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Database: PDB
Entry: 5VGZ
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Original site: 5VGZ 
HEADER    HYDROLASE                               12-APR-17   5VGZ              
TITLE     CONFORMATIONAL LANDSCAPE OF THE P28-BOUND HUMAN PROTEASOME REGULATORY 
TITLE    2 PARTICLE                                                             
CAVEAT     5VGZ    ENTRY CONTAINS IMPROPER PEPTIDE LINKAGES.                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 26S PROTEASOME REGULATORY SUBUNIT 7;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: 26S PROTEASOME AAA-ATPASE SUBUNIT RPT1,PROTEASOME 26S       
COMPND   5 SUBUNIT ATPASE 2,PROTEIN MSS1;                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: 26S PROTEASOME REGULATORY SUBUNIT 4;                       
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: P26S4,26S PROTEASOME AAA-ATPASE SUBUNIT RPT2,PROTEASOME 26S 
COMPND  11 SUBUNIT ATPASE 1;                                                    
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: 26S PROTEASOME REGULATORY SUBUNIT 8;                       
COMPND  15 CHAIN: C;                                                            
COMPND  16 SYNONYM: 26S PROTEASOME AAA-ATPASE SUBUNIT RPT6,PROTEASOME 26S       
COMPND  17 SUBUNIT ATPASE 5,PROTEASOME SUBUNIT P45,THYROID HORMONE RECEPTOR-    
COMPND  18 INTERACTING PROTEIN 1,TRIP1,P45/SUG;                                 
COMPND  19 ENGINEERED: YES;                                                     
COMPND  20 MOL_ID: 4;                                                           
COMPND  21 MOLECULE: 26S PROTEASOME REGULATORY SUBUNIT 6B;                      
COMPND  22 CHAIN: D;                                                            
COMPND  23 SYNONYM: 26S PROTEASOME AAA-ATPASE SUBUNIT RPT3,MB67-INTERACTING     
COMPND  24 PROTEIN,MIP224,PROTEASOME 26S SUBUNIT ATPASE 4,TAT-BINDING PROTEIN 7,
COMPND  25 TBP-7;                                                               
COMPND  26 ENGINEERED: YES;                                                     
COMPND  27 MOL_ID: 5;                                                           
COMPND  28 MOLECULE: 26S PROTEASOME REGULATORY SUBUNIT 10B;                     
COMPND  29 CHAIN: E;                                                            
COMPND  30 SYNONYM: 26S PROTEASOME AAA-ATPASE SUBUNIT RPT4,PROTEASOME 26S       
COMPND  31 SUBUNIT ATPASE 6,PROTEASOME SUBUNIT P42;                             
COMPND  32 ENGINEERED: YES;                                                     
COMPND  33 MOL_ID: 6;                                                           
COMPND  34 MOLECULE: 26S PROTEASOME REGULATORY SUBUNIT 6A;                      
COMPND  35 CHAIN: F;                                                            
COMPND  36 SYNONYM: 26S PROTEASOME AAA-ATPASE SUBUNIT RPT5,PROTEASOME 26S       
COMPND  37 SUBUNIT ATPASE 3,PROTEASOME SUBUNIT P50,TAT-BINDING PROTEIN 1,TBP-1; 
COMPND  38 ENGINEERED: YES;                                                     
COMPND  39 MOL_ID: 7;                                                           
COMPND  40 MOLECULE: 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 1;            
COMPND  41 CHAIN: U;                                                            
COMPND  42 SYNONYM: 26S PROTEASOME REGULATORY SUBUNIT RPN2,26S PROTEASOME       
COMPND  43 REGULATORY SUBUNIT S1,26S PROTEASOME SUBUNIT P112;                   
COMPND  44 ENGINEERED: YES;                                                     
COMPND  45 MOL_ID: 8;                                                           
COMPND  46 MOLECULE: 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 3;            
COMPND  47 CHAIN: V;                                                            
COMPND  48 SYNONYM: 26S PROTEASOME REGULATORY SUBUNIT RPN3,26S PROTEASOME       
COMPND  49 REGULATORY SUBUNIT S3,PROTEASOME SUBUNIT P58;                        
COMPND  50 ENGINEERED: YES;                                                     
COMPND  51 MOL_ID: 9;                                                           
COMPND  52 MOLECULE: 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 12;           
COMPND  53 CHAIN: W;                                                            
COMPND  54 SYNONYM: 26S PROTEASOME REGULATORY SUBUNIT RPN5,26S PROTEASOME       
COMPND  55 REGULATORY SUBUNIT P55;                                              
COMPND  56 ENGINEERED: YES;                                                     
COMPND  57 MOL_ID: 10;                                                          
COMPND  58 MOLECULE: 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 11;           
COMPND  59 CHAIN: X;                                                            
COMPND  60 SYNONYM: 26S PROTEASOME REGULATORY SUBUNIT RPN6,26S PROTEASOME       
COMPND  61 REGULATORY SUBUNIT S9,26S PROTEASOME REGULATORY SUBUNIT P44.5;       
COMPND  62 ENGINEERED: YES;                                                     
COMPND  63 MOL_ID: 11;                                                          
COMPND  64 MOLECULE: 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 6;            
COMPND  65 CHAIN: Y;                                                            
COMPND  66 SYNONYM: 26S PROTEASOME REGULATORY SUBUNIT RPN7,26S PROTEASOME       
COMPND  67 REGULATORY SUBUNIT S10,BREAST CANCER-ASSOCIATED PROTEIN SGA-113M,    
COMPND  68 PHOSPHONOFORMATE IMMUNO-ASSOCIATED PROTEIN 4,PROTEASOME REGULATORY   
COMPND  69 PARTICLE SUBUNIT P44S10,P42A;                                        
COMPND  70 ENGINEERED: YES;                                                     
COMPND  71 MOL_ID: 12;                                                          
COMPND  72 MOLECULE: 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 7;            
COMPND  73 CHAIN: Z;                                                            
COMPND  74 SYNONYM: 26S PROTEASOME REGULATORY SUBUNIT RPN8,26S PROTEASOME       
COMPND  75 REGULATORY SUBUNIT S12,MOV34 PROTEIN HOMOLOG,PROTEASOME SUBUNIT P40; 
COMPND  76 ENGINEERED: YES;                                                     
COMPND  77 MOL_ID: 13;                                                          
COMPND  78 MOLECULE: 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 13;           
COMPND  79 CHAIN: a;                                                            
COMPND  80 SYNONYM: 26S PROTEASOME REGULATORY SUBUNIT RPN9,26S PROTEASOME       
COMPND  81 REGULATORY SUBUNIT S11,26S PROTEASOME REGULATORY SUBUNIT P40.5;      
COMPND  82 ENGINEERED: YES;                                                     
COMPND  83 MOL_ID: 14;                                                          
COMPND  84 MOLECULE: 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 4;            
COMPND  85 CHAIN: b;                                                            
COMPND  86 SYNONYM: 26S PROTEASOME REGULATORY SUBUNIT RPN10,26S PROTEASOME      
COMPND  87 REGULATORY SUBUNIT S5A,ANTISECRETORY FACTOR 1,ASF,MULTIUBIQUITIN     
COMPND  88 CHAIN-BINDING PROTEIN;                                               
COMPND  89 ENGINEERED: YES;                                                     
COMPND  90 MOL_ID: 15;                                                          
COMPND  91 MOLECULE: 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 14;           
COMPND  92 CHAIN: c;                                                            
COMPND  93 SYNONYM: 26S PROTEASOME REGULATORY SUBUNIT RPN11,26S PROTEASOME-     
COMPND  94 ASSOCIATED PAD1 HOMOLOG 1;                                           
COMPND  95 EC: 3.4.19.-;                                                        
COMPND  96 ENGINEERED: YES;                                                     
COMPND  97 MOL_ID: 16;                                                          
COMPND  98 MOLECULE: 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 8;            
COMPND  99 CHAIN: d;                                                            
COMPND 100 SYNONYM: 26S PROTEASOME REGULATORY SUBUNIT RPN12,26S PROTEASOME      
COMPND 101 REGULATORY SUBUNIT S14,P31;                                          
COMPND 102 ENGINEERED: YES;                                                     
COMPND 103 MOL_ID: 17;                                                          
COMPND 104 MOLECULE: 26S PROTEASOME COMPLEX SUBUNIT SEM1;                       
COMPND 105 CHAIN: e;                                                            
COMPND 106 SYNONYM: 26S PROTEASOME COMPLEX SUBUNIT DSS1, DELETED IN SPLIT       
COMPND 107 HAND/SPLIT FOOT PROTEIN 1, SPLIT HAND/FOOT DELETED PROTEIN 1, SPLIT  
COMPND 108 HAND/FOOT MALFORMATION TYPE 1 PROTEIN, SEM1;                         
COMPND 109 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: PSMC2, MSS1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: PSMC1;                                                         
SOURCE  14 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  15 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 GENE: PSMC5, SUG1;                                                   
SOURCE  22 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  23 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  25 MOL_ID: 4;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  27 ORGANISM_COMMON: HUMAN;                                              
SOURCE  28 ORGANISM_TAXID: 9606;                                                
SOURCE  29 GENE: PSMC4, MIP224, TBP7;                                           
SOURCE  30 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  31 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  32 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  33 MOL_ID: 5;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  35 ORGANISM_COMMON: HUMAN;                                              
SOURCE  36 ORGANISM_TAXID: 9606;                                                
SOURCE  37 GENE: PSMC6, SUG2;                                                   
SOURCE  38 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  39 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  40 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  41 MOL_ID: 6;                                                           
SOURCE  42 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  43 ORGANISM_COMMON: HUMAN;                                              
SOURCE  44 ORGANISM_TAXID: 9606;                                                
SOURCE  45 GENE: PSMC3, TBP1;                                                   
SOURCE  46 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  47 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  48 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  49 MOL_ID: 7;                                                           
SOURCE  50 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  51 ORGANISM_COMMON: HUMAN;                                              
SOURCE  52 ORGANISM_TAXID: 9606;                                                
SOURCE  53 GENE: PSMD1;                                                         
SOURCE  54 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  55 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  56 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  57 MOL_ID: 8;                                                           
SOURCE  58 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  59 ORGANISM_COMMON: HUMAN;                                              
SOURCE  60 ORGANISM_TAXID: 9606;                                                
SOURCE  61 GENE: PSMD3;                                                         
SOURCE  62 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  63 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  64 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  65 MOL_ID: 9;                                                           
SOURCE  66 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  67 ORGANISM_COMMON: HUMAN;                                              
SOURCE  68 ORGANISM_TAXID: 9606;                                                
SOURCE  69 GENE: PSMD12;                                                        
SOURCE  70 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  71 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  72 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  73 MOL_ID: 10;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  75 ORGANISM_COMMON: HUMAN;                                              
SOURCE  76 ORGANISM_TAXID: 9606;                                                
SOURCE  77 GENE: PSMD11;                                                        
SOURCE  78 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  79 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  80 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  81 MOL_ID: 11;                                                          
SOURCE  82 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  83 ORGANISM_COMMON: HUMAN;                                              
SOURCE  84 ORGANISM_TAXID: 9606;                                                
SOURCE  85 GENE: PSMD6, KIAA0107, PFAAP4;                                       
SOURCE  86 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  87 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  88 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  89 MOL_ID: 12;                                                          
SOURCE  90 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  91 ORGANISM_COMMON: HUMAN;                                              
SOURCE  92 ORGANISM_TAXID: 9606;                                                
SOURCE  93 GENE: PSMD7, MOV34L;                                                 
SOURCE  94 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  95 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  96 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  97 MOL_ID: 13;                                                          
SOURCE  98 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  99 ORGANISM_COMMON: HUMAN;                                              
SOURCE 100 ORGANISM_TAXID: 9606;                                                
SOURCE 101 GENE: PSMD13;                                                        
SOURCE 102 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE 103 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE 104 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE 105 MOL_ID: 14;                                                          
SOURCE 106 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 107 ORGANISM_COMMON: HUMAN;                                              
SOURCE 108 ORGANISM_TAXID: 9606;                                                
SOURCE 109 GENE: PSMD4, MCB1;                                                   
SOURCE 110 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE 111 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE 112 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE 113 MOL_ID: 15;                                                          
SOURCE 114 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 115 ORGANISM_COMMON: HUMAN;                                              
SOURCE 116 ORGANISM_TAXID: 9606;                                                
SOURCE 117 GENE: PSMD14, POH1;                                                  
SOURCE 118 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE 119 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE 120 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE 121 MOL_ID: 16;                                                          
SOURCE 122 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 123 ORGANISM_COMMON: HUMAN;                                              
SOURCE 124 ORGANISM_TAXID: 9606;                                                
SOURCE 125 GENE: PSMD8;                                                         
SOURCE 126 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE 127 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE 128 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE 129 MOL_ID: 17;                                                          
SOURCE 130 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 131 ORGANISM_COMMON: HUMAN;                                              
SOURCE 132 ORGANISM_TAXID: 9606;                                                
SOURCE 133 GENE: SEM1, C7ORF76, DSS1, SHFDG1, SHFM1;                            
SOURCE 134 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE 135 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE 136 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    P28, 26S PROTEASOME, REGULATORY PARTICLE, 19S, GANKYRIN, HYDROLASE    
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    Y.LU,J.WU,Y.DONG,S.CHEN,S.SUN,Y.B.MA,Q.OUYANG,D.FINLEY,M.W.KIRSCHNER, 
AUTHOR   2 Y.MAO                                                                
REVDAT   2   22-AUG-18 5VGZ    1       REMARK                                   
REVDAT   1   23-AUG-17 5VGZ    0                                                
JRNL        AUTH   Y.LU,J.WU,Y.DONG,S.CHEN,S.SUN,Y.B.MA,Q.OUYANG,D.FINLEY,      
JRNL        AUTH 2 M.W.KIRSCHNER,Y.MAO                                          
JRNL        TITL   CONFORMATIONAL LANDSCAPE OF THE P28-BOUND HUMAN PROTEASOME   
JRNL        TITL 2 REGULATORY PARTICLE.                                         
JRNL        REF    MOL. CELL                     V.  67   322 2017              
JRNL        REFN                   ISSN 1097-4164                               
JRNL        PMID   28689658                                                     
JRNL        DOI    10.1016/J.MOLCEL.2017.06.007                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.70 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)  : 4.500                          
REMARK   3   NUMBER OF PARTICLES               : 117471                         
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 5VGZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-APR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227414.                                   
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                 : PROTEASOME REGULATORY PARTICLE    
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 TECNAI ARCTICA             
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 50.00                          
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)         : 200                            
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: HEPTADECAMERIC                    
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, U, V, W, X,         
REMARK 350                    AND CHAINS: Y, Z, a, b, c, d, e                   
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     ASN F   102                                                      
REMARK 465     ASP F   103                                                      
REMARK 465     GLN F   104                                                      
REMARK 465     GLU F   105                                                      
REMARK 465     GLU F   106                                                      
REMARK 465     ASP F   107                                                      
REMARK 465     GLY F   108                                                      
REMARK 465     ALA F   109                                                      
REMARK 465     ASN F   110                                                      
REMARK 465     ILE F   111                                                      
REMARK 465     ASP F   112                                                      
REMARK 465     LEU F   113                                                      
REMARK 465     ASP F   114                                                      
REMARK 465     SER F   115                                                      
REMARK 465     ILE U   275                                                      
REMARK 465     ALA U   276                                                      
REMARK 465     SER U   277                                                      
REMARK 465     VAL U   278                                                      
REMARK 465     PRO U   279                                                      
REMARK 465     GLY U   280                                                      
REMARK 465     SER U   281                                                      
REMARK 465     THR U   282                                                      
REMARK 465     ASN U   283                                                      
REMARK 465     THR U   284                                                      
REMARK 465     GLY U   285                                                      
REMARK 465     THR U   286                                                      
REMARK 465     VAL U   287                                                      
REMARK 465     PRO U   288                                                      
REMARK 465     GLY U   289                                                      
REMARK 465     SER U   290                                                      
REMARK 465     GLU U   291                                                      
REMARK 465     LYS U   292                                                      
REMARK 465     ASP U   293                                                      
REMARK 465     SER U   294                                                      
REMARK 465     ASP U   295                                                      
REMARK 465     SER U   296                                                      
REMARK 465     MET U   297                                                      
REMARK 465     GLU U   298                                                      
REMARK 465     THR U   299                                                      
REMARK 465     GLU U   300                                                      
REMARK 465     GLU U   301                                                      
REMARK 465     LYS U   302                                                      
REMARK 465     THR U   303                                                      
REMARK 465     SER U   304                                                      
REMARK 465     SER U   305                                                      
REMARK 465     ALA U   306                                                      
REMARK 465     PHE U   307                                                      
REMARK 465     VAL U   308                                                      
REMARK 465     GLY U   309                                                      
REMARK 465     LYS U   310                                                      
REMARK 465     THR U   311                                                      
REMARK 465     PRO U   312                                                      
REMARK 465     GLU U   313                                                      
REMARK 465     ALA U   314                                                      
REMARK 465     SER U   315                                                      
REMARK 465     PRO U   316                                                      
REMARK 465     LYS U   821                                                      
REMARK 465     GLU U   822                                                      
REMARK 465     LYS U   823                                                      
REMARK 465     GLU U   824                                                      
REMARK 465     LYS U   825                                                      
REMARK 465     GLU U   826                                                      
REMARK 465     LYS U   827                                                      
REMARK 465     VAL U   828                                                      
REMARK 465     SER U   829                                                      
REMARK 465     THR U   830                                                      
REMARK 465     ALA U   831                                                      
REMARK 465     VAL U   832                                                      
REMARK 465     LEU U   833                                                      
REMARK 465     GLU U   845                                                      
REMARK 465     LYS U   846                                                      
REMARK 465     GLU U   847                                                      
REMARK 465     LYS U   848                                                      
REMARK 465     LYS U   849                                                      
REMARK 465     GLU U   850                                                      
REMARK 465     GLU U   851                                                      
REMARK 465     GLU U   852                                                      
REMARK 465     LYS U   853                                                      
REMARK 465     MET U   854                                                      
REMARK 465     GLU U   855                                                      
REMARK 465     VAL U   856                                                      
REMARK 465     ASP U   857                                                      
REMARK 465     GLU U   858                                                      
REMARK 465     ALA U   859                                                      
REMARK 465     GLU U   860                                                      
REMARK 465     LYS U   861                                                      
REMARK 465     LYS U   862                                                      
REMARK 465     GLU U   863                                                      
REMARK 465     GLU U   864                                                      
REMARK 465     LYS U   865                                                      
REMARK 465     GLU U   866                                                      
REMARK 465     LYS U   867                                                      
REMARK 465     LYS U   868                                                      
REMARK 465     LYS U   869                                                      
REMARK 465     GLU U   870                                                      
REMARK 465     PRO U   871                                                      
REMARK 465     GLU U   872                                                      
REMARK 465     PRO U   873                                                      
REMARK 465     ASN U   874                                                      
REMARK 465     PHE U   875                                                      
REMARK 465     GLN U   876                                                      
REMARK 465     LEU U   877                                                      
REMARK 465     LEU U   878                                                      
REMARK 465     ASP U   879                                                      
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   NH2  ARG W   417     O    PRO W   418              0.87            
REMARK 500   NH1  ARG W   417     OD2  ASP W   420              1.04            
REMARK 500   CD   LYS U   146     NE2  GLN U   149              1.16            
REMARK 500   CZ   ARG W   417     O    PRO W   418              1.45            
REMARK 500   O    GLU V   268     OG   SER V   272              1.58            
REMARK 500   N    LEU V   270     CE   LYS V   273              1.58            
REMARK 500   CA   LEU V   270     CD   LYS V   273              1.59            
REMARK 500   O    LEU V   224     OD1  ASP V   225              1.64            
REMARK 500   NH2  ARG W   417     C    PRO W   418              1.72            
REMARK 500   NH1  ARG W   417     CG   ASP W   420              1.73            
REMARK 500   N    LEU V   270     CD   LYS V   273              1.74            
REMARK 500   O    GLU W   220     N    LEU W   222              1.78            
REMARK 500   CD   LYS U   146     CD   GLN U   149              1.78            
REMARK 500   OD2  ASP U   127     NH1  ARG U   129              1.87            
REMARK 500   CG   LYS U   146     OE1  GLN U   149              1.89            
REMARK 500   CE2  TYR C    23     NE2  GLN V   193              1.91            
REMARK 500   NZ   LYS A   116     OE2  GLU B   130              1.95            
REMARK 500   NZ   LYS U   799     OE2  GLU U   926              1.98            
REMARK 500   OH   TYR Y   292     NH1  ARG e    57              2.03            
REMARK 500   CD   LYS U   146     OE1  GLN U   149              2.08            
REMARK 500   NZ   LYS U   498     OD2  ASP U   531              2.09            
REMARK 500   O    GLN A    94     NH1  ARG A   144              2.09            
REMARK 500   NH1  ARG U   628     OE1  GLN U   749              2.09            
REMARK 500   OD1  ASN V   311     NZ   LYS V   315              2.10            
REMARK 500   OG1  THR E    74     NH1  ARG E    97              2.10            
REMARK 500   NH1  ARG U   684     OD2  ASP U   723              2.11            
REMARK 500   O    LEU U   155     NH1  ARG U   158              2.11            
REMARK 500   O    TRP U   392     NH1  ARG U   395              2.11            
REMARK 500   NH1  ARG Y   179     OE1  GLU Y   212              2.12            
REMARK 500   CZ   ARG W   417     OD2  ASP W   420              2.12            
REMARK 500   OE2  GLU X   362     NE2  GLN X   380              2.12            
REMARK 500   O    GLU Z   173     NH1  ARG Z   177              2.13            
REMARK 500   CA   LEU V   270     CG   LYS V   273              2.13            
REMARK 500   O    MET Y    42     NH1  ARG Y    46              2.13            
REMARK 500   NZ   LYS U    26     OD1  ASN d    34              2.13            
REMARK 500   NE   ARG X   142     OE2  GLU X   145              2.13            
REMARK 500   C    LEU V   270     CG   LYS V   273              2.15            
REMARK 500   NZ   LYS a    58     OE1  GLN a    86              2.15            
REMARK 500   O    ALA V   267     CB   VAL V   271              2.15            
REMARK 500   O    PRO V    29     N    ALA V    31              2.16            
REMARK 500   ND2  ASN X   182     OE2  GLU Y   248              2.16            
REMARK 500   O    GLU V   268     NZ   LYS V   273              2.16            
REMARK 500   O    PRO D    86     NZ   LYS D   134              2.17            
REMARK 500   NH1  ARG V   479     OD1  ASP Y   374              2.17            
REMARK 500   OD1  ASP c    71     NH1  ARG c   104              2.18            
REMARK 500   OD2  ASP c   158     OG   SER c   202              2.18            
REMARK 500   O    MET Z   112     OG   SER Z   119              2.18            
REMARK 500   O    GLN Y   280     NZ   LYS Y   284              2.19            
REMARK 500   NZ   LYS V   153     O    ASN V   199              2.19            
REMARK 500   O    GLU V   268     CE   LYS V   273              2.19            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      52 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU U 252   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    LEU V 170   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    PRO Z 221   C   -  N   -  CA  ANGL. DEV. =  11.8 DEGREES          
REMARK 500    PRO a 189   C   -  N   -  CA  ANGL. DEV. =  14.9 DEGREES          
REMARK 500    PRO a 189   C   -  N   -  CD  ANGL. DEV. = -13.1 DEGREES          
REMARK 500    PRO c  50   C   -  N   -  CA  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    LEU d 122   CA  -  CB  -  CG  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    LEU e  56   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  97       39.97    -91.34                                   
REMARK 500    LEU B 136     -167.67   -128.46                                   
REMARK 500    PHE B 138       -5.67     70.41                                   
REMARK 500    LYS B 141       -3.92     64.16                                   
REMARK 500    GLU B 145       79.86     57.01                                   
REMARK 500    LEU B 152     -169.83   -121.09                                   
REMARK 500    LYS B 155     -155.52    -85.35                                   
REMARK 500    VAL B 156        6.54    -67.28                                   
REMARK 500    PRO C  91      157.02    -14.63                                   
REMARK 500    LEU E  64      -61.96    -92.71                                   
REMARK 500    THR E 104       -3.98     68.67                                   
REMARK 500    LYS F  84       33.97    -89.06                                   
REMARK 500    LEU F 134      149.88   -170.26                                   
REMARK 500    THR U   3      -56.33   -120.34                                   
REMARK 500    ASP U  15     -164.33    -78.33                                   
REMARK 500    GLU U  16       77.63     45.99                                   
REMARK 500    HIS U 145      -23.26     71.58                                   
REMARK 500    LYS U 148      -54.30   -163.18                                   
REMARK 500    LYS U 191       -6.96     72.34                                   
REMARK 500    PHE U 222      -61.01   -108.77                                   
REMARK 500    ALA U 256      -10.01     74.22                                   
REMARK 500    GLN U 258      -57.11   -121.20                                   
REMARK 500    VAL U 364      -61.16    -97.28                                   
REMARK 500    PRO U 428       51.74    -91.82                                   
REMARK 500    HIS U 450       33.88    -92.66                                   
REMARK 500    ALA U 563       21.19    -79.98                                   
REMARK 500    THR U 663     -169.09   -105.89                                   
REMARK 500    HIS U 742       -4.66     71.74                                   
REMARK 500    CYS U 787     -169.46   -162.39                                   
REMARK 500    VAL U 819       74.96     51.77                                   
REMARK 500    GLU U 922       65.35     61.32                                   
REMARK 500    PRO V  27      -67.00    -97.31                                   
REMARK 500    PRO V  30       56.16    -47.39                                   
REMARK 500    ALA V  31      -44.20   -147.48                                   
REMARK 500    GLU V  77       32.34    -90.17                                   
REMARK 500    ARG V  99      -10.87     72.99                                   
REMARK 500    PRO V 133       49.99    -83.06                                   
REMARK 500    ASP V 140      -63.83    -99.32                                   
REMARK 500    ALA V 143      -52.99   -121.23                                   
REMARK 500    LEU V 145       -4.03     69.87                                   
REMARK 500    PHE V 147       30.81    -95.35                                   
REMARK 500    LEU V 169       61.09     60.16                                   
REMARK 500    ASP V 189      -49.95   -160.08                                   
REMARK 500    ASP V 190      177.21    142.30                                   
REMARK 500    GLN V 193      -76.09     -8.14                                   
REMARK 500    LEU V 221      -40.44   -130.59                                   
REMARK 500    ASP V 225       30.13   -176.58                                   
REMARK 500    VAL V 226      -98.20   -160.51                                   
REMARK 500    THR V 239      -15.74     91.20                                   
REMARK 500    LEU V 240      -30.54     95.00                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     154 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN c 400                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-8672   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8674   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8675   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8676   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8677   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8678   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8679   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8680   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8681   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8682   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8683   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8684   RELATED DB: EMDB                              
REMARK 900 RELATED ID: 5VHF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VHH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VHI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VHJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VHM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VHN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VHO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VHP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VHQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VHR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VHS   RELATED DB: PDB                                   
DBREF  5VGZ A   73   155  UNP    P35998   PRS7_HUMAN      73    155             
DBREF  5VGZ B   93   165  UNP    P62191   PRS4_HUMAN      93    165             
DBREF  5VGZ C   11   128  UNP    P62195   PRS8_HUMAN      11    128             
DBREF  5VGZ D   39   145  UNP    P43686   PRS6B_HUMAN     39    145             
DBREF  5VGZ E   11   114  UNP    P62333   PRS10_HUMAN     11    114             
DBREF  5VGZ F   53   167  UNP    P17980   PRS6A_HUMAN     53    167             
DBREF  5VGZ U    1   935  UNP    Q99460   PSMD1_HUMAN      1    935             
DBREF  5VGZ V   18   505  UNP    O43242   PSMD3_HUMAN     18    505             
DBREF  5VGZ W    1   456  UNP    O00232   PSD12_HUMAN      1    456             
DBREF  5VGZ X   38   422  UNP    O00231   PSD11_HUMAN     38    422             
DBREF  5VGZ Y   12   389  UNP    Q15008   PSMD6_HUMAN     12    389             
DBREF  5VGZ Z    5   290  UNP    P51665   PSMD7_HUMAN      5    290             
DBREF  5VGZ a    3   376  UNP    Q9UNM6   PSD13_HUMAN      3    376             
DBREF  5VGZ b    1   191  UNP    P55036   PSMD4_HUMAN      1    191             
DBREF  5VGZ c   24   310  UNP    O00487   PSDE_HUMAN      24    310             
DBREF  5VGZ d    1   257  UNP    P48556   PSMD8_HUMAN     94    350             
DBREF  5VGZ e    1    70  UNP    P60896   SEM1_HUMAN       1     70             
SEQRES   1 A   83  ALA PRO PRO ALA LEU TRP ASP LEU ALA ALA ASP LYS GLN          
SEQRES   2 A   83  THR LEU GLN SER GLU GLN PRO LEU GLN VAL ALA ARG CYS          
SEQRES   3 A   83  THR LYS ILE ILE ASN ALA ASP SER GLU ASP PRO LYS TYR          
SEQRES   4 A   83  ILE ILE ASN VAL LYS GLN PHE ALA LYS PHE VAL VAL ASP          
SEQRES   5 A   83  LEU SER ASP GLN VAL ALA PRO THR ASP ILE GLU GLU GLY          
SEQRES   6 A   83  MET ARG VAL GLY VAL ASP ARG ASN LYS TYR GLN ILE HIS          
SEQRES   7 A   83  ILE PRO LEU PRO PRO                                          
SEQRES   1 B   73  GLU GLU GLU ARG SER LYS VAL ASP ASP LEU ARG GLY THR          
SEQRES   2 B   73  PRO MET SER VAL GLY THR LEU GLU GLU ILE ILE ASP ASP          
SEQRES   3 B   73  ASN HIS ALA ILE VAL SER THR SER VAL GLY SER GLU HIS          
SEQRES   4 B   73  TYR VAL SER ILE LEU SER PHE VAL ASP LYS ASP LEU LEU          
SEQRES   5 B   73  GLU PRO GLY CYS SER VAL LEU LEU ASN HIS LYS VAL HIS          
SEQRES   6 B   73  ALA VAL ILE GLY VAL LEU MET ASP                              
SEQRES   1 C  118  LEU GLU GLU GLY LYS ALA GLY SER GLY LEU ARG GLN TYR          
SEQRES   2 C  118  TYR LEU SER LYS ILE GLU GLU LEU GLN LEU ILE VAL ASN          
SEQRES   3 C  118  ASP LYS SER GLN ASN LEU ARG ARG LEU GLN ALA GLN ARG          
SEQRES   4 C  118  ASN GLU LEU ASN ALA LYS VAL ARG LEU LEU ARG GLU GLU          
SEQRES   5 C  118  LEU GLN LEU LEU GLN GLU GLN GLY SER TYR VAL GLY GLU          
SEQRES   6 C  118  VAL VAL ARG ALA MET ASP LYS LYS LYS VAL LEU VAL LYS          
SEQRES   7 C  118  VAL HIS PRO GLU GLY LYS PHE VAL VAL ASP VAL ASP LYS          
SEQRES   8 C  118  ASN ILE ASP ILE ASN ASP VAL THR PRO ASN CYS ARG VAL          
SEQRES   9 C  118  ALA LEU ARG ASN ASP SER TYR THR LEU HIS LYS ILE LEU          
SEQRES  10 C  118  PRO                                                          
SEQRES   1 D  107  ASP LEU TYR SER ARG TYR LYS LYS LEU GLN GLN GLU LEU          
SEQRES   2 D  107  GLU PHE LEU GLU VAL GLN GLU GLU TYR ILE LYS ASP GLU          
SEQRES   3 D  107  GLN LYS ASN LEU LYS LYS GLU PHE LEU HIS ALA GLN GLU          
SEQRES   4 D  107  GLU VAL LYS ARG ILE GLN SER ILE PRO LEU VAL ILE GLY          
SEQRES   5 D  107  GLN PHE LEU GLU ALA VAL ASP GLN ASN THR ALA ILE VAL          
SEQRES   6 D  107  GLY SER THR THR GLY SER ASN TYR TYR VAL ARG ILE LEU          
SEQRES   7 D  107  SER THR ILE ASP ARG GLU LEU LEU LYS PRO ASN ALA SER          
SEQRES   8 D  107  VAL ALA LEU HIS LYS HIS SER ASN ALA LEU VAL ASP VAL          
SEQRES   9 D  107  LEU PRO PRO                                                  
SEQRES   1 E  104  ASP TYR ARG LYS LYS LEU LEU GLU HIS LYS GLU ILE ASP          
SEQRES   2 E  104  GLY ARG LEU LYS GLU LEU ARG GLU GLN LEU LYS GLU LEU          
SEQRES   3 E  104  THR LYS GLN TYR GLU LYS SER GLU ASN ASP LEU LYS ALA          
SEQRES   4 E  104  LEU GLN SER VAL GLY GLN ILE VAL GLY GLU VAL LEU LYS          
SEQRES   5 E  104  GLN LEU THR GLU GLU LYS PHE ILE VAL LYS ALA THR ASN          
SEQRES   6 E  104  GLY PRO ARG TYR VAL VAL GLY CYS ARG ARG GLN LEU ASP          
SEQRES   7 E  104  LYS SER LYS LEU LYS PRO GLY THR ARG VAL ALA LEU ASP          
SEQRES   8 E  104  MET THR THR LEU THR ILE MET ARG TYR LEU PRO ARG GLU          
SEQRES   1 F  115  LYS ILE MET LYS SER GLU VAL LEU ARG VAL THR HIS GLU          
SEQRES   2 F  115  LEU GLN ALA MET LYS ASP LYS ILE LYS GLU ASN SER GLU          
SEQRES   3 F  115  LYS ILE LYS VAL ASN LYS THR LEU PRO TYR LEU VAL SER          
SEQRES   4 F  115  ASN VAL ILE GLU LEU LEU ASP VAL ASP PRO ASN ASP GLN          
SEQRES   5 F  115  GLU GLU ASP GLY ALA ASN ILE ASP LEU ASP SER GLN ARG          
SEQRES   6 F  115  LYS GLY LYS CYS ALA VAL ILE LYS THR SER THR ARG GLN          
SEQRES   7 F  115  THR TYR PHE LEU PRO VAL ILE GLY LEU VAL ASP ALA GLU          
SEQRES   8 F  115  LYS LEU LYS PRO GLY ASP LEU VAL GLY VAL ASN LYS ASP          
SEQRES   9 F  115  SER TYR LEU ILE LEU GLU THR LEU PRO THR GLU                  
SEQRES   1 U  935  MET ILE THR SER ALA ALA GLY ILE ILE SER LEU LEU ASP          
SEQRES   2 U  935  GLU ASP GLU PRO GLN LEU LYS GLU PHE ALA LEU HIS LYS          
SEQRES   3 U  935  LEU ASN ALA VAL VAL ASN ASP PHE TRP ALA GLU ILE SER          
SEQRES   4 U  935  GLU SER VAL ASP LYS ILE GLU VAL LEU TYR GLU ASP GLU          
SEQRES   5 U  935  GLY PHE ARG SER ARG GLN PHE ALA ALA LEU VAL ALA SER          
SEQRES   6 U  935  LYS VAL PHE TYR HIS LEU GLY ALA PHE GLU GLU SER LEU          
SEQRES   7 U  935  ASN TYR ALA LEU GLY ALA GLY ASP LEU PHE ASN VAL ASN          
SEQRES   8 U  935  ASP ASN SER GLU TYR VAL GLU THR ILE ILE ALA LYS CYS          
SEQRES   9 U  935  ILE ASP HIS TYR THR LYS GLN CYS VAL GLU ASN ALA ASP          
SEQRES  10 U  935  LEU PRO GLU GLY GLU LYS LYS PRO ILE ASP GLN ARG LEU          
SEQRES  11 U  935  GLU GLY ILE VAL ASN LYS MET PHE GLN ARG CYS LEU ASP          
SEQRES  12 U  935  ASP HIS LYS TYR LYS GLN ALA ILE GLY ILE ALA LEU GLU          
SEQRES  13 U  935  THR ARG ARG LEU ASP VAL PHE GLU LYS THR ILE LEU GLU          
SEQRES  14 U  935  SER ASN ASP VAL PRO GLY MET LEU ALA TYR SER LEU LYS          
SEQRES  15 U  935  LEU CYS MET SER LEU MET GLN ASN LYS GLN PHE ARG ASN          
SEQRES  16 U  935  LYS VAL LEU ARG VAL LEU VAL LYS ILE TYR MET ASN LEU          
SEQRES  17 U  935  GLU LYS PRO ASP PHE ILE ASN VAL CYS GLN CYS LEU ILE          
SEQRES  18 U  935  PHE LEU ASP ASP PRO GLN ALA VAL SER ASP ILE LEU GLU          
SEQRES  19 U  935  LYS LEU VAL LYS GLU ASP ASN LEU LEU MET ALA TYR GLN          
SEQRES  20 U  935  ILE CYS PHE ASP LEU TYR GLU SER ALA SER GLN GLN PHE          
SEQRES  21 U  935  LEU SER SER VAL ILE GLN ASN LEU ARG THR VAL GLY THR          
SEQRES  22 U  935  PRO ILE ALA SER VAL PRO GLY SER THR ASN THR GLY THR          
SEQRES  23 U  935  VAL PRO GLY SER GLU LYS ASP SER ASP SER MET GLU THR          
SEQRES  24 U  935  GLU GLU LYS THR SER SER ALA PHE VAL GLY LYS THR PRO          
SEQRES  25 U  935  GLU ALA SER PRO GLU PRO LYS ASP GLN THR LEU LYS MET          
SEQRES  26 U  935  ILE LYS ILE LEU SER GLY GLU MET ALA ILE GLU LEU HIS          
SEQRES  27 U  935  LEU GLN PHE LEU ILE ARG ASN ASN ASN THR ASP LEU MET          
SEQRES  28 U  935  ILE LEU LYS ASN THR LYS ASP ALA VAL ARG ASN SER VAL          
SEQRES  29 U  935  CYS HIS THR ALA THR VAL ILE ALA ASN SER PHE MET HIS          
SEQRES  30 U  935  CYS GLY THR THR SER ASP GLN PHE LEU ARG ASP ASN LEU          
SEQRES  31 U  935  GLU TRP LEU ALA ARG ALA THR ASN TRP ALA LYS PHE THR          
SEQRES  32 U  935  ALA THR ALA SER LEU GLY VAL ILE HIS LYS GLY HIS GLU          
SEQRES  33 U  935  LYS GLU ALA LEU GLN LEU MET ALA THR TYR LEU PRO LYS          
SEQRES  34 U  935  ASP THR SER PRO GLY SER ALA TYR GLN GLU GLY GLY GLY          
SEQRES  35 U  935  LEU TYR ALA LEU GLY LEU ILE HIS ALA ASN HIS GLY GLY          
SEQRES  36 U  935  ASP ILE ILE ASP TYR LEU LEU ASN GLN LEU LYS ASN ALA          
SEQRES  37 U  935  SER ASN ASP ILE VAL ARG HIS GLY GLY SER LEU GLY LEU          
SEQRES  38 U  935  GLY LEU ALA ALA MET GLY THR ALA ARG GLN ASP VAL TYR          
SEQRES  39 U  935  ASP LEU LEU LYS THR ASN LEU TYR GLN ASP ASP ALA VAL          
SEQRES  40 U  935  THR GLY GLU ALA ALA GLY LEU ALA LEU GLY LEU VAL MET          
SEQRES  41 U  935  LEU GLY SER LYS ASN ALA GLN ALA ILE GLU ASP MET VAL          
SEQRES  42 U  935  GLY TYR ALA GLN GLU THR GLN HIS GLU LYS ILE LEU ARG          
SEQRES  43 U  935  GLY LEU ALA VAL GLY ILE ALA LEU VAL MET TYR GLY ARG          
SEQRES  44 U  935  MET GLU GLU ALA ASP ALA LEU ILE GLU SER LEU CYS ARG          
SEQRES  45 U  935  ASP LYS ASP PRO ILE LEU ARG ARG SER GLY MET TYR THR          
SEQRES  46 U  935  VAL ALA MET ALA TYR CYS GLY SER GLY ASN ASN LYS ALA          
SEQRES  47 U  935  ILE ARG ARG LEU LEU HIS VAL ALA VAL SER ASP VAL ASN          
SEQRES  48 U  935  ASP ASP VAL ARG ARG ALA ALA VAL GLU SER LEU GLY PHE          
SEQRES  49 U  935  ILE LEU PHE ARG THR PRO GLU GLN CYS PRO SER VAL VAL          
SEQRES  50 U  935  SER LEU LEU SER GLU SER TYR ASN PRO HIS VAL ARG TYR          
SEQRES  51 U  935  GLY ALA ALA MET ALA LEU GLY ILE CYS CYS ALA GLY THR          
SEQRES  52 U  935  GLY ASN LYS GLU ALA ILE ASN LEU LEU GLU PRO MET THR          
SEQRES  53 U  935  ASN ASP PRO VAL ASN TYR VAL ARG GLN GLY ALA LEU ILE          
SEQRES  54 U  935  ALA SER ALA LEU ILE MET ILE GLN GLN THR GLU ILE THR          
SEQRES  55 U  935  CYS PRO LYS VAL ASN GLN PHE ARG GLN LEU TYR SER LYS          
SEQRES  56 U  935  VAL ILE ASN ASP LYS HIS ASP ASP VAL MET ALA LYS PHE          
SEQRES  57 U  935  GLY ALA ILE LEU ALA GLN GLY ILE LEU ASP ALA GLY GLY          
SEQRES  58 U  935  HIS ASN VAL THR ILE SER LEU GLN SER ARG THR GLY HIS          
SEQRES  59 U  935  THR HIS MET PRO SER VAL VAL GLY VAL LEU VAL PHE THR          
SEQRES  60 U  935  GLN PHE TRP PHE TRP PHE PRO LEU SER HIS PHE LEU SER          
SEQRES  61 U  935  LEU ALA TYR THR PRO THR CYS VAL ILE GLY LEU ASN LYS          
SEQRES  62 U  935  ASP LEU LYS MET PRO LYS VAL GLN TYR LYS SER ASN CYS          
SEQRES  63 U  935  LYS PRO SER THR PHE ALA TYR PRO ALA PRO LEU GLU VAL          
SEQRES  64 U  935  PRO LYS GLU LYS GLU LYS GLU LYS VAL SER THR ALA VAL          
SEQRES  65 U  935  LEU SER ILE THR ALA LYS ALA LYS LYS LYS GLU LYS GLU          
SEQRES  66 U  935  LYS GLU LYS LYS GLU GLU GLU LYS MET GLU VAL ASP GLU          
SEQRES  67 U  935  ALA GLU LYS LYS GLU GLU LYS GLU LYS LYS LYS GLU PRO          
SEQRES  68 U  935  GLU PRO ASN PHE GLN LEU LEU ASP ASN PRO ALA ARG VAL          
SEQRES  69 U  935  MET PRO ALA GLN LEU LYS VAL LEU THR MET PRO GLU THR          
SEQRES  70 U  935  CYS ARG TYR GLN PRO PHE LYS PRO LEU SER ILE GLY GLY          
SEQRES  71 U  935  ILE ILE ILE LEU LYS ASP THR SER GLU ASP ILE GLU GLU          
SEQRES  72 U  935  LEU VAL GLU PRO VAL ALA ALA HIS GLY PRO LYS ILE              
SEQRES   1 V  488  PRO PRO GLY GLY GLY GLU GLN GLU PRO PRO PRO PRO PRO          
SEQRES   2 V  488  ALA PRO GLN ASP VAL GLU MET LYS GLU GLU ALA ALA THR          
SEQRES   3 V  488  GLY GLY GLY SER THR GLY GLU ALA ASP GLY LYS THR ALA          
SEQRES   4 V  488  ALA ALA ALA ALA GLU HIS SER GLN ARG GLU LEU ASP THR          
SEQRES   5 V  488  VAL THR LEU GLU ASP ILE LYS GLU HIS VAL LYS GLN LEU          
SEQRES   6 V  488  GLU LYS ALA VAL SER GLY LYS GLU PRO ARG PHE VAL LEU          
SEQRES   7 V  488  ARG ALA LEU ARG MET LEU PRO SER THR SER ARG ARG LEU          
SEQRES   8 V  488  ASN HIS TYR VAL LEU TYR LYS ALA VAL GLN GLY PHE PHE          
SEQRES   9 V  488  THR SER ASN ASN ALA THR ARG ASP PHE LEU LEU PRO PHE          
SEQRES  10 V  488  LEU GLU GLU PRO MET ASP THR GLU ALA ASP LEU GLN PHE          
SEQRES  11 V  488  ARG PRO ARG THR GLY LYS ALA ALA SER THR PRO LEU LEU          
SEQRES  12 V  488  PRO GLU VAL GLU ALA TYR LEU GLN LEU LEU VAL VAL ILE          
SEQRES  13 V  488  PHE MET MET ASN SER LYS ARG TYR LYS GLU ALA GLN LYS          
SEQRES  14 V  488  ILE SER ASP ASP LEU MET GLN LYS ILE SER THR GLN ASN          
SEQRES  15 V  488  ARG ARG ALA LEU ASP LEU VAL ALA ALA LYS CYS TYR TYR          
SEQRES  16 V  488  TYR HIS ALA ARG VAL TYR GLU PHE LEU ASP LYS LEU ASP          
SEQRES  17 V  488  VAL VAL ARG SER PHE LEU HIS ALA ARG LEU ARG THR ALA          
SEQRES  18 V  488  THR LEU ARG HIS ASP ALA ASP GLY GLN ALA THR LEU LEU          
SEQRES  19 V  488  ASN LEU LEU LEU ARG ASN TYR LEU HIS TYR SER LEU TYR          
SEQRES  20 V  488  ASP GLN ALA GLU LYS LEU VAL SER LYS SER VAL PHE PRO          
SEQRES  21 V  488  GLU GLN ALA ASN ASN ASN GLU TRP ALA ARG TYR LEU TYR          
SEQRES  22 V  488  TYR THR GLY ARG ILE LYS ALA ILE GLN LEU GLU TYR SER          
SEQRES  23 V  488  GLU ALA ARG ARG THR MET THR ASN ALA LEU ARG LYS ALA          
SEQRES  24 V  488  PRO GLN HIS THR ALA VAL GLY PHE LYS GLN THR VAL HIS          
SEQRES  25 V  488  LYS LEU LEU ILE VAL VAL GLU LEU LEU LEU GLY GLU ILE          
SEQRES  26 V  488  PRO ASP ARG LEU GLN PHE ARG GLN PRO SER LEU LYS ARG          
SEQRES  27 V  488  SER LEU MET PRO TYR PHE LEU LEU THR GLN ALA VAL ARG          
SEQRES  28 V  488  THR GLY ASN LEU ALA LYS PHE ASN GLN VAL LEU ASP GLN          
SEQRES  29 V  488  PHE GLY GLU LYS PHE GLN ALA ASP GLY THR TYR THR LEU          
SEQRES  30 V  488  ILE ILE ARG LEU ARG HIS ASN VAL ILE LYS THR GLY VAL          
SEQRES  31 V  488  ARG MET ILE SER LEU SER TYR SER ARG ILE SER LEU ALA          
SEQRES  32 V  488  ASP ILE ALA GLN LYS LEU GLN LEU ASP SER PRO GLU ASP          
SEQRES  33 V  488  ALA GLU PHE ILE VAL ALA LYS ALA ILE ARG ASP GLY VAL          
SEQRES  34 V  488  ILE GLU ALA SER ILE ASN HIS GLU LYS GLY TYR VAL GLN          
SEQRES  35 V  488  SER LYS GLU MET ILE ASP ILE TYR SER THR ARG GLU PRO          
SEQRES  36 V  488  GLN LEU ALA PHE HIS GLN ARG ILE SER PHE CYS LEU ASP          
SEQRES  37 V  488  ILE HIS ASN MET SER VAL LYS ALA MET ARG PHE PRO PRO          
SEQRES  38 V  488  LYS SER TYR ASN LYS ASP LEU                                  
SEQRES   1 W  456  MET ALA ASP GLY GLY SER GLU ARG ALA ASP GLY ARG ILE          
SEQRES   2 W  456  VAL LYS MET GLU VAL ASP TYR SER ALA THR VAL ASP GLN          
SEQRES   3 W  456  ARG LEU PRO GLU CYS ALA LYS LEU ALA LYS GLU GLY ARG          
SEQRES   4 W  456  LEU GLN GLU VAL ILE GLU THR LEU LEU SER LEU GLU LYS          
SEQRES   5 W  456  GLN THR ARG THR ALA SER ASP MET VAL SER THR SER ARG          
SEQRES   6 W  456  ILE LEU VAL ALA VAL VAL LYS MET CYS TYR GLU ALA LYS          
SEQRES   7 W  456  GLU TRP ASP LEU LEU ASN GLU ASN ILE MET LEU LEU SER          
SEQRES   8 W  456  LYS ARG ARG SER GLN LEU LYS GLN ALA VAL ALA LYS MET          
SEQRES   9 W  456  VAL GLN GLN CYS CYS THR TYR VAL GLU GLU ILE THR ASP          
SEQRES  10 W  456  LEU PRO ILE LYS LEU ARG LEU ILE ASP THR LEU ARG MET          
SEQRES  11 W  456  VAL THR GLU GLY LYS ILE TYR VAL GLU ILE GLU ARG ALA          
SEQRES  12 W  456  ARG LEU THR LYS THR LEU ALA THR ILE LYS GLU GLN ASN          
SEQRES  13 W  456  GLY ASP VAL LYS GLU ALA ALA SER ILE LEU GLN GLU LEU          
SEQRES  14 W  456  GLN VAL GLU THR TYR GLY SER MET GLU LYS LYS GLU ARG          
SEQRES  15 W  456  VAL GLU PHE ILE LEU GLU GLN MET ARG LEU CYS LEU ALA          
SEQRES  16 W  456  VAL LYS ASP TYR ILE ARG THR GLN ILE ILE SER LYS LYS          
SEQRES  17 W  456  ILE ASN THR LYS PHE PHE GLN GLU GLU ASN THR GLU LYS          
SEQRES  18 W  456  LEU LYS LEU LYS TYR TYR ASN LEU MET ILE GLN LEU ASP          
SEQRES  19 W  456  GLN HIS GLU GLY SER TYR LEU SER ILE CYS LYS HIS TYR          
SEQRES  20 W  456  ARG ALA ILE TYR ASP THR PRO CYS ILE GLN ALA GLU SER          
SEQRES  21 W  456  GLU LYS TRP GLN GLN ALA LEU LYS SER VAL VAL LEU TYR          
SEQRES  22 W  456  VAL ILE LEU ALA PRO PHE ASP ASN GLU GLN SER ASP LEU          
SEQRES  23 W  456  VAL HIS ARG ILE SER GLY ASP LYS LYS LEU GLU GLU ILE          
SEQRES  24 W  456  PRO LYS TYR LYS ASP LEU LEU LYS LEU PHE THR THR MET          
SEQRES  25 W  456  GLU LEU MET ARG TRP SER THR LEU VAL GLU ASP TYR GLY          
SEQRES  26 W  456  MET GLU LEU ARG LYS GLY SER LEU GLU SER PRO ALA THR          
SEQRES  27 W  456  ASP VAL PHE GLY SER THR GLU GLU GLY GLU LYS ARG TRP          
SEQRES  28 W  456  LYS ASP LEU LYS ASN ARG VAL VAL GLU HIS ASN ILE ARG          
SEQRES  29 W  456  ILE MET ALA LYS TYR TYR THR ARG ILE THR MET LYS ARG          
SEQRES  30 W  456  MET ALA GLN LEU LEU ASP LEU SER VAL ASP GLU SER GLU          
SEQRES  31 W  456  ALA PHE LEU SER ASN LEU VAL VAL ASN LYS THR ILE PHE          
SEQRES  32 W  456  ALA LYS VAL ASP ARG LEU ALA GLY ILE ILE ASN PHE GLN          
SEQRES  33 W  456  ARG PRO LYS ASP PRO ASN ASN LEU LEU ASN ASP TRP SER          
SEQRES  34 W  456  GLN LYS LEU ASN SER LEU MET SER LEU VAL ASN LYS THR          
SEQRES  35 W  456  THR HIS LEU ILE ALA LYS GLU GLU MET ILE HIS ASN LEU          
SEQRES  36 W  456  GLN                                                          
SEQRES   1 X  385  ASN ASP GLU GLU ALA VAL GLN VAL LYS GLU GLN SER ILE          
SEQRES   2 X  385  LEU GLU LEU GLY SER LEU LEU ALA LYS THR GLY GLN ALA          
SEQRES   3 X  385  ALA GLU LEU GLY GLY LEU LEU LYS TYR VAL ARG PRO PHE          
SEQRES   4 X  385  LEU ASN SER ILE SER LYS ALA LYS ALA ALA ARG LEU VAL          
SEQRES   5 X  385  ARG SER LEU LEU ASP LEU PHE LEU ASP MET GLU ALA ALA          
SEQRES   6 X  385  THR GLY GLN GLU VAL GLU LEU CYS LEU GLU CYS ILE GLU          
SEQRES   7 X  385  TRP ALA LYS SER GLU LYS ARG THR PHE LEU ARG GLN ALA          
SEQRES   8 X  385  LEU GLU ALA ARG LEU VAL SER LEU TYR PHE ASP THR LYS          
SEQRES   9 X  385  ARG TYR GLN GLU ALA LEU HIS LEU GLY SER GLN LEU LEU          
SEQRES  10 X  385  ARG GLU LEU LYS LYS MET ASP ASP LYS ALA LEU LEU VAL          
SEQRES  11 X  385  GLU VAL GLN LEU LEU GLU SER LYS THR TYR HIS ALA LEU          
SEQRES  12 X  385  SER ASN LEU PRO LYS ALA ARG ALA ALA LEU THR SER ALA          
SEQRES  13 X  385  ARG THR THR ALA ASN ALA ILE TYR CYS PRO PRO LYS LEU          
SEQRES  14 X  385  GLN ALA THR LEU ASP MET GLN SER GLY ILE ILE HIS ALA          
SEQRES  15 X  385  ALA GLU GLU LYS ASP TRP LYS THR ALA TYR SER TYR PHE          
SEQRES  16 X  385  TYR GLU ALA PHE GLU GLY TYR ASP SER ILE ASP SER PRO          
SEQRES  17 X  385  LYS ALA ILE THR SER LEU LYS TYR MET LEU LEU CYS LYS          
SEQRES  18 X  385  ILE MET LEU ASN THR PRO GLU ASP VAL GLN ALA LEU VAL          
SEQRES  19 X  385  SER GLY LYS LEU ALA LEU ARG TYR ALA GLY ARG GLN THR          
SEQRES  20 X  385  GLU ALA LEU LYS CYS VAL ALA GLN ALA SER LYS ASN ARG          
SEQRES  21 X  385  SER LEU ALA ASP PHE GLU LYS ALA LEU THR ASP TYR ARG          
SEQRES  22 X  385  ALA GLU LEU ARG ASP ASP PRO ILE ILE SER THR HIS LEU          
SEQRES  23 X  385  ALA LYS LEU TYR ASP ASN LEU LEU GLU GLN ASN LEU ILE          
SEQRES  24 X  385  ARG VAL ILE GLU PRO PHE SER ARG VAL GLN ILE GLU HIS          
SEQRES  25 X  385  ILE SER SER LEU ILE LYS LEU SER LYS ALA ASP VAL GLU          
SEQRES  26 X  385  ARG LYS LEU SER GLN MET ILE LEU ASP LYS LYS PHE HIS          
SEQRES  27 X  385  GLY ILE LEU ASP GLN GLY GLU GLY VAL LEU ILE ILE PHE          
SEQRES  28 X  385  ASP GLU PRO PRO VAL ASP LYS THR TYR GLU ALA ALA LEU          
SEQRES  29 X  385  GLU THR ILE GLN ASN MET SER LYS VAL VAL ASP SER LEU          
SEQRES  30 X  385  TYR ASN LYS ALA LYS LYS LEU THR                              
SEQRES   1 Y  378  PRO LYS ASN PRO ASP LEU ARG ILE ALA GLN LEU ARG PHE          
SEQRES   2 Y  378  LEU LEU SER LEU PRO GLU HIS ARG GLY ASP ALA ALA VAL          
SEQRES   3 Y  378  ARG ASP GLU LEU MET ALA ALA VAL ARG ASP ASN ASN MET          
SEQRES   4 Y  378  ALA PRO TYR TYR GLU ALA LEU CYS LYS SER LEU ASP TRP          
SEQRES   5 Y  378  GLN ILE ASP VAL ASP LEU LEU ASN LYS MET LYS LYS ALA          
SEQRES   6 Y  378  ASN GLU ASP GLU LEU LYS ARG LEU ASP GLU GLU LEU GLU          
SEQRES   7 Y  378  ASP ALA GLU LYS ASN LEU GLY GLU SER GLU ILE ARG ASP          
SEQRES   8 Y  378  ALA MET MET ALA LYS ALA GLU TYR LEU CYS ARG ILE GLY          
SEQRES   9 Y  378  ASP LYS GLU GLY ALA LEU THR ALA PHE ARG LYS THR TYR          
SEQRES  10 Y  378  ASP LYS THR VAL ALA LEU GLY HIS ARG LEU ASP ILE VAL          
SEQRES  11 Y  378  PHE TYR LEU LEU ARG ILE GLY LEU PHE TYR MET ASP ASN          
SEQRES  12 Y  378  ASP LEU ILE THR ARG ASN THR GLU LYS ALA LYS SER LEU          
SEQRES  13 Y  378  ILE GLU GLU GLY GLY ASP TRP ASP ARG ARG ASN ARG LEU          
SEQRES  14 Y  378  LYS VAL TYR GLN GLY LEU TYR CYS VAL ALA ILE ARG ASP          
SEQRES  15 Y  378  PHE LYS GLN ALA ALA GLU LEU PHE LEU ASP THR VAL SER          
SEQRES  16 Y  378  THR PHE THR SER TYR GLU LEU MET ASP TYR LYS THR PHE          
SEQRES  17 Y  378  VAL THR TYR THR VAL TYR VAL SER MET ILE ALA LEU GLU          
SEQRES  18 Y  378  ARG PRO ASP LEU ARG GLU LYS VAL ILE LYS GLY ALA GLU          
SEQRES  19 Y  378  ILE LEU GLU VAL LEU HIS SER LEU PRO ALA VAL ARG GLN          
SEQRES  20 Y  378  TYR LEU PHE SER LEU TYR GLU CYS ARG TYR SER VAL PHE          
SEQRES  21 Y  378  PHE GLN SER LEU ALA VAL VAL GLU GLN GLU MET LYS LYS          
SEQRES  22 Y  378  ASP TRP LEU PHE ALA PRO HIS TYR ARG TYR TYR VAL ARG          
SEQRES  23 Y  378  GLU MET ARG ILE HIS ALA TYR SER GLN LEU LEU GLU SER          
SEQRES  24 Y  378  TYR ARG SER LEU THR LEU GLY TYR MET ALA GLU ALA PHE          
SEQRES  25 Y  378  GLY VAL GLY VAL GLU PHE ILE ASP GLN GLU LEU SER ARG          
SEQRES  26 Y  378  PHE ILE ALA ALA GLY ARG LEU HIS CYS LYS ILE ASP LYS          
SEQRES  27 Y  378  VAL ASN GLU ILE VAL GLU THR ASN ARG PRO ASP SER LYS          
SEQRES  28 Y  378  ASN TRP GLN TYR GLN GLU THR ILE LYS LYS GLY ASP LEU          
SEQRES  29 Y  378  LEU LEU ASN ARG VAL GLN LYS LEU SER ARG VAL ILE ASN          
SEQRES  30 Y  378  MET                                                          
SEQRES   1 Z  286  ALA VAL GLN LYS VAL VAL VAL HIS PRO LEU VAL LEU LEU          
SEQRES   2 Z  286  SER VAL VAL ASP HIS PHE ASN ARG ILE GLY LYS VAL GLY          
SEQRES   3 Z  286  ASN GLN LYS ARG VAL VAL GLY VAL LEU LEU GLY SER TRP          
SEQRES   4 Z  286  GLN LYS LYS VAL LEU ASP VAL SER ASN SER PHE ALA VAL          
SEQRES   5 Z  286  PRO PHE ASP GLU ASP ASP LYS ASP ASP SER VAL TRP PHE          
SEQRES   6 Z  286  LEU ASP HIS ASP TYR LEU GLU ASN MET TYR GLY MET PHE          
SEQRES   7 Z  286  LYS LYS VAL ASN ALA ARG GLU ARG ILE VAL GLY TRP TYR          
SEQRES   8 Z  286  HIS THR GLY PRO LYS LEU HIS LYS ASN ASP ILE ALA ILE          
SEQRES   9 Z  286  ASN GLU LEU MET LYS ARG TYR CYS PRO ASN SER VAL LEU          
SEQRES  10 Z  286  VAL ILE ILE ASP VAL LYS PRO LYS ASP LEU GLY LEU PRO          
SEQRES  11 Z  286  THR GLU ALA TYR ILE SER VAL GLU GLU VAL HIS ASP ASP          
SEQRES  12 Z  286  GLY THR PRO THR SER LYS THR PHE GLU HIS VAL THR SER          
SEQRES  13 Z  286  GLU ILE GLY ALA GLU GLU ALA GLU GLU VAL GLY VAL GLU          
SEQRES  14 Z  286  HIS LEU LEU ARG ASP ILE LYS ASP THR THR VAL GLY THR          
SEQRES  15 Z  286  LEU SER GLN ARG ILE THR ASN GLN VAL HIS GLY LEU LYS          
SEQRES  16 Z  286  GLY LEU ASN SER LYS LEU LEU ASP ILE ARG SER TYR LEU          
SEQRES  17 Z  286  GLU LYS VAL ALA THR GLY LYS LEU PRO ILE ASN HIS GLN          
SEQRES  18 Z  286  ILE ILE TYR GLN LEU GLN ASP VAL PHE ASN LEU LEU PRO          
SEQRES  19 Z  286  ASP VAL SER LEU GLN GLU PHE VAL LYS ALA PHE TYR LEU          
SEQRES  20 Z  286  LYS THR ASN ASP GLN MET VAL VAL VAL TYR LEU ALA SER          
SEQRES  21 Z  286  LEU ILE ARG SER VAL VAL ALA LEU HIS ASN LEU ILE ASN          
SEQRES  22 Z  286  ASN LYS ILE ALA ASN ARG ASP ALA GLU LYS LYS GLU GLY          
SEQRES   1 a  374  ASP VAL PRO GLY PHE LEU GLN GLN SER GLN ASN SER GLY          
SEQRES   2 a  374  PRO GLY GLN PRO ALA VAL TRP HIS ARG LEU GLU GLU LEU          
SEQRES   3 a  374  TYR THR LYS LYS LEU TRP HIS GLN LEU THR LEU GLN VAL          
SEQRES   4 a  374  LEU ASP PHE VAL GLN ASP PRO CYS PHE ALA GLN GLY ASP          
SEQRES   5 a  374  GLY LEU ILE LYS LEU TYR GLU ASN PHE ILE SER GLU PHE          
SEQRES   6 a  374  GLU HIS ARG VAL ASN PRO LEU SER LEU VAL GLU ILE ILE          
SEQRES   7 a  374  LEU HIS VAL VAL ARG GLN MET THR ASP PRO ASN VAL ALA          
SEQRES   8 a  374  LEU THR PHE LEU GLU LYS THR ARG GLU LYS VAL LYS SER          
SEQRES   9 a  374  SER ASP GLU ALA VAL ILE LEU CYS LYS THR ALA ILE GLY          
SEQRES  10 a  374  ALA LEU LYS LEU ASN ILE GLY ASP LEU GLN VAL THR LYS          
SEQRES  11 a  374  GLU THR ILE GLU ASP VAL GLU GLU MET LEU ASN ASN LEU          
SEQRES  12 a  374  PRO GLY VAL THR SER VAL HIS SER ARG PHE TYR ASP LEU          
SEQRES  13 a  374  SER SER LYS TYR TYR GLN THR ILE GLY ASN HIS ALA SER          
SEQRES  14 a  374  TYR TYR LYS ASP ALA LEU ARG PHE LEU GLY CYS VAL ASP          
SEQRES  15 a  374  ILE LYS ASP LEU PRO VAL SER GLU GLN GLN GLU ARG ALA          
SEQRES  16 a  374  PHE THR LEU GLY LEU ALA GLY LEU LEU GLY GLU GLY VAL          
SEQRES  17 a  374  PHE ASN PHE GLY GLU LEU LEU MET HIS PRO VAL LEU GLU          
SEQRES  18 a  374  SER LEU ARG ASN THR ASP ARG GLN TRP LEU ILE ASP THR          
SEQRES  19 a  374  LEU TYR ALA PHE ASN SER GLY ASN VAL GLU ARG PHE GLN          
SEQRES  20 a  374  THR LEU LYS THR ALA TRP GLY GLN GLN PRO ASP LEU ALA          
SEQRES  21 a  374  ALA ASN GLU ALA GLN LEU LEU ARG LYS ILE GLN LEU LEU          
SEQRES  22 a  374  CYS LEU MET GLU MET THR PHE THR ARG PRO ALA ASN HIS          
SEQRES  23 a  374  ARG GLN LEU THR PHE GLU GLU ILE ALA LYS SER ALA LYS          
SEQRES  24 a  374  ILE THR VAL ASN GLU VAL GLU LEU LEU VAL MET LYS ALA          
SEQRES  25 a  374  LEU SER VAL GLY LEU VAL LYS GLY SER ILE ASP GLU VAL          
SEQRES  26 a  374  ASP LYS ARG VAL HIS MET THR TRP VAL GLN PRO ARG VAL          
SEQRES  27 a  374  LEU ASP LEU GLN GLN ILE LYS GLY MET LYS ASP ARG LEU          
SEQRES  28 a  374  GLU PHE TRP CYS THR ASP VAL LYS SER MET GLU MET LEU          
SEQRES  29 a  374  VAL GLU HIS GLN ALA HIS ASP ILE LEU THR                      
SEQRES   1 b  191  MET VAL LEU GLU SER THR MET VAL CYS VAL ASP ASN SER          
SEQRES   2 b  191  GLU TYR MET ARG ASN GLY ASP PHE LEU PRO THR ARG LEU          
SEQRES   3 b  191  GLN ALA GLN GLN ASP ALA VAL ASN ILE VAL CYS HIS SER          
SEQRES   4 b  191  LYS THR ARG SER ASN PRO GLU ASN ASN VAL GLY LEU ILE          
SEQRES   5 b  191  THR LEU ALA ASN ASP CYS GLU VAL LEU THR THR LEU THR          
SEQRES   6 b  191  PRO ASP THR GLY ARG ILE LEU SER LYS LEU HIS THR VAL          
SEQRES   7 b  191  GLN PRO LYS GLY LYS ILE THR PHE CYS THR GLY ILE ARG          
SEQRES   8 b  191  VAL ALA HIS LEU ALA LEU LYS HIS ARG GLN GLY LYS ASN          
SEQRES   9 b  191  HIS LYS MET ARG ILE ILE ALA PHE VAL GLY SER PRO VAL          
SEQRES  10 b  191  GLU ASP ASN GLU LYS ASP LEU VAL LYS LEU ALA LYS ARG          
SEQRES  11 b  191  LEU LYS LYS GLU LYS VAL ASN VAL ASP ILE ILE ASN PHE          
SEQRES  12 b  191  GLY GLU GLU GLU VAL ASN THR GLU LYS LEU THR ALA PHE          
SEQRES  13 b  191  VAL ASN THR LEU ASN GLY LYS ASP GLY THR GLY SER HIS          
SEQRES  14 b  191  LEU VAL THR VAL PRO PRO GLY PRO SER LEU ALA ASP ALA          
SEQRES  15 b  191  LEU ILE SER SER PRO ILE LEU ALA GLY                          
SEQRES   1 c  287  ALA VAL ASP THR ALA GLU GLN VAL TYR ILE SER SER LEU          
SEQRES   2 c  287  ALA LEU LEU LYS MET LEU LYS HIS GLY ARG ALA GLY VAL          
SEQRES   3 c  287  PRO MET GLU VAL MET GLY LEU MET LEU GLY GLU PHE VAL          
SEQRES   4 c  287  ASP ASP TYR THR VAL ARG VAL ILE ASP VAL PHE ALA MET          
SEQRES   5 c  287  PRO GLN SER GLY THR GLY VAL SER VAL GLU ALA VAL ASP          
SEQRES   6 c  287  PRO VAL PHE GLN ALA LYS MET LEU ASP MET LEU LYS GLN          
SEQRES   7 c  287  THR GLY ARG PRO GLU MET VAL VAL GLY TRP TYR HIS SER          
SEQRES   8 c  287  HIS PRO GLY PHE GLY CYS TRP LEU SER GLY VAL ASP ILE          
SEQRES   9 c  287  ASN THR GLN GLN SER PHE GLU ALA LEU SER GLU ARG ALA          
SEQRES  10 c  287  VAL ALA VAL VAL VAL ASP PRO ILE GLN SER VAL LYS GLY          
SEQRES  11 c  287  LYS VAL VAL ILE ASP ALA PHE ARG LEU ILE ASN ALA ASN          
SEQRES  12 c  287  MET MET VAL LEU GLY HIS GLU PRO ARG GLN THR THR SER          
SEQRES  13 c  287  ASN LEU GLY HIS LEU ASN LYS PRO SER ILE GLN ALA LEU          
SEQRES  14 c  287  ILE HIS GLY LEU ASN ARG HIS TYR TYR SER ILE THR ILE          
SEQRES  15 c  287  ASN TYR ARG LYS ASN GLU LEU GLU GLN LYS MET LEU LEU          
SEQRES  16 c  287  ASN LEU HIS LYS LYS SER TRP MET GLU GLY LEU THR LEU          
SEQRES  17 c  287  GLN ASP TYR SER GLU HIS CYS LYS HIS ASN GLU SER VAL          
SEQRES  18 c  287  VAL LYS GLU MET LEU GLU LEU ALA LYS ASN TYR ASN LYS          
SEQRES  19 c  287  ALA VAL GLU GLU GLU ASP LYS MET THR PRO GLU GLN LEU          
SEQRES  20 c  287  ALA ILE LYS ASN VAL GLY LYS GLN ASP PRO LYS ARG HIS          
SEQRES  21 c  287  LEU GLU GLU HIS VAL ASP VAL LEU MET THR SER ASN ILE          
SEQRES  22 c  287  VAL GLN CYS LEU ALA ALA MET LEU ASP THR VAL VAL PHE          
SEQRES  23 c  287  LYS                                                          
SEQRES   1 d  257  MET TYR GLU GLN LEU LYS GLY GLU TRP ASN ARG LYS SER          
SEQRES   2 d  257  PRO ASN LEU SER LYS CYS GLY GLU GLU LEU GLY ARG LEU          
SEQRES   3 d  257  LYS LEU VAL LEU LEU GLU LEU ASN PHE LEU PRO THR THR          
SEQRES   4 d  257  GLY THR LYS LEU THR LYS GLN GLN LEU ILE LEU ALA ARG          
SEQRES   5 d  257  ASP ILE LEU GLU ILE GLY ALA GLN TRP SER ILE LEU ARG          
SEQRES   6 d  257  LYS ASP ILE PRO SER PHE GLU ARG TYR MET ALA GLN LEU          
SEQRES   7 d  257  LYS CYS TYR TYR PHE ASP TYR LYS GLU GLN LEU PRO GLU          
SEQRES   8 d  257  SER ALA TYR MET HIS GLN LEU LEU GLY LEU ASN LEU LEU          
SEQRES   9 d  257  PHE LEU LEU SER GLN ASN ARG VAL ALA GLU PHE HIS THR          
SEQRES  10 d  257  GLU LEU GLU ARG LEU PRO ALA LYS ASP ILE GLN THR ASN          
SEQRES  11 d  257  VAL TYR ILE LYS HIS PRO VAL SER LEU GLU GLN TYR LEU          
SEQRES  12 d  257  MET GLU GLY SER TYR ASN LYS VAL PHE LEU ALA LYS GLY          
SEQRES  13 d  257  ASN ILE PRO ALA GLU SER TYR THR PHE PHE ILE ASP ILE          
SEQRES  14 d  257  LEU LEU ASP THR ILE ARG ASP GLU ILE ALA GLY CYS ILE          
SEQRES  15 d  257  GLU LYS ALA TYR GLU LYS ILE LEU PHE THR GLU ALA THR          
SEQRES  16 d  257  ARG ILE LEU PHE PHE ASN THR PRO LYS LYS MET THR ASP          
SEQRES  17 d  257  TYR ALA LYS LYS ARG GLY TRP VAL LEU GLY PRO ASN ASN          
SEQRES  18 d  257  TYR TYR SER PHE ALA SER GLN GLN GLN LYS PRO GLU ASP          
SEQRES  19 d  257  THR THR ILE PRO SER THR GLU LEU ALA LYS GLN VAL ILE          
SEQRES  20 d  257  GLU TYR ALA ARG GLN LEU GLU MET ILE VAL                      
SEQRES   1 e   70  MET SER GLU LYS LYS GLN PRO VAL ASP LEU GLY LEU LEU          
SEQRES   2 e   70  GLU GLU ASP ASP GLU PHE GLU GLU PHE PRO ALA GLU ASP          
SEQRES   3 e   70  TRP ALA GLY LEU ASP GLU ASP GLU ASP ALA HIS VAL TRP          
SEQRES   4 e   70  GLU ASP ASN TRP ASP ASP ASP ASN VAL GLU ASP ASP PHE          
SEQRES   5 e   70  SER ASN GLN LEU ARG ALA GLU LEU GLU LYS HIS GLY TYR          
SEQRES   6 e   70  LYS MET GLU THR SER                                          
HET     ZN  c 400       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL  18   ZN    ZN 2+                                                        
HELIX    1 AA1 PRO A   74  ALA A   82  1                                   9    
HELIX    2 AA2 LYS A   84  SER A   89  1                                   6    
HELIX    3 AA3 ALA A  130  ILE A  134  5                                   5    
HELIX    4 AA4 LYS B   98  LEU B  102  5                                   5    
HELIX    5 AA5 ALA C   16  GLU C   68  1                                  53    
HELIX    6 AA6 TYR D   41  VAL D   56  1                                  16    
HELIX    7 AA7 VAL D   56  ARG D   81  1                                  26    
HELIX    8 AA8 ASP D  120  LYS D  125  5                                   6    
HELIX    9 AA9 TYR E   12  GLU E   28  1                                  17    
HELIX   10 AB1 ARG E   30  GLU E   35  1                                   6    
HELIX   11 AB2 GLU E   35  LEU E   50  1                                  16    
HELIX   12 AB3 ILE F   54  SER F   57  5                                   4    
HELIX   13 AB4 GLU F   58  SER F   77  1                                  20    
HELIX   14 AB5 SER F   77  LYS F   84  1                                   8    
HELIX   15 AB6 ALA U    6  ASP U   13  1                                   8    
HELIX   16 AB7 LEU U   19  VAL U   31  1                                  13    
HELIX   17 AB8 SER U   41  ASP U   51  1                                  11    
HELIX   18 AB9 SER U   56  GLY U   72  1                                  17    
HELIX   19 AC1 ALA U   73  LEU U   82  1                                  10    
HELIX   20 AC2 SER U   94  ASN U  115  1                                  22    
HELIX   21 AC3 ASP U  127  LEU U  142  1                                  16    
HELIX   22 AC4 ASP U  143  TYR U  147  5                                   5    
HELIX   23 AC5 LYS U  148  THR U  157  1                                  10    
HELIX   24 AC6 ASP U  172  MET U  185  1                                  14    
HELIX   25 AC7 PHE U  193  VAL U  202  1                                  10    
HELIX   26 AC8 ASP U  212  ILE U  221  1                                  10    
HELIX   27 AC9 ASP U  225  ALA U  228  5                                   4    
HELIX   28 AD1 VAL U  229  ASP U  240  1                                  12    
HELIX   29 AD2 ASN U  241  SER U  255  1                                  15    
HELIX   30 AD3 GLN U  258  VAL U  271  1                                  14    
HELIX   31 AD4 PRO U  318  LEU U  329  1                                  12    
HELIX   32 AD5 GLY U  331  ASN U  345  1                                  15    
HELIX   33 AD6 ASP U  349  VAL U  360  1                                  12    
HELIX   34 AD7 VAL U  364  HIS U  377  1                                  14    
HELIX   35 AD8 TRP U  399  HIS U  412  1                                  14    
HELIX   36 AD9 LYS U  417  THR U  425  1                                   9    
HELIX   37 AE1 ALA U  436  HIS U  450  1                                  15    
HELIX   38 AE2 ILE U  457  LYS U  466  1                                  10    
HELIX   39 AE3 ARG U  474  ALA U  485  1                                  12    
HELIX   40 AE4 ARG U  490  TYR U  502  1                                  13    
HELIX   41 AE5 ASP U  505  MET U  520  1                                  16    
HELIX   42 AE6 ASN U  525  GLN U  537  1                                  13    
HELIX   43 AE7 GLU U  542  VAL U  555  1                                  14    
HELIX   44 AE8 ALA U  563  ARG U  572  1                                  10    
HELIX   45 AE9 ASP U  575  CYS U  591  1                                  17    
HELIX   46 AF1 LYS U  597  ASP U  609  1                                  13    
HELIX   47 AF2 ASN U  611  ALA U  617  1                                   7    
HELIX   48 AF3 ALA U  618  LEU U  626  1                                   9    
HELIX   49 AF4 PHE U  627  THR U  629  5                                   3    
HELIX   50 AF5 GLU U  631  VAL U  637  1                                   7    
HELIX   51 AF6 VAL U  637  GLU U  642  1                                   6    
HELIX   52 AF7 ASN U  645  CYS U  660  1                                  16    
HELIX   53 AF8 ASN U  665  ASN U  670  1                                   6    
HELIX   54 AF9 LEU U  671  THR U  676  1                                   6    
HELIX   55 AG1 VAL U  680  LEU U  693  1                                  14    
HELIX   56 AG2 LYS U  705  SER U  714  1                                  10    
HELIX   57 AG3 ILE U  717  HIS U  721  5                                   5    
HELIX   58 AG4 ASP U  723  ASP U  738  1                                  16    
HELIX   59 AG5 ALA U  739  HIS U  742  5                                   4    
HELIX   60 AG6 HIS U  756  GLN U  768  1                                  13    
HELIX   61 AG7 TRP U  772  LEU U  781  5                                  10    
HELIX   62 AG8 LYS U  807  ALA U  812  5                                   6    
HELIX   63 AG9 MET U  885  LYS U  890  5                                   6    
HELIX   64 AH1 PRO V   19  GLN V   24  1                                   6    
HELIX   65 AH2 ALA V   31  ASP V   52  1                                  22    
HELIX   66 AH3 HIS V   62  GLU V   73  1                                  12    
HELIX   67 AH4 VAL V   86  GLU V   90  5                                   5    
HELIX   68 AH5 THR V  104  GLN V  118  1                                  15    
HELIX   69 AH6 LEU V  131  PHE V  134  5                                   4    
HELIX   70 AH7 LEU V  135  THR V  141  1                                   7    
HELIX   71 AH8 PHE V  147  GLU V  164  1                                  18    
HELIX   72 AH9 LEU V  170  LYS V  186  1                                  17    
HELIX   73 AI1 THR V  197  HIS V  214  1                                  18    
HELIX   74 AI2 HIS V  214  ASP V  222  1                                   9    
HELIX   75 AI3 VAL V  226  ARG V  236  1                                  11    
HELIX   76 AI4 ALA V  244  TYR V  261  1                                  18    
HELIX   77 AI5 ALA V  267  SER V  272  1                                   6    
HELIX   78 AI6 ASN V  283  LYS V  296  1                                  14    
HELIX   79 AI7 SER V  303  LYS V  315  1                                  13    
HELIX   80 AI8 PHE V  324  LEU V  337  1                                  14    
HELIX   81 AI9 LEU V  338  GLY V  340  5                                   3    
HELIX   82 AJ1 SER V  352  MET V  358  1                                   7    
HELIX   83 AJ2 TYR V  360  GLY V  370  1                                  11    
HELIX   84 AJ3 ASN V  371  PHE V  382  1                                  12    
HELIX   85 AJ4 TYR V  392  ARG V  399  1                                   8    
HELIX   86 AJ5 ASN V  401  LEU V  412  1                                  12    
HELIX   87 AJ6 ALA V  420  LEU V  426  1                                   7    
HELIX   88 AJ7 SER V  430  ARG V  443  1                                  14    
HELIX   89 AJ8 GLU V  471  ALA V  493  1                                  23    
HELIX   90 AJ9 ARG V  495  LYS V  503  1                                   9    
HELIX   91 AK1 ALA W    2  MET W   16  1                                  15    
HELIX   92 AK2 TYR W   20  GLU W   37  1                                  18    
HELIX   93 AK3 ILE W   44  SER W   49  1                                   6    
HELIX   94 AK4 LEU W   50  THR W   63  1                                  14    
HELIX   95 AK5 ALA W   69  GLU W   79  1                                  11    
HELIX   96 AK6 LEU W   82  ILE W   87  1                                   6    
HELIX   97 AK7 GLN W   96  TYR W  111  1                                  16    
HELIX   98 AK8 THR W  116  LYS W  135  1                                  20    
HELIX   99 AK9 ILE W  140  GLY W  157  1                                  18    
HELIX  100 AL1 ASP W  158  LYS W  160  5                                   3    
HELIX  101 AL2 GLU W  161  GLU W  172  1                                  12    
HELIX  102 AL3 LYS W  179  ILE W  186  1                                   8    
HELIX  103 AL4 LEU W  187  GLN W  189  5                                   3    
HELIX  104 AL5 LEU W  192  LYS W  197  1                                   6    
HELIX  105 AL6 ASP W  198  ILE W  205  1                                   8    
HELIX  106 AL7 LYS W  207  ASN W  210  1                                   4    
HELIX  107 AL8 LEU W  222  GLY W  238  1                                  17    
HELIX  108 AL9 TYR W  240  CYS W  244  5                                   5    
HELIX  109 AM1 ASP W  252  GLN W  257  1                                   6    
HELIX  110 AM2 LYS W  268  LEU W  276  1                                   9    
HELIX  111 AM3 ASN W  281  SER W  291  1                                  11    
HELIX  112 AM4 ASP W  293  GLU W  298  1                                   6    
HELIX  113 AM5 LYS W  301  LEU W  308  1                                   8    
HELIX  114 AM6 TRP W  317  LYS W  330  1                                  14    
HELIX  115 AM7 PRO W  336  PHE W  341  1                                   6    
HELIX  116 AM8 GLU W  345  ALA W  367  1                                  23    
HELIX  117 AM9 THR W  374  LEU W  382  1                                   9    
HELIX  118 AN1 SER W  385  VAL W  398  1                                  14    
HELIX  119 AN2 LEU W  424  ILE W  452  1                                  29    
HELIX  120 AN3 HIS W  453  GLN W  456  5                                   4    
HELIX  121 AN4 ASP X   39  THR X   60  1                                  22    
HELIX  122 AN5 ALA X   63  VAL X   73  1                                  11    
HELIX  123 AN6 PHE X   76  ILE X   80  5                                   5    
HELIX  124 AN7 SER X   81  ASP X   98  1                                  18    
HELIX  125 AN8 ALA X  102  GLU X  120  1                                  19    
HELIX  126 AN9 ARG X  122  LYS X  141  1                                  20    
HELIX  127 AO1 ARG X  142  GLU X  156  1                                  15    
HELIX  128 AO2 ASP X  162  LEU X  180  1                                  19    
HELIX  129 AO3 ASN X  182  ALA X  197  1                                  16    
HELIX  130 AO4 PRO X  203  GLU X  222  1                                  20    
HELIX  131 AO5 ASP X  224  TYR X  239  1                                  16    
HELIX  132 AO6 ASP X  243  LEU X  261  1                                  19    
HELIX  133 AO7 THR X  263  VAL X  271  1                                   9    
HELIX  134 AO8 GLY X  273  ARG X  278  1                                   6    
HELIX  135 AO9 GLY X  281  ASN X  296  1                                  16    
HELIX  136 AP1 LEU X  299  TYR X  309  1                                  11    
HELIX  137 AP2 ILE X  319  ILE X  339  1                                  21    
HELIX  138 AP3 GLN X  346  SER X  352  1                                   7    
HELIX  139 AP4 SER X  357  ASP X  371  1                                  15    
HELIX  140 AP5 VAL X  393  THR X  422  1                                  30    
HELIX  141 AP6 PRO Y   15  ALA Y   20  1                                   6    
HELIX  142 AP7 LEU Y   22  LEU Y   28  1                                   7    
HELIX  143 AP8 ASP Y   34  ALA Y   43  1                                  10    
HELIX  144 AP9 ALA Y   44  ARG Y   46  5                                   3    
HELIX  145 AQ1 ASN Y   49  ALA Y   56  1                                   8    
HELIX  146 AQ2 LEU Y   57  SER Y   60  5                                   4    
HELIX  147 AQ3 ILE Y   65  GLU Y   92  1                                  28    
HELIX  148 AQ4 GLU Y   97  GLY Y  115  1                                  19    
HELIX  149 AQ5 ASP Y  116  LYS Y  130  1                                  15    
HELIX  150 AQ6 ALA Y  133  MET Y  152  1                                  20    
HELIX  151 AQ7 ASN Y  154  ALA Y  164  1                                  11    
HELIX  152 AQ8 ASP Y  175  ILE Y  191  1                                  17    
HELIX  153 AQ9 GLU Y  199  THR Y  204  5                                   6    
HELIX  154 AR1 ASP Y  215  LEU Y  231  1                                  17    
HELIX  155 AR2 GLU Y  232  LYS Y  239  1                                   8    
HELIX  156 AR3 ALA Y  244  LEU Y  250  1                                   7    
HELIX  157 AR4 LEU Y  253  GLU Y  265  1                                  13    
HELIX  158 AR5 ARG Y  267  LYS Y  283  1                                  17    
HELIX  159 AR6 HIS Y  291  SER Y  310  1                                  20    
HELIX  160 AR7 LEU Y  316  GLY Y  324  1                                   9    
HELIX  161 AR8 GLY Y  326  ALA Y  340  1                                  15    
HELIX  162 AR9 ASN Y  363  GLU Y  368  1                                   6    
HELIX  163 AS1 THR Y  369  ILE Y  387  1                                  19    
HELIX  164 AS2 HIS Z   12  PHE Z   23  1                                  12    
HELIX  165 AS3 ASP Z   71  ASN Z   86  1                                  16    
HELIX  166 AS4 ASN Z  104  TYR Z  115  1                                  12    
HELIX  167 AS5 GLU Z  166  ARG Z  177  1                                  12    
HELIX  168 AS6 THR Z  186  THR Z  217  1                                  32    
HELIX  169 AS7 GLN Z  225  ASN Z  235  1                                  11    
HELIX  170 AS8 PHE Z  245  LYS Z  288  1                                  44    
HELIX  171 AS9 VAL a    4  GLY a    6  5                                   3    
HELIX  172 AT1 PHE a    7  ASN a   13  1                                   7    
HELIX  173 AT2 GLN a   18  LYS a   32  1                                  15    
HELIX  174 AT3 LEU a   33  ASP a   47  1                                  15    
HELIX  175 AT4 ASP a   54  PHE a   67  1                                  14    
HELIX  176 AT5 PRO a   73  THR a   88  1                                  16    
HELIX  177 AT6 ASP a   89  VAL a  104  1                                  16    
HELIX  178 AT7 ALA a  110  LEU a  123  1                                  14    
HELIX  179 AT8 LEU a  128  LEU a  142  1                                  15    
HELIX  180 AT9 THR a  149  THR a  165  1                                  17    
HELIX  181 AU1 HIS a  169  VAL a  183  1                                  15    
HELIX  182 AU2 PRO a  189  GLY a  207  1                                  19    
HELIX  183 AU3 PHE a  213  HIS a  219  1                                   7    
HELIX  184 AU4 HIS a  219  LEU a  225  1                                   7    
HELIX  185 AU5 GLN a  231  GLY a  243  1                                  13    
HELIX  186 AU6 PHE a  248  THR a  253  1                                   6    
HELIX  187 AU7 ASP a  260  PHE a  282  1                                  23    
HELIX  188 AU8 THR a  292  LYS a  301  1                                  10    
HELIX  189 AU9 GLU a  306  GLY a  318  1                                  13    
HELIX  190 AV1 ASP a  342  LEU a  375  1                                  34    
HELIX  191 AV2 SER b   13  ARG b   17  5                                   5    
HELIX  192 AV3 THR b   24  ASN b   44  1                                  21    
HELIX  193 AV4 THR b   68  LEU b   75  1                                   8    
HELIX  194 AV5 PHE b   86  LEU b   95  1                                  10    
HELIX  195 AV6 ALA b   96  ARG b  100  5                                   5    
HELIX  196 AV7 ASN b  120  LYS b  135  1                                  16    
HELIX  197 AV8 GLU b  151  ASN b  161  1                                  11    
HELIX  198 AV9 ALA b  180  SER b  185  1                                   6    
HELIX  199 AW1 SER c   34  ALA c   47  1                                  14    
HELIX  200 AW2 ASP c   88  GLN c  101  1                                  14    
HELIX  201 AW3 SER c  123  GLU c  134  1                                  12    
HELIX  202 AW4 ASN c  164  VAL c  169  5                                   6    
HELIX  203 AW5 ASN c  180  ASN c  185  1                                   6    
HELIX  204 AW6 ASN c  210  SER c  224  1                                  15    
HELIX  205 AW7 ASP c  233  VAL c  244  1                                  12    
HELIX  206 AW8 VAL c  244  LYS c  264  1                                  21    
HELIX  207 AW9 MET c  265  LEU c  270  1                                   6    
HELIX  208 AX1 LEU c  284  ASN c  295  1                                  12    
HELIX  209 AX2 ASN c  295  LYS c  310  1                                  16    
HELIX  210 AX3 LEU d   16  LEU d   30  1                                  15    
HELIX  211 AX4 THR d   44  ARG d   65  1                                  22    
HELIX  212 AX5 ASP d   67  PHE d   83  1                                  17    
HELIX  213 AX6 TYR d   94  GLN d  109  1                                  16    
HELIX  214 AX7 ARG d  111  LEU d  119  1                                   9    
HELIX  215 AX8 ASN d  130  GLY d  146  1                                  17    
HELIX  216 AX9 TYR d  148  ALA d  154  1                                   7    
HELIX  217 AY1 TYR d  163  GLU d  183  1                                  21    
HELIX  218 AY2 PHE d  191  LEU d  198  1                                   8    
HELIX  219 AY3 PRO d  203  ARG d  213  1                                  11    
HELIX  220 AY4 THR d  235  GLU d  254  1                                  20    
HELIX  221 AY5 LYS e    4  ASP e   17  1                                  14    
HELIX  222 AY6 GLU e   21  ASP e   35  1                                  15    
HELIX  223 AY7 GLU e   40  GLN e   55  1                                  16    
HELIX  224 AY8 GLU e   59  SER e   70  1                                  12    
SHEET    1 AA1 3 ILE A 101  ASP A 105  0                                        
SHEET    2 AA1 3 LYS A 110  ASN A 114 -1  O  ILE A 112   N  ASN A 103           
SHEET    3 AA1 3 LYS A 120  ASP A 124 -1  O  PHE A 121   N  ILE A 113           
SHEET    1 AA2 3 ILE B 122  SER B 124  0                                        
SHEET    2 AA2 3 SER B 108  GLU B 114 -1  N  THR B 111   O  SER B 124           
SHEET    3 AA2 3 SER B 149  LEU B 152 -1  O  LEU B 152   N  SER B 108           
SHEET    1 AA3 4 SER C  71  TYR C  72  0                                        
SHEET    2 AA3 4 ASN D 110  ARG D 114 -1  O  TYR D 112   N  SER C  71           
SHEET    3 AA3 4 THR D 100  GLY D 104 -1  N  VAL D 103   O  TYR D 111           
SHEET    4 AA3 4 GLN D  91  ASP D  97 -1  N  GLN D  91   O  GLY D 104           
SHEET    1 AA4 4 VAL C  87  LYS C  88  0                                        
SHEET    2 AA4 4 GLU C  75  VAL C  76 -1  N  GLU C  75   O  LYS C  88           
SHEET    3 AA4 4 CYS C 112  LEU C 116 -1  O  CYS C 112   N  VAL C  76           
SHEET    4 AA4 4 LEU C 123  LEU C 127 -1  O  HIS C 124   N  ALA C 115           
SHEET    1 AA5 6 LEU D  87  VAL D  88  0                                        
SHEET    2 AA5 6 ARG E  78  VAL E  80 -1  O  VAL E  80   N  LEU D  87           
SHEET    3 AA5 6 ILE E  70  LYS E  72 -1  N  VAL E  71   O  TYR E  79           
SHEET    4 AA5 6 GLN E  55  VAL E  60 -1  N  GLU E  59   O  LYS E  72           
SHEET    5 AA5 6 ARG E  97  ASP E 101 -1  O  LEU E 100   N  ILE E  56           
SHEET    6 AA5 6 ILE E 107  TYR E 110 -1  O  ARG E 109   N  ALA E  99           
SHEET    1 AA6 7 LEU D  87  VAL D  88  0                                        
SHEET    2 AA6 7 ARG E  78  VAL E  80 -1  O  VAL E  80   N  LEU D  87           
SHEET    3 AA6 7 ILE E  70  LYS E  72 -1  N  VAL E  71   O  TYR E  79           
SHEET    4 AA6 7 GLN E  55  VAL E  60 -1  N  GLU E  59   O  LYS E  72           
SHEET    5 AA6 7 TYR F 132  LEU F 134 -1  O  PHE F 133   N  GLN E  55           
SHEET    6 AA6 7 ALA F 122  THR F 126 -1  N  ALA F 122   O  LEU F 134           
SHEET    7 AA6 7 SER F  91  GLU F  95 -1  N  ILE F  94   O  VAL F 123           
SHEET    1 AA7 2 SER D 129  ALA D 131  0                                        
SHEET    2 AA7 2 ASP D 141  LEU D 143 -1  O  LEU D 143   N  SER D 129           
SHEET    1 AA8 2 VAL U 744  ILE U 746  0                                        
SHEET    2 AA8 2 TYR U 783  PRO U 785 -1  O  THR U 784   N  THR U 745           
SHEET    1 AA9 2 ILE U 789  GLY U 790  0                                        
SHEET    2 AA9 2 ILE U 911  ILE U 912  1  O  ILE U 912   N  ILE U 789           
SHEET    1 AB1 2 LYS U 803  SER U 804  0                                        
SHEET    2 AB1 2 LEU U 892  THR U 893 -1  O  THR U 893   N  LYS U 803           
SHEET    1 AB2 3 LEU X 378  ASP X 379  0                                        
SHEET    2 AB2 3 TYR Y 311  THR Y 315  1  O  ARG Y 312   N  LEU X 378           
SHEET    3 AB2 3 ILE Y 353  GLU Y 355 -1  O  VAL Y 354   N  LEU Y 314           
SHEET    1 AB3 8 LEU Z  48  VAL Z  50  0                                        
SHEET    2 AB3 8 LYS Z   8  VAL Z  11  1  N  VAL Z  10   O  VAL Z  50           
SHEET    3 AB3 8 SER Z 152  ILE Z 162  1  O  GLU Z 161   N  VAL Z  11           
SHEET    4 AB3 8 GLU Z 136  GLU Z 143 -1  N  ALA Z 137   O  VAL Z 158           
SHEET    5 AB3 8 LEU Z 121  ILE Z 123 -1  N  LEU Z 121   O  TYR Z 138           
SHEET    6 AB3 8 ARG Z  90  HIS Z  96  1  N  HIS Z  96   O  VAL Z 122           
SHEET    7 AB3 8 GLY Z  37  GLY Z  41 -1  N  GLY Z  41   O  ARG Z  90           
SHEET    8 AB3 8 SER Z  53  ALA Z  55 -1  O  PHE Z  54   N  VAL Z  38           
SHEET    1 AB4 2 ASP Z  59  GLU Z  60  0                                        
SHEET    2 AB4 2 TRP Z  68  PHE Z  69 -1  O  PHE Z  69   N  ASP Z  59           
SHEET    1 AB5 6 THR b  62  THR b  65  0                                        
SHEET    2 AB5 6 VAL b  49  THR b  53 -1  N  LEU b  51   O  THR b  62           
SHEET    3 AB5 6 GLU b   4  VAL b  10  1  N  THR b   6   O  GLY b  50           
SHEET    4 AB5 6 LYS b 106  VAL b 113  1  O  PHE b 112   N  CYS b   9           
SHEET    5 AB5 6 ASN b 137  ASN b 142  1  O  ILE b 141   N  VAL b 113           
SHEET    6 AB5 6 LEU b 170  THR b 172  1  O  VAL b 171   N  ILE b 140           
SHEET    1 AB6 8 TYR c 200  ILE c 203  0                                        
SHEET    2 AB6 8 ASP c 158  LEU c 162 -1  N  ARG c 161   O  TYR c 201           
SHEET    3 AB6 8 VAL c 141  VAL c 145 -1  N  ALA c 142   O  PHE c 160           
SHEET    4 AB6 8 MET c 107  SER c 114  1  N  HIS c 113   O  VAL c 143           
SHEET    5 AB6 8 MET c  54  GLU c  60 -1  N  MET c  57   O  VAL c 109           
SHEET    6 AB6 8 THR c  66  MET c  75 -1  O  ASP c  71   N  LEU c  58           
SHEET    7 AB6 8 GLN c  30  ILE c  33  1  N  TYR c  32   O  VAL c  67           
SHEET    8 AB6 8 ILE c 205  TYR c 207  1  O  ASN c 206   N  VAL c  31           
SHEET    1 AB7 2 ILE d 189  LEU d 190  0                                        
SHEET    2 AB7 2 ASN d 221  TYR d 222 -1  O  TYR d 222   N  ILE d 189           
SITE     1 AC1  1 PHE c 118                                                     
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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