67  1                                  16    
HELIX    3 AA3 LEU A   70  ARG A   84  1                                  15    
HELIX    4 AA4 VAL A   88  SER A  104  1                                  17    
HELIX    5 AA5 ASP A  127  SER A  156  1                                  30    
HELIX    6 AA6 ILE A  157  GLY A  176  1                                  20    
HELIX    7 AA7 SER A  179  ALA A  188  1                                  10    
HELIX    8 AA8 SER A  194  GLN A  213  1                                  20    
HELIX    9 AA9 TRP A  215  THR A  228  1                                  14    
HELIX   10 AB1 ALA A  244  ARG A  261  1                                  18    
HELIX   11 AB2 LYS A  262  LEU A  271  1                                  10    
HELIX   12 AB3 SER A  285  ALA A  299  1                                  15    
HELIX   13 AB4 ASP A  302  VAL A  310  1                                   9    
HELIX   14 AB5 PHE A  316  GLU A  323  1                                   8    
HELIX   15 AB6 GLU A  323  SER A  336  1                                  14    
HELIX   16 AB7 LYS A  337  ASP A  355  1                                  19    
HELIX   17 AB8 PRO A  360  SER A  379  1                                  20    
HELIX   18 AB9 MET A  386  ASN A  394  1                                   9    
HELIX   19 AC1 THR A  396  GLU A  410  1                                  15    
HELIX   20 AC2 ASP A  430  ASN A  462  1                                  33    
HELIX   21 AC3 ASP B   31  LYS B   43  1                                  13    
HELIX   22 AC4 ALA B   49  LEU B   60  1                                  12    
HELIX   23 AC5 GLY B   65  LEU B   82  1                                  18    
HELIX   24 AC6 ASN B   84  THR B   97  1                                  14    
HELIX   25 AC7 THR B  104  LYS B  123  1                                  20    
HELIX   26 AC8 GLN B  124  LEU B  139  1                                  16    
HELIX   27 AC9 ASN B  144  GLU B  163  1                                  20    
HELIX   28 AD1 TYR B  165  HIS B  176  1                                  12    
HELIX   29 AD2 GLN B  193  LYS B  209  1                                  17    
HELIX   30 AD3 ASN B  210  HIS B  223  1                                  14    
HELIX   31 AD4 ILE B  224  ALA B  227  5                                   4    
HELIX   32 AD5 LEU B  232  GLY B  249  1                                  18    
HELIX   33 AD6 GLU B  250  GLY B  269  1                                  20    
HELIX   34 AD7 ARG B  272  MET B  287  1                                  16    
HELIX   35 AD8 PRO B  301  ASN B  304  5                                   4    
HELIX   36 AD9 ASP B  305  ASN B  321  1                                  17    
HELIX   37 AE1 ASP B  322  ASN B  333  1                                  12    
HELIX   38 AE2 ASN B  333  ASP B  339  1                                   7    
HELIX   39 AE3 ASP B  340  ILE B  363  1                                  24    
HELIX   40 AE4 ILE B  371  ASN B  379  1                                   9    
HELIX   41 AE5 ASP B  381  ASN B  396  1                                  16    
HELIX   42 AE6 GLY B  418  LYS B  441  1                                  24    
HELIX   43 AE7 SER C    3  SER C   11  1                                   9    
HELIX   44 AE8 SER C   11  SER C   16  1                                   6    
HELIX   45 AE9 MET C   21  SER C   31  1                                  11    
HELIX   46 AF1 ALA C   36  LEU C   46  5                                  11    
HELIX   47 AF2 HIS C   54  VAL C   64  1                                  11    
HELIX   48 AF3 ASP C   73  THR C   87  1                                  15    
HELIX   49 AF4 HIS C   92  TYR C   95  5                                   4    
HELIX   50 AF5 ALA C   96  ARG C  114  1                                  19    
HELIX   51 AF6 PRO C  117  LYS C  130  1                                  14    
HELIX   52 AF7 SER C  140  ALA C  152  1                                  13    
HELIX   53 AF8 PHE C  155  PRO C  157  5                                   3    
HELIX   54 AF9 ALA C  158  VAL C  164  1                                   7    
HELIX   55 AG1 ASP C  177  LYS C  196  1                                  20    
HELIX   56 AG2 ASN C  197  ALA C  208  1                                  12    
HELIX   57 AG3 SER C  217  LEU C  235  1                                  19    
HELIX   58 AG4 GLN C  247  PHE C  252  1                                   6    
HELIX   59 AG5 PHE C  252  SER C  257  1                                   6    
HELIX   60 AG6 SER C  257  ASN C  270  1                                  14    
HELIX   61 AG7 ASN C  271  HIS C  282  1                                  12    
HELIX   62 AG8 HIS C  282  ASN C  290  1                                   9    
HELIX   63 AG9 GLY C  293  THR C  313  1                                  21    
HELIX   64 AH1 LEU C  319  VAL C  326  1                                   8    
HELIX   65 AH2 GLY C  330  GLY C  345  1                                  16    
HELIX   66 AH3 ASN C  369  ASN C  400  1                                  32    
HELIX   67 AH4 ALA D    2  ASN D   14  1                                  13    
HELIX   68 AH5 SER D   18  GLN D   35  1                                  18    
HELIX   69 AH6 GLY D   38  ASN D   54  1                                  17    
HELIX   70 AH7 SER D   58  LEU D   73  1                                  16    
HELIX   71 AH8 PRO D   74  LEU D   76  5                                   3    
HELIX   72 AH9 PRO D   77  GLN D   93  1                                  17    
HELIX   73 AI1 PRO D   94  SER D   98  5                                   5    
HELIX   74 AI2 PHE D   99  GLU D  118  1                                  20    
HELIX   75 AI3 ASP D  119  GLY D  129  1                                  11    
HELIX   76 AI4 ASN D  140  ASP D  158  1                                  19    
HELIX   77 AI5 ASP D  160  ASN D  176  1                                  17    
HELIX   78 AI6 ASN D  180  ARG D  198  1                                  19    
HELIX   79 AI7 LYS D  200  LYS D  214  1                                  15    
HELIX   80 AI8 HIS D  218  ALA D  236  1                                  19    
HELIX   81 AI9 GLN D  240  LYS D  251  1                                  12    
HELIX   82 AJ1 ASP D  252  LEU D  258  5                                   7    
HELIX   83 AJ2 ALA D  260  LEU D  269  1                                  10    
HELIX   84 AJ3 ARG D  274  LEU D  285  1                                  12    
HELIX   85 AJ4 MET D  286  LYS D  290  5                                   5    
HELIX   86 AJ5 LEU D  300  LYS D  314  1                                  15    
HELIX   87 AJ6 PHE D  321  GLU D  329  1                                   9    
HELIX   88 AJ7 PRO D  331  GLU D  345  1                                  15    
HELIX   89 AJ8 ALA D  366  ALA D  392  1                                  27    
HELIX   90 AJ9 ALA D  392  GLN D  406  1                                  15    
HELIX   91 AK1 ASP E   32  LYS E   43  1                                  12    
HELIX   92 AK2 PRO E   44  LYS E   47  5                                   4    
HELIX   93 AK3 SER E   58  GLY E   73  1                                  16    
HELIX   94 AK4 ALA E  109  GLY E  128  1                                  20    
HELIX   95 AK5 SER E  148  GLN E  162  1                                  15    
HELIX   96 AK6 THR E  173  GLY E  179  1                                   7    
HELIX   97 AK7 LYS E  210  CYS E  218  1                                   9    
HELIX   98 AK8 ASP E  234  TRP E  246  1                                  13    
HELIX   99 AK9 VAL E  247  SER E  252  5                                   6    
HELIX  100 AL1 SER E  253  ASN E  258  1                                   6    
HELIX  101 AL2 ASN E  258  GLY E  283  1                                  26    
HELIX  102 AL3 ASP E  298  GLN E  330  1                                  33    
HELIX  103 AL4 PRO F   45  GLY F   63  1                                  19    
HELIX  104 AL5 ASP F  101  PHE F  116  1                                  16    
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 SER F  215  GLY F  248  1                                  34    
HELIX  108 AL9 HIS F  254  CYS F  266  1                                  13    
HELIX  109 AM1 THR F  272  TYR F  313  1                                  42    
HELIX  110 AM2 SER H   12  ALA H   27  1                                  16    
HELIX  111 AM3 THR H   33  ASN H   48  1                                  16    
HELIX  112 AM4 ASP H   49  ILE H   60  1                                  12    
HELIX  113 AM5 PRO H   61  ASN H   68  1                                   8    
HELIX  114 AM6 SER H   69  ARG H   84  1                                  16    
HELIX  115 AM7 ASP H   85  HIS H   96  1                                  12    
HELIX  116 AM8 VAL H  102  ALA H  124  1                                  23    
HELIX  117 AM9 ALA H  130  GLY H  138  1                                   9    
HELIX  118 AN1 PRO H  140  GLY H  152  1                                  13    
HELIX  119 AN2 ALA H  198  ASN H  209  1                                  12    
HELIX  120 AN3 SER G    9  THR G   22  1                                  14    
HELIX  121 AN4 GLY G   24  ALA G   37  1                                  14    
HELIX  122 AN5 GLY G   44  LEU G   49  1                                   6    
HELIX  123 AN6 LEU G   49  GLU G   54  1                                   6    
HELIX  124 AN7 ASN G   60  GLY G   73  1                                  14    
HELIX  125 AN8 THR G   74  ASN G   81  1                                   8    
HELIX  126 AN9 SER G   89  MET G  108  1                                  20    
HELIX  127 AO1 TYR G  113  GLU G  121  1                                   9    
HELIX  128 AO2 ASN G  124  ASP G  139  1                                  16    
HELIX  129 AO3 ILE G  167  ASN G  215  1                                  49    
HELIX  130 AO4 THR V  157  VAL V  170  1                                  14    
HELIX  131 AO5 LYS V  171  TYR V  175  5                                   5    
HELIX  132 AO6 VAL V  181  ASP V  190  1                                  10    
HELIX  133 AO7 ASN V  193  GLN V  209  1                                  17    
HELIX  134 AO8 THR P   23  LYS P   36  1                                  14    
HELIX  135 AO9 THR P   56  GLY P   61  1                                   6    
HELIX  136 AP1 PRO Q   14  ALA Q   16  5                                   3    
HELIX  137 AP2 ARG Q   33  LEU Q   37  1                                   5    
HELIX  138 AP3 SER Q   39  GLY Q   48  1                                  10    
HELIX  139 AP4 PRO Q   66  THR Q   84  1                                  19    
HELIX  140 AP5 ILE Q   99  ASP Q  111  1                                  13    
HELIX  141 AP6 ASP O    9  VAL O   25  1                                  17    
HELIX  142 AP7 MET O   26  GLU O   28  5                                   3    
HELIX  143 AP8 GLU O   31  ALA O   48  1                                  18    
HELIX  144 AP9 PRO O   52  SER O   79  1                                  28    
HELIX  145 AQ1 GLN O   82  TYR O  105  1                                  24    
HELIX  146 AQ2 TYR O  105  PHE O  112  1                                   8    
HELIX  147 AQ3 GLU O  138  ARG O  148  1                                  11    
HELIX  148 AQ4 LYS O  149  MET O  151  5                                   3    
HELIX  149 AQ5 LEU O  155  ASN O  169  1                                  15    
HELIX  150 AQ6 ASN O  177  VAL O  191  1                                  15    
HELIX  151 AQ7 LEU O  200  PHE O  207  1                                   8    
HELIX  152 AQ8 PHE O  207  SER O  230  1                                  24    
HELIX  153 AQ9 ASN O  231  LEU O  254  1                                  24    
HELIX  154 AR1 HIS O  255  VAL O  271  1                                  17    
HELIX  155 AR2 HIS O  274  GLN O  288  1                                  15    
HELIX  156 AR3 LYS O  290  VAL O  304  1                                  15    
HELIX  157 AR4 GLY O  307  ASN O  329  1                                  23    
HELIX  158 AR5 MET O  335  VAL O  357  1                                  23    
HELIX  159 AR6 ASP O  361  TYR O  378  1                                  18    
HELIX  160 AR7 CYS O  385  LYS O  400  1                                  16    
HELIX  161 AR8 ASN O  409  LYS O  423  1                                  15    
HELIX  162 AR9 ASP O  427  GLY O  446  1                                  20    
HELIX  163 AS1 SER O  450  GLY O  466  1                                  17    
HELIX  164 AS2 GLY O  466  PHE O  493  1                                  28    
HELIX  165 AS3 PRO O  530  PHE O  548  1                                  19    
HELIX  166 AS4 THR O  579  ALA O  587  1                                   9    
HELIX  167 AS5 PHE O  588  ASN O  590  5                                   3    
HELIX  168 AS6 SER O  595  GLN O  604  1                                  10    
HELIX  169 AS7 ASN O  606  VAL O  620  1                                  15    
HELIX  170 AS8 LYS O  659  ALA O  690  1                                  32    
HELIX  171 AS9 HIS O  696  ARG O  708  1                                  13    
HELIX  172 AT1 SER O  714  LYS O  728  1                                  15    
HELIX  173 AT2 CYS R   53  GLN R   60  1                                   8    
HELIX  174 AT3 PHE R   81  LYS R   89  1                                   9    
HELIX  175 AT4 VAL N   23  GLY N   35  1                                  13    
SHEET    1 AA112 ILE B 369  HIS B 370  0                                        
SHEET    2 AA112 LEU B 408  LEU B 411 -1  O  LEU B 409   N  ILE B 369           
SHEET    3 AA112 GLY B 400  ASP B 403 -1  N  ARG B 401   O  GLU B 410           
SHEET    4 AA112 TYR A 381  ASP A 385  1  N  SER A 383   O  ILE B 402           
SHEET    5 AA112 ILE A 423  TYR A 425 -1  O  LEU A 424   N  ALA A 384           
SHEET    6 AA112 ARG A 416  ASP A 418 -1  N  ASP A 418   O  ILE A 423           
SHEET    7 AA112 PHE C 314  SER C 318  1  O  LEU C 315   N  VAL A 417           
SHEET    8 AA112 MET C 357  PHE C 360 -1  O  PHE C 360   N  LEU C 315           
SHEET    9 AA112 ALA C 349  ASN C 352 -1  N  ASN C 352   O  MET C 357           
SHEET   10 AA112 TYR H 125  ILE H 129  1  O  THR H 126   N  ILE C 351           
SHEET   11 AA112 MET H 161  LEU H 163 -1  O  VAL H 162   N  ILE H 128           
SHEET   12 AA112 GLN H 154  ASP H 156 -1  N  ASP H 156   O  MET H 161           
SHEET    1 AA2 3 ILE D 319  THR D 320  0                                        
SHEET    2 AA2 3 ILE D 358  PHE D 361 -1  O  VAL D 359   N  ILE D 319           
SHEET    3 AA2 3 GLY D 350  ASP D 353 -1  N  ASP D 353   O  ILE D 358           
SHEET    1 AA3 8 TYR E  54  ILE E  57  0                                        
SHEET    2 AA3 8 THR E  89  ALA E  97  1  O  MET E  90   N  LYS E  56           
SHEET    3 AA3 8 MET E  78  ASP E  86 -1  N  LYS E  84   O  ILE E  91           
SHEET    4 AA3 8 ALA E 133  SER E 139 -1  O  TYR E 137   N  GLY E  79           
SHEET    5 AA3 8 ALA E 167  ILE E 170  1  O  VAL E 168   N  HIS E 138           
SHEET    6 AA3 8 LEU E 183  THR E 188 -1  O  PHE E 186   N  ALA E 167           
SHEET    7 AA3 8 TYR E 221  SER E 227 -1  O  LEU E 224   N  ALA E 185           
SHEET    8 AA3 8 TYR E  54  ILE E  57  1  N  CYS E  55   O  GLU E 225           
SHEET    1 AA4 8 GLU F 178  LEU F 186  0                                        
SHEET    2 AA4 8 VAL F 165  ILE F 175 -1  N  VAL F 171   O  LEU F 182           
SHEET    3 AA4 8 PHE F 151  LEU F 154 -1  N  PHE F 151   O  PHE F 168           
SHEET    4 AA4 8 GLU F 120  THR F 127  1  N  THR F 126   O  LEU F 152           
SHEET    5 AA4 8 GLY F  70  GLU F  77 -1  N  GLY F  74   O  GLU F 120           
SHEET    6 AA4 8 ASN F  80  GLU F  88 -1  O  GLU F  82   N  LYS F  75           
SHEET    7 AA4 8 SER F  40  ALA F  42  1  N  SER F  40   O  ILE F  81           
SHEET    8 AA4 8 TYR F 188  THR F 189  1  O  THR F 189   N  VAL F  41           
SHEET    1 AA5 2 SER F  91  VAL F  94  0                                        
SHEET    2 AA5 2 LYS F  97  ILE F 100 -1  O  ILE F  99   N  HIS F  92           
SHEET    1 AA6 3 CYS G 110  PRO G 112  0                                        
SHEET    2 AA6 3 LEU G 151  PHE G 156 -1  O  LEU G 152   N  ILE G 111           
SHEET    3 AA6 3 GLN G 142  ASP G 146 -1  N  LYS G 144   O  GLU G 153           
SHEET    1 AA7 4 GLY V 106  TYR V 112  0                                        
SHEET    2 AA7 4 PRO V  71  ASN V  78 -1  N  VAL V  74   O  ILE V 109           
SHEET    3 AA7 4 ILE V 147  THR V 152  1  O  ILE V 151   N  CYS V  77           
SHEET    4 AA7 4 LEU V 129  VAL V 130 -1  N  LEU V 129   O  THR V 152           
SHEET    1 AA8 3 PRO V  95  PRO V  97  0                                        
SHEET    2 AA8 3 VAL V  84  LEU V  89 -1  N  TRP V  88   O  GLN V  96           
SHEET    3 AA8 3 LEU V 116  ASP V 121 -1  O  ARG V 120   N  LEU V  85           
SHEET    1 AA9 7 ARG P  43  TYR P  45  0                                        
SHEET    2 AA9 7 ALA P  73  ALA P  78 -1  O  GLY P  76   N  TYR P  45           
SHEET    3 AA9 7 ASP P   2  ARG P   9  1  N  ARG P   8   O  VAL P  75           
SHEET    4 AA9 7 THR P  12  LYS P  19 -1  O  ALA P  18   N  VAL P   3           
SHEET    5 AA9 7 GLU Q  28  LYS Q  32  1  O  ILE Q  30   N  THR P  13           
SHEET    6 AA9 7 TYR Q  18  ILE Q  22 -1  N  VAL Q  19   O  VAL Q  31           
SHEET    7 AA9 7 VAL Q  60  ASN Q  61  1  O  VAL Q  60   N  ILE Q  22           
SHEET    1 AB1 2 THR O 554  TRP O 555  0                                        
SHEET    2 AB1 2 ALA R  31  LEU R  32 -1  O  LEU R  32   N  THR O 554           
SHEET    1 AB2 2 THR O 561  LYS O 565  0                                        
SHEET    2 AB2 2 VAL O 574  THR O 578 -1  O  ALA O 575   N  VAL O 564           
SHEET    1 AB3 3 THR O 593  VAL O 594  0                                        
SHEET    2 AB3 3 PHE O 638  LEU O 640 -1  O  PHE O 638   N  VAL O 594           
SHEET    3 AB3 3 ILE O 623  ASN O 624 -1  N  ASN O 624   O  SER O 639           
SHEET    1 AB4 3 VAL O 693  ARG O 695  0                                        
SHEET    2 AB4 3 GLU O 740  TYR O 743 -1  O  TYR O 741   N  LEU O 694           
SHEET    3 AB4 3 ILE O 731  ARG O 733 -1  N  GLU O 732   O  SER O 742           
SHEET    1 AB5 2 VAL R  70  TRP R  72  0                                        
SHEET    2 AB5 2 ALA R  78  HIS R  80 -1  O  PHE R  79   N  ALA R  71           
SHEET    1 AB6 5 GLU N  12  ASP N  16  0                                        
SHEET    2 AB6 5 LEU N   2  LYS N   6 -1  N  VAL N   5   O  ILE N  13           
SHEET    3 AB6 5 VAL N  66  VAL N  70  1  O  LEU N  67   N  LYS N   6           
SHEET    4 AB6 5 ARG N  42  TYR N  45 -1  N  ILE N  44   O  HIS N  68           
SHEET    5 AB6 5 LYS N  48  GLN N  49 -1  O  LYS N  48   N  TYR N  45           
CISPEP   1 LYS B   64    GLY B   65          0       -11.05                     
CISPEP   2 SER B  270    PRO B  271          0        -9.65                     
CISPEP   3 LYS B  288    SER B  289          0         4.31                     
CISPEP   4 GLU E  163    PRO E  164          0        -8.73                     
CISPEP   5 LEU F  267    PRO F  268          0       -11.54                     
CISPEP   6 GLY Q   48    PRO Q   49          0        -5.61                     
CISPEP   7 PRO Q   49    GLY Q   50          0        -0.92                     
CISPEP   8 GLU O  174    ASP O  175          0        -8.82                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1                      
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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