GenomeNet

Database: PDB
Entry: 5IY9
LinkDB: 5IY9
Original site: 5IY9 
HEADER    TRANSCRIPTION, TRANSFERASE/DNA/RNA      24-MAR-16   5IY9              
TITLE     HUMAN HOLO-PIC IN THE INITIAL TRANSCRIBING STATE (NO IIS)             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: RNA POLYMERASE II SUBUNIT B1, DNA-DIRECTED RNA POLYMERASE II
COMPND   5 SUBUNIT A, DNA-DIRECTED RNA POLYMERASE III LARGEST SUBUNIT, RNA-     
COMPND   6 DIRECTED RNA POLYMERASE II SUBUNIT RPB1;                             
COMPND   7 EC: 2.7.7.6,2.7.7.48;                                                
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB2;               
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: DNA-DIRECTED RNA POLYMERASE II 140 KDA POLYPEPTIDE, DNA-    
COMPND  12 DIRECTED RNA POLYMERASE II SUBUNIT B, RNA POLYMERASE II SUBUNIT 2,   
COMPND  13 RNA POLYMERASE II SUBUNIT B2;                                        
COMPND  14 EC: 2.7.7.6;                                                         
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB3;               
COMPND  17 CHAIN: C;                                                            
COMPND  18 SYNONYM: RNA POLYMERASE II SUBUNIT B3, DNA-DIRECTED RNA POLYMERASE II
COMPND  19 33 KDA POLYPEPTIDE, RPB33, DNA-DIRECTED RNA POLYMERASE II SUBUNIT C, 
COMPND  20 RPB31;                                                               
COMPND  21 MOL_ID: 4;                                                           
COMPND  22 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB4;               
COMPND  23 CHAIN: D;                                                            
COMPND  24 SYNONYM: RNA POLYMERASE II SUBUNIT B4, DNA-DIRECTED RNA POLYMERASE II
COMPND  25 SUBUNIT D, RNA POLYMERASE II 16 KDA SUBUNIT, RPB16;                  
COMPND  26 MOL_ID: 5;                                                           
COMPND  27 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB5;               
COMPND  28 CHAIN: E;                                                            
COMPND  29 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC1, DNA-DIRECTED RNA 
COMPND  30 DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC1,          
COMPND  31 POLYMERASE II 23 KDA POLYPEPTIDE, DNA-DIRECTED RNA POLYMERASE II     
COMPND  32 SUBUNIT E, XAP4;                                                     
COMPND  33 MOL_ID: 6;                                                           
COMPND  34 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB6;               
COMPND  35 CHAIN: F;                                                            
COMPND  36 SYNONYM: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC2, 
COMPND  37 RNA POLYMERASES I,II,AND III SUBUNIT ABC2, DNA-DIRECTED RNA          
COMPND  38 POLYMERASE II SUBUNIT F, DNA-DIRECTED RNA POLYMERASES I,AND III 14.4 
COMPND  39 KDA POLYPEPTIDE, RPABC14.4, RPB14.4, RPC15;                          
COMPND  40 MOL_ID: 7;                                                           
COMPND  41 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB7;               
COMPND  42 CHAIN: G;                                                            
COMPND  43 SYNONYM: RNA POLYMERASE II SUBUNIT B7, DNA-DIRECTED RNA POLYMERASE II
COMPND  44 SUBUNIT G, RNA POLYMERASE II 19 KDA SUBUNIT, RPB19;                  
COMPND  45 MOL_ID: 8;                                                           
COMPND  46 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB8;               
COMPND  47 CHAIN: H;                                                            
COMPND  48 SYNONYM: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC3, 
COMPND  49 RNA POLYMERASES I,II,AND III SUBUNIT ABC3, DNA-DIRECTED RNA          
COMPND  50 POLYMERASE II SUBUNIT H, DNA-DIRECTED RNA POLYMERASES I, II, AND III 
COMPND  51 17.1 KDA POLYPEPTIDE, RPB17, HRPB8;                                  
COMPND  52 MOL_ID: 9;                                                           
COMPND  53 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB9;               
COMPND  54 CHAIN: I;                                                            
COMPND  55 SYNONYM: RNA POLYMERASE II SUBUNIT B9, DNA-DIRECTED RNA POLYMERASE II
COMPND  56 SUBUNIT I, RNA POLYMERASE II 14.5 KDA SUBUNIT, RPB14.5;              
COMPND  57 MOL_ID: 10;                                                          
COMPND  58 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB10;              
COMPND  59 CHAIN: J;                                                            
COMPND  60 SYNONYM: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC5, 
COMPND  61 RNA POLYMERASES I,II,AND III SUBUNIT ABC5, DNA-DIRECTED RNA          
COMPND  62 POLYMERASE III SUBUNIT L, RNA POLYMERASE II 7.6 KDA SUBUNIT, RPB7.6; 
COMPND  63 MOL_ID: 11;                                                          
COMPND  64 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB11-A;            
COMPND  65 CHAIN: K;                                                            
COMPND  66 SYNONYM: RPB11A, DNA-DIRECTED RNA POLYMERASE II SUBUNIT J-1, RNA     
COMPND  67 POLYMERASE II 13.3 KDA SUBUNIT;                                      
COMPND  68 MOL_ID: 12;                                                          
COMPND  69 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB12;              
COMPND  70 CHAIN: L;                                                            
COMPND  71 SYNONYM: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC4, 
COMPND  72 RNA POLYMERASES I,II,AND III SUBUNIT ABC4, ABC10-ALPHA, DNA-DIRECTED 
COMPND  73 RNA POLYMERASE II SUBUNIT K, RNA POLYMERASE II 7.0 KDA SUBUNIT,      
COMPND  74 RPB7.0, RPB10ALPHA;                                                  
COMPND  75 MOL_ID: 13;                                                          
COMPND  76 MOLECULE: TRANSCRIPTION INITIATION FACTOR IIB;                       
COMPND  77 CHAIN: M;                                                            
COMPND  78 SYNONYM: GENERAL TRANSCRIPTION FACTOR TFIIB, S300-II;                
COMPND  79 ENGINEERED: YES;                                                     
COMPND  80 MOL_ID: 14;                                                          
COMPND  81 MOLECULE: TRANSCRIPTION INITIATION FACTOR IIA SUBUNIT 1;             
COMPND  82 CHAIN: N;                                                            
COMPND  83 SYNONYM: GENERAL TRANSCRIPTION FACTOR IIA SUBUNIT 1, TFIIAL,         
COMPND  84 TRANSCRIPTION INITIATION FACTOR TFIIA 42 KDA SUBUNIT, TFIIA-42;      
COMPND  85 ENGINEERED: YES;                                                     
COMPND  86 MOL_ID: 15;                                                          
COMPND  87 MOLECULE: TRANSCRIPTION INITIATION FACTOR IIA SUBUNIT 2;             
COMPND  88 CHAIN: O;                                                            
COMPND  89 SYNONYM: GENERAL TRANSCRIPTION FACTOR IIA SUBUNIT 2, TFIIA P12       
COMPND  90 SUBUNIT, TFIIAS, TRANSCRIPTION INITIATION FACTOR IIA GAMMA CHAIN,    
COMPND  91 TFIIA-GAMMA;                                                         
COMPND  92 ENGINEERED: YES;                                                     
COMPND  93 MOL_ID: 16;                                                          
COMPND  94 MOLECULE: TATA-BOX-BINDING PROTEIN;                                  
COMPND  95 CHAIN: P;                                                            
COMPND  96 SYNONYM: TATA SEQUENCE-BINDING PROTEIN, TATA-BINDING FACTOR, TATA-BOX
COMPND  97 FACTOR, TRANSCRIPTION INITIATION FACTOR TFIID TBP SUBUNIT;           
COMPND  98 ENGINEERED: YES;                                                     
COMPND  99 MOL_ID: 17;                                                          
COMPND 100 MOLECULE: GENERAL TRANSCRIPTION FACTOR IIE SUBUNIT 1;                
COMPND 101 CHAIN: Q;                                                            
COMPND 102 SYNONYM: GENERAL TRANSCRIPTION FACTOR IIE 56 KDA SUBUNIT,            
COMPND 103 TRANSCRIPTION INITIATION FACTOR IIE SUBUNIT ALPHA, TFIIE-ALPHA;      
COMPND 104 ENGINEERED: YES;                                                     
COMPND 105 MOL_ID: 18;                                                          
COMPND 106 MOLECULE: TRANSCRIPTION INITIATION FACTOR IIE SUBUNIT BETA;          
COMPND 107 CHAIN: R;                                                            
COMPND 108 SYNONYM: TFIIE-BETA, GENERAL TRANSCRIPTION FACTOR IIE SUBUNIT 2;     
COMPND 109 ENGINEERED: YES;                                                     
COMPND 110 MOL_ID: 19;                                                          
COMPND 111 MOLECULE: GENERAL TRANSCRIPTION FACTOR IIF SUBUNIT 1;                
COMPND 112 CHAIN: S;                                                            
COMPND 113 SYNONYM: GENERAL TRANSCRIPTION FACTOR IIF 74 KDA SUBUNIT,            
COMPND 114 TRANSCRIPTION INITIATION FACTOR IIF SUBUNIT ALPHA, TFIIF-ALPHA,      
COMPND 115 TRANSCRIPTION INITIATION FACTOR RAP74;                               
COMPND 116 ENGINEERED: YES;                                                     
COMPND 117 MOL_ID: 20;                                                          
COMPND 118 MOLECULE: GENERAL TRANSCRIPTION FACTOR IIF SUBUNIT 2;                
COMPND 119 CHAIN: T;                                                            
COMPND 120 SYNONYM: ATP-DEPENDENT HELICASE GTF2F2, GENERAL TRANSCRIPTION FACTOR 
COMPND 121 IIF 30 KDA SUBUNIT, TRANSCRIPTION INITIATION FACTOR IIF SUBUNIT BETA,
COMPND 122 TFIIF-BETA, TRANSCRIPTION INITIATION FACTOR RAP30;                   
COMPND 123 EC: 3.6.4.12;                                                        
COMPND 124 ENGINEERED: YES;                                                     
COMPND 125 MOL_ID: 21;                                                          
COMPND 126 MOLECULE: TFIIH BASAL TRANSCRIPTION FACTOR COMPLEX HELICASE XPB      
COMPND 127 SUBUNIT;                                                             
COMPND 128 CHAIN: V;                                                            
COMPND 129 SYNONYM: BASIC TRANSCRIPTION FACTOR 2 89 KDA SUBUNIT, BTF2 P89, DNA  
COMPND 130 EXCISION REPAIR PROTEIN ERCC-3, DNA REPAIR PROTEIN COMPLEMENTING XP-B
COMPND 131 CELLS, TFIIH BASAL TRANSCRIPTION FACTOR COMPLEX 89 KDA SUBUNIT, TFIIH
COMPND 132 P89, XERODERMA PIGMENTOSUM GROUP B-COMPLEMENTING PROTEIN;            
COMPND 133 EC: 3.6.4.12;                                                        
COMPND 134 MOL_ID: 22;                                                          
COMPND 135 MOLECULE: TFIIH BASAL TRANSCRIPTION FACTOR COMPLEX HELICASE XPD      
COMPND 136 SUBUNIT;                                                             
COMPND 137 CHAIN: W;                                                            
COMPND 138 SYNONYM: BASIC TRANSCRIPTION FACTOR 2 80 KDA SUBUNIT,BTF2 P80, CXPD, 
COMPND 139 DNA EXCISION REPAIR PROTEIN ERCC-2, DNA REPAIR PROTEIN COMPLEMENTING 
COMPND 140 XP-D CELLS, TFIIH BASAL TRANSCRIPTION FACTOR COMPLEX 80 KDA SUBUNIT, 
COMPND 141 TFIIH P80, XERODERMA PIGMENTOSUM GROUP D-COMPLEMENTING PROTEIN;      
COMPND 142 EC: 3.6.4.12;                                                        
COMPND 143 MOL_ID: 23;                                                          
COMPND 144 MOLECULE: GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 2;                
COMPND 145 CHAIN: 0;                                                            
COMPND 146 SYNONYM: BASIC TRANSCRIPTION FACTOR 2 44 KDA SUBUNIT,BTF2 P44,       
COMPND 147 GENERAL TRANSCRIPTION FACTOR IIH POLYPEPTIDE 2, TFIIH BASAL          
COMPND 148 TRANSCRIPTION FACTOR COMPLEX P44 SUBUNIT;                            
COMPND 149 MOL_ID: 24;                                                          
COMPND 150 MOLECULE: GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 5;                
COMPND 151 CHAIN: 1;                                                            
COMPND 152 SYNONYM: GENERAL TRANSCRIPTION FACTOR IIH POLYPEPTIDE 5, TFB5        
COMPND 153 ORTHOLOG,TFIIH BASAL TRANSCRIPTION FACTOR COMPLEX TTD-A SUBUNIT;     
COMPND 154 MOL_ID: 25;                                                          
COMPND 155 MOLECULE: GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 4;                
COMPND 156 CHAIN: 2;                                                            
COMPND 157 SYNONYM: BASIC TRANSCRIPTION FACTOR 2 52 KDA SUBUNIT, BTF2 P52,      
COMPND 158 GENERAL TRANSCRIPTION FACTOR IIH POLYPEPTIDE 4, TFIIH BASAL          
COMPND 159 TRANSCRIPTION FACTOR COMPLEX P52 SUBUNIT;                            
COMPND 160 MOL_ID: 26;                                                          
COMPND 161 MOLECULE: GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 3;                
COMPND 162 CHAIN: 3;                                                            
COMPND 163 SYNONYM: BASIC TRANSCRIPTION FACTOR 2 34 KDA SUBUNIT, BTF2 P34,      
COMPND 164 GENERAL TRANSCRIPTION FACTOR IIH POLYPEPTIDE 3, TFIIH BASAL          
COMPND 165 TRANSCRIPTION FACTOR COMPLEX P34 SUBUNIT;                            
COMPND 166 MOL_ID: 27;                                                          
COMPND 167 MOLECULE: SCP-X;                                                     
COMPND 168 CHAIN: X;                                                            
COMPND 169 ENGINEERED: YES;                                                     
COMPND 170 MOL_ID: 28;                                                          
COMPND 171 MOLECULE: SCP-Y;                                                     
COMPND 172 CHAIN: Y;                                                            
COMPND 173 ENGINEERED: YES;                                                     
COMPND 174 MOL_ID: 29;                                                          
COMPND 175 MOLECULE: RNA;                                                       
COMPND 176 CHAIN: Z;                                                            
COMPND 177 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606;                                                
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 MOL_ID: 5;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 MOL_ID: 6;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 MOL_ID: 7;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  27 ORGANISM_COMMON: HUMAN;                                              
SOURCE  28 ORGANISM_TAXID: 9606;                                                
SOURCE  29 MOL_ID: 8;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  31 ORGANISM_COMMON: HUMAN;                                              
SOURCE  32 ORGANISM_TAXID: 9606;                                                
SOURCE  33 MOL_ID: 9;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  35 ORGANISM_COMMON: HUMAN;                                              
SOURCE  36 ORGANISM_TAXID: 9606;                                                
SOURCE  37 MOL_ID: 10;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  39 ORGANISM_COMMON: HUMAN;                                              
SOURCE  40 ORGANISM_TAXID: 9606;                                                
SOURCE  41 MOL_ID: 11;                                                          
SOURCE  42 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  43 ORGANISM_COMMON: HUMAN;                                              
SOURCE  44 ORGANISM_TAXID: 9606;                                                
SOURCE  45 MOL_ID: 12;                                                          
SOURCE  46 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  47 ORGANISM_COMMON: HUMAN;                                              
SOURCE  48 ORGANISM_TAXID: 9606;                                                
SOURCE  49 MOL_ID: 13;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  51 ORGANISM_COMMON: HUMAN;                                              
SOURCE  52 ORGANISM_TAXID: 9606;                                                
SOURCE  53 GENE: GTF2B, TF2B, TFIIB;                                            
SOURCE  54 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  55 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  56 MOL_ID: 14;                                                          
SOURCE  57 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  58 ORGANISM_COMMON: HUMAN;                                              
SOURCE  59 ORGANISM_TAXID: 9606;                                                
SOURCE  60 GENE: GTF2A1, TF2A1;                                                 
SOURCE  61 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  62 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  63 MOL_ID: 15;                                                          
SOURCE  64 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  65 ORGANISM_COMMON: HUMAN;                                              
SOURCE  66 ORGANISM_TAXID: 9606;                                                
SOURCE  67 GENE: GTF2A2, TF2A2;                                                 
SOURCE  68 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  69 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  70 MOL_ID: 16;                                                          
SOURCE  71 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  72 ORGANISM_COMMON: HUMAN;                                              
SOURCE  73 ORGANISM_TAXID: 9606;                                                
SOURCE  74 GENE: TBP, GTF2D1, TF2D, TFIID;                                      
SOURCE  75 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  76 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  77 MOL_ID: 17;                                                          
SOURCE  78 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  79 ORGANISM_COMMON: HUMAN;                                              
SOURCE  80 ORGANISM_TAXID: 9606;                                                
SOURCE  81 GENE: GTF2E1, TF2E1;                                                 
SOURCE  82 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  83 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  84 MOL_ID: 18;                                                          
SOURCE  85 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  86 ORGANISM_COMMON: HUMAN;                                              
SOURCE  87 ORGANISM_TAXID: 9606;                                                
SOURCE  88 GENE: GTF2E2, TF2E2;                                                 
SOURCE  89 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  90 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  91 MOL_ID: 19;                                                          
SOURCE  92 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  93 ORGANISM_COMMON: HUMAN;                                              
SOURCE  94 ORGANISM_TAXID: 9606;                                                
SOURCE  95 GENE: GTF2F1, RAP74;                                                 
SOURCE  96 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  97 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  98 MOL_ID: 20;                                                          
SOURCE  99 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 100 ORGANISM_COMMON: HUMAN;                                              
SOURCE 101 ORGANISM_TAXID: 9606;                                                
SOURCE 102 GENE: GTF2F2, RAP30;                                                 
SOURCE 103 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE 104 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE 105 MOL_ID: 21;                                                          
SOURCE 106 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 107 ORGANISM_COMMON: HUMAN;                                              
SOURCE 108 ORGANISM_TAXID: 9606;                                                
SOURCE 109 MOL_ID: 22;                                                          
SOURCE 110 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 111 ORGANISM_COMMON: HUMAN;                                              
SOURCE 112 ORGANISM_TAXID: 9606;                                                
SOURCE 113 MOL_ID: 23;                                                          
SOURCE 114 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 115 ORGANISM_COMMON: HUMAN;                                              
SOURCE 116 ORGANISM_TAXID: 9606;                                                
SOURCE 117 MOL_ID: 24;                                                          
SOURCE 118 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 119 ORGANISM_COMMON: HUMAN;                                              
SOURCE 120 ORGANISM_TAXID: 9606;                                                
SOURCE 121 MOL_ID: 25;                                                          
SOURCE 122 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 123 ORGANISM_COMMON: HUMAN;                                              
SOURCE 124 ORGANISM_TAXID: 9606;                                                
SOURCE 125 MOL_ID: 26;                                                          
SOURCE 126 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 127 ORGANISM_COMMON: HUMAN;                                              
SOURCE 128 ORGANISM_TAXID: 9606;                                                
SOURCE 129 MOL_ID: 27;                                                          
SOURCE 130 SYNTHETIC: YES;                                                      
SOURCE 131 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 132 ORGANISM_COMMON: HUMAN;                                              
SOURCE 133 ORGANISM_TAXID: 9606;                                                
SOURCE 134 MOL_ID: 28;                                                          
SOURCE 135 SYNTHETIC: YES;                                                      
SOURCE 136 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 137 ORGANISM_COMMON: HUMAN;                                              
SOURCE 138 ORGANISM_TAXID: 9606;                                                
SOURCE 139 MOL_ID: 29;                                                          
SOURCE 140 SYNTHETIC: YES;                                                      
SOURCE 141 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 142 ORGANISM_COMMON: HUMAN;                                              
SOURCE 143 ORGANISM_TAXID: 9606                                                 
KEYWDS    INITIATION, RNA POLYMERASE II, HUMAN, TRANSCRIPTION, TRANSFERASE-DNA- 
KEYWDS   2 RNA COMPLEX                                                          
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    Y.HE,C.YAN,J.FANG,C.INOUYE,R.TJIAN,I.IVANOV,E.NOGALES                 
REVDAT   5   20-NOV-19 5IY9    1       REMARK                                   
REVDAT   4   13-SEP-17 5IY9    1       JRNL                                     
REVDAT   3   22-JUN-16 5IY9    1       JRNL                                     
REVDAT   2   25-MAY-16 5IY9    1       JRNL                                     
REVDAT   1   18-MAY-16 5IY9    0                                                
JRNL        AUTH   Y.HE,C.YAN,J.FANG,C.INOUYE,R.TJIAN,I.IVANOV,E.NOGALES        
JRNL        TITL   NEAR-ATOMIC RESOLUTION VISUALIZATION OF HUMAN TRANSCRIPTION  
JRNL        TITL 2 PROMOTER OPENING.                                            
JRNL        REF    NATURE                        V. 533   359 2016              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   27193682                                                     
JRNL        DOI    10.1038/NATURE17970                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    6.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : RELION                                    
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : FLEXIBLE FIT                        
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)  : 6.300                          
REMARK   3   NUMBER OF PARTICLES               : 91642                          
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 5IY9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000219628.                                   
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                 : HUMAN HOLO-PIC IN THE INITIAL     
REMARK 245                                    TRANSCRIBING STATE (NO IIS);      
REMARK 245                                    RNA POLYMERASE II; GENERAL        
REMARK 245                                    TRANSCRIPTION FACTORS; SUPER      
REMARK 245                                    CORE PROMOTER                     
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.30                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : BLOT FOR 4 SECONDS BEFORE         
REMARK 245                                    PLUNGING INTO LIQUID ETHANE       
REMARK 245                                    (FEI VITROBOT MARK IV).           
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.90                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : 2000.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 4000.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 42.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 27500                          
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 29-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, N, O, P, Q, R, S,            
REMARK 350                    AND CHAINS: T, V, W, 0, 1, 2, 3, X, Y, Z          
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 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   CB   VAL R   223     CG2  THR R   224              0.90            
REMARK 500   CZ   PHE Q   180     CA   ASP R   213              1.15            
REMARK 500   CD2  LEU 3    57     OH   TYR 3    71              1.20            
REMARK 500   CD1  LEU 0    55     OE1  GLN 3   205              1.23            
REMARK 500   O    SER P   159     N    ILE P   161              1.27            
REMARK 500   C    VAL A   264     ND2  ASN A   272              1.34            
REMARK 500   C    HIS I    84     CD   PRO I    85              1.37            
REMARK 500   OH   TYR V   522     OD2  ASP 1    62              1.39            
REMARK 500   O    ALA H    85     OE1  GLN H    87              1.42            
REMARK 500   CD1  LEU A  1158     CD1  TYR A  1308              1.44            
REMARK 500   N    ARG 0    54     CG1  ILE 3   209              1.46            
REMARK 500   O    ALA H    85     N    GLN H    87              1.47            
REMARK 500   O    ALA W   297     CE2  PHE W   421              1.49            
REMARK 500   O    GLU I    61     N    ASP I    63              1.51            
REMARK 500   OH   TYR W   584     C    TYR W   614              1.51            
REMARK 500   O    GLU I   105     N    ALA I   107              1.51            
REMARK 500   CD1  PHE W   421     CG   PRO W   431              1.56            
REMARK 500   CD1  PHE Q    25     CD1  LEU R   219              1.57            
REMARK 500   OD1  ASN 2   117     ND2  ASN 3   108              1.57            
REMARK 500   CB   SER A  1290     OG   SER B   250              1.58            
REMARK 500   CD2  LEU A  1158     CE1  TYR A  1308              1.58            
REMARK 500   O    PHE V   615     N    LEU V   617              1.60            
REMARK 500   C    ARG E    52     CD   PRO E    53              1.63            
REMARK 500   OH   TYR 2    35     CB   PRO 3   221              1.63            
REMARK 500   OH   TYR W   584     O    TYR W   614              1.63            
REMARK 500   C    LYS 0    77     CD   PRO 0    78              1.65            
REMARK 500   O    GLU H   107     O    ALA H   108              1.66            
REMARK 500   O    ARG I   103     N    GLU I   105              1.66            
REMARK 500   N    VAL A   265     ND2  ASN A   272              1.67            
REMARK 500   CB   SER A  1290     CB   SER B   250              1.71            
REMARK 500   C    TYR 3    71     CD   PRO 3    72              1.71            
REMARK 500   O    VAL A   264     ND2  ASN A   272              1.71            
REMARK 500   C    SER A   622     CD   PRO A   623              1.71            
REMARK 500   CE2  PHE E    40     OD2  ASP E    46              1.72            
REMARK 500   OG   SER A  1290     OG   SER B   250              1.73            
REMARK 500   CG   LEU 0    55     OE1  GLN 3   205              1.73            
REMARK 500   O    PRO A  1098     NE2  GLN A  1101              1.74            
REMARK 500   N    ALA 3    58     OH   TYR 3    71              1.74            
REMARK 500   OE2  GLU 1    59     NH2  ARG 2   402              1.75            
REMARK 500   CA   VAL R   223     CG2  THR R   224              1.75            
REMARK 500   CD2  LEU 2   118     OD1  ASP 3    39              1.75            
REMARK 500   O    ASN A   152     CG1  ILE A   153              1.75            
REMARK 500   OD2  ASP M    94     O    GLY M    97              1.76            
REMARK 500   ND2  ASN 2   117     CB   ASN 3   108              1.76            
REMARK 500   CE2  PHE Q   180     OD1  ASP R   213              1.76            
REMARK 500   O    GLN A   273     O    ASP A   274              1.76            
REMARK 500   CA   ARG 0    54     CG1  ILE 3   209              1.77            
REMARK 500   NH2  ARG Q    23     O    SER R   207              1.78            
REMARK 500   CD1  LEU A  1158     CE1  TYR A  1308              1.79            
REMARK 500   OH   TYR Q   105     OE1  GLU R   234              1.80            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     140 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 500   CG    GLU A 500   CD      0.092                       
REMARK 500    CYS J  44   CB    CYS J  44   SG     -0.105                       
REMARK 500    ARG V 325   CZ    ARG V 325   NH1    -0.086                       
REMARK 500    ARG V 391   CZ    ARG V 391   NH2    -0.091                       
REMARK 500    ARG V 453   CZ    ARG V 453   NH2    -0.078                       
REMARK 500    HIS V 461   CG    HIS V 461   CD2     0.062                       
REMARK 500    ARG V 554   NE    ARG V 554   CZ      0.081                       
REMARK 500    PHE V 606   CG    PHE V 606   CD1     0.095                       
REMARK 500    ARG V 633   CZ    ARG V 633   NH1    -0.086                       
REMARK 500    TYR V 672   CE1   TYR V 672   CZ      0.101                       
REMARK 500    PHE W 104   CG    PHE W 104   CD1     0.108                       
REMARK 500    SER W 110   CA    SER W 110   CB      0.101                       
REMARK 500    TYR W 158   CE1   TYR W 158   CZ      0.104                       
REMARK 500    SER W 208   CB    SER W 208   OG     -0.082                       
REMARK 500    HIS W 474   NE2   HIS W 474   CD2    -0.072                       
REMARK 500    GLY W 521   N     GLY W 521   CA      0.097                       
REMARK 500    ARG W 683   CZ    ARG W 683   NH2    -0.082                       
REMARK 500    GLY 0 122   N     GLY 0 122   CA      0.097                       
REMARK 500     DA X  66   C5'    DA X  66   C4'     0.054                       
REMARK 500     DA X  69   C4'    DA X  69   C3'     0.086                       
REMARK 500     DA X  71   P      DA X  71   O5'    -0.099                       
REMARK 500     DA X  71   C3'    DA X  71   C2'     0.075                       
REMARK 500     DA X  71   O4'    DA X  71   C4'    -0.060                       
REMARK 500     DC X  72   C5'    DC X  72   C4'     0.051                       
REMARK 500     DG X  73   C5'    DG X  73   C4'     0.048                       
REMARK 500     DG X  75   C5'    DG X  75   C4'     0.070                       
REMARK 500     DG X  75   O4'    DG X  75   C4'    -0.063                       
REMARK 500     DC X  76   C5'    DC X  76   C4'     0.044                       
REMARK 500     DC X  77   C5'    DC X  77   C4'     0.083                       
REMARK 500     DT X  78   C5'    DT X  78   C4'     0.045                       
REMARK 500     DA X  79   C5'    DA X  79   C4'     0.092                       
REMARK 500     DC X  80   C4'    DC X  80   C3'     0.067                       
REMARK 500     DG X  81   C5'    DG X  81   C4'     0.077                       
REMARK 500     DA X  83   O3'    DA X  83   C3'    -0.037                       
REMARK 500     DT Y  11   C5'    DT Y  11   C4'     0.045                       
REMARK 500     DC Y  12   C5'    DC Y  12   C4'     0.053                       
REMARK 500     DC Y  12   O4'    DC Y  12   C4'    -0.065                       
REMARK 500     DG Y  14   C2'    DG Y  14   C1'     0.069                       
REMARK 500     DT Y  15   C4'    DT Y  15   C3'     0.080                       
REMARK 500     DG Y  17   P      DG Y  17   O5'    -0.070                       
REMARK 500     DG Y  17   O4'    DG Y  17   C1'    -0.074                       
REMARK 500     DG Y  18   C5'    DG Y  18   C4'     0.062                       
REMARK 500     DG Y  18   O4'    DG Y  18   C1'    -0.094                       
REMARK 500     DA Y  20   P      DA Y  20   O5'     0.080                       
REMARK 500     DT Y  25   P      DT Y  25   O5'    -0.062                       
REMARK 500     DT Y  25   O3'    DT Y  25   C3'    -0.047                       
REMARK 500     DT Y  25   O3'    DG Y  26   P       0.127                       
REMARK 500     DC Y  29   C5'    DC Y  29   C4'     0.049                       
REMARK 500     DG Y  31   O3'    DC Y  32   P      -0.108                       
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    PRO A 414   C   -  N   -  CA  ANGL. DEV. = -12.6 DEGREES          
REMARK 500    PHE A 458   N   -  CA  -  CB  ANGL. DEV. = -11.4 DEGREES          
REMARK 500    MET A 501   CA  -  CB  -  CG  ANGL. DEV. =  13.7 DEGREES          
REMARK 500    PRO A 623   C   -  N   -  CD  ANGL. DEV. = -53.3 DEGREES          
REMARK 500    CYS A 641   CA  -  CB  -  SG  ANGL. DEV. = -10.8 DEGREES          
REMARK 500    GLU B 112   OE1 -  CD  -  OE2 ANGL. DEV. = -10.1 DEGREES          
REMARK 500    LEU B 479   CB  -  CG  -  CD2 ANGL. DEV. = -11.9 DEGREES          
REMARK 500    ARG B 588   CB  -  CG  -  CD  ANGL. DEV. = -19.9 DEGREES          
REMARK 500    LEU B 880   N   -  CA  -  C   ANGL. DEV. =  17.5 DEGREES          
REMARK 500    SER B 882   N   -  CA  -  C   ANGL. DEV. = -20.0 DEGREES          
REMARK 500    PRO C   7   C   -  N   -  CD  ANGL. DEV. = -20.8 DEGREES          
REMARK 500    PRO E  53   C   -  N   -  CD  ANGL. DEV. = -57.6 DEGREES          
REMARK 500    LEU H 148   CA  -  CB  -  CG  ANGL. DEV. =  14.8 DEGREES          
REMARK 500    ARG I  15   N   -  CA  -  C   ANGL. DEV. = -18.7 DEGREES          
REMARK 500    PRO I  85   C   -  N   -  CD  ANGL. DEV. = -70.4 DEGREES          
REMARK 500    ARG I 103   N   -  CA  -  C   ANGL. DEV. = -22.6 DEGREES          
REMARK 500    PRO J  64   C   -  N   -  CD  ANGL. DEV. = -17.4 DEGREES          
REMARK 500    ASP M  43   N   -  CA  -  C   ANGL. DEV. = -17.9 DEGREES          
REMARK 500    ASP M  94   N   -  CA  -  C   ANGL. DEV. = -20.6 DEGREES          
REMARK 500    ARG R  88   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    GLY R 164   C   -  N   -  CA  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    PRO R 195   C   -  N   -  CD  ANGL. DEV. = -46.9 DEGREES          
REMARK 500    LYS R 206   N   -  CA  -  C   ANGL. DEV. =  17.1 DEGREES          
REMARK 500    LEU T 141   N   -  CA  -  C   ANGL. DEV. = -22.5 DEGREES          
REMARK 500    PHE V 249   CB  -  CG  -  CD2 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    GLU V 264   OE1 -  CD  -  OE2 ANGL. DEV. = -11.0 DEGREES          
REMARK 500    ARG V 283   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG V 283   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG V 298   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG V 332   NH1 -  CZ  -  NH2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    ARG V 332   NE  -  CZ  -  NH1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG V 334   CD  -  NE  -  CZ  ANGL. DEV. =  13.3 DEGREES          
REMARK 500    ARG V 334   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ALA V 344   N   -  CA  -  CB  ANGL. DEV. =  -8.7 DEGREES          
REMARK 500    ARG V 358   NH1 -  CZ  -  NH2 ANGL. DEV. =  -8.6 DEGREES          
REMARK 500    ARG V 358   NE  -  CZ  -  NH2 ANGL. DEV. =   8.9 DEGREES          
REMARK 500    VAL V 369   CA  -  CB  -  CG1 ANGL. DEV. =   9.5 DEGREES          
REMARK 500    ASP V 385   CB  -  CG  -  OD1 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ASP V 386   CB  -  CG  -  OD2 ANGL. DEV. =  -7.1 DEGREES          
REMARK 500    ARG V 391   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    SER V 404   CB  -  CA  -  C   ANGL. DEV. =  12.3 DEGREES          
REMARK 500    TYR V 410   CB  -  CG  -  CD1 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    TYR V 410   CZ  -  CE2 -  CD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    HIS V 415   CG  -  CD2 -  NE2 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500    ARG V 419   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    TRP V 421   CD1 -  NE1 -  CE2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    TRP V 421   NE1 -  CE2 -  CZ2 ANGL. DEV. =   8.3 DEGREES          
REMARK 500    TRP V 421   NE1 -  CE2 -  CD2 ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    TRP V 421   CE2 -  CD2 -  CE3 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    TRP V 421   CE2 -  CD2 -  CG  ANGL. DEV. =   6.1 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     279 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  12       34.92     33.65                                   
REMARK 500    ASP A  29      -74.82    -66.53                                   
REMARK 500    GLU A  38      -76.08     60.90                                   
REMARK 500    ILE A  41      -15.74    -48.09                                   
REMARK 500    THR A  47     -106.86   -128.23                                   
REMARK 500    GLU A  48      -37.06     94.49                                   
REMARK 500    LEU A  54     -170.62     57.86                                   
REMARK 500    ASP A  59       74.71     43.04                                   
REMARK 500    ARG A  61      -19.65   -167.86                                   
REMARK 500    GLN A  62     -148.49    -76.12                                   
REMARK 500    ILE A  65     -157.76   -128.21                                   
REMARK 500    GLU A  66       37.96     70.99                                   
REMARK 500    ARG A  70      119.33     62.17                                   
REMARK 500    CYS A  71       80.51   -166.50                                   
REMARK 500    GLN A  72     -122.41     62.17                                   
REMARK 500    ALA A  75     -128.23     49.62                                   
REMARK 500    ASN A  77     -159.15   -160.51                                   
REMARK 500    PHE A 113      -42.98     70.92                                   
REMARK 500    SER A 115       -6.11     64.16                                   
REMARK 500    LYS A 132       50.42    -45.50                                   
REMARK 500    SER A 133       -8.50     72.94                                   
REMARK 500    LYS A 134      -30.46     56.94                                   
REMARK 500    ILE A 153       64.86    139.19                                   
REMARK 500    GLU A 155     -143.28   -113.05                                   
REMARK 500    CYS A 184       90.87     46.87                                   
REMARK 500    HIS A 204      -58.46    115.76                                   
REMARK 500    VAL A 205     -156.14     -4.42                                   
REMARK 500    GLU A 207      -59.00    109.19                                   
REMARK 500    ASP A 208      -60.20     25.82                                   
REMARK 500    GLN A 210     -168.32     33.35                                   
REMARK 500    LYS A 212       15.85    111.51                                   
REMARK 500    PRO A 262       40.42    -96.95                                   
REMARK 500    VAL A 264      -14.18    -22.52                                   
REMARK 500    VAL A 265      -79.74     38.40                                   
REMARK 500    MET A 266       82.02     41.63                                   
REMARK 500    GLN A 267     -134.79     55.74                                   
REMARK 500    ALA A 270      -18.26    105.48                                   
REMARK 500    ARG A 271       87.66    -59.93                                   
REMARK 500    ASN A 272       43.06    179.06                                   
REMARK 500    ASP A 274      162.94     -8.61                                   
REMARK 500    ASN A 296     -151.72    -92.13                                   
REMARK 500    LEU A 354      -47.30   -156.80                                   
REMARK 500    PHE A 361       65.28     61.77                                   
REMARK 500    LYS A 434      108.44   -168.62                                   
REMARK 500    ASP A 452       58.89    -68.17                                   
REMARK 500    LYS A 466      -32.89    -31.69                                   
REMARK 500    TRP A 479     -174.04     70.29                                   
REMARK 500    ASP A 495     -153.36   -122.94                                   
REMARK 500    ASP A 497        4.10    -63.13                                   
REMARK 500    ILE A 525      -56.00   -122.73                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     589 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ILE H   99     GLU H  100                  -85.60                    
REMARK 500 ALA Q  125     SER Q  126                 -141.55                    
REMARK 500 PHE R  139     LYS R  140                  -33.84                    
REMARK 500 ASP R  213     GLU R  214                  144.63                    
REMARK 500 SER R  222     VAL R  223                  132.82                    
REMARK 500 VAL R  223     THR R  224                   95.50                    
REMARK 500 THR R  224     VAL R  225                  136.91                    
REMARK 500 MET R  228     ASP R  229                 -127.24                    
REMARK 500 ASN T  123     TYR T  124                  140.36                    
REMARK 500 THR V  417     LYS V  418                 -140.55                    
REMARK 500 MET V  427     GLU V  428                 -144.20                    
REMARK 500 ALA V  503     LYS V  504                  147.21                    
REMARK 500 THR W  409     TYR W  410                  121.16                    
REMARK 500 PHE 2  403     THR 2  404                  145.82                    
REMARK 500 GLY 2  406     VAL 2  407                 -143.87                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ASN A1291         0.07    SIDE CHAIN                              
REMARK 500    GLU O  86         0.07    SIDE CHAIN                              
REMARK 500    GLN P 242         0.07    SIDE CHAIN                              
REMARK 500    ARG Q 112         0.13    SIDE CHAIN                              
REMARK 500    ASP R 100         0.12    SIDE CHAIN                              
REMARK 500    GLU R 105         0.08    SIDE CHAIN                              
REMARK 500    GLN R 209         0.08    SIDE CHAIN                              
REMARK 500    ASP R 213         0.09    SIDE CHAIN                              
REMARK 500    ASP R 229         0.11    SIDE CHAIN                              
REMARK 500    GLU R 235         0.10    SIDE CHAIN                              
REMARK 500    PHE V 251         0.10    SIDE CHAIN                              
REMARK 500    TYR V 319         0.08    SIDE CHAIN                              
REMARK 500    PHE V 378         0.06    SIDE CHAIN                              
REMARK 500    TYR V 489         0.07    SIDE CHAIN                              
REMARK 500    TYR V 519         0.07    SIDE CHAIN                              
REMARK 500    ARG V 530         0.11    SIDE CHAIN                              
REMARK 500    TYR V 534         0.10    SIDE CHAIN                              
REMARK 500    ARG V 676         0.15    SIDE CHAIN                              
REMARK 500    PHE V 679         0.09    SIDE CHAIN                              
REMARK 500    PHE V 703         0.09    SIDE CHAIN                              
REMARK 500    TYR W  72         0.07    SIDE CHAIN                              
REMARK 500    PHE W 104         0.09    SIDE CHAIN                              
REMARK 500    TYR W 175         0.09    SIDE CHAIN                              
REMARK 500    TYR W 197         0.09    SIDE CHAIN                              
REMARK 500    TYR W 211         0.07    SIDE CHAIN                              
REMARK 500    ARG W 282         0.10    SIDE CHAIN                              
REMARK 500    ARG W 286         0.08    SIDE CHAIN                              
REMARK 500    ARG W 293         0.12    SIDE CHAIN                              
REMARK 500    TYR W 553         0.11    SIDE CHAIN                              
REMARK 500    TYR W 614         0.09    SIDE CHAIN                              
REMARK 500    ARG W 616         0.08    SIDE CHAIN                              
REMARK 500    ARG W 641         0.11    SIDE CHAIN                              
REMARK 500    ARG W 669         0.07    SIDE CHAIN                              
REMARK 500    TYR W 674         0.07    SIDE CHAIN                              
REMARK 500    TYR W 719         0.06    SIDE CHAIN                              
REMARK 500    ARG 0 165         0.13    SIDE CHAIN                              
REMARK 500    ASP 2 389         0.10    SIDE CHAIN                              
REMARK 500    ASP 2 399         0.10    SIDE CHAIN                              
REMARK 500    TYR 2 409         0.07    SIDE CHAIN                              
REMARK 500     DG X  65         0.07    SIDE CHAIN                              
REMARK 500     DA X  66         0.10    SIDE CHAIN                              
REMARK 500     DC X  72         0.08    SIDE CHAIN                              
REMARK 500     DT Y  23         0.08    SIDE CHAIN                              
REMARK 500     DC Y  24         0.08    SIDE CHAIN                              
REMARK 500     DG Y  26         0.06    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLN A 210         10.12                                           
REMARK 500    LEU R 109        -11.43                                           
REMARK 500    PHE R 139        -12.28                                           
REMARK 500    ASN R 204        -10.47                                           
REMARK 500    GLU R 215        -10.80                                           
REMARK 500    VAL R 223        -10.39                                           
REMARK 500    THR R 224        -11.19                                           
REMARK 500    VAL R 225         11.81                                           
REMARK 500    MET R 228        -12.92                                           
REMARK 500    ASP V 247         11.42                                           
REMARK 500    MET V 427         11.48                                           
REMARK 500    THR V 674        -12.24                                           
REMARK 500    VAL W 206         10.52                                           
REMARK 500    SER W 208        -11.42                                           
REMARK 500    PRO 0 143        -10.04                                           
REMARK 500    LYS 1  17        -10.29                                           
REMARK 500    ASP 2 389        -12.88                                           
REMARK 500    PHE 2 403        -11.43                                           
REMARK 500    ALA 2 425         10.35                                           
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 MG A 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN I 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN I 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN J 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN L 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN M 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN Q 501                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-8134   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-3307   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8135   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8132   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8133   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8136   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8137   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8138   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8131   RELATED DB: EMDB                              
REMARK 900 RELATED ID: 5IVW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5IY6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5IYA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5IY7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5IY8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5IYB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5IYC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5IYD   RELATED DB: PDB                                   
DBREF  5IY9 A    1  1970  UNP    P24928   RPB1_HUMAN       1   1970             
DBREF  5IY9 B    1  1174  UNP    P30876   RPB2_HUMAN       1   1174             
DBREF  5IY9 C    1   275  UNP    P19387   RPB3_HUMAN       1    275             
DBREF  5IY9 D    1   142  UNP    O15514   RPB4_HUMAN       1    142             
DBREF  5IY9 E    1   210  UNP    P19388   RPAB1_HUMAN      1    210             
DBREF  5IY9 F    1   127  UNP    P61218   RPAB2_HUMAN      1    127             
DBREF  5IY9 G    1   172  UNP    P62487   RPB7_HUMAN       1    172             
DBREF  5IY9 H    1   150  UNP    P52434   RPAB3_HUMAN      1    150             
DBREF  5IY9 I    1   125  UNP    P36954   RPB9_HUMAN       1    125             
DBREF  5IY9 J    1    67  UNP    P62875   RPAB5_HUMAN      1     67             
DBREF  5IY9 K    1   117  UNP    P52435   RPB11_HUMAN      1    117             
DBREF  5IY9 L    1    58  UNP    P53803   RPAB4_HUMAN      1     58             
DBREF  5IY9 M    1   316  UNP    Q00403   TF2B_HUMAN       1    316             
DBREF  5IY9 N    1   376  UNP    P52655   TF2AA_HUMAN      1    376             
DBREF  5IY9 O    1   109  UNP    P52657   T2AG_HUMAN       1    109             
DBREF  5IY9 P    1   339  UNP    P20226   TBP_HUMAN        1    339             
DBREF  5IY9 Q    1   439  UNP    P29083   T2EA_HUMAN       1    439             
DBREF  5IY9 R    1   291  UNP    P29084   T2EB_HUMAN       1    291             
DBREF  5IY9 S    1   517  UNP    P35269   T2FA_HUMAN       1    517             
DBREF  5IY9 T    1   249  UNP    P13984   T2FB_HUMAN       1    249             
DBREF  5IY9 V    1   782  UNP    P19447   ERCC3_HUMAN      1    782             
DBREF  5IY9 W    1   760  UNP    P18074   ERCC2_HUMAN      1    760             
DBREF  5IY9 0    1   395  UNP    Q13888   TF2H2_HUMAN      1    395             
DBREF  5IY9 1    1    71  UNP    Q6ZYL4   TF2H5_HUMAN      1     71             
DBREF  5IY9 2    1   462  UNP    Q92759   TF2H4_HUMAN      1    462             
DBREF  5IY9 3    1   308  UNP    Q13889   TF2H3_HUMAN      1    308             
DBREF  5IY9 X    1    83  PDB    5IY9     5IY9             1     83             
DBREF  5IY9 Y   11    93  PDB    5IY9     5IY9            11     93             
DBREF  5IY9 Z    1     6  PDB    5IY9     5IY9             1      6             
SEQRES   1 A 1970  MET HIS GLY GLY GLY PRO PRO SER GLY ASP SER ALA CYS          
SEQRES   2 A 1970  PRO LEU ARG THR ILE LYS ARG VAL GLN PHE GLY VAL LEU          
SEQRES   3 A 1970  SER PRO ASP GLU LEU LYS ARG MET SER VAL THR GLU GLY          
SEQRES   4 A 1970  GLY ILE LYS TYR PRO GLU THR THR GLU GLY GLY ARG PRO          
SEQRES   5 A 1970  LYS LEU GLY GLY LEU MET ASP PRO ARG GLN GLY VAL ILE          
SEQRES   6 A 1970  GLU ARG THR GLY ARG CYS GLN THR CYS ALA GLY ASN MET          
SEQRES   7 A 1970  THR GLU CYS PRO GLY HIS PHE GLY HIS ILE GLU LEU ALA          
SEQRES   8 A 1970  LYS PRO VAL PHE HIS VAL GLY PHE LEU VAL LYS THR MET          
SEQRES   9 A 1970  LYS VAL LEU ARG CYS VAL CYS PHE PHE CYS SER LYS LEU          
SEQRES  10 A 1970  LEU VAL ASP SER ASN ASN PRO LYS ILE LYS ASP ILE LEU          
SEQRES  11 A 1970  ALA LYS SER LYS GLY GLN PRO LYS LYS ARG LEU THR HIS          
SEQRES  12 A 1970  VAL TYR ASP LEU CYS LYS GLY LYS ASN ILE CYS GLU GLY          
SEQRES  13 A 1970  GLY GLU GLU MET ASP ASN LYS PHE GLY VAL GLU GLN PRO          
SEQRES  14 A 1970  GLU GLY ASP GLU ASP LEU THR LYS GLU LYS GLY HIS GLY          
SEQRES  15 A 1970  GLY CYS GLY ARG TYR GLN PRO ARG ILE ARG ARG SER GLY          
SEQRES  16 A 1970  LEU GLU LEU TYR ALA GLU TRP LYS HIS VAL ASN GLU ASP          
SEQRES  17 A 1970  SER GLN GLU LYS LYS ILE LEU LEU SER PRO GLU ARG VAL          
SEQRES  18 A 1970  HIS GLU ILE PHE LYS ARG ILE SER ASP GLU GLU CYS PHE          
SEQRES  19 A 1970  VAL LEU GLY MET GLU PRO ARG TYR ALA ARG PRO GLU TRP          
SEQRES  20 A 1970  MET ILE VAL THR VAL LEU PRO VAL PRO PRO LEU SER VAL          
SEQRES  21 A 1970  ARG PRO ALA VAL VAL MET GLN GLY SER ALA ARG ASN GLN          
SEQRES  22 A 1970  ASP ASP LEU THR HIS LYS LEU ALA ASP ILE VAL LYS ILE          
SEQRES  23 A 1970  ASN ASN GLN LEU ARG ARG ASN GLU GLN ASN GLY ALA ALA          
SEQRES  24 A 1970  ALA HIS VAL ILE ALA GLU ASP VAL LYS LEU LEU GLN PHE          
SEQRES  25 A 1970  HIS VAL ALA THR MET VAL ASP ASN GLU LEU PRO GLY LEU          
SEQRES  26 A 1970  PRO ARG ALA MET GLN LYS SER GLY ARG PRO LEU LYS SER          
SEQRES  27 A 1970  LEU LYS GLN ARG LEU LYS GLY LYS GLU GLY ARG VAL ARG          
SEQRES  28 A 1970  GLY ASN LEU MET GLY LYS ARG VAL ASP PHE SER ALA ARG          
SEQRES  29 A 1970  THR VAL ILE THR PRO ASP PRO ASN LEU SER ILE ASP GLN          
SEQRES  30 A 1970  VAL GLY VAL PRO ARG SER ILE ALA ALA ASN MET THR PHE          
SEQRES  31 A 1970  ALA GLU ILE VAL THR PRO PHE ASN ILE ASP ARG LEU GLN          
SEQRES  32 A 1970  GLU LEU VAL ARG ARG GLY ASN SER GLN TYR PRO GLY ALA          
SEQRES  33 A 1970  LYS TYR ILE ILE ARG ASP ASN GLY ASP ARG ILE ASP LEU          
SEQRES  34 A 1970  ARG PHE HIS PRO LYS PRO SER ASP LEU HIS LEU GLN THR          
SEQRES  35 A 1970  GLY TYR LYS VAL GLU ARG HIS MET CYS ASP GLY ASP ILE          
SEQRES  36 A 1970  VAL ILE PHE ASN ARG GLN PRO THR LEU HIS LYS MET SER          
SEQRES  37 A 1970  MET MET GLY HIS ARG VAL ARG ILE LEU PRO TRP SER THR          
SEQRES  38 A 1970  PHE ARG LEU ASN LEU SER VAL THR THR PRO TYR ASN ALA          
SEQRES  39 A 1970  ASP PHE ASP GLY ASP GLU MET ASN LEU HIS LEU PRO GLN          
SEQRES  40 A 1970  SER LEU GLU THR ARG ALA GLU ILE GLN GLU LEU ALA MET          
SEQRES  41 A 1970  VAL PRO ARG MET ILE VAL THR PRO GLN SER ASN ARG PRO          
SEQRES  42 A 1970  VAL MET GLY ILE VAL GLN ASP THR LEU THR ALA VAL ARG          
SEQRES  43 A 1970  LYS PHE THR LYS ARG ASP VAL PHE LEU GLU ARG GLY GLU          
SEQRES  44 A 1970  VAL MET ASN LEU LEU MET PHE LEU SER THR TRP ASP GLY          
SEQRES  45 A 1970  LYS VAL PRO GLN PRO ALA ILE LEU LYS PRO ARG PRO LEU          
SEQRES  46 A 1970  TRP THR GLY LYS GLN ILE PHE SER LEU ILE ILE PRO GLY          
SEQRES  47 A 1970  HIS ILE ASN CYS ILE ARG THR HIS SER THR HIS PRO ASP          
SEQRES  48 A 1970  ASP GLU ASP SER GLY PRO TYR LYS HIS ILE SER PRO GLY          
SEQRES  49 A 1970  ASP THR LYS VAL VAL VAL GLU ASN GLY GLU LEU ILE MET          
SEQRES  50 A 1970  GLY ILE LEU CYS LYS LYS SER LEU GLY THR SER ALA GLY          
SEQRES  51 A 1970  SER LEU VAL HIS ILE SER TYR LEU GLU MET GLY HIS ASP          
SEQRES  52 A 1970  ILE THR ARG LEU PHE TYR SER ASN ILE GLN THR VAL ILE          
SEQRES  53 A 1970  ASN ASN TRP LEU LEU ILE GLU GLY HIS THR ILE GLY ILE          
SEQRES  54 A 1970  GLY ASP SER ILE ALA ASP SER LYS THR TYR GLN ASP ILE          
SEQRES  55 A 1970  GLN ASN THR ILE LYS LYS ALA LYS GLN ASP VAL ILE GLU          
SEQRES  56 A 1970  VAL ILE GLU LYS ALA HIS ASN ASN GLU LEU GLU PRO THR          
SEQRES  57 A 1970  PRO GLY ASN THR LEU ARG GLN THR PHE GLU ASN GLN VAL          
SEQRES  58 A 1970  ASN ARG ILE LEU ASN ASP ALA ARG ASP LYS THR GLY SER          
SEQRES  59 A 1970  SER ALA GLN LYS SER LEU SER GLU TYR ASN ASN PHE LYS          
SEQRES  60 A 1970  SER MET VAL VAL SER GLY ALA LYS GLY SER LYS ILE ASN          
SEQRES  61 A 1970  ILE SER GLN VAL ILE ALA VAL VAL GLY GLN GLN ASN VAL          
SEQRES  62 A 1970  GLU GLY LYS ARG ILE PRO PHE GLY PHE LYS HIS ARG THR          
SEQRES  63 A 1970  LEU PRO HIS PHE ILE LYS ASP ASP TYR GLY PRO GLU SER          
SEQRES  64 A 1970  ARG GLY PHE VAL GLU ASN SER TYR LEU ALA GLY LEU THR          
SEQRES  65 A 1970  PRO THR GLU PHE PHE PHE HIS ALA MET GLY GLY ARG GLU          
SEQRES  66 A 1970  GLY LEU ILE ASP THR ALA VAL LYS THR ALA GLU THR GLY          
SEQRES  67 A 1970  TYR ILE GLN ARG ARG LEU ILE LYS SER MET GLU SER VAL          
SEQRES  68 A 1970  MET VAL LYS TYR ASP ALA THR VAL ARG ASN SER ILE ASN          
SEQRES  69 A 1970  GLN VAL VAL GLN LEU ARG TYR GLY GLU ASP GLY LEU ALA          
SEQRES  70 A 1970  GLY GLU SER VAL GLU PHE GLN ASN LEU ALA THR LEU LYS          
SEQRES  71 A 1970  PRO SER ASN LYS ALA PHE GLU LYS LYS PHE ARG PHE ASP          
SEQRES  72 A 1970  TYR THR ASN GLU ARG ALA LEU ARG ARG THR LEU GLN GLU          
SEQRES  73 A 1970  ASP LEU VAL LYS ASP VAL LEU SER ASN ALA HIS ILE GLN          
SEQRES  74 A 1970  ASN GLU LEU GLU ARG GLU PHE GLU ARG MET ARG GLU ASP          
SEQRES  75 A 1970  ARG GLU VAL LEU ARG VAL ILE PHE PRO THR GLY ASP SER          
SEQRES  76 A 1970  LYS VAL VAL LEU PRO CYS ASN LEU LEU ARG MET ILE TRP          
SEQRES  77 A 1970  ASN ALA GLN LYS ILE PHE HIS ILE ASN PRO ARG LEU PRO          
SEQRES  78 A 1970  SER ASP LEU HIS PRO ILE LYS VAL VAL GLU GLY VAL LYS          
SEQRES  79 A 1970  GLU LEU SER LYS LYS LEU VAL ILE VAL ASN GLY ASP ASP          
SEQRES  80 A 1970  PRO LEU SER ARG GLN ALA GLN GLU ASN ALA THR LEU LEU          
SEQRES  81 A 1970  PHE ASN ILE HIS LEU ARG SER THR LEU CYS SER ARG ARG          
SEQRES  82 A 1970  MET ALA GLU GLU PHE ARG LEU SER GLY GLU ALA PHE ASP          
SEQRES  83 A 1970  TRP LEU LEU GLY GLU ILE GLU SER LYS PHE ASN GLN ALA          
SEQRES  84 A 1970  ILE ALA HIS PRO GLY GLU MET VAL GLY ALA LEU ALA ALA          
SEQRES  85 A 1970  GLN SER LEU GLY GLU PRO ALA THR GLN MET THR LEU ASN          
SEQRES  86 A 1970  THR PHE HIS TYR ALA GLY VAL SER ALA LYS ASN VAL THR          
SEQRES  87 A 1970  LEU GLY VAL PRO ARG LEU LYS GLU LEU ILE ASN ILE SER          
SEQRES  88 A 1970  LYS LYS PRO LYS THR PRO SER LEU THR VAL PHE LEU LEU          
SEQRES  89 A 1970  GLY GLN SER ALA ARG ASP ALA GLU ARG ALA LYS ASP ILE          
SEQRES  90 A 1970  LEU CYS ARG LEU GLU HIS THR THR LEU ARG LYS VAL THR          
SEQRES  91 A 1970  ALA ASN THR ALA ILE TYR TYR ASP PRO ASN PRO GLN SER          
SEQRES  92 A 1970  THR VAL VAL ALA GLU ASP GLN GLU TRP VAL ASN VAL TYR          
SEQRES  93 A 1970  TYR GLU MET PRO ASP PHE ASP VAL ALA ARG ILE SER PRO          
SEQRES  94 A 1970  TRP LEU LEU ARG VAL GLU LEU ASP ARG LYS HIS MET THR          
SEQRES  95 A 1970  ASP ARG LYS LEU THR MET GLU GLN ILE ALA GLU LYS ILE          
SEQRES  96 A 1970  ASN ALA GLY PHE GLY ASP ASP LEU ASN CYS ILE PHE ASN          
SEQRES  97 A 1970  ASP ASP ASN ALA GLU LYS LEU VAL LEU ARG ILE ARG ILE          
SEQRES  98 A 1970  MET ASN SER ASP GLU ASN LYS MET GLN GLU GLU GLU GLU          
SEQRES  99 A 1970  VAL VAL ASP LYS MET ASP ASP ASP VAL PHE LEU ARG CYS          
SEQRES 100 A 1970  ILE GLU SER ASN MET LEU THR ASP MET THR LEU GLN GLY          
SEQRES 101 A 1970  ILE GLU GLN ILE SER LYS VAL TYR MET HIS LEU PRO GLN          
SEQRES 102 A 1970  THR ASP ASN LYS LYS LYS ILE ILE ILE THR GLU ASP GLY          
SEQRES 103 A 1970  GLU PHE LYS ALA LEU GLN GLU TRP ILE LEU GLU THR ASP          
SEQRES 104 A 1970  GLY VAL SER LEU MET ARG VAL LEU SER GLU LYS ASP VAL          
SEQRES 105 A 1970  ASP PRO VAL ARG THR THR SER ASN ASP ILE VAL GLU ILE          
SEQRES 106 A 1970  PHE THR VAL LEU GLY ILE GLU ALA VAL ARG LYS ALA LEU          
SEQRES 107 A 1970  GLU ARG GLU LEU TYR HIS VAL ILE SER PHE ASP GLY SER          
SEQRES 108 A 1970  TYR VAL ASN TYR ARG HIS LEU ALA LEU LEU CYS ASP THR          
SEQRES 109 A 1970  MET THR CYS ARG GLY HIS LEU MET ALA ILE THR ARG HIS          
SEQRES 110 A 1970  GLY VAL ASN ARG GLN ASP THR GLY PRO LEU MET LYS CYS          
SEQRES 111 A 1970  SER PHE GLU GLU THR VAL ASP VAL LEU MET GLU ALA ALA          
SEQRES 112 A 1970  ALA HIS GLY GLU SER ASP PRO MET LYS GLY VAL SER GLU          
SEQRES 113 A 1970  ASN ILE MET LEU GLY GLN LEU ALA PRO ALA GLY THR GLY          
SEQRES 114 A 1970  CYS PHE ASP LEU LEU LEU ASP ALA GLU LYS CYS LYS TYR          
SEQRES 115 A 1970  GLY MET GLU ILE PRO THR ASN ILE PRO GLY LEU GLY ALA          
SEQRES 116 A 1970  ALA GLY PRO THR GLY MET PHE PHE GLY SER ALA PRO SER          
SEQRES 117 A 1970  PRO MET GLY GLY ILE SER PRO ALA MET THR PRO TRP ASN          
SEQRES 118 A 1970  GLN GLY ALA THR PRO ALA TYR GLY ALA TRP SER PRO SER          
SEQRES 119 A 1970  VAL GLY SER GLY MET THR PRO GLY ALA ALA GLY PHE SER          
SEQRES 120 A 1970  PRO SER ALA ALA SER ASP ALA SER GLY PHE SER PRO GLY          
SEQRES 121 A 1970  TYR SER PRO ALA TRP SER PRO THR PRO GLY SER PRO GLY          
SEQRES 122 A 1970  SER PRO GLY PRO SER SER PRO TYR ILE PRO SER PRO GLY          
SEQRES 123 A 1970  GLY ALA MET SER PRO SER TYR SER PRO THR SER PRO ALA          
SEQRES 124 A 1970  TYR GLU PRO ARG SER PRO GLY GLY TYR THR PRO GLN SER          
SEQRES 125 A 1970  PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO THR          
SEQRES 126 A 1970  SER PRO SER TYR SER PRO THR SER PRO ASN TYR SER PRO          
SEQRES 127 A 1970  THR SER PRO SER TYR SER PRO THR SER PRO SER TYR SER          
SEQRES 128 A 1970  PRO THR SER PRO SER TYR SER PRO THR SER PRO SER TYR          
SEQRES 129 A 1970  SER PRO THR SER PRO SER TYR SER PRO THR SER PRO SER          
SEQRES 130 A 1970  TYR SER PRO THR SER PRO SER TYR SER PRO THR SER PRO          
SEQRES 131 A 1970  SER TYR SER PRO THR SER PRO SER TYR SER PRO THR SER          
SEQRES 132 A 1970  PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO THR          
SEQRES 133 A 1970  SER PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO          
SEQRES 134 A 1970  THR SER PRO SER TYR SER PRO THR SER PRO SER TYR SER          
SEQRES 135 A 1970  PRO THR SER PRO ASN TYR SER PRO THR SER PRO ASN TYR          
SEQRES 136 A 1970  THR PRO THR SER PRO SER TYR SER PRO THR SER PRO SER          
SEQRES 137 A 1970  TYR SER PRO THR SER PRO ASN TYR THR PRO THR SER PRO          
SEQRES 138 A 1970  ASN TYR SER PRO THR SER PRO SER TYR SER PRO THR SER          
SEQRES 139 A 1970  PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO SER          
SEQRES 140 A 1970  SER PRO ARG TYR THR PRO GLN SER PRO THR TYR THR PRO          
SEQRES 141 A 1970  SER SER PRO SER TYR SER PRO SER SER PRO SER TYR SER          
SEQRES 142 A 1970  PRO ALA SER PRO LYS TYR THR PRO THR SER PRO SER TYR          
SEQRES 143 A 1970  SER PRO SER SER PRO GLU TYR THR PRO THR SER PRO LYS          
SEQRES 144 A 1970  TYR SER PRO THR SER PRO LYS TYR SER PRO THR SER PRO          
SEQRES 145 A 1970  LYS TYR SER PRO THR SER PRO THR TYR SER PRO THR THR          
SEQRES 146 A 1970  PRO LYS TYR SER PRO THR SER PRO THR TYR SER PRO THR          
SEQRES 147 A 1970  SER PRO VAL TYR THR PRO THR SER PRO LYS TYR SER PRO          
SEQRES 148 A 1970  THR SER PRO THR TYR SER PRO THR SER PRO LYS TYR SER          
SEQRES 149 A 1970  PRO THR SER PRO THR TYR SER PRO THR SER PRO LYS GLY          
SEQRES 150 A 1970  SER THR TYR SER PRO THR SER PRO GLY TYR SER PRO THR          
SEQRES 151 A 1970  SER PRO THR TYR SER LEU THR SER PRO ALA ILE SER PRO          
SEQRES 152 A 1970  ASP ASP SER ASP GLU GLU ASN                                  
SEQRES   1 B 1174  MET TYR ASP ALA ASP GLU ASP MET GLN TYR ASP GLU ASP          
SEQRES   2 B 1174  ASP ASP GLU ILE THR PRO ASP LEU TRP GLN GLU ALA CYS          
SEQRES   3 B 1174  TRP ILE VAL ILE SER SER TYR PHE ASP GLU LYS GLY LEU          
SEQRES   4 B 1174  VAL ARG GLN GLN LEU ASP SER PHE ASP GLU PHE ILE GLN          
SEQRES   5 B 1174  MET SER VAL GLN ARG ILE VAL GLU ASP ALA PRO PRO ILE          
SEQRES   6 B 1174  ASP LEU GLN ALA GLU ALA GLN HIS ALA SER GLY GLU VAL          
SEQRES   7 B 1174  GLU GLU PRO PRO ARG TYR LEU LEU LYS PHE GLU GLN ILE          
SEQRES   8 B 1174  TYR LEU SER LYS PRO THR HIS TRP GLU ARG ASP GLY ALA          
SEQRES   9 B 1174  PRO SER PRO MET MET PRO ASN GLU ALA ARG LEU ARG ASN          
SEQRES  10 B 1174  LEU THR TYR SER ALA PRO LEU TYR VAL ASP ILE THR LYS          
SEQRES  11 B 1174  THR VAL ILE LYS GLU GLY GLU GLU GLN LEU GLN THR GLN          
SEQRES  12 B 1174  HIS GLN LYS THR PHE ILE GLY LYS ILE PRO ILE MET LEU          
SEQRES  13 B 1174  ARG SER THR TYR CYS LEU LEU ASN GLY LEU THR ASP ARG          
SEQRES  14 B 1174  ASP LEU CYS GLU LEU ASN GLU CYS PRO LEU ASP PRO GLY          
SEQRES  15 B 1174  GLY TYR PHE ILE ILE ASN GLY SER GLU LYS VAL LEU ILE          
SEQRES  16 B 1174  ALA GLN GLU LYS MET ALA THR ASN THR VAL TYR VAL PHE          
SEQRES  17 B 1174  ALA LYS LYS ASP SER LYS TYR ALA TYR THR GLY GLU CYS          
SEQRES  18 B 1174  ARG SER CYS LEU GLU ASN SER SER ARG PRO THR SER THR          
SEQRES  19 B 1174  ILE TRP VAL SER MET LEU ALA ARG GLY GLY GLN GLY ALA          
SEQRES  20 B 1174  LYS LYS SER ALA ILE GLY GLN ARG ILE VAL ALA THR LEU          
SEQRES  21 B 1174  PRO TYR ILE LYS GLN GLU VAL PRO ILE ILE ILE VAL PHE          
SEQRES  22 B 1174  ARG ALA LEU GLY PHE VAL SER ASP ARG ASP ILE LEU GLU          
SEQRES  23 B 1174  HIS ILE ILE TYR ASP PHE GLU ASP PRO GLU MET MET GLU          
SEQRES  24 B 1174  MET VAL LYS PRO SER LEU ASP GLU ALA PHE VAL ILE GLN          
SEQRES  25 B 1174  GLU GLN ASN VAL ALA LEU ASN PHE ILE GLY SER ARG GLY          
SEQRES  26 B 1174  ALA LYS PRO GLY VAL THR LYS GLU LYS ARG ILE LYS TYR          
SEQRES  27 B 1174  ALA LYS GLU VAL LEU GLN LYS GLU MET LEU PRO HIS VAL          
SEQRES  28 B 1174  GLY VAL SER ASP PHE CYS GLU THR LYS LYS ALA TYR PHE          
SEQRES  29 B 1174  LEU GLY TYR MET VAL HIS ARG LEU LEU LEU ALA ALA LEU          
SEQRES  30 B 1174  GLY ARG ARG GLU LEU ASP ASP ARG ASP HIS TYR GLY ASN          
SEQRES  31 B 1174  LYS ARG LEU ASP LEU ALA GLY PRO LEU LEU ALA PHE LEU          
SEQRES  32 B 1174  PHE ARG GLY MET PHE LYS ASN LEU LEU LYS GLU VAL ARG          
SEQRES  33 B 1174  ILE TYR ALA GLN LYS PHE ILE ASP ARG GLY LYS ASP PHE          
SEQRES  34 B 1174  ASN LEU GLU LEU ALA ILE LYS THR ARG ILE ILE SER ASP          
SEQRES  35 B 1174  GLY LEU LYS TYR SER LEU ALA THR GLY ASN TRP GLY ASP          
SEQRES  36 B 1174  GLN LYS LYS ALA HIS GLN ALA ARG ALA GLY VAL SER GLN          
SEQRES  37 B 1174  VAL LEU ASN ARG LEU THR PHE ALA SER THR LEU SER HIS          
SEQRES  38 B 1174  LEU ARG ARG LEU ASN SER PRO ILE GLY ARG ASP GLY LYS          
SEQRES  39 B 1174  LEU ALA LYS PRO ARG GLN LEU HIS ASN THR LEU TRP GLY          
SEQRES  40 B 1174  MET VAL CYS PRO ALA GLU THR PRO GLU GLY HIS ALA VAL          
SEQRES  41 B 1174  GLY LEU VAL LYS ASN LEU ALA LEU MET ALA TYR ILE SER          
SEQRES  42 B 1174  VAL GLY SER GLN PRO SER PRO ILE LEU GLU PHE LEU GLU          
SEQRES  43 B 1174  GLU TRP SER MET GLU ASN LEU GLU GLU ILE SER PRO ALA          
SEQRES  44 B 1174  ALA ILE ALA ASP ALA THR LYS ILE PHE VAL ASN GLY CYS          
SEQRES  45 B 1174  TRP VAL GLY ILE HIS LYS ASP PRO GLU GLN LEU MET ASN          
SEQRES  46 B 1174  THR LEU ARG LYS LEU ARG ARG GLN MET ASP ILE ILE VAL          
SEQRES  47 B 1174  SER GLU VAL SER MET ILE ARG ASP ILE ARG GLU ARG GLU          
SEQRES  48 B 1174  ILE ARG ILE TYR THR ASP ALA GLY ARG ILE CYS ARG PRO          
SEQRES  49 B 1174  LEU LEU ILE VAL GLU LYS GLN LYS LEU LEU LEU LYS LYS          
SEQRES  50 B 1174  ARG HIS ILE ASP GLN LEU LYS GLU ARG GLU TYR ASN ASN          
SEQRES  51 B 1174  TYR SER TRP GLN ASP LEU VAL ALA SER GLY VAL VAL GLU          
SEQRES  52 B 1174  TYR ILE ASP THR LEU GLU GLU GLU THR VAL MET LEU ALA          
SEQRES  53 B 1174  MET THR PRO ASP ASP LEU GLN GLU LYS GLU VAL ALA TYR          
SEQRES  54 B 1174  CYS SER THR TYR THR HIS CYS GLU ILE HIS PRO SER MET          
SEQRES  55 B 1174  ILE LEU GLY VAL CYS ALA SER ILE ILE PRO PHE PRO ASP          
SEQRES  56 B 1174  HIS ASN GLN SER PRO ARG ASN THR TYR GLN SER ALA MET          
SEQRES  57 B 1174  GLY LYS GLN ALA MET GLY VAL TYR ILE THR ASN PHE HIS          
SEQRES  58 B 1174  VAL ARG MET ASP THR LEU ALA HIS VAL LEU TYR TYR PRO          
SEQRES  59 B 1174  GLN LYS PRO LEU VAL THR THR ARG SER MET GLU TYR LEU          
SEQRES  60 B 1174  ARG PHE ARG GLU LEU PRO ALA GLY ILE ASN SER ILE VAL          
SEQRES  61 B 1174  ALA ILE ALA SER TYR THR GLY TYR ASN GLN GLU ASP SER          
SEQRES  62 B 1174  VAL ILE MET ASN ARG SER ALA VAL ASP ARG GLY PHE PHE          
SEQRES  63 B 1174  ARG SER VAL PHE TYR ARG SER TYR LYS GLU GLN GLU SER          
SEQRES  64 B 1174  LYS LYS GLY PHE ASP GLN GLU GLU VAL PHE GLU LYS PRO          
SEQRES  65 B 1174  THR ARG GLU THR CYS GLN GLY MET ARG HIS ALA ILE TYR          
SEQRES  66 B 1174  ASP LYS LEU ASP ASP ASP GLY LEU ILE ALA PRO GLY VAL          
SEQRES  67 B 1174  ARG VAL SER GLY ASP ASP VAL ILE ILE GLY LYS THR VAL          
SEQRES  68 B 1174  THR LEU PRO GLU ASN GLU ASP GLU LEU GLU SER THR ASN          
SEQRES  69 B 1174  ARG ARG TYR THR LYS ARG ASP CYS SER THR PHE LEU ARG          
SEQRES  70 B 1174  THR SER GLU THR GLY ILE VAL ASP GLN VAL MET VAL THR          
SEQRES  71 B 1174  LEU ASN GLN GLU GLY TYR LYS PHE CYS LYS ILE ARG VAL          
SEQRES  72 B 1174  ARG SER VAL ARG ILE PRO GLN ILE GLY ASP LYS PHE ALA          
SEQRES  73 B 1174  SER ARG HIS GLY GLN LYS GLY THR CYS GLY ILE GLN TYR          
SEQRES  74 B 1174  ARG GLN GLU ASP MET PRO PHE THR CYS GLU GLY ILE THR          
SEQRES  75 B 1174  PRO ASP ILE ILE ILE ASN PRO HIS ALA ILE PRO SER ARG          
SEQRES  76 B 1174  MET THR ILE GLY HIS LEU ILE GLU CYS LEU GLN GLY LYS          
SEQRES  77 B 1174  VAL SER ALA ASN LYS GLY GLU ILE GLY ASP ALA THR PRO          
SEQRES  78 B 1174  PHE ASN ASP ALA VAL ASN VAL GLN LYS ILE SER ASN LEU          
SEQRES  79 B 1174  LEU SER ASP TYR GLY TYR HIS LEU ARG GLY ASN GLU VAL          
SEQRES  80 B 1174  LEU TYR ASN GLY PHE THR GLY ARG LYS ILE THR SER GLN          
SEQRES  81 B 1174  ILE PHE ILE GLY PRO THR TYR TYR GLN ARG LEU LYS HIS          
SEQRES  82 B 1174  MET VAL ASP ASP LYS ILE HIS SER ARG ALA ARG GLY PRO          
SEQRES  83 B 1174  ILE GLN ILE LEU ASN ARG GLN PRO MET GLU GLY ARG SER          
SEQRES  84 B 1174  ARG ASP GLY GLY LEU ARG PHE GLY GLU MET GLU ARG ASP          
SEQRES  85 B 1174  CYS GLN ILE ALA HIS GLY ALA ALA GLN PHE LEU ARG GLU          
SEQRES  86 B 1174  ARG LEU PHE GLU ALA SER ASP PRO TYR GLN VAL HIS VAL          
SEQRES  87 B 1174  CYS ASN LEU CYS GLY ILE MET ALA ILE ALA ASN THR ARG          
SEQRES  88 B 1174  THR HIS THR TYR GLU CYS ARG GLY CYS ARG ASN LYS THR          
SEQRES  89 B 1174  GLN ILE SER LEU VAL ARG MET PRO TYR ALA CYS LYS LEU          
SEQRES  90 B 1174  LEU PHE GLN GLU LEU MET SER MET SER ILE ALA PRO ARG          
SEQRES  91 B 1174  MET MET SER VAL                                              
SEQRES   1 C  275  MET PRO TYR ALA ASN GLN PRO THR VAL ARG ILE THR GLU          
SEQRES   2 C  275  LEU THR ASP GLU ASN VAL LYS PHE ILE ILE GLU ASN THR          
SEQRES   3 C  275  ASP LEU ALA VAL ALA ASN SER ILE ARG ARG VAL PHE ILE          
SEQRES   4 C  275  ALA GLU VAL PRO ILE ILE ALA ILE ASP TRP VAL GLN ILE          
SEQRES   5 C  275  ASP ALA ASN SER SER VAL LEU HIS ASP GLU PHE ILE ALA          
SEQRES   6 C  275  HIS ARG LEU GLY LEU ILE PRO LEU ILE SER ASP ASP ILE          
SEQRES   7 C  275  VAL ASP LYS LEU GLN TYR SER ARG ASP CYS THR CYS GLU          
SEQRES   8 C  275  GLU PHE CYS PRO GLU CYS SER VAL GLU PHE THR LEU ASP          
SEQRES   9 C  275  VAL ARG CYS ASN GLU ASP GLN THR ARG HIS VAL THR SER          
SEQRES  10 C  275  ARG ASP LEU ILE SER ASN SER PRO ARG VAL ILE PRO VAL          
SEQRES  11 C  275  THR SER ARG ASN ARG ASP ASN ASP PRO ASN ASP TYR VAL          
SEQRES  12 C  275  GLU GLN ASP ASP ILE LEU ILE VAL LYS LEU ARG LYS GLY          
SEQRES  13 C  275  GLN GLU LEU ARG LEU ARG ALA TYR ALA LYS LYS GLY PHE          
SEQRES  14 C  275  GLY LYS GLU HIS ALA LYS TRP ASN PRO THR ALA GLY VAL          
SEQRES  15 C  275  ALA PHE GLU TYR ASP PRO ASP ASN ALA LEU ARG HIS THR          
SEQRES  16 C  275  VAL TYR PRO LYS PRO GLU GLU TRP PRO LYS SER GLU TYR          
SEQRES  17 C  275  SER GLU LEU ASP GLU ASP GLU SER GLN ALA PRO TYR ASP          
SEQRES  18 C  275  PRO ASN GLY LYS PRO GLU ARG PHE TYR TYR ASN VAL GLU          
SEQRES  19 C  275  SER CYS GLY SER LEU ARG PRO GLU THR ILE VAL LEU SER          
SEQRES  20 C  275  ALA LEU SER GLY LEU LYS LYS LYS LEU SER ASP LEU GLN          
SEQRES  21 C  275  THR GLN LEU SER HIS GLU ILE GLN SER ASP VAL LEU THR          
SEQRES  22 C  275  ILE ASN                                                      
SEQRES   1 D  142  MET ALA ALA GLY GLY SER ASP PRO ARG ALA GLY ASP VAL          
SEQRES   2 D  142  GLU GLU ASP ALA SER GLN LEU ILE PHE PRO LYS GLU PHE          
SEQRES   3 D  142  GLU THR ALA GLU THR LEU LEU ASN SER GLU VAL HIS MET          
SEQRES   4 D  142  LEU LEU GLU HIS ARG LYS GLN GLN ASN GLU SER ALA GLU          
SEQRES   5 D  142  ASP GLU GLN GLU LEU SER GLU VAL PHE MET LYS THR LEU          
SEQRES   6 D  142  ASN TYR THR ALA ARG PHE SER ARG PHE LYS ASN ARG GLU          
SEQRES   7 D  142  THR ILE ALA SER VAL ARG SER LEU LEU LEU GLN LYS LYS          
SEQRES   8 D  142  LEU HIS LYS PHE GLU LEU ALA CYS LEU ALA ASN LEU CYS          
SEQRES   9 D  142  PRO GLU THR ALA GLU GLU SER LYS ALA LEU ILE PRO SER          
SEQRES  10 D  142  LEU GLU GLY ARG PHE GLU ASP GLU GLU LEU GLN GLN ILE          
SEQRES  11 D  142  LEU ASP ASP ILE GLN THR LYS ARG SER PHE GLN TYR              
SEQRES   1 E  210  MET ASP ASP GLU GLU GLU THR TYR ARG LEU TRP LYS ILE          
SEQRES   2 E  210  ARG LYS THR ILE MET GLN LEU CYS HIS ASP ARG GLY TYR          
SEQRES   3 E  210  LEU VAL THR GLN ASP GLU LEU ASP GLN THR LEU GLU GLU          
SEQRES   4 E  210  PHE LYS ALA GLN SER GLY ASP LYS PRO SER GLU GLY ARG          
SEQRES   5 E  210  PRO ARG ARG THR ASP LEU THR VAL LEU VAL ALA HIS ASN          
SEQRES   6 E  210  ASP ASP PRO THR ASP GLN MET PHE VAL PHE PHE PRO GLU          
SEQRES   7 E  210  GLU PRO LYS VAL GLY ILE LYS THR ILE LYS VAL TYR CYS          
SEQRES   8 E  210  GLN ARG MET GLN GLU GLU ASN ILE THR ARG ALA LEU ILE          
SEQRES   9 E  210  VAL VAL GLN GLN GLY MET THR PRO SER ALA LYS GLN SER          
SEQRES  10 E  210  LEU VAL ASP MET ALA PRO LYS TYR ILE LEU GLU GLN PHE          
SEQRES  11 E  210  LEU GLN GLN GLU LEU LEU ILE ASN ILE THR GLU HIS GLU          
SEQRES  12 E  210  LEU VAL PRO GLU HIS VAL VAL MET THR LYS GLU GLU VAL          
SEQRES  13 E  210  THR GLU LEU LEU ALA ARG TYR LYS LEU ARG GLU ASN GLN          
SEQRES  14 E  210  LEU PRO ARG ILE GLN ALA GLY ASP PRO VAL ALA ARG TYR          
SEQRES  15 E  210  PHE GLY ILE LYS ARG GLY GLN VAL VAL LYS ILE ILE ARG          
SEQRES  16 E  210  PRO SER GLU THR ALA GLY ARG TYR ILE THR TYR ARG LEU          
SEQRES  17 E  210  VAL GLN                                                      
SEQRES   1 F  127  MET SER ASP ASN GLU ASP ASN PHE ASP GLY ASP ASP PHE          
SEQRES   2 F  127  ASP ASP VAL GLU GLU ASP GLU GLY LEU ASP ASP LEU GLU          
SEQRES   3 F  127  ASN ALA GLU GLU GLU GLY GLN GLU ASN VAL GLU ILE LEU          
SEQRES   4 F  127  PRO SER GLY GLU ARG PRO GLN ALA ASN GLN LYS ARG ILE          
SEQRES   5 F  127  THR THR PRO TYR MET THR LYS TYR GLU ARG ALA ARG VAL          
SEQRES   6 F  127  LEU GLY THR ARG ALA LEU GLN ILE ALA MET CYS ALA PRO          
SEQRES   7 F  127  VAL MET VAL GLU LEU GLU GLY GLU THR ASP PRO LEU LEU          
SEQRES   8 F  127  ILE ALA MET LYS GLU LEU LYS ALA ARG LYS ILE PRO ILE          
SEQRES   9 F  127  ILE ILE ARG ARG TYR LEU PRO ASP GLY SER TYR GLU ASP          
SEQRES  10 F  127  TRP GLY VAL ASP GLU LEU ILE ILE THR ASP                      
SEQRES   1 G  172  MET PHE TYR HIS ILE SER LEU GLU HIS GLU ILE LEU LEU          
SEQRES   2 G  172  HIS PRO ARG TYR PHE GLY PRO ASN LEU LEU ASN THR VAL          
SEQRES   3 G  172  LYS GLN LYS LEU PHE THR GLU VAL GLU GLY THR CYS THR          
SEQRES   4 G  172  GLY LYS TYR GLY PHE VAL ILE ALA VAL THR THR ILE ASP          
SEQRES   5 G  172  ASN ILE GLY ALA GLY VAL ILE GLN PRO GLY ARG GLY PHE          
SEQRES   6 G  172  VAL LEU TYR PRO VAL LYS TYR LYS ALA ILE VAL PHE ARG          
SEQRES   7 G  172  PRO PHE LYS GLY GLU VAL VAL ASP ALA VAL VAL THR GLN          
SEQRES   8 G  172  VAL ASN LYS VAL GLY LEU PHE THR GLU ILE GLY PRO MET          
SEQRES   9 G  172  SER CYS PHE ILE SER ARG HIS SER ILE PRO SER GLU MET          
SEQRES  10 G  172  GLU PHE ASP PRO ASN SER ASN PRO PRO CYS TYR LYS THR          
SEQRES  11 G  172  MET ASP GLU ASP ILE VAL ILE GLN GLN ASP ASP GLU ILE          
SEQRES  12 G  172  ARG LEU LYS ILE VAL GLY THR ARG VAL ASP LYS ASN ASP          
SEQRES  13 G  172  ILE PHE ALA ILE GLY SER LEU MET ASP ASP TYR LEU GLY          
SEQRES  14 G  172  LEU VAL SER                                                  
SEQRES   1 H  150  MET ALA GLY ILE LEU PHE GLU ASP ILE PHE ASP VAL LYS          
SEQRES   2 H  150  ASP ILE ASP PRO GLU GLY LYS LYS PHE ASP ARG VAL SER          
SEQRES   3 H  150  ARG LEU HIS CYS GLU SER GLU SER PHE LYS MET ASP LEU          
SEQRES   4 H  150  ILE LEU ASP VAL ASN ILE GLN ILE TYR PRO VAL ASP LEU          
SEQRES   5 H  150  GLY ASP LYS PHE ARG LEU VAL ILE ALA SER THR LEU TYR          
SEQRES   6 H  150  GLU ASP GLY THR LEU ASP ASP GLY GLU TYR ASN PRO THR          
SEQRES   7 H  150  ASP ASP ARG PRO SER ARG ALA ASP GLN PHE GLU TYR VAL          
SEQRES   8 H  150  MET TYR GLY LYS VAL TYR ARG ILE GLU GLY ASP GLU THR          
SEQRES   9 H  150  SER THR GLU ALA ALA THR ARG LEU SER ALA TYR VAL SER          
SEQRES  10 H  150  TYR GLY GLY LEU LEU MET ARG LEU GLN GLY ASP ALA ASN          
SEQRES  11 H  150  ASN LEU HIS GLY PHE GLU VAL ASP SER ARG VAL TYR LEU          
SEQRES  12 H  150  LEU MET LYS LYS LEU ALA PHE                                  
SEQRES   1 I  125  MET GLU PRO ASP GLY THR TYR GLU PRO GLY PHE VAL GLY          
SEQRES   2 I  125  ILE ARG PHE CYS GLN GLU CYS ASN ASN MET LEU TYR PRO          
SEQRES   3 I  125  LYS GLU ASP LYS GLU ASN ARG ILE LEU LEU TYR ALA CYS          
SEQRES   4 I  125  ARG ASN CYS ASP TYR GLN GLN GLU ALA ASP ASN SER CYS          
SEQRES   5 I  125  ILE TYR VAL ASN LYS ILE THR HIS GLU VAL ASP GLU LEU          
SEQRES   6 I  125  THR GLN ILE ILE ALA ASP VAL SER GLN ASP PRO THR LEU          
SEQRES   7 I  125  PRO ARG THR GLU ASP HIS PRO CYS GLN LYS CYS GLY HIS          
SEQRES   8 I  125  LYS GLU ALA VAL PHE PHE GLN SER HIS SER ALA ARG ALA          
SEQRES   9 I  125  GLU ASP ALA MET ARG LEU TYR TYR VAL CYS THR ALA PRO          
SEQRES  10 I  125  HIS CYS GLY HIS ARG TRP THR GLU                              
SEQRES   1 J   67  MET ILE ILE PRO VAL ARG CYS PHE THR CYS GLY LYS ILE          
SEQRES   2 J   67  VAL GLY ASN LYS TRP GLU ALA TYR LEU GLY LEU LEU GLN          
SEQRES   3 J   67  ALA GLU TYR THR GLU GLY ASP ALA LEU ASP ALA LEU GLY          
SEQRES   4 J   67  LEU LYS ARG TYR CYS CYS ARG ARG MET LEU LEU ALA HIS          
SEQRES   5 J   67  VAL ASP LEU ILE GLU LYS LEU LEU ASN TYR ALA PRO LEU          
SEQRES   6 J   67  GLU LYS                                                      
SEQRES   1 K  117  MET ASN ALA PRO PRO ALA PHE GLU SER PHE LEU LEU PHE          
SEQRES   2 K  117  GLU GLY GLU LYS LYS ILE THR ILE ASN LYS ASP THR LYS          
SEQRES   3 K  117  VAL PRO ASN ALA CYS LEU PHE THR ILE ASN LYS GLU ASP          
SEQRES   4 K  117  HIS THR LEU GLY ASN ILE ILE LYS SER GLN LEU LEU LYS          
SEQRES   5 K  117  ASP PRO GLN VAL LEU PHE ALA GLY TYR LYS VAL PRO HIS          
SEQRES   6 K  117  PRO LEU GLU HIS LYS ILE ILE ILE ARG VAL GLN THR THR          
SEQRES   7 K  117  PRO ASP TYR SER PRO GLN GLU ALA PHE THR ASN ALA ILE          
SEQRES   8 K  117  THR ASP LEU ILE SER GLU LEU SER LEU LEU GLU GLU ARG          
SEQRES   9 K  117  PHE ARG VAL ALA ILE LYS ASP LYS GLN GLU GLY ILE GLU          
SEQRES   1 L   58  MET ASP THR GLN LYS ASP VAL GLN PRO PRO LYS GLN GLN          
SEQRES   2 L   58  PRO MET ILE TYR ILE CYS GLY GLU CYS HIS THR GLU ASN          
SEQRES   3 L   58  GLU ILE LYS SER ARG ASP PRO ILE ARG CYS ARG GLU CYS          
SEQRES   4 L   58  GLY TYR ARG ILE MET TYR LYS LYS ARG THR LYS ARG LEU          
SEQRES   5 L   58  VAL VAL PHE ASP ALA ARG                                      
SEQRES   1 M  316  MET ALA SER THR SER ARG LEU ASP ALA LEU PRO ARG VAL          
SEQRES   2 M  316  THR CYS PRO ASN HIS PRO ASP ALA ILE LEU VAL GLU ASP          
SEQRES   3 M  316  TYR ARG ALA GLY ASP MET ILE CYS PRO GLU CYS GLY LEU          
SEQRES   4 M  316  VAL VAL GLY ASP ARG VAL ILE ASP VAL GLY SER GLU TRP          
SEQRES   5 M  316  ARG THR PHE SER ASN ASP LYS ALA THR LYS ASP PRO SER          
SEQRES   6 M  316  ARG VAL GLY ASP SER GLN ASN PRO LEU LEU SER ASP GLY          
SEQRES   7 M  316  ASP LEU SER THR MET ILE GLY LYS GLY THR GLY ALA ALA          
SEQRES   8 M  316  SER PHE ASP GLU PHE GLY ASN SER LYS TYR GLN ASN ARG          
SEQRES   9 M  316  ARG THR MET SER SER SER ASP ARG ALA MET MET ASN ALA          
SEQRES  10 M  316  PHE LYS GLU ILE THR THR MET ALA ASP ARG ILE ASN LEU          
SEQRES  11 M  316  PRO ARG ASN ILE VAL ASP ARG THR ASN ASN LEU PHE LYS          
SEQRES  12 M  316  GLN VAL TYR GLU GLN LYS SER LEU LYS GLY ARG ALA ASN          
SEQRES  13 M  316  ASP ALA ILE ALA SER ALA CYS LEU TYR ILE ALA CYS ARG          
SEQRES  14 M  316  GLN GLU GLY VAL PRO ARG THR PHE LYS GLU ILE CYS ALA          
SEQRES  15 M  316  VAL SER ARG ILE SER LYS LYS GLU ILE GLY ARG CYS PHE          
SEQRES  16 M  316  LYS LEU ILE LEU LYS ALA LEU GLU THR SER VAL ASP LEU          
SEQRES  17 M  316  ILE THR THR GLY ASP PHE MET SER ARG PHE CYS SER ASN          
SEQRES  18 M  316  LEU CYS LEU PRO LYS GLN VAL GLN MET ALA ALA THR HIS          
SEQRES  19 M  316  ILE ALA ARG LYS ALA VAL GLU LEU ASP LEU VAL PRO GLY          
SEQRES  20 M  316  ARG SER PRO ILE SER VAL ALA ALA ALA ALA ILE TYR MET          
SEQRES  21 M  316  ALA SER GLN ALA SER ALA GLU LYS ARG THR GLN LYS GLU          
SEQRES  22 M  316  ILE GLY ASP ILE ALA GLY VAL ALA ASP VAL THR ILE ARG          
SEQRES  23 M  316  GLN SER TYR ARG LEU ILE TYR PRO ARG ALA PRO ASP LEU          
SEQRES  24 M  316  PHE PRO THR ASP PHE LYS PHE ASP THR PRO VAL ASP LYS          
SEQRES  25 M  316  LEU PRO GLN LEU                                              
SEQRES   1 N  376  MET ALA ASN SER ALA ASN THR ASN THR VAL PRO LYS LEU          
SEQRES   2 N  376  TYR ARG SER VAL ILE GLU ASP VAL ILE ASN ASP VAL ARG          
SEQRES   3 N  376  ASP ILE PHE LEU ASP ASP GLY VAL ASP GLU GLN VAL LEU          
SEQRES   4 N  376  MET GLU LEU LYS THR LEU TRP GLU ASN LYS LEU MET GLN          
SEQRES   5 N  376  SER ARG ALA VAL ASP GLY PHE HIS SER GLU GLU GLN GLN          
SEQRES   6 N  376  LEU LEU LEU GLN VAL GLN GLN GLN HIS GLN PRO GLN GLN          
SEQRES   7 N  376  GLN GLN HIS HIS HIS HIS HIS HIS HIS GLN GLN ALA GLN          
SEQRES   8 N  376  PRO GLN GLN THR VAL PRO GLN GLN ALA GLN THR GLN GLN          
SEQRES   9 N  376  VAL LEU ILE PRO ALA SER GLN GLN ALA THR ALA PRO GLN          
SEQRES  10 N  376  VAL ILE VAL PRO ASP SER LYS LEU ILE GLN HIS MET ASN          
SEQRES  11 N  376  ALA SER ASN MET SER ALA ALA ALA THR ALA ALA THR LEU          
SEQRES  12 N  376  ALA LEU PRO ALA GLY VAL THR PRO VAL GLN GLN ILE LEU          
SEQRES  13 N  376  THR ASN SER GLY GLN LEU LEU GLN VAL VAL ARG ALA ALA          
SEQRES  14 N  376  ASN GLY ALA GLN TYR ILE PHE GLN PRO GLN GLN SER VAL          
SEQRES  15 N  376  VAL LEU GLN GLN GLN VAL ILE PRO GLN MET GLN PRO GLY          
SEQRES  16 N  376  GLY VAL GLN ALA PRO VAL ILE GLN GLN VAL LEU ALA PRO          
SEQRES  17 N  376  LEU PRO GLY GLY ILE SER PRO GLN THR GLY VAL ILE ILE          
SEQRES  18 N  376  GLN PRO GLN GLN ILE LEU PHE THR GLY ASN LYS THR GLN          
SEQRES  19 N  376  VAL ILE PRO THR THR VAL ALA ALA PRO THR PRO ALA GLN          
SEQRES  20 N  376  ALA GLN ILE THR ALA THR GLY GLN GLN GLN PRO GLN ALA          
SEQRES  21 N  376  GLN PRO ALA GLN THR GLN ALA PRO LEU VAL LEU GLN VAL          
SEQRES  22 N  376  ASP GLY THR GLY ASP THR SER SER GLU GLU ASP GLU ASP          
SEQRES  23 N  376  GLU GLU GLU ASP TYR ASP ASP ASP GLU GLU GLU ASP LYS          
SEQRES  24 N  376  GLU LYS ASP GLY ALA GLU ASP GLY GLN VAL GLU GLU GLU          
SEQRES  25 N  376  PRO LEU ASN SER GLU ASP ASP VAL SER ASP GLU GLU GLY          
SEQRES  26 N  376  GLN GLU LEU PHE ASP THR GLU ASN VAL VAL VAL CYS GLN          
SEQRES  27 N  376  TYR ASP LYS ILE HIS ARG SER LYS ASN LYS TRP LYS PHE          
SEQRES  28 N  376  HIS LEU LYS ASP GLY ILE MET ASN LEU ASN GLY ARG ASP          
SEQRES  29 N  376  TYR ILE PHE SER LYS ALA ILE GLY ASP ALA GLU TRP              
SEQRES   1 O  109  MET ALA TYR GLN LEU TYR ARG ASN THR THR LEU GLY ASN          
SEQRES   2 O  109  SER LEU GLN GLU SER LEU ASP GLU LEU ILE GLN SER GLN          
SEQRES   3 O  109  GLN ILE THR PRO GLN LEU ALA LEU GLN VAL LEU LEU GLN          
SEQRES   4 O  109  PHE ASP LYS ALA ILE ASN ALA ALA LEU ALA GLN ARG VAL          
SEQRES   5 O  109  ARG ASN ARG VAL ASN PHE ARG GLY SER LEU ASN THR TYR          
SEQRES   6 O  109  ARG PHE CYS ASP ASN VAL TRP THR PHE VAL LEU ASN ASP          
SEQRES   7 O  109  VAL GLU PHE ARG GLU VAL THR GLU LEU ILE LYS VAL ASP          
SEQRES   8 O  109  LYS VAL LYS ILE VAL ALA CYS ASP GLY LYS ASN THR GLY          
SEQRES   9 O  109  SER ASN THR THR GLU                                          
SEQRES   1 P  339  MET ASP GLN ASN ASN SER LEU PRO PRO TYR ALA GLN GLY          
SEQRES   2 P  339  LEU ALA SER PRO GLN GLY ALA MET THR PRO GLY ILE PRO          
SEQRES   3 P  339  ILE PHE SER PRO MET MET PRO TYR GLY THR GLY LEU THR          
SEQRES   4 P  339  PRO GLN PRO ILE GLN ASN THR ASN SER LEU SER ILE LEU          
SEQRES   5 P  339  GLU GLU GLN GLN ARG GLN GLN GLN GLN GLN GLN GLN GLN          
SEQRES   6 P  339  GLN GLN GLN GLN GLN GLN GLN GLN GLN GLN GLN GLN GLN          
SEQRES   7 P  339  GLN GLN GLN GLN GLN GLN GLN GLN GLN GLN GLN GLN GLN          
SEQRES   8 P  339  GLN GLN GLN GLN ALA VAL ALA ALA ALA ALA VAL GLN GLN          
SEQRES   9 P  339  SER THR SER GLN GLN ALA THR GLN GLY THR SER GLY GLN          
SEQRES  10 P  339  ALA PRO GLN LEU PHE HIS SER GLN THR LEU THR THR ALA          
SEQRES  11 P  339  PRO LEU PRO GLY THR THR PRO LEU TYR PRO SER PRO MET          
SEQRES  12 P  339  THR PRO MET THR PRO ILE THR PRO ALA THR PRO ALA SER          
SEQRES  13 P  339  GLU SER SER GLY ILE VAL PRO GLN LEU GLN ASN ILE VAL          
SEQRES  14 P  339  SER THR VAL ASN LEU GLY CYS LYS LEU ASP LEU LYS THR          
SEQRES  15 P  339  ILE ALA LEU ARG ALA ARG ASN ALA GLU TYR ASN PRO LYS          
SEQRES  16 P  339  ARG PHE ALA ALA VAL ILE MET ARG ILE ARG GLU PRO ARG          
SEQRES  17 P  339  THR THR ALA LEU ILE PHE SER SER GLY LYS MET VAL CYS          
SEQRES  18 P  339  THR GLY ALA LYS SER GLU GLU GLN SER ARG LEU ALA ALA          
SEQRES  19 P  339  ARG LYS TYR ALA ARG VAL VAL GLN LYS LEU GLY PHE PRO          
SEQRES  20 P  339  ALA LYS PHE LEU ASP PHE LYS ILE GLN ASN MET VAL GLY          
SEQRES  21 P  339  SER CYS ASP VAL LYS PHE PRO ILE ARG LEU GLU GLY LEU          
SEQRES  22 P  339  VAL LEU THR HIS GLN GLN PHE SER SER TYR GLU PRO GLU          
SEQRES  23 P  339  LEU PHE PRO GLY LEU ILE TYR ARG MET ILE LYS PRO ARG          
SEQRES  24 P  339  ILE VAL LEU LEU ILE PHE VAL SER GLY LYS VAL VAL LEU          
SEQRES  25 P  339  THR GLY ALA LYS VAL ARG ALA GLU ILE TYR GLU ALA PHE          
SEQRES  26 P  339  GLU ASN ILE TYR PRO ILE LEU LYS GLY PHE ARG LYS THR          
SEQRES  27 P  339  THR                                                          
SEQRES   1 Q  439  MET ALA ASP PRO ASP VAL LEU THR GLU VAL PRO ALA ALA          
SEQRES   2 Q  439  LEU LYS ARG LEU ALA LYS TYR VAL ILE ARG GLY PHE TYR          
SEQRES   3 Q  439  GLY ILE GLU HIS ALA LEU ALA LEU ASP ILE LEU ILE ARG          
SEQRES   4 Q  439  ASN SER CYS VAL LYS GLU GLU ASP MET LEU GLU LEU LEU          
SEQRES   5 Q  439  LYS PHE ASP ARG LYS GLN LEU ARG SER VAL LEU ASN ASN          
SEQRES   6 Q  439  LEU LYS GLY ASP LYS PHE ILE LYS CYS ARG MET ARG VAL          
SEQRES   7 Q  439  GLU THR ALA ALA ASP GLY LYS THR THR ARG HIS ASN TYR          
SEQRES   8 Q  439  TYR PHE ILE ASN TYR ARG THR LEU VAL ASN VAL VAL LYS          
SEQRES   9 Q  439  TYR LYS LEU ASP HIS MET ARG ARG ARG ILE GLU THR ASP          
SEQRES  10 Q  439  GLU ARG ASP SER THR ASN ARG ALA SER PHE LYS CYS PRO          
SEQRES  11 Q  439  VAL CYS SER SER THR PHE THR ASP LEU GLU ALA ASN GLN          
SEQRES  12 Q  439  LEU PHE ASP PRO MET THR GLY THR PHE ARG CYS THR PHE          
SEQRES  13 Q  439  CYS HIS THR GLU VAL GLU GLU ASP GLU SER ALA MET PRO          
SEQRES  14 Q  439  LYS LYS ASP ALA ARG THR LEU LEU ALA ARG PHE ASN GLU          
SEQRES  15 Q  439  GLN ILE GLU PRO ILE TYR ALA LEU LEU ARG GLU THR GLU          
SEQRES  16 Q  439  ASP VAL ASN LEU ALA TYR GLU ILE LEU GLU PRO GLU PRO          
SEQRES  17 Q  439  THR GLU ILE PRO ALA LEU LYS GLN SER LYS ASP HIS ALA          
SEQRES  18 Q  439  ALA THR THR ALA GLY ALA ALA SER LEU ALA GLY GLY HIS          
SEQRES  19 Q  439  HIS ARG GLU ALA TRP ALA THR LYS GLY PRO SER TYR GLU          
SEQRES  20 Q  439  ASP LEU TYR THR GLN ASN VAL VAL ILE ASN MET ASP ASP          
SEQRES  21 Q  439  GLN GLU ASP LEU HIS ARG ALA SER LEU GLU GLY LYS SER          
SEQRES  22 Q  439  ALA LYS GLU ARG PRO ILE TRP LEU ARG GLU SER THR VAL          
SEQRES  23 Q  439  GLN GLY ALA TYR GLY SER GLU ASP MET LYS GLU GLY GLY          
SEQRES  24 Q  439  ILE ASP MET ASP ALA PHE GLN GLU ARG GLU GLU GLY HIS          
SEQRES  25 Q  439  ALA GLY PRO ASP ASP ASN GLU GLU VAL MET ARG ALA LEU          
SEQRES  26 Q  439  LEU ILE HIS GLU LYS LYS THR SER SER ALA MET ALA GLY          
SEQRES  27 Q  439  SER VAL GLY ALA ALA ALA PRO VAL THR ALA ALA ASN GLY          
SEQRES  28 Q  439  SER ASP SER GLU SER GLU THR SER GLU SER ASP ASP ASP          
SEQRES  29 Q  439  SER PRO PRO ARG PRO ALA ALA VAL ALA VAL HIS LYS ARG          
SEQRES  30 Q  439  GLU GLU ASP GLU GLU GLU ASP ASP GLU PHE GLU GLU VAL          
SEQRES  31 Q  439  ALA ASP ASP PRO ILE VAL MET VAL ALA GLY ARG PRO PHE          
SEQRES  32 Q  439  SER TYR SER GLU VAL SER GLN ARG PRO GLU LEU VAL ALA          
SEQRES  33 Q  439  GLN MET THR PRO GLU GLU LYS GLU ALA TYR ILE ALA MET          
SEQRES  34 Q  439  GLY GLN ARG MET PHE GLU ASP LEU PHE GLU                      
SEQRES   1 R  291  MET ASP PRO SER LEU LEU ARG GLU ARG GLU LEU PHE LYS          
SEQRES   2 R  291  LYS ARG ALA LEU SER THR PRO VAL VAL GLU LYS ARG SER          
SEQRES   3 R  291  ALA SER SER GLU SER SER SER SER SER SER LYS LYS LYS          
SEQRES   4 R  291  LYS THR LYS VAL GLU HIS GLY GLY SER SER GLY SER LYS          
SEQRES   5 R  291  GLN ASN SER ASP HIS SER ASN GLY SER PHE ASN LEU LYS          
SEQRES   6 R  291  ALA LEU SER GLY SER SER GLY TYR LYS PHE GLY VAL LEU          
SEQRES   7 R  291  ALA LYS ILE VAL ASN TYR MET LYS THR ARG HIS GLN ARG          
SEQRES   8 R  291  GLY ASP THR HIS PRO LEU THR LEU ASP GLU ILE LEU ASP          
SEQRES   9 R  291  GLU THR GLN HIS LEU ASP ILE GLY LEU LYS GLN LYS GLN          
SEQRES  10 R  291  TRP LEU MET THR GLU ALA LEU VAL ASN ASN PRO LYS ILE          
SEQRES  11 R  291  GLU VAL ILE ASP GLY LYS TYR ALA PHE LYS PRO LYS TYR          
SEQRES  12 R  291  ASN VAL ARG ASP LYS LYS ALA LEU LEU ARG LEU LEU ASP          
SEQRES  13 R  291  GLN HIS ASP GLN ARG GLY LEU GLY GLY ILE LEU LEU GLU          
SEQRES  14 R  291  ASP ILE GLU GLU ALA LEU PRO ASN SER GLN LYS ALA VAL          
SEQRES  15 R  291  LYS ALA LEU GLY ASP GLN ILE LEU PHE VAL ASN ARG PRO          
SEQRES  16 R  291  ASP LYS LYS LYS ILE LEU PHE PHE ASN ASP LYS SER CYS          
SEQRES  17 R  291  GLN PHE SER VAL ASP GLU GLU PHE GLN LYS LEU TRP ARG          
SEQRES  18 R  291  SER VAL THR VAL ASP SER MET ASP GLU GLU LYS ILE GLU          
SEQRES  19 R  291  GLU TYR LEU LYS ARG GLN GLY ILE SER SER MET GLN GLU          
SEQRES  20 R  291  SER GLY PRO LYS LYS VAL ALA PRO ILE GLN ARG ARG LYS          
SEQRES  21 R  291  LYS PRO ALA SER GLN LYS LYS ARG ARG PHE LYS THR HIS          
SEQRES  22 R  291  ASN GLU HIS LEU ALA GLY VAL LEU LYS ASP TYR SER ASP          
SEQRES  23 R  291  ILE THR SER SER LYS                                          
SEQRES   1 S  517  MET ALA ALA LEU GLY PRO SER SER GLN ASN VAL THR GLU          
SEQRES   2 S  517  TYR VAL VAL ARG VAL PRO LYS ASN THR THR LYS LYS TYR          
SEQRES   3 S  517  ASN ILE MET ALA PHE ASN ALA ALA ASP LYS VAL ASN PHE          
SEQRES   4 S  517  ALA THR TRP ASN GLN ALA ARG LEU GLU ARG ASP LEU SER          
SEQRES   5 S  517  ASN LYS LYS ILE TYR GLN GLU GLU GLU MET PRO GLU SER          
SEQRES   6 S  517  GLY ALA GLY SER GLU PHE ASN ARG LYS LEU ARG GLU GLU          
SEQRES   7 S  517  ALA ARG ARG LYS LYS TYR GLY ILE VAL LEU LYS GLU PHE          
SEQRES   8 S  517  ARG PRO GLU ASP GLN PRO TRP LEU LEU ARG VAL ASN GLY          
SEQRES   9 S  517  LYS SER GLY ARG LYS PHE LYS GLY ILE LYS LYS GLY GLY          
SEQRES  10 S  517  VAL THR GLU ASN THR SER TYR TYR ILE PHE THR GLN CYS          
SEQRES  11 S  517  PRO ASP GLY ALA PHE GLU ALA PHE PRO VAL HIS ASN TRP          
SEQRES  12 S  517  TYR ASN PHE THR PRO LEU ALA ARG HIS ARG THR LEU THR          
SEQRES  13 S  517  ALA GLU GLU ALA GLU GLU GLU TRP GLU ARG ARG ASN LYS          
SEQRES  14 S  517  VAL LEU ASN HIS PHE SER ILE MET GLN GLN ARG ARG LEU          
SEQRES  15 S  517  LYS ASP GLN ASP GLN ASP GLU ASP GLU GLU GLU LYS GLU          
SEQRES  16 S  517  LYS ARG GLY ARG ARG LYS ALA SER GLU LEU ARG ILE HIS          
SEQRES  17 S  517  ASP LEU GLU ASP ASP LEU GLU MET SER SER ASP ALA SER          
SEQRES  18 S  517  ASP ALA SER GLY GLU GLU GLY GLY ARG VAL PRO LYS ALA          
SEQRES  19 S  517  LYS LYS LYS ALA PRO LEU ALA LYS GLY GLY ARG LYS LYS          
SEQRES  20 S  517  LYS LYS LYS LYS GLY SER ASP ASP GLU ALA PHE GLU ASP          
SEQRES  21 S  517  SER ASP ASP GLY ASP PHE GLU GLY GLN GLU VAL ASP TYR          
SEQRES  22 S  517  MET SER ASP GLY SER SER SER SER GLN GLU GLU PRO GLU          
SEQRES  23 S  517  SER LYS ALA LYS ALA PRO GLN GLN GLU GLU GLY PRO LYS          
SEQRES  24 S  517  GLY VAL ASP GLU GLN SER ASP SER SER GLU GLU SER GLU          
SEQRES  25 S  517  GLU GLU LYS PRO PRO GLU GLU ASP LYS GLU GLU GLU GLU          
SEQRES  26 S  517  GLU LYS LYS ALA PRO THR PRO GLN GLU LYS LYS ARG ARG          
SEQRES  27 S  517  LYS ASP SER SER GLU GLU SER ASP SER SER GLU GLU SER          
SEQRES  28 S  517  ASP ILE ASP SER GLU ALA SER SER ALA LEU PHE MET ALA          
SEQRES  29 S  517  LYS LYS LYS THR PRO PRO LYS ARG GLU ARG LYS PRO SER          
SEQRES  30 S  517  GLY GLY SER SER ARG GLY ASN SER ARG PRO GLY THR PRO          
SEQRES  31 S  517  SER ALA GLU GLY GLY SER THR SER SER THR LEU ARG ALA          
SEQRES  32 S  517  ALA ALA SER LYS LEU GLU GLN GLY LYS ARG VAL SER GLU          
SEQRES  33 S  517  MET PRO ALA ALA LYS ARG LEU ARG LEU ASP THR GLY PRO          
SEQRES  34 S  517  GLN SER LEU SER GLY LYS SER THR PRO GLN PRO PRO SER          
SEQRES  35 S  517  GLY LYS THR THR PRO ASN SER GLY ASP VAL GLN VAL THR          
SEQRES  36 S  517  GLU ASP ALA VAL ARG ARG TYR LEU THR ARG LYS PRO MET          
SEQRES  37 S  517  THR THR LYS ASP LEU LEU LYS LYS PHE GLN THR LYS LYS          
SEQRES  38 S  517  THR GLY LEU SER SER GLU GLN THR VAL ASN VAL LEU ALA          
SEQRES  39 S  517  GLN ILE LEU LYS ARG LEU ASN PRO GLU ARG LYS MET ILE          
SEQRES  40 S  517  ASN ASP LYS MET HIS PHE SER LEU LYS GLU                      
SEQRES   1 T  249  MET ALA GLU ARG GLY GLU LEU ASP LEU THR GLY ALA LYS          
SEQRES   2 T  249  GLN ASN THR GLY VAL TRP LEU VAL LYS VAL PRO LYS TYR          
SEQRES   3 T  249  LEU SER GLN GLN TRP ALA LYS ALA SER GLY ARG GLY GLU          
SEQRES   4 T  249  VAL GLY LYS LEU ARG ILE ALA LYS THR GLN GLY ARG THR          
SEQRES   5 T  249  GLU VAL SER PHE THR LEU ASN GLU ASP LEU ALA ASN ILE          
SEQRES   6 T  249  HIS ASP ILE GLY GLY LYS PRO ALA SER VAL SER ALA PRO          
SEQRES   7 T  249  ARG GLU HIS PRO PHE VAL LEU GLN SER VAL GLY GLY GLN          
SEQRES   8 T  249  THR LEU THR VAL PHE THR GLU SER SER SER ASP LYS LEU          
SEQRES   9 T  249  SER LEU GLU GLY ILE VAL VAL GLN ARG ALA GLU CYS ARG          
SEQRES  10 T  249  PRO ALA ALA SER GLU ASN TYR MET ARG LEU LYS ARG LEU          
SEQRES  11 T  249  GLN ILE GLU GLU SER SER LYS PRO VAL ARG LEU SER GLN          
SEQRES  12 T  249  GLN LEU ASP LYS VAL VAL THR THR ASN TYR LYS PRO VAL          
SEQRES  13 T  249  ALA ASN HIS GLN TYR ASN ILE GLU TYR GLU ARG LYS LYS          
SEQRES  14 T  249  LYS GLU ASP GLY LYS ARG ALA ARG ALA ASP LYS GLN HIS          
SEQRES  15 T  249  VAL LEU ASP MET LEU PHE SER ALA PHE GLU LYS HIS GLN          
SEQRES  16 T  249  TYR TYR ASN LEU LYS ASP LEU VAL ASP ILE THR LYS GLN          
SEQRES  17 T  249  PRO VAL VAL TYR LEU LYS GLU ILE LEU LYS GLU ILE GLY          
SEQRES  18 T  249  VAL GLN ASN VAL LYS GLY ILE HIS LYS ASN THR TRP GLU          
SEQRES  19 T  249  LEU LYS PRO GLU TYR ARG HIS TYR GLN GLY GLU GLU LYS          
SEQRES  20 T  249  SER ASP                                                      
SEQRES   1 V  782  MET GLY LYS ARG ASP ARG ALA ASP ARG ASP LYS LYS LYS          
SEQRES   2 V  782  SER ARG LYS ARG HIS TYR GLU ASP GLU GLU ASP ASP GLU          
SEQRES   3 V  782  GLU ASP ALA PRO GLY ASN ASP PRO GLN GLU ALA VAL PRO          
SEQRES   4 V  782  SER ALA ALA GLY LYS GLN VAL ASP GLU SER GLY THR LYS          
SEQRES   5 V  782  VAL ASP GLU TYR GLY ALA LYS ASP TYR ARG LEU GLN MET          
SEQRES   6 V  782  PRO LEU LYS ASP ASP HIS THR SER ARG PRO LEU TRP VAL          
SEQRES   7 V  782  ALA PRO ASP GLY HIS ILE PHE LEU GLU ALA PHE SER PRO          
SEQRES   8 V  782  VAL TYR LYS TYR ALA GLN ASP PHE LEU VAL ALA ILE ALA          
SEQRES   9 V  782  GLU PRO VAL CYS ARG PRO THR HIS VAL HIS GLU TYR LYS          
SEQRES  10 V  782  LEU THR ALA TYR SER LEU TYR ALA ALA VAL SER VAL GLY          
SEQRES  11 V  782  LEU GLN THR SER ASP ILE THR GLU TYR LEU ARG LYS LEU          
SEQRES  12 V  782  SER LYS THR GLY VAL PRO ASP GLY ILE MET GLN PHE ILE          
SEQRES  13 V  782  LYS LEU CYS THR VAL SER TYR GLY LYS VAL LYS LEU VAL          
SEQRES  14 V  782  LEU LYS HIS ASN ARG TYR PHE VAL GLU SER CYS HIS PRO          
SEQRES  15 V  782  ASP VAL ILE GLN HIS LEU LEU GLN ASP PRO VAL ILE ARG          
SEQRES  16 V  782  GLU CYS ARG LEU ARG ASN SER GLU GLY GLU ALA THR GLU          
SEQRES  17 V  782  LEU ILE THR GLU THR PHE THR SER LYS SER ALA ILE SER          
SEQRES  18 V  782  LYS THR ALA GLU SER SER GLY GLY PRO SER THR SER ARG          
SEQRES  19 V  782  VAL THR ASP PRO GLN GLY LYS SER ASP ILE PRO MET ASP          
SEQRES  20 V  782  LEU PHE ASP PHE TYR GLU GLN MET ASP LYS ASP GLU GLU          
SEQRES  21 V  782  GLU GLU GLU GLU THR GLN THR VAL SER PHE GLU VAL LYS          
SEQRES  22 V  782  GLN GLU MET ILE GLU GLU LEU GLN LYS ARG CYS ILE HIS          
SEQRES  23 V  782  LEU GLU TYR PRO LEU LEU ALA GLU TYR ASP PHE ARG ASN          
SEQRES  24 V  782  ASP SER VAL ASN PRO ASP ILE ASN ILE ASP LEU LYS PRO          
SEQRES  25 V  782  THR ALA VAL LEU ARG PRO TYR GLN GLU LYS SER LEU ARG          
SEQRES  26 V  782  LYS MET PHE GLY ASN GLY ARG ALA ARG SER GLY VAL ILE          
SEQRES  27 V  782  VAL LEU PRO CYS GLY ALA GLY LYS SER LEU VAL GLY VAL          
SEQRES  28 V  782  THR ALA ALA CYS THR VAL ARG LYS ARG CYS LEU VAL LEU          
SEQRES  29 V  782  GLY ASN SER ALA VAL SER VAL GLU GLN TRP LYS ALA GLN          
SEQRES  30 V  782  PHE LYS MET TRP SER THR ILE ASP ASP SER GLN ILE CYS          
SEQRES  31 V  782  ARG PHE THR SER ASP ALA LYS ASP LYS PRO ILE GLY CYS          
SEQRES  32 V  782  SER VAL ALA ILE SER THR TYR SER MET LEU GLY HIS THR          
SEQRES  33 V  782  THR LYS ARG SER TRP GLU ALA GLU ARG VAL MET GLU TRP          
SEQRES  34 V  782  LEU LYS THR GLN GLU TRP GLY LEU MET ILE LEU ASP GLU          
SEQRES  35 V  782  VAL HIS THR ILE PRO ALA LYS MET PHE ARG ARG VAL LEU          
SEQRES  36 V  782  THR ILE VAL GLN ALA HIS CYS LYS LEU GLY LEU THR ALA          
SEQRES  37 V  782  THR LEU VAL ARG GLU ASP ASP LYS ILE VAL ASP LEU ASN          
SEQRES  38 V  782  PHE LEU ILE GLY PRO LYS LEU TYR GLU ALA ASN TRP MET          
SEQRES  39 V  782  GLU LEU GLN ASN ASN GLY TYR ILE ALA LYS VAL GLN CYS          
SEQRES  40 V  782  ALA GLU VAL TRP CYS PRO MET SER PRO GLU PHE TYR ARG          
SEQRES  41 V  782  GLU TYR VAL ALA ILE LYS THR LYS LYS ARG ILE LEU LEU          
SEQRES  42 V  782  TYR THR MET ASN PRO ASN LYS PHE ARG ALA CYS GLN PHE          
SEQRES  43 V  782  LEU ILE LYS PHE HIS GLU ARG ARG ASN ASP LYS ILE ILE          
SEQRES  44 V  782  VAL PHE ALA ASP ASN VAL PHE ALA LEU LYS GLU TYR ALA          
SEQRES  45 V  782  ILE ARG LEU ASN LYS PRO TYR ILE TYR GLY PRO THR SER          
SEQRES  46 V  782  GLN GLY GLU ARG MET GLN ILE LEU GLN ASN PHE LYS HIS          
SEQRES  47 V  782  ASN PRO LYS ILE ASN THR ILE PHE ILE SER LYS VAL GLY          
SEQRES  48 V  782  ASP THR SER PHE ASP LEU PRO GLU ALA ASN VAL LEU ILE          
SEQRES  49 V  782  GLN ILE SER SER HIS GLY GLY SER ARG ARG GLN GLU ALA          
SEQRES  50 V  782  GLN ARG LEU GLY ARG VAL LEU ARG ALA LYS LYS GLY MET          
SEQRES  51 V  782  VAL ALA GLU GLU TYR ASN ALA PHE PHE TYR SER LEU VAL          
SEQRES  52 V  782  SER GLN ASP THR GLN GLU MET ALA TYR SER THR LYS ARG          
SEQRES  53 V  782  GLN ARG PHE LEU VAL ASP GLN GLY TYR SER PHE LYS VAL          
SEQRES  54 V  782  ILE THR LYS LEU ALA GLY MET GLU GLU GLU ASP LEU ALA          
SEQRES  55 V  782  PHE SER THR LYS GLU GLU GLN GLN GLN LEU LEU GLN LYS          
SEQRES  56 V  782  VAL LEU ALA ALA THR ASP LEU ASP ALA GLU GLU GLU VAL          
SEQRES  57 V  782  VAL ALA GLY GLU PHE GLY SER ARG SER SER GLN ALA SER          
SEQRES  58 V  782  ARG ARG PHE GLY THR MET SER SER MET SER GLY ALA ASP          
SEQRES  59 V  782  ASP THR VAL TYR MET GLU TYR HIS SER SER ARG SER LYS          
SEQRES  60 V  782  ALA PRO SER LYS HIS VAL HIS PRO LEU PHE LYS ARG PHE          
SEQRES  61 V  782  ARG LYS                                                      
SEQRES   1 W  760  MET LYS LEU ASN VAL ASP GLY LEU LEU VAL TYR PHE PRO          
SEQRES   2 W  760  TYR ASP TYR ILE TYR PRO GLU GLN PHE SER TYR MET ARG          
SEQRES   3 W  760  GLU LEU LYS ARG THR LEU ASP ALA LYS GLY HIS GLY VAL          
SEQRES   4 W  760  LEU GLU MET PRO SER GLY THR GLY LYS THR VAL SER LEU          
SEQRES   5 W  760  LEU ALA LEU ILE MET ALA TYR GLN ARG ALA TYR PRO LEU          
SEQRES   6 W  760  GLU VAL THR LYS LEU ILE TYR CYS SER ARG THR VAL PRO          
SEQRES   7 W  760  GLU ILE GLU LYS VAL ILE GLU GLU LEU ARG LYS LEU LEU          
SEQRES   8 W  760  ASN PHE TYR GLU LYS GLN GLU GLY GLU LYS LEU PRO PHE          
SEQRES   9 W  760  LEU GLY LEU ALA LEU SER SER ARG LYS ASN LEU CYS ILE          
SEQRES  10 W  760  HIS PRO GLU VAL THR PRO LEU ARG PHE GLY LYS ASP VAL          
SEQRES  11 W  760  ASP GLY LYS CYS HIS SER LEU THR ALA SER TYR VAL ARG          
SEQRES  12 W  760  ALA GLN TYR GLN HIS ASP THR SER LEU PRO HIS CYS ARG          
SEQRES  13 W  760  PHE TYR GLU GLU PHE ASP ALA HIS GLY ARG GLU VAL PRO          
SEQRES  14 W  760  LEU PRO ALA GLY ILE TYR ASN LEU ASP ASP LEU LYS ALA          
SEQRES  15 W  760  LEU GLY ARG ARG GLN GLY TRP CYS PRO TYR PHE LEU ALA          
SEQRES  16 W  760  ARG TYR SER ILE LEU HIS ALA ASN VAL VAL VAL TYR SER          
SEQRES  17 W  760  TYR HIS TYR LEU LEU ASP PRO LYS ILE ALA ASP LEU VAL          
SEQRES  18 W  760  SER LYS GLU LEU ALA ARG LYS ALA VAL VAL VAL PHE ASP          
SEQRES  19 W  760  GLU ALA HIS ASN ILE ASP ASN VAL CYS ILE ASP SER MET          
SEQRES  20 W  760  SER VAL ASN LEU THR ARG ARG THR LEU ASP ARG CYS GLN          
SEQRES  21 W  760  GLY ASN LEU GLU THR LEU GLN LYS THR VAL LEU ARG ILE          
SEQRES  22 W  760  LYS GLU THR ASP GLU GLN ARG LEU ARG ASP GLU TYR ARG          
SEQRES  23 W  760  ARG LEU VAL GLU GLY LEU ARG GLU ALA SER ALA ALA ARG          
SEQRES  24 W  760  GLU THR ASP ALA HIS LEU ALA ASN PRO VAL LEU PRO ASP          
SEQRES  25 W  760  GLU VAL LEU GLN GLU ALA VAL PRO GLY SER ILE ARG THR          
SEQRES  26 W  760  ALA GLU HIS PHE LEU GLY PHE LEU ARG ARG LEU LEU GLU          
SEQRES  27 W  760  TYR VAL LYS TRP ARG LEU ARG VAL GLN HIS VAL VAL GLN          
SEQRES  28 W  760  GLU SER PRO PRO ALA PHE LEU SER GLY LEU ALA GLN ARG          
SEQRES  29 W  760  VAL CYS ILE GLN ARG LYS PRO LEU ARG PHE CYS ALA GLU          
SEQRES  30 W  760  ARG LEU ARG SER LEU LEU HIS THR LEU GLU ILE THR ASP          
SEQRES  31 W  760  LEU ALA ASP PHE SER PRO LEU THR LEU LEU ALA ASN PHE          
SEQRES  32 W  760  ALA THR LEU VAL SER THR TYR ALA LYS GLY PHE THR ILE          
SEQRES  33 W  760  ILE ILE GLU PRO PHE ASP ASP ARG THR PRO THR ILE ALA          
SEQRES  34 W  760  ASN PRO ILE LEU HIS PHE SER CYS MET ASP ALA SER LEU          
SEQRES  35 W  760  ALA ILE LYS PRO VAL PHE GLU ARG PHE GLN SER VAL ILE          
SEQRES  36 W  760  ILE THR SER GLY THR LEU SER PRO LEU ASP ILE TYR PRO          
SEQRES  37 W  760  LYS ILE LEU ASP PHE HIS PRO VAL THR MET ALA THR PHE          
SEQRES  38 W  760  THR MET THR LEU ALA ARG VAL CYS LEU CYS PRO MET ILE          
SEQRES  39 W  760  ILE GLY ARG GLY ASN ASP GLN VAL ALA ILE SER SER LYS          
SEQRES  40 W  760  PHE GLU THR ARG GLU ASP ILE ALA VAL ILE ARG ASN TYR          
SEQRES  41 W  760  GLY ASN LEU LEU LEU GLU MET SER ALA VAL VAL PRO ASP          
SEQRES  42 W  760  GLY ILE VAL ALA PHE PHE THR SER TYR GLN TYR MET GLU          
SEQRES  43 W  760  SER THR VAL ALA SER TRP TYR GLU GLN GLY ILE LEU GLU          
SEQRES  44 W  760  ASN ILE GLN ARG ASN LYS LEU LEU PHE ILE GLU THR GLN          
SEQRES  45 W  760  ASP GLY ALA GLU THR SER VAL ALA LEU GLU LYS TYR GLN          
SEQRES  46 W  760  GLU ALA CYS GLU ASN GLY ARG GLY ALA ILE LEU LEU SER          
SEQRES  47 W  760  VAL ALA ARG GLY LYS VAL SER GLU GLY ILE ASP PHE VAL          
SEQRES  48 W  760  HIS HIS TYR GLY ARG ALA VAL ILE MET PHE GLY VAL PRO          
SEQRES  49 W  760  TYR VAL TYR THR GLN SER ARG ILE LEU LYS ALA ARG LEU          
SEQRES  50 W  760  GLU TYR LEU ARG ASP GLN PHE GLN ILE ARG GLU ASN ASP          
SEQRES  51 W  760  PHE LEU THR PHE ASP ALA MET ARG HIS ALA ALA GLN CYS          
SEQRES  52 W  760  VAL GLY ARG ALA ILE ARG GLY LYS THR ASP TYR GLY LEU          
SEQRES  53 W  760  MET VAL PHE ALA ASP LYS ARG PHE ALA ARG GLY ASP LYS          
SEQRES  54 W  760  ARG GLY LYS LEU PRO ARG TRP ILE GLN GLU HIS LEU THR          
SEQRES  55 W  760  ASP ALA ASN LEU ASN LEU THR VAL ASP GLU GLY VAL GLN          
SEQRES  56 W  760  VAL ALA LYS TYR PHE LEU ARG GLN MET ALA GLN PRO PHE          
SEQRES  57 W  760  HIS ARG GLU ASP GLN LEU GLY LEU SER LEU LEU SER LEU          
SEQRES  58 W  760  GLU GLN LEU GLU SER GLU GLU THR LEU LYS ARG ILE GLU          
SEQRES  59 W  760  GLN ILE ALA GLN GLN LEU                                      
SEQRES   1 0  395  MET ASP GLU GLU PRO GLU ARG THR LYS ARG TRP GLU GLY          
SEQRES   2 0  395  GLY TYR GLU ARG THR TRP GLU ILE LEU LYS GLU ASP GLU          
SEQRES   3 0  395  SER GLY SER LEU LYS ALA THR ILE GLU ASP ILE LEU PHE          
SEQRES   4 0  395  LYS ALA LYS ARG LYS ARG VAL PHE GLU HIS HIS GLY GLN          
SEQRES   5 0  395  VAL ARG LEU GLY MET MET ARG HIS LEU TYR VAL VAL VAL          
SEQRES   6 0  395  ASP GLY SER ARG THR MET GLU ASP GLN ASP LEU LYS PRO          
SEQRES   7 0  395  ASN ARG LEU THR CYS THR LEU LYS LEU LEU GLU TYR PHE          
SEQRES   8 0  395  VAL GLU GLU TYR PHE ASP GLN ASN PRO ILE SER GLN ILE          
SEQRES   9 0  395  GLY ILE ILE VAL THR LYS SER LYS ARG ALA GLU LYS LEU          
SEQRES  10 0  395  THR GLU LEU SER GLY ASN PRO ARG LYS HIS ILE THR SER          
SEQRES  11 0  395  LEU LYS LYS ALA VAL ASP MET THR CYS HIS GLY GLU PRO          
SEQRES  12 0  395  SER LEU TYR ASN SER LEU SER ILE ALA MET GLN THR LEU          
SEQRES  13 0  395  LYS HIS MET PRO GLY HIS THR SER ARG GLU VAL LEU ILE          
SEQRES  14 0  395  ILE PHE SER SER LEU THR THR CYS ASP PRO SER ASN ILE          
SEQRES  15 0  395  TYR ASP LEU ILE LYS THR LEU LYS ALA ALA LYS ILE ARG          
SEQRES  16 0  395  VAL SER VAL ILE GLY LEU SER ALA GLU VAL ARG VAL CYS          
SEQRES  17 0  395  THR VAL LEU ALA ARG GLU THR GLY GLY THR TYR HIS VAL          
SEQRES  18 0  395  ILE LEU ASP GLU SER HIS TYR LYS GLU LEU LEU THR HIS          
SEQRES  19 0  395  HIS VAL SER PRO PRO PRO ALA SER SER SER SER GLU CYS          
SEQRES  20 0  395  SER LEU ILE ARG MET GLY PHE PRO GLN HIS THR ILE ALA          
SEQRES  21 0  395  SER LEU SER ASP GLN ASP ALA LYS PRO SER PHE SER MET          
SEQRES  22 0  395  ALA HIS LEU ASP GLY ASN THR GLU PRO GLY LEU THR LEU          
SEQRES  23 0  395  GLY GLY TYR PHE CYS PRO GLN CYS ARG ALA LYS TYR CYS          
SEQRES  24 0  395  GLU LEU PRO VAL GLU CYS LYS ILE CYS GLY LEU THR LEU          
SEQRES  25 0  395  VAL SER ALA PRO HIS LEU ALA ARG SER TYR HIS HIS LEU          
SEQRES  26 0  395  PHE PRO LEU ASP ALA PHE GLN GLU ILE PRO LEU GLU GLU          
SEQRES  27 0  395  TYR ASN GLY GLU ARG PHE CYS TYR GLY CYS GLN GLY GLU          
SEQRES  28 0  395  LEU LYS ASP GLN HIS VAL TYR VAL CYS ALA VAL CYS GLN          
SEQRES  29 0  395  ASN VAL PHE CYS VAL ASP CYS ASP VAL PHE VAL HIS ASP          
SEQRES  30 0  395  SER LEU HIS CYS CYS PRO GLY CYS ILE HIS LYS ILE PRO          
SEQRES  31 0  395  ALA PRO SER GLY VAL                                          
SEQRES   1 1   71  MET VAL ASN VAL LEU LYS GLY VAL LEU ILE GLU CYS ASP          
SEQRES   2 1   71  PRO ALA MET LYS GLN PHE LEU LEU TYR LEU ASP GLU SER          
SEQRES   3 1   71  ASN ALA LEU GLY LYS LYS PHE ILE ILE GLN ASP ILE ASP          
SEQRES   4 1   71  ASP THR HIS VAL PHE VAL ILE ALA GLU LEU VAL ASN VAL          
SEQRES   5 1   71  LEU GLN GLU ARG VAL GLY GLU LEU MET ASP GLN ASN ALA          
SEQRES   6 1   71  PHE SER LEU THR GLN LYS                                      
SEQRES   1 2  462  MET GLU SER THR PRO SER ARG GLY LEU ASN ARG VAL HIS          
SEQRES   2 2  462  LEU GLN CYS ARG ASN LEU GLN GLU PHE LEU GLY GLY LEU          
SEQRES   3 2  462  SER PRO GLY VAL LEU ASP ARG LEU TYR GLY HIS PRO ALA          
SEQRES   4 2  462  THR CYS LEU ALA VAL PHE ARG GLU LEU PRO SER LEU ALA          
SEQRES   5 2  462  LYS ASN TRP VAL MET ARG MET LEU PHE LEU GLU GLN PRO          
SEQRES   6 2  462  LEU PRO GLN ALA ALA VAL ALA LEU TRP VAL LYS LYS GLU          
SEQRES   7 2  462  PHE SER LYS ALA GLN GLU GLU SER THR GLY LEU LEU SER          
SEQRES   8 2  462  GLY LEU ARG ILE TRP HIS THR GLN LEU LEU PRO GLY GLY          
SEQRES   9 2  462  LEU GLN GLY LEU ILE LEU ASN PRO ILE PHE ARG GLN ASN          
SEQRES  10 2  462  LEU ARG ILE ALA LEU LEU GLY GLY GLY LYS ALA TRP SER          
SEQRES  11 2  462  ASP ASP THR SER GLN LEU GLY PRO ASP LYS HIS ALA ARG          
SEQRES  12 2  462  ASP VAL PRO SER LEU ASP LYS TYR ALA GLU GLU ARG TRP          
SEQRES  13 2  462  GLU VAL VAL LEU HIS PHE MET VAL GLY SER PRO SER ALA          
SEQRES  14 2  462  ALA VAL SER GLN ASP LEU ALA GLN LEU LEU SER GLN ALA          
SEQRES  15 2  462  GLY LEU MET LYS SER THR GLU PRO GLY GLU PRO PRO CYS          
SEQRES  16 2  462  ILE THR SER ALA GLY PHE GLN PHE LEU LEU LEU ASP THR          
SEQRES  17 2  462  PRO ALA GLN LEU TRP TYR PHE MET LEU GLN TYR LEU GLN          
SEQRES  18 2  462  THR ALA GLN SER ARG GLY MET ASP LEU VAL GLU ILE LEU          
SEQRES  19 2  462  SER PHE LEU PHE GLN LEU SER PHE SER THR LEU GLY LYS          
SEQRES  20 2  462  ASP TYR SER VAL GLU GLY MET SER ASP SER LEU LEU ASN          
SEQRES  21 2  462  PHE LEU GLN HIS LEU ARG GLU PHE GLY LEU VAL PHE GLN          
SEQRES  22 2  462  ARG LYS ARG LYS SER ARG ARG TYR TYR PRO THR ARG LEU          
SEQRES  23 2  462  ALA ILE ASN LEU SER SER GLY VAL SER GLY ALA GLY GLY          
SEQRES  24 2  462  THR VAL HIS GLN PRO GLY PHE ILE VAL VAL GLU THR ASN          
SEQRES  25 2  462  TYR ARG LEU TYR ALA TYR THR GLU SER GLU LEU GLN ILE          
SEQRES  26 2  462  ALA LEU ILE ALA LEU PHE SER GLU MET LEU TYR ARG PHE          
SEQRES  27 2  462  PRO ASN MET VAL VAL ALA GLN VAL THR ARG GLU SER VAL          
SEQRES  28 2  462  GLN GLN ALA ILE ALA SER GLY ILE THR ALA GLN GLN ILE          
SEQRES  29 2  462  ILE HIS PHE LEU ARG THR ARG ALA HIS PRO VAL MET LEU          
SEQRES  30 2  462  LYS GLN THR PRO VAL LEU PRO PRO THR ILE THR ASP GLN          
SEQRES  31 2  462  ILE ARG LEU TRP GLU LEU GLU ARG ASP ARG LEU ARG PHE          
SEQRES  32 2  462  THR GLU GLY VAL LEU TYR ASN GLN PHE LEU SER GLN VAL          
SEQRES  33 2  462  ASP PHE GLU LEU LEU LEU ALA HIS ALA ARG GLU LEU GLY          
SEQRES  34 2  462  VAL LEU VAL PHE GLU ASN SER ALA LYS ARG LEU MET VAL          
SEQRES  35 2  462  VAL THR PRO ALA GLY HIS SER ASP VAL LYS ARG PHE TRP          
SEQRES  36 2  462  LYS ARG GLN LYS HIS SER SER                                  
SEQRES   1 3  308  MET VAL SER ASP GLU ASP GLU LEU ASN LEU LEU VAL ILE          
SEQRES   2 3  308  VAL VAL ASP ALA ASN PRO ILE TRP TRP GLY LYS GLN ALA          
SEQRES   3 3  308  LEU LYS GLU SER GLN PHE THR LEU SER LYS CYS ILE ASP          
SEQRES   4 3  308  ALA VAL MET VAL LEU GLY ASN SER HIS LEU PHE MET ASN          
SEQRES   5 3  308  ARG SER ASN LYS LEU ALA VAL ILE ALA SER HIS ILE GLN          
SEQRES   6 3  308  GLU SER ARG PHE LEU TYR PRO GLY LYS ASN GLY ARG LEU          
SEQRES   7 3  308  GLY ASP PHE PHE GLY ASP PRO GLY ASN PRO PRO GLU PHE          
SEQRES   8 3  308  ASN PRO SER GLY SER LYS ASP GLY LYS TYR GLU LEU LEU          
SEQRES   9 3  308  THR SER ALA ASN GLU VAL ILE VAL GLU GLU ILE LYS ASP          
SEQRES  10 3  308  LEU MET THR LYS SER ASP ILE LYS GLY GLN HIS THR GLU          
SEQRES  11 3  308  THR LEU LEU ALA GLY SER LEU ALA LYS ALA LEU CYS TYR          
SEQRES  12 3  308  ILE HIS ARG MET ASN LYS GLU VAL LYS ASP ASN GLN GLU          
SEQRES  13 3  308  MET LYS SER ARG ILE LEU VAL ILE LYS ALA ALA GLU ASP          
SEQRES  14 3  308  SER ALA LEU GLN TYR MET ASN PHE MET ASN VAL ILE PHE          
SEQRES  15 3  308  ALA ALA GLN LYS GLN ASN ILE LEU ILE ASP ALA CYS VAL          
SEQRES  16 3  308  LEU ASP SER ASP SER GLY LEU LEU GLN GLN ALA CYS ASP          
SEQRES  17 3  308  ILE THR GLY GLY LEU TYR LEU LYS VAL PRO GLN MET PRO          
SEQRES  18 3  308  SER LEU LEU GLN TYR LEU LEU TRP VAL PHE LEU PRO ASP          
SEQRES  19 3  308  GLN ASP GLN ARG SER GLN LEU ILE LEU PRO PRO PRO VAL          
SEQRES  20 3  308  HIS VAL ASP TYR ARG ALA ALA CYS PHE CYS HIS ARG ASN          
SEQRES  21 3  308  LEU ILE GLU ILE GLY TYR VAL CYS SER VAL CYS LEU SER          
SEQRES  22 3  308  ILE PHE CYS ASN PHE SER PRO ILE CYS THR THR CYS GLU          
SEQRES  23 3  308  THR ALA PHE LYS ILE SER LEU PRO PRO VAL LEU LYS ALA          
SEQRES  24 3  308  LYS LYS LYS LYS LEU LYS VAL SER ALA                          
SEQRES   1 X   83   DG  DA  DA  DG  DG  DG  DC  DG  DC  DC  DT  DA  DT          
SEQRES   2 X   83   DA  DA  DA  DA  DG  DG  DG  DG  DG  DT  DG  DG  DG          
SEQRES   3 X   83   DG  DG  DC  DG  DT  DT  DT  DT  DT  DT  DT  DT  DT          
SEQRES   4 X   83   DT  DT  DT  DT  DT  DT  DT  DT  DT  DT  DT  DC  DG          
SEQRES   5 X   83   DA  DA  DC  DA  DC  DT  DC  DG  DA  DG  DC  DC  DG          
SEQRES   6 X   83   DA  DG  DC  DA  DG  DA  DC  DG  DT  DG  DC  DC  DT          
SEQRES   7 X   83   DA  DC  DG  DG  DA                                          
SEQRES   1 Y   83   DT  DC  DC  DG  DT  DA  DG  DG  DC  DA  DC  DG  DT          
SEQRES   2 Y   83   DC  DT  DG  DC  DT  DC  DG  DG  DC  DT  DC  DG  DA          
SEQRES   3 Y   83   DG  DT  DG  DT  DT  DC  DG  DA  DT  DC  DG  DC  DG          
SEQRES   4 Y   83   DA  DC  DT  DG  DA  DG  DG  DA  DC  DG  DA  DA  DC          
SEQRES   5 Y   83   DG  DC  DG  DC  DC  DC  DC  DC  DA  DC  DC  DC  DC          
SEQRES   6 Y   83   DC  DT  DT  DC  DT  DA  DT  DA  DG  DG  DC  DG  DC          
SEQRES   7 Y   83   DC  DC  DT  DT  DC                                          
SEQRES   1 Z    6    A   G   U   C   G   C                                      
HET     MG  A2001       1                                                       
HET     MG  A2002       1                                                       
HET     ZN  A2003       1                                                       
HET     ZN  A2004       1                                                       
HET     ZN  B1201       1                                                       
HET     ZN  C 301       1                                                       
HET     ZN  I 201       1                                                       
HET     ZN  I 202       1                                                       
HET     ZN  J 101       1                                                       
HET     ZN  L 101       1                                                       
HET     ZN  M 401       1                                                       
HET     ZN  Q 501       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      ZN ZINC ION                                                         
FORMUL  30   MG    2(MG 2+)                                                     
FORMUL  32   ZN    10(ZN 2+)                                                    
HELIX    1 AA1 SER A   27  SER A   35  1                                   9    
HELIX    2 AA2 PHE A   99  VAL A  110  1                                  12    
HELIX    3 AA3 ASN A  123  LYS A  132  1                                  10    
HELIX    4 AA4 GLN A  136  LYS A  151  1                                  16    
HELIX    5 AA5 SER A  217  ILE A  228  1                                  12    
HELIX    6 AA6 SER A  229  LEU A  236  1                                   8    
HELIX    7 AA7 ARG A  244  TRP A  247  5                                   4    
HELIX    8 AA8 ASP A  274  ASN A  296  1                                  23    
HELIX    9 AA9 ALA A  299  ASP A  319  1                                  21    
HELIX   10 AB1 SER A  338  GLY A  345  1                                   8    
HELIX   11 AB2 ARG A  382  MET A  388  1                                   7    
HELIX   12 AB3 ASN A  398  GLY A  409  1                                  12    
HELIX   13 AB4 ASN A  410  GLN A  412  5                                   3    
HELIX   14 AB5 LYS A  434  LEU A  438  5                                   5    
HELIX   15 AB6 HIS A  465  MET A  467  5                                   3    
HELIX   16 AB7 LEU A  486  THR A  490  5                                   5    
HELIX   17 AB8 SER A  508  LEU A  518  1                                  11    
HELIX   18 AB9 MET A  520  MET A  524  5                                   5    
HELIX   19 AC1 VAL A  538  LYS A  550  1                                  13    
HELIX   20 AC2 GLU A  556  LEU A  567  1                                  12    
HELIX   21 AC3 GLY A  588  ILE A  596  1                                   9    
HELIX   22 AC4 SER A  615  LYS A  619  5                                   5    
HELIX   23 AC5 CYS A  641  GLY A  646  1                                   6    
HELIX   24 AC6 SER A  651  GLY A  661  1                                  11    
HELIX   25 AC7 GLY A  661  GLY A  684  1                                  24    
HELIX   26 AC8 GLY A  688  ILE A  693  1                                   6    
HELIX   27 AC9 ASP A  695  ASN A  722  1                                  28    
HELIX   28 AD1 THR A  732  LEU A  760  1                                  29    
HELIX   29 AD2 ASN A  764  GLY A  773  1                                  10    
HELIX   30 AD3 SER A  777  ALA A  786  1                                  10    
HELIX   31 AD4 THR A  832  GLU A  869  1                                  38    
HELIX   32 AD5 ARG A  890  ASP A  894  5                                   5    
HELIX   33 AD6 SER A  912  ARG A  921  1                                  10    
HELIX   34 AD7 ASP A  937  VAL A  942  5                                   6    
HELIX   35 AD8 ASN A  945  PHE A  970  1                                  26    
HELIX   36 AD9 ASN A  982  HIS A  995  1                                  14    
HELIX   37 AE1 HIS A 1005  LEU A 1020  1                                  16    
HELIX   38 AE2 ASP A 1027  LEU A 1049  1                                  23    
HELIX   39 AE3 CYS A 1050  GLU A 1057  1                                   8    
HELIX   40 AE4 SER A 1061  ILE A 1080  1                                  20    
HELIX   41 AE5 VAL A 1087  GLU A 1097  1                                  11    
HELIX   42 AE6 PRO A 1098  GLN A 1101  5                                   4    
HELIX   43 AE7 GLY A 1120  ILE A 1130  1                                  11    
HELIX   44 AE8 LEU A 1144  ASP A 1150  1                                   7    
HELIX   45 AE9 ASP A 1150  GLU A 1162  1                                  13    
HELIX   46 AF1 THR A 1165  VAL A 1169  1                                   5    
HELIX   47 AF2 ASN A 1180  THR A 1184  5                                   5    
HELIX   48 AF3 VAL A 1186  GLU A 1188  5                                   3    
HELIX   49 AF4 ASP A 1189  TYR A 1196  1                                   8    
HELIX   50 AF5 PHE A 1202  ARG A 1206  5                                   5    
HELIX   51 AF6 ASP A 1217  ARG A 1224  1                                   8    
HELIX   52 AF7 THR A 1227  GLY A 1240  1                                  14    
HELIX   53 AF8 SER A 1264  LYS A 1268  5                                   5    
HELIX   54 AF9 ASP A 1280  ASP A 1295  1                                  16    
HELIX   55 AG1 SER A 1342  SER A 1348  1                                   7    
HELIX   56 AG2 ASP A 1361  GLY A 1370  1                                  10    
HELIX   57 AG3 GLY A 1370  ASP A 1389  1                                  20    
HELIX   58 AG4 ASN A 1394  CYS A 1407  1                                  14    
HELIX   59 AG5 THR A 1415  ASN A 1420  1                                   6    
HELIX   60 AG6 GLY A 1425  SER A 1431  1                                   7    
HELIX   61 AG7 THR A 1435  GLY A 1446  1                                  12    
HELIX   62 AG8 GLY A 1453  GLY A 1461  1                                   9    
HELIX   63 AG9 ALA A 1466  GLY A 1469  5                                   4    
HELIX   64 AH1 ASP A 1476  MET A 1484  1                                   9    
HELIX   65 AH2 TRP B   22  LYS B   37  1                                  16    
HELIX   66 AH3 VAL B   40  MET B   53  1                                  14    
HELIX   67 AH4 MET B   53  GLU B   60  1                                   8    
HELIX   68 AH5 MET B  109  ARG B  116  1                                   8    
HELIX   69 AH6 LEU B  162  LEU B  166  5                                   5    
HELIX   70 AH7 THR B  167  ASN B  175  1                                   9    
HELIX   71 AH8 ILE B  269  LEU B  276  1                                   8    
HELIX   72 AH9 SER B  280  ILE B  289  1                                  10    
HELIX   73 AI1 ASP B  294  PHE B  309  1                                  16    
HELIX   74 AI2 GLU B  313  ALA B  326  1                                  14    
HELIX   75 AI3 LYS B  332  GLU B  346  1                                  15    
HELIX   76 AI4 LEU B  348  GLY B  352  5                                   5    
HELIX   77 AI5 SER B  354  PHE B  356  5                                   3    
HELIX   78 AI6 CYS B  357  GLY B  378  1                                  22    
HELIX   79 AI7 HIS B  387  GLY B  389  5                                   3    
HELIX   80 AI8 LEU B  395  GLY B  426  1                                  32    
HELIX   81 AI9 ASN B  430  ILE B  435  1                                   6    
HELIX   82 AJ1 THR B  437  GLY B  451  1                                  15    
HELIX   83 AJ2 THR B  474  ARG B  483  1                                  10    
HELIX   84 AJ3 PRO B  538  SER B  549  1                                  12    
HELIX   85 AJ4 GLU B  554  ILE B  556  5                                   3    
HELIX   86 AJ5 ASP B  579  GLN B  593  1                                  15    
HELIX   87 AJ6 ILE B  607  GLU B  609  5                                   3    
HELIX   88 AJ7 LYS B  636  ARG B  646  1                                  11    
HELIX   89 AJ8 GLU B  647  ASN B  649  5                                   3    
HELIX   90 AJ9 SER B  652  SER B  659  1                                   8    
HELIX   91 AK1 LEU B  668  THR B  672  5                                   5    
HELIX   92 AK2 THR B  678  LYS B  685  1                                   8    
HELIX   93 AK3 HIS B  699  LEU B  704  5                                   6    
HELIX   94 AK4 VAL B  706  ILE B  710  5                                   5    
HELIX   95 AK5 PHE B  713  ASN B  717  5                                   5    
HELIX   96 AK6 GLN B  718  ALA B  732  1                                  15    
HELIX   97 AK7 ILE B  737  ARG B  743  5                                   7    
HELIX   98 AK8 THR B  761  ARG B  768  5                                   8    
HELIX   99 AK9 ARG B  798  ARG B  803  1                                   6    
HELIX  100 AL1 ILE B  844  LEU B  848  5                                   5    
HELIX  101 AL2 HIS B  970  MET B  976  1                                   7    
HELIX  102 AL3 THR B  977  GLY B  994  1                                  18    
HELIX  103 AL4 VAL B 1006  GLY B 1019  1                                  14    
HELIX  104 AL5 MET B 1054  ILE B 1059  1                                   6    
HELIX  105 AL6 GLY B 1077  ASP B 1081  5                                   5    
HELIX  106 AL7 GLY B 1087  GLY B 1098  1                                  12    
HELIX  107 AL8 ALA B 1099  LEU B 1107  1                                   9    
HELIX  108 AL9 PRO B 1152  MET B 1165  1                                  14    
HELIX  109 AM1 ASP C   27  GLU C   41  1                                  15    
HELIX  110 AM2 HIS C   60  GLY C   69  1                                  10    
HELIX  111 AM3 ILE C   78  LEU C   82  5                                   5    
HELIX  112 AM4 ARG C  118  LEU C  120  5                                   3    
HELIX  113 AM5 HIS C  173  ASN C  177  5                                   5    
HELIX  114 AM6 LYS C  199  TRP C  203  5                                   5    
HELIX  115 AM7 ARG C  240  SER C  269  1                                  30    
HELIX  116 AM8 ASP D   16  LEU D   20  5                                   5    
HELIX  117 AM9 PRO D   23  THR D   28  1                                   6    
HELIX  118 AN1 LEU D   33  GLU D   52  1                                  20    
HELIX  119 AN2 SER D   58  PHE D   71  1                                  14    
HELIX  120 AN3 ASN D   76  GLN D   89  1                                  14    
HELIX  121 AN4 HIS D   93  CYS D  104  1                                  12    
HELIX  122 AN5 THR D  107  ILE D  115  1                                   9    
HELIX  123 AN6 PRO D  116  ARG D  121  5                                   6    
HELIX  124 AN7 GLU D  123  ARG D  138  1                                  16    
HELIX  125 AN8 ASP E    2  GLY E   25  1                                  24    
HELIX  126 AN9 THR E   29  ASP E   34  1                                   6    
HELIX  127 AO1 THR E   36  SER E   44  1                                   9    
HELIX  128 AO2 PRO E   53  LEU E   58  1                                   6    
HELIX  129 AO3 GLY E   83  ASN E   98  1                                  16    
HELIX  130 AO4 THR E  111  ALA E  122  1                                  12    
HELIX  131 AO5 GLN E  132  LEU E  136  1                                   5    
HELIX  132 AO6 ASN E  138  HIS E  142  5                                   5    
HELIX  133 AO7 THR E  152  LYS E  164  1                                  13    
HELIX  134 AO8 ARG E  166  LEU E  170  5                                   5    
HELIX  135 AO9 ASP E  177  GLY E  184  1                                   8    
HELIX  136 AP1 THR F   58  ALA F   74  1                                  17    
HELIX  137 AP2 ASP F   88  ARG F  100  1                                  13    
HELIX  138 AP3 HIS G   14  PHE G   18  5                                   5    
HELIX  139 AP4 ASN G   21  GLU G   35  1                                  15    
HELIX  140 AP5 ILE I   69  ASP I   75  5                                   7    
HELIX  141 AP6 VAL J   14  ASN J   16  5                                   3    
HELIX  142 AP7 LYS J   17  GLU J   28  1                                  12    
HELIX  143 AP8 THR J   30  LEU J   38  1                                   9    
HELIX  144 AP9 ARG J   42  HIS J   52  1                                  11    
HELIX  145 AQ1 LEU J   55  LEU J   60  1                                   6    
HELIX  146 AQ2 PRO K    5  PHE K   10  5                                   6    
HELIX  147 AQ3 ASP K   39  ASP K   53  1                                  15    
HELIX  148 AQ4 SER K   82  ASP K  111  1                                  30    
HELIX  149 AQ5 ASP M   47  TRP M   52  1                                   6    
HELIX  150 AQ6 SER M  108  SER M  110  5                                   3    
HELIX  151 AQ7 ASP M  111  ILE M  128  1                                  18    
HELIX  152 AQ8 PRO M  131  LYS M  149  1                                  19    
HELIX  153 AQ9 ALA M  155  GLU M  171  1                                  17    
HELIX  154 AR1 THR M  176  SER M  184  1                                   9    
HELIX  155 AR2 SER M  187  LEU M  202  1                                  16    
HELIX  156 AR3 THR M  211  LEU M  222  1                                  12    
HELIX  157 AR4 PRO M  225  LEU M  242  1                                  18    
HELIX  158 AR5 SER M  249  ALA M  264  1                                  16    
HELIX  159 AR6 THR M  270  GLY M  279  1                                  10    
HELIX  160 AR7 ALA M  281  TYR M  293  1                                  13    
HELIX  161 AR8 ARG M  295  PHE M  300  1                                   6    
HELIX  162 AR9 PRO M  309  LEU M  313  5                                   5    
HELIX  163 AS1 VAL N   10  GLY N   33  1                                  24    
HELIX  164 AS2 ASP N   35  MET N   51  1                                  17    
HELIX  165 AS3 PRO N  313  ASP N  318  5                                   6    
HELIX  166 AS4 TYR O    3  ASN O    8  5                                   6    
HELIX  167 AS5 THR O    9  SER O   25  1                                  17    
HELIX  168 AS6 THR O   29  ARG O   51  1                                  23    
HELIX  169 AS7 THR P  153  GLU P  157  5                                   5    
HELIX  170 AS8 ASP P  179  ALA P  187  1                                   9    
HELIX  171 AS9 SER P  226  LYS P  243  1                                  18    
HELIX  172 AT1 ARG P  269  HIS P  277  1                                   9    
HELIX  173 AT2 VAL P  317  PHE P  335  1                                  19    
HELIX  174 AT3 ALA Q   12  TYR Q   26  1                                  15    
HELIX  175 AT4 GLY Q   27  ARG Q   39  1                                  13    
HELIX  176 AT5 LYS Q   44  LYS Q   53  1                                  10    
HELIX  177 AT6 ASP Q   55  ASP Q   69  1                                  15    
HELIX  178 AT7 VAL Q  102  ARG Q  119  1                                  18    
HELIX  179 AT8 THR Q  137  LEU Q  144  1                                   8    
HELIX  180 AT9 ARG Q  174  TYR Q  188  1                                  15    
HELIX  181 AU1 TYR Q  188  GLU Q  202  1                                  15    
HELIX  182 AU2 GLY R   76  GLY R   92  1                                  17    
HELIX  183 AU3 THR R   98  THR R  106  1                                   9    
HELIX  184 AU4 GLY R  112  GLU R  122  1                                  11    
HELIX  185 AU5 GLU R  122  ASN R  127  1                                   6    
HELIX  186 AU6 LEU R  151  ASP R  156  1                                   6    
HELIX  187 AU7 LEU R  167  ALA R  174  1                                   8    
HELIX  188 AU8 PRO R  176  LEU R  185  1                                  10    
HELIX  189 AU9 GLU R  215  VAL R  223  1                                   9    
HELIX  190 AV1 ASP R  229  ARG R  239  1                                  11    
HELIX  191 AV2 ALA S   34  LYS S   36  5                                   3    
HELIX  192 AV3 ASN S   38  TRP S   42  5                                   5    
HELIX  193 AV4 ALA S  160  ARG S  167  1                                   8    
HELIX  194 AV5 HIS S  173  ARG S  180  1                                   8    
HELIX  195 AV6 LEU T    9  ASN T   15  1                                   7    
HELIX  196 AV7 LYS T   25  LYS T   33  1                                   9    
HELIX  197 AV8 ASN T  123  SER T  136  1                                  14    
HELIX  198 AV9 ASN T  158  LYS T  169  1                                  12    
HELIX  199 AW1 ASP T  179  HIS T  194  1                                  16    
HELIX  200 AW2 LEU T  199  LYS T  207  1                                   9    
HELIX  201 AW3 PRO T  209  GLY T  221  1                                  13    
HELIX  202 AW4 LYS V  282  HIS V  286  5                                   5    
HELIX  203 AW5 LEU V  287  GLU V  294  1                                   8    
HELIX  204 AW6 ARG V  317  GLY V  331  1                                  15    
HELIX  205 AW7 ARG V  332  SER V  335  5                                   4    
HELIX  206 AW8 GLY V  345  ARG V  358  1                                  14    
HELIX  207 AW9 SER V  367  PHE V  378  1                                  12    
HELIX  208 AX1 LYS V  379  TRP V  381  5                                   3    
HELIX  209 AX2 THR V  417  ALA V  423  1                                   7    
HELIX  210 AX3 VAL V  443  ILE V  446  5                                   4    
HELIX  211 AX4 PHE V  451  ILE V  457  1                                   7    
HELIX  212 AX5 LYS V  476  ILE V  484  1                                   9    
HELIX  213 AX6 TRP V  493  GLN V  497  5                                   5    
HELIX  214 AX7 GLU V  517  ILE V  525  1                                   9    
HELIX  215 AX8 LYS V  529  ASN V  537  1                                   9    
HELIX  216 AX9 ASN V  537  ARG V  554  1                                  18    
HELIX  217 AY1 ASN V  564  ASN V  576  1                                  13    
HELIX  218 AY2 SER V  585  ASN V  599  1                                  15    
HELIX  219 AY3 LYS V  609  ASP V  612  5                                   4    
HELIX  220 AY4 SER V  632  LEU V  644  1                                  13    
HELIX  221 AY5 THR V  667  ALA V  671  5                                   5    
HELIX  222 AY6 TYR V  672  GLN V  683  1                                  12    
HELIX  223 AY7 GLY V  695  GLU V  699  5                                   5    
HELIX  224 AY8 THR V  705  ALA V  718  1                                  14    
HELIX  225 AY9 TYR W   18  ALA W   34  1                                  17    
HELIX  226 AZ1 GLY W   47  ALA W   58  1                                  12    
HELIX  227 AZ2 THR W   76  ASN W   92  1                                  17    
HELIX  228 AZ3 SER W  111  CYS W  116  1                                   6    
HELIX  229 AZ4 ILE W  117  THR W  122  1                                   6    
HELIX  230 AZ5 ASP W  129  GLN W  147  1                                  19    
HELIX  231 AZ6 TYR W  158  ASP W  162  5                                   5    
HELIX  232 AZ7 ALA W  163  VAL W  168  1                                   6    
HELIX  233 AZ8 VAL W  168  ILE W  174  1                                   7    
HELIX  234 AZ9 ASN W  176  GLY W  188  1                                  13    
HELIX  235 BA1 CYS W  190  ILE W  199  1                                  10    
HELIX  236 BA2 LEU W  200  ALA W  202  5                                   3    
HELIX  237 BA3 TYR W  209  ASP W  214  1                                   6    
HELIX  238 BA4 ASP W  214  ALA W  226  1                                  13    
HELIX  239 BA5 ASN W  238  SER W  248  1                                  11    
HELIX  240 BA6 THR W  252  LEU W  266  1                                  15    
HELIX  241 BA7 ASP W  277  SER W  296  1                                  20    
HELIX  242 BA8 PRO W  308  GLU W  317  1                                  10    
HELIX  243 BA9 VAL W  319  ARG W  343  1                                  25    
HELIX  244 BB1 SER W  395  SER W  408  1                                  14    
HELIX  245 BB2 ASP W  439  LYS W  445  1                                   7    
HELIX  246 BB3 PRO W  446  PHE W  448  5                                   3    
HELIX  247 BB4 ASP W  465  ASP W  472  1                                   8    
HELIX  248 BB5 LEU W  485  ARG W  487  5                                   3    
HELIX  249 BB6 GLU W  512  ARG W  518  1                                   7    
HELIX  250 BB7 ARG W  518  VAL W  531  1                                  14    
HELIX  251 BB8 SER W  541  VAL W  549  1                                   9    
HELIX  252 BB9 ASP W  573  ALA W  587  1                                  15    
HELIX  253 BC1 GLY W  602  GLY W  607  5                                   6    
HELIX  254 BC2 ARG W  631  GLN W  645  1                                  15    
HELIX  255 BC3 ILE W  646  LEU W  652  1                                   7    
HELIX  256 BC4 LEU W  652  ARG W  669  1                                  18    
HELIX  257 BC5 ARG W  683  LYS W  689  1                                   7    
HELIX  258 BC6 ARG W  690  LYS W  692  5                                   3    
HELIX  259 BC7 GLU W  699  ASP W  703  5                                   5    
HELIX  260 BC8 ASP W  711  GLN W  726  1                                  16    
HELIX  261 BC9 SER 0   68  ASP 0   73  5                                   6    
HELIX  262 BD1 ARG 0   80  ASN 0   99  1                                  20    
HELIX  263 BD2 ASN 0  123  ASP 0  136  1                                  14    
HELIX  264 BD3 SER 0  144  HIS 0  158  1                                  15    
HELIX  265 BD4 ASN 0  181  LYS 0  193  1                                  13    
HELIX  266 BD5 VAL 0  205  GLY 0  216  1                                  12    
HELIX  267 BD6 ASP 0  224  SER 0  237  1                                  14    
HELIX  268 BD7 LYS 1   17  SER 1   26  1                                  10    
HELIX  269 BD8 LEU 1   49  MET 1   61  1                                  13    
HELIX  270 BD9 GLY 2   29  PHE 2   45  1                                  17    
HELIX  271 BE1 LEU 2   51  LEU 2   62  1                                  12    
HELIX  272 BE2 LYS 2   77  GLU 2   84  1                                   8    
HELIX  273 BE3 GLU 2   85  LEU 2  101  1                                  17    
HELIX  274 BE4 LEU 2  118  TRP 2  129  1                                  12    
HELIX  275 BE5 TRP 2  129  HIS 2  141  1                                  13    
HELIX  276 BE6 LEU 2  160  GLN 2  177  1                                  18    
HELIX  277 BE7 SER 2  180  MET 2  185  1                                   6    
HELIX  278 BE8 SER 2  187  ALA 2  199  1                                  13    
HELIX  279 BE9 PHE 2  203  GLN 2  221  1                                  19    
HELIX  280 BF1 MET 2  228  ILE 2  233  1                                   6    
HELIX  281 BF2 LEU 2  234  PHE 2  238  5                                   5    
HELIX  282 BF3 GLN 2  239  ASP 2  248  1                                  10    
HELIX  283 BF4 VAL 2  251  PHE 2  268  1                                  18    
HELIX  284 BF5 GLN 2  390  ASP 2  399  1                                  10    
HELIX  285 BF6 GLN 2  415  LEU 2  428  1                                  14    
HELIX  286 BF7 HIS 2  448  LYS 2  456  1                                   9    
HELIX  287 BF8 ILE 3   20  GLN 3   25  1                                   6    
HELIX  288 BF9 LEU 3   34  ASN 3   52  1                                  19    
HELIX  289 BG1 LYS 3  100  GLU 3  102  5                                   3    
HELIX  290 BG2 LEU 3  103  MET 3  119  1                                  17    
HELIX  291 BG3 ILE 3  124  HIS 3  128  5                                   5    
HELIX  292 BG4 LEU 3  132  ASN 3  154  1                                  23    
HELIX  293 BG5 GLN 3  173  ASN 3  188  1                                  16    
HELIX  294 BG6 SER 3  200  GLY 3  211  1                                  12    
HELIX  295 BG7 GLN 3  219  PRO 3  221  5                                   3    
HELIX  296 BG8 SER 3  222  PHE 3  231  1                                  10    
SHEET    1 AA1 3 SER A1448  ASP A1449  0                                        
SHEET    2 AA1 3 ARG A  20  GLN A  22 -1  N  VAL A  21   O  ASP A1449           
SHEET    3 AA1 3 ARG B1170  MET B1172 -1  O  MET B1172   N  ARG A  20           
SHEET    1 AA2 2 GLY A  86  PHE A  95  0                                        
SHEET    2 AA2 2 ILE A 249  VAL A 255 -1  O  VAL A 250   N  VAL A  94           
SHEET    1 AA3 2 ARG A 192  SER A 194  0                                        
SHEET    2 AA3 2 GLU A 197  TYR A 199 -1  O  GLU A 197   N  SER A 194           
SHEET    1 AA4 3 ARG A 334  PRO A 335  0                                        
SHEET    2 AA4 3 ALA A 328  GLN A 330 -1  N  GLN A 330   O  ARG A 334           
SHEET    3 AA4 3 MET M  83  ILE M  84 -1  O  MET M  83   N  MET A 329           
SHEET    1 AA5 2 ARG A 358  VAL A 359  0                                        
SHEET    2 AA5 2 LEU B1084  ARG B1085 -1  O  LEU B1084   N  VAL A 359           
SHEET    1 AA6 8 HIS B1060  ARG B1062  0                                        
SHEET    2 AA6 8 SER A 362  PRO A 369 -1  N  ARG A 364   O  HIS B1060           
SHEET    3 AA6 8 GLU A 500  HIS A 504 -1  O  LEU A 503   N  ALA A 363           
SHEET    4 AA6 8 ILE A 455  ASN A 459 -1  N  ASN A 459   O  ASN A 502           
SHEET    5 AA6 8 MET A 469  LEU A 477 -1  O  HIS A 472   N  VAL A 456           
SHEET    6 AA6 8 GLN A 377  PRO A 381  1  N  VAL A 378   O  ARG A 473           
SHEET    7 AA6 8 PHE A 482  LEU A 484 -1  O  ARG A 483   N  GLY A 379           
SHEET    8 AA6 8 SER A 362  PRO A 369  1  N  THR A 368   O  PHE A 482           
SHEET    1 AA7 4 THR A 389  ILE A 393  0                                        
SHEET    2 AA7 4 LYS A 445  HIS A 449 -1  O  VAL A 446   N  GLU A 392           
SHEET    3 AA7 4 ALA A 416  ILE A 420 -1  N  ILE A 420   O  LYS A 445           
SHEET    4 AA7 4 ARG A 426  ASP A 428 -1  O  ILE A 427   N  ILE A 419           
SHEET    1 AA8 2 PHE A 554  LEU A 555  0                                        
SHEET    2 AA8 2 TRP A 586  THR A 587 -1  O  TRP A 586   N  LEU A 555           
SHEET    1 AA910 ILE A 579  LYS A 581  0                                        
SHEET    2 AA910 TYR H  90  GLU H 100 -1  O  VAL H  91   N  LEU A 580           
SHEET    3 AA910 VAL H 141  LYS H 146 -1  O  MET H 145   N  TYR H  90           
SHEET    4 AA910 LYS H  55  ALA H  61 -1  N  VAL H  59   O  LEU H 144           
SHEET    5 AA910 ILE H   4  ASP H  14 -1  N  PHE H  10   O  PHE H  56           
SHEET    6 AA910 VAL H  25  SER H  32 -1  O  HIS H  29   N  ASP H  14           
SHEET    7 AA910 ASP H  38  ASN H  44 -1  O  LEU H  41   N  LEU H  28           
SHEET    8 AA910 LEU H 121  GLY H 127 -1  O  GLN H 126   N  ASP H  38           
SHEET    9 AA910 LEU H 112  TYR H 118 -1  N  TYR H 118   O  LEU H 121           
SHEET   10 AA910 TYR H  90  GLU H 100 -1  N  LYS H  95   O  SER H 117           
SHEET    1 AB1 2 VAL A 629  GLU A 631  0                                        
SHEET    2 AB1 2 GLU A 634  MET A 637 -1  O  GLU A 634   N  GLU A 631           
SHEET    1 AB2 3 MET A 872  VAL A 873  0                                        
SHEET    2 AB2 3 VAL A 879  ARG A 880 -1  O  ARG A 880   N  MET A 872           
SHEET    3 AB2 3 VAL A 886  GLN A 888 -1  O  VAL A 887   N  VAL A 879           
SHEET    1 AB3 2 VAL A 901  ASN A 905  0                                        
SHEET    2 AB3 2 LYS A 976  PRO A 980 -1  O  VAL A 977   N  GLN A 904           
SHEET    1 AB4 4 MET A1309  GLN A1313  0                                        
SHEET    2 AB4 4 GLU A1333  THR A1338 -1  O  GLU A1337   N  MET A1309           
SHEET    3 AB4 4 LEU A1139  PHE A1142 -1  N  VAL A1141   O  LEU A1336           
SHEET    4 AB4 4 THR A1358  SER A1359 -1  O  THR A1358   N  THR A1140           
SHEET    1 AB5 5 LEU A1243  PHE A1247  0                                        
SHEET    2 AB5 5 LEU A1255  ILE A1261 -1  O  ARG A1260   N  ASN A1244           
SHEET    3 AB5 5 TRP A1210  LEU A1216 -1  N  LEU A1212   O  ILE A1259           
SHEET    4 AB5 5 THR A1170  TYR A1177 -1  N  ALA A1174   O  ARG A1213           
SHEET    5 AB5 5 CYS I  52  ASN I  56 -1  O  ASN I  56   N  THR A1173           
SHEET    1 AB6 2 ILE A1320  ILE A1322  0                                        
SHEET    2 AB6 2 PHE A1328  ALA A1330 -1  O  LYS A1329   N  ILE A1321           
SHEET    1 AB7 7 GLU D  30  THR D  31  0                                        
SHEET    2 AB7 7 PHE G   2  LEU G  13 -1  O  HIS G   4   N  GLU D  30           
SHEET    3 AB7 7 VAL G  66  PHE G  77 -1  O  TYR G  72   N  LEU G   7           
SHEET    4 AB7 7 GLY G  57  ILE G  59 -1  N  VAL G  58   O  LEU G  67           
SHEET    5 AB7 7 PHE A1471  LEU A1475 -1  N  LEU A1473   O  ILE G  59           
SHEET    6 AB7 7 ILE F 104  TYR F 109 -1  O  ILE F 105   N  LEU A1474           
SHEET    7 AB7 7 TYR F 115  GLY F 119 -1  O  TRP F 118   N  ILE F 106           
SHEET    1 AB8 5 GLU D  30  THR D  31  0                                        
SHEET    2 AB8 5 PHE G   2  LEU G  13 -1  O  HIS G   4   N  GLU D  30           
SHEET    3 AB8 5 VAL G  66  PHE G  77 -1  O  TYR G  72   N  LEU G   7           
SHEET    4 AB8 5 GLY G  43  ILE G  54 -1  N  ASN G  53   O  LYS G  71           
SHEET    5 AB8 5 CYS G  38  THR G  39 -1  N  THR G  39   O  GLY G  43           
SHEET    1 AB9 4 ILE B  65  GLN B  68  0                                        
SHEET    2 AB9 4 ARG B  83  LEU B  93 -1  O  LEU B  86   N  ILE B  65           
SHEET    3 AB9 4 SER B 121  THR B 131 -1  O  TYR B 125   N  TYR B  92           
SHEET    4 AB9 4 THR B 142  PRO B 153 -1  O  ILE B 152   N  ALA B 122           
SHEET    1 AC1 2 THR B  97  TRP B  99  0                                        
SHEET    2 AC1 2 PRO B 105  PRO B 107 -1  O  SER B 106   N  HIS B  98           
SHEET    1 AC2 3 PHE B 185  ILE B 187  0                                        
SHEET    2 AC2 3 SER B 190  LEU B 194 -1  O  SER B 190   N  ILE B 187           
SHEET    3 AC2 3 SER B 467  VAL B 469 -1  O  GLN B 468   N  VAL B 193           
SHEET    1 AC3 4 LYS B 391  ASP B 394  0                                        
SHEET    2 AC3 4 ALA B 196  MET B 200 -1  N  GLN B 197   O  ASP B 394           
SHEET    3 AC3 4 ARG B 484  ASN B 486  1  O  ASN B 486   N  ALA B 196           
SHEET    4 AC3 4 VAL B 523  ASN B 525 -1  O  LYS B 524   N  LEU B 485           
SHEET    1 AC4 5 TYR B 206  PHE B 208  0                                        
SHEET    2 AC4 5 TYR B 215  ARG B 222 -1  O  THR B 218   N  PHE B 208           
SHEET    3 AC4 5 THR B 234  LEU B 240 -1  O  VAL B 237   N  GLY B 219           
SHEET    4 AC4 5 ARG B 255  THR B 259 -1  O  VAL B 257   N  SER B 238           
SHEET    5 AC4 5 VAL B 267  PRO B 268 -1  O  VAL B 267   N  ALA B 258           
SHEET    1 AC5 3 TYR B 531  ILE B 532  0                                        
SHEET    2 AC5 3 ILE B 621  GLU B 629 -1  O  CYS B 622   N  TYR B 531           
SHEET    3 AC5 3 VAL B 662  ASP B 666 -1  O  GLU B 663   N  LEU B 625           
SHEET    1 AC6 4 LYS B 632  LEU B 633  0                                        
SHEET    2 AC6 4 ILE B 621  GLU B 629 -1  N  GLU B 629   O  LYS B 632           
SHEET    3 AC6 4 HIS B 695  CYS B 696 -1  O  CYS B 696   N  LEU B 626           
SHEET    4 AC6 4 LEU B 675  ALA B 676  1  N  ALA B 676   O  HIS B 695           
SHEET    1 AC7 5 GLU B 551  ASN B 552  0                                        
SHEET    2 AC7 5 CYS B 572  HIS B 577 -1  O  ILE B 576   N  GLU B 551           
SHEET    3 AC7 5 THR B 565  VAL B 569 -1  N  THR B 565   O  HIS B 577           
SHEET    4 AC7 5 GLU B 611  TYR B 615  1  O  ILE B 612   N  PHE B 568           
SHEET    5 AC7 5 SER B 602  ARG B 605 -1  N  ILE B 604   O  ARG B 613           
SHEET    1 AC8 5 LEU B 747  LEU B 751  0                                        
SHEET    2 AC8 5 SER B 808  GLN B 817 -1  O  TYR B 811   N  ALA B 748           
SHEET    3 AC8 5 LYS B 917  ARG B 927 -1  O  SER B 925   N  PHE B 810           
SHEET    4 AC8 5 THR B 901  LEU B 911 -1  N  THR B 910   O  PHE B 918           
SHEET    5 AC8 5 ARG B 859  SER B 861 -1  N  VAL B 860   O  GLY B 902           
SHEET    1 AC9 5 LEU B 747  LEU B 751  0                                        
SHEET    2 AC9 5 SER B 808  GLN B 817 -1  O  TYR B 811   N  ALA B 748           
SHEET    3 AC9 5 LYS B 917  ARG B 927 -1  O  SER B 925   N  PHE B 810           
SHEET    4 AC9 5 THR B 901  LEU B 911 -1  N  THR B 910   O  PHE B 918           
SHEET    5 AC9 5 MET L  44  TYR L  45 -1  O  MET L  44   N  VAL B 909           
SHEET    1 AD1 2 VAL B 759  THR B 760  0                                        
SHEET    2 AD1 2 GLY B 997  ASP B 998  1  O  GLY B 997   N  THR B 760           
SHEET    1 AD2 8 ASN B1025  GLU B1026  0                                        
SHEET    2 AD2 8 ILE B1041  ARG B1050 -1  O  ILE B1041   N  GLU B1026           
SHEET    3 AD2 8 LYS B 934  SER B 937 -1  N  ALA B 936   O  GLN B1049           
SHEET    4 AD2 8 GLN B 941  TYR B 949 -1  O  GLY B 943   N  PHE B 935           
SHEET    5 AD2 8 SER B 793  ASN B 797  1  N  MET B 796   O  TYR B 949           
SHEET    6 AD2 8 ILE B 965  ILE B 967 -1  O  ILE B 966   N  ILE B 795           
SHEET    7 AD2 8 ILE B 776  ILE B 782  1  N  ALA B 781   O  ILE B 965           
SHEET    8 AD2 8 ILE B1041  ARG B1050 -1  O  THR B1046   N  SER B 778           
SHEET    1 AD3 3 GLU B 826  PHE B 829  0                                        
SHEET    2 AD3 3 LYS B 869  THR B 872 -1  O  THR B 872   N  GLU B 826           
SHEET    3 AD3 3 LYS B 889  ASP B 891 -1  O  ARG B 890   N  VAL B 871           
SHEET    1 AD4 2 PHE B 956  THR B 957  0                                        
SHEET    2 AD4 2 LEU B1028  TYR B1029 -1  O  TYR B1029   N  PHE B 956           
SHEET    1 AD5 2 TYR B1114  CYS B1119  0                                        
SHEET    2 AD5 2 ILE B1146  MET B1151 -1  O  VAL B1149   N  VAL B1116           
SHEET    1 AD6 4 THR C   8  LEU C  14  0                                        
SHEET    2 AD6 4 ASN C  18  GLU C  24 -1  O  ILE C  22   N  ARG C  10           
SHEET    3 AD6 4 PHE C 229  SER C 235 -1  O  VAL C 233   N  VAL C  19           
SHEET    4 AD6 4 THR C 179  TYR C 186 -1  N  GLU C 185   O  TYR C 230           
SHEET    1 AD7 5 ILE C 121  SER C 122  0                                        
SHEET    2 AD7 5 VAL C  99  ARG C 106 -1  N  THR C 102   O  ILE C 121           
SHEET    3 AD7 5 GLU C 158  PHE C 169 -1  O  LEU C 159   N  VAL C 105           
SHEET    4 AD7 5 PRO C  43  ASN C  55 -1  N  GLN C  51   O  ARG C 162           
SHEET    5 AD7 5 VAL L  54  PHE L  55 -1  O  PHE L  55   N  VAL C  50           
SHEET    1 AD8 2 ARG C 113  THR C 116  0                                        
SHEET    2 AD8 2 LEU C 149  LEU C 153 -1  O  LEU C 153   N  ARG C 113           
SHEET    1 AD9 4 VAL E  60  VAL E  62  0                                        
SHEET    2 AD9 4 MET E  72  PHE E  75 -1  O  MET E  72   N  VAL E  62           
SHEET    3 AD9 4 ARG E 101  VAL E 106  1  O  LEU E 103   N  PHE E  73           
SHEET    4 AD9 4 ILE E 126  LEU E 131  1  O  PHE E 130   N  ILE E 104           
SHEET    1 AE1 2 LYS E  81  VAL E  82  0                                        
SHEET    2 AE1 2 GLY E 109  MET E 110  1  O  GLY E 109   N  VAL E  82           
SHEET    1 AE2 4 GLU E 147  VAL E 150  0                                        
SHEET    2 AE2 4 VAL E 190  PRO E 196 -1  O  LYS E 192   N  VAL E 149           
SHEET    3 AE2 4 ARG E 202  GLN E 210 -1  O  THR E 205   N  ILE E 193           
SHEET    4 AE2 4 ARG E 172  GLN E 174  1  N  ILE E 173   O  GLN E 210           
SHEET    1 AE3 2 TYR F  56  MET F  57  0                                        
SHEET    2 AE3 2 ILE F 124  ILE F 125  1  O  ILE F 124   N  MET F  57           
SHEET    1 AE4 6 VAL G  84  ASN G  93  0                                        
SHEET    2 AE4 6 GLY G  96  ILE G 101 -1  O  PHE G  98   N  THR G  90           
SHEET    3 AE4 6 MET G 104  SER G 109 -1  O  ILE G 108   N  LEU G  97           
SHEET    4 AE4 6 ASP G 156  SER G 162  1  O  ALA G 159   N  SER G 105           
SHEET    5 AE4 6 GLU G 142  ASP G 153 -1  N  ASP G 153   O  ASP G 156           
SHEET    6 AE4 6 VAL G  84  ASN G  93 -1  N  ALA G  87   O  ILE G 143           
SHEET    1 AE5 3 MET G 117  ASP G 120  0                                        
SHEET    2 AE5 3 CYS G 127  THR G 130 -1  O  LYS G 129   N  GLU G 118           
SHEET    3 AE5 3 VAL G 136  ILE G 137 -1  O  ILE G 137   N  TYR G 128           
SHEET    1 AE6 3 TYR I  25  ASP I  29  0                                        
SHEET    2 AE6 3 ILE I  34  ALA I  38 -1  O  LEU I  36   N  LYS I  27           
SHEET    3 AE6 3 GLN I  45  GLU I  47 -1  O  GLN I  46   N  TYR I  37           
SHEET    1 AE7 4 ARG I  80  THR I  81  0                                        
SHEET    2 AE7 4 ALA I  94  GLN I  98 -1  O  ALA I  94   N  THR I  81           
SHEET    3 AE7 4 LEU I 110  CYS I 114 -1  O  VAL I 113   N  VAL I  95           
SHEET    4 AE7 4 ARG I 122  THR I 124 -1  O  TRP I 123   N  TYR I 112           
SHEET    1 AE8 4 ILE K  19  LYS K  23  0                                        
SHEET    2 AE8 4 ALA K  30  ASN K  36 -1  O  LEU K  32   N  ASN K  22           
SHEET    3 AE8 4 LYS K  70  THR K  77 -1  O  ILE K  71   N  ILE K  35           
SHEET    4 AE8 4 VAL K  56  LYS K  62 -1  N  GLY K  60   O  ARG K  74           
SHEET    1 AE9 2 VAL M  24  ASP M  26  0                                        
SHEET    2 AE9 2 ASP M  31  ILE M  33 -1  O  ILE M  33   N  VAL M  24           
SHEET    1 AF116 LEU P 291  MET P 295  0                                        
SHEET    2 AF116 ILE P 300  ILE P 304 -1  O  LEU P 302   N  TYR P 293           
SHEET    3 AF116 LYS P 309  ALA P 315 -1  O  THR P 313   N  VAL P 301           
SHEET    4 AF116 LYS P 254  ASP P 263 -1  N  GLY P 260   O  LEU P 312           
SHEET    5 AF116 GLN P 164  ASN P 173 -1  N  VAL P 169   O  GLN P 256           
SHEET    6 AF116 LYS P 218  THR P 222 -1  O  MET P 219   N  VAL P 172           
SHEET    7 AF116 THR P 209  ILE P 213 -1  N  LEU P 212   O  VAL P 220           
SHEET    8 AF116 VAL P 200  ILE P 204 -1  N  MET P 202   O  ALA P 211           
SHEET    9 AF116 ALA P 190  TYR P 192 -1  N  GLU P 191   O  ILE P 201           
SHEET   10 AF116 ARG O  55  CYS O  68  1  N  PHE O  67   O  TYR P 192           
SHEET   11 AF116 VAL O  71  GLU O  83 -1  O  THR O  73   N  ARG O  66           
SHEET   12 AF116 GLU O  86  CYS O  98 -1  O  ALA O  97   N  TRP O  72           
SHEET   13 AF116 ASN N 333  SER N 345  1  N  CYS N 337   O  VAL O  96           
SHEET   14 AF116 LYS N 348  LEU N 360 -1  O  LYS N 348   N  SER N 345           
SHEET   15 AF116 ARG N 363  GLU N 375 -1  O  ALA N 370   N  LEU N 353           
SHEET   16 AF116 ARG O  55  CYS O  68  1  O  LEU O  62   N  GLU N 375           
SHEET    1 AF2 2 ILE Q  72  MET Q  76  0                                        
SHEET    2 AF2 2 ILE Q  94  THR Q  98 -1  O  ASN Q  95   N  ARG Q  75           
SHEET    1 AF3 2 PHE Q 145  ASP Q 146  0                                        
SHEET    2 AF3 2 THR Q 151  PHE Q 152 -1  O  THR Q 151   N  ASP Q 146           
SHEET    1 AF4 2 GLU R 131  ILE R 133  0                                        
SHEET    2 AF4 2 LYS R 136  ALA R 138 -1  O  ALA R 138   N  GLU R 131           
SHEET    1 AF5 3 GLY R 165  ILE R 166  0                                        
SHEET    2 AF5 3 LEU R 201  ASN R 204 -1  O  PHE R 202   N  GLY R 165           
SHEET    3 AF5 3 ILE R 189  VAL R 192 -1  N  VAL R 192   O  LEU R 201           
SHEET    1 AF614 ALA S  45  ARG S  49  0                                        
SHEET    2 AF614 TRP S  98  VAL S 102 -1  O  ARG S 101   N  ARG S  46           
SHEET    3 AF614 LYS S 109  LYS S 114 -1  O  GLY S 112   N  TRP S  98           
SHEET    4 AF614 ASN S 142  LEU S 149 -1  O  ASN S 145   N  ILE S 113           
SHEET    5 AF614 LYS S  24  ASN S  32  1  N  ALA S  30   O  PHE S 146           
SHEET    6 AF614 GLN T  91  SER T  99 -1  O  THR T  94   N  MET S  29           
SHEET    7 AF614 LEU T 104  CYS T 116 -1  O  GLY T 108   N  VAL T  95           
SHEET    8 AF614 GLY T  17  PRO T  24  1  N  LEU T  20   O  GLN T 112           
SHEET    9 AF614 THR S 122  GLN S 129 -1  N  PHE S 127   O  TRP T  19           
SHEET   10 AF614 PHE S 135  PRO S 139 -1  O  GLU S 136   N  THR S 128           
SHEET   11 AF614 ASN S  10  ARG S  17  1  N  VAL S  15   O  PHE S 135           
SHEET   12 AF614 GLY T  41  THR T  48 -1  O  LYS T  47   N  ASN S  10           
SHEET   13 AF614 ARG T  51  LEU T  58 -1  O  GLU T  53   N  ALA T  46           
SHEET   14 AF614 HIS T  81  GLN T  86 -1  O  HIS T  81   N  PHE T  56           
SHEET    1 AF7 8 ALA S  45  ARG S  49  0                                        
SHEET    2 AF7 8 TRP S  98  VAL S 102 -1  O  ARG S 101   N  ARG S  46           
SHEET    3 AF7 8 LYS S 109  LYS S 114 -1  O  GLY S 112   N  TRP S  98           
SHEET    4 AF7 8 ASN S 142  LEU S 149 -1  O  ASN S 145   N  ILE S 113           
SHEET    5 AF7 8 LYS S  24  ASN S  32  1  N  ALA S  30   O  PHE S 146           
SHEET    6 AF7 8 GLN T  91  SER T  99 -1  O  THR T  94   N  MET S  29           
SHEET    7 AF7 8 LEU T 104  CYS T 116 -1  O  GLY T 108   N  VAL T  95           
SHEET    8 AF7 8 LEU T   7  ASP T   8  1  N  ASP T   8   O  LEU T 106           
SHEET    1 AF8 3 TYR T 197  ASN T 198  0                                        
SHEET    2 AF8 3 LYS T 230  GLU T 234 -1  O  TRP T 233   N  TYR T 197           
SHEET    3 AF8 3 VAL T 222  LYS T 226 -1  N  ASN T 224   O  THR T 232           
SHEET    1 AF9 3 PHE V 251  GLU V 253  0                                        
SHEET    2 AF9 3 ASP V 256  GLU V 259 -1  O  ASP V 256   N  GLU V 253           
SHEET    3 AF9 3 ILE V 277  LEU V 280 -1  O  ILE V 277   N  GLU V 259           
SHEET    1 AG1 6 ALA V 406  THR V 409  0                                        
SHEET    2 AG1 6 CYS V 361  GLY V 365  1  N  VAL V 363   O  SER V 408           
SHEET    3 AG1 6 LEU V 437  ASP V 441  1  O  ILE V 439   N  LEU V 364           
SHEET    4 AG1 6 CYS V 462  THR V 467  1  O  LEU V 464   N  MET V 438           
SHEET    5 AG1 6 VAL V 337  VAL V 339  1  N  ILE V 338   O  GLY V 465           
SHEET    6 AG1 6 LYS V 487  TYR V 489  1  O  LEU V 488   N  VAL V 337           
SHEET    1 AG2 2 ILE V 389  CYS V 390  0                                        
SHEET    2 AG2 2 ILE V 401  GLY V 402  1  O  ILE V 401   N  CYS V 390           
SHEET    1 AG3 7 TYR V 579  ILE V 580  0                                        
SHEET    2 AG3 7 THR V 604  ILE V 607  1  O  PHE V 606   N  ILE V 580           
SHEET    3 AG3 7 ILE V 558  PHE V 561  1  N  VAL V 560   O  ILE V 605           
SHEET    4 AG3 7 VAL V 622  GLN V 625  1  O  ILE V 624   N  PHE V 561           
SHEET    5 AG3 7 ALA V 657  SER V 664  1  O  TYR V 660   N  GLN V 625           
SHEET    6 AG3 7 VAL V 505  CYS V 512  1  N  VAL V 510   O  SER V 661           
SHEET    7 AG3 7 PHE V 687  ILE V 690  1  O  ILE V 690   N  GLU V 509           
SHEET    1 AG4 2 GLY W  38  GLU W  41  0                                        
SHEET    2 AG4 2 VAL W 476  ALA W 479  1  O  VAL W 476   N  VAL W  39           
SHEET    1 AG5 5 GLY W 106  ALA W 108  0                                        
SHEET    2 AG5 5 VAL W 204  SER W 208  1  O  VAL W 206   N  LEU W 107           
SHEET    3 AG5 5 LYS W  69  SER W  74  1  N  TYR W  72   O  VAL W 205           
SHEET    4 AG5 5 ALA W 229  ASP W 234  1  O  VAL W 230   N  LYS W  69           
SHEET    5 AG5 5 GLN W 452  THR W 457  1  O  SER W 453   N  VAL W 231           
SHEET    1 AG6 3 VAL W 249  LEU W 251  0                                        
SHEET    2 AG6 3 ILE W 432  SER W 436 -1  O  LEU W 433   N  LEU W 251           
SHEET    3 AG6 3 THR W 415  GLU W 419 -1  N  ILE W 417   O  HIS W 434           
SHEET    1 AG7 3 CYS W 489  LEU W 490  0                                        
SHEET    2 AG7 3 GLY W 675  ALA W 680  1  O  MET W 677   N  LEU W 490           
SHEET    3 AG7 3 MET W 493  ILE W 494  1  N  ILE W 494   O  PHE W 679           
SHEET    1 AG8 5 CYS W 489  LEU W 490  0                                        
SHEET    2 AG8 5 GLY W 675  ALA W 680  1  O  MET W 677   N  LEU W 490           
SHEET    3 AG8 5 ALA W 617  PHE W 621  1  N  VAL W 618   O  VAL W 678           
SHEET    4 AG8 5 ILE W 535  PHE W 539  1  N  PHE W 538   O  PHE W 621           
SHEET    5 AG8 5 LEU W 596  VAL W 599  1  O  LEU W 596   N  ALA W 537           
SHEET    1 AG9 6 ARG 0 113  SER 0 121  0                                        
SHEET    2 AG9 6 SER 0 102  LYS 0 110 -1  N  VAL 0 108   O  GLU 0 115           
SHEET    3 AG9 6 ARG 0  59  ASP 0  66  1  N  ARG 0  59   O  GLN 0 103           
SHEET    4 AG9 6 SER 0 164  PHE 0 171  1  O  GLU 0 166   N  TYR 0  62           
SHEET    5 AG9 6 ILE 0 194  LEU 0 201  1  O  ILE 0 199   N  ILE 0 169           
SHEET    6 AG9 6 THR 0 218  ILE 0 222  1  O  HIS 0 220   N  GLY 0 200           
SHEET    1 AH1 6 ILE 1  35  ASP 1  37  0                                        
SHEET    2 AH1 6 VAL 1  43  ILE 1  46 -1  O  VAL 1  45   N  ASP 1  37           
SHEET    3 AH1 6 VAL 1   4  CYS 1  12 -1  N  GLU 1  11   O  PHE 1  44           
SHEET    4 AH1 6 GLU 2 405  GLN 2 411 -1  O  VAL 2 407   N  VAL 1   8           
SHEET    5 AH1 6 VAL 2 442  PRO 2 445 -1  O  THR 2 444   N  LEU 2 408           
SHEET    6 AH1 6 GLU 2 434  ASN 2 435 -1  N  GLU 2 434   O  VAL 2 443           
SHEET    1 AH2 6 SER 3  67  TYR 3  71  0                                        
SHEET    2 AH2 6 ASN 3  55  SER 3  62 -1  N  ALA 3  61   O  ARG 3  68           
SHEET    3 AH2 6 LEU 3   8  ASP 3  16  1  N  VAL 3  15   O  ILE 3  60           
SHEET    4 AH2 6 MET 3 157  LYS 3 165  1  O  LEU 3 162   N  VAL 3  14           
SHEET    5 AH2 6 ILE 3 191  VAL 3 195  1  O  ASP 3 192   N  ILE 3 161           
SHEET    6 AH2 6 TYR 3 214  LYS 3 216  1  O  LEU 3 215   N  VAL 3 195           
SSBOND   1 CYS A   71    CYS A   81                          1555   1555  2.95  
SSBOND   2 CYS A  111    CYS A  154                          1555   1555  2.95  
CISPEP   1 GLN A  461    PRO A  462          0        -0.65                     
CISPEP   2 LYS A  581    PRO A  582          0        10.81                     
SITE     1 AC1  4 ASP A 495  ASP A 497  ASP A 499    C Z   6                    
SITE     1 AC2  2 ALA A 494  ASP A 495                                          
SITE     1 AC3  4 CYS A  71  CYS A  74  CYS A  81  HIS A  84                    
SITE     1 AC4  4 CYS A 111  CYS A 114  CYS A 154  CYS A 184                    
SITE     1 AC5  4 CYS B1119  CYS B1122  CYS B1137  CYS B1140                    
SITE     1 AC6  4 CYS C  88  CYS C  90  CYS C  94  CYS C  97                    
SITE     1 AC7  6 CYS I  17  GLU I  19  CYS I  20  CYS I  39                    
SITE     2 AC7  6 ASN I  41  CYS I  42                                          
SITE     1 AC8  4 CYS I  86  CYS I  89  CYS I 114  CYS I 119                    
SITE     1 AC9  4 CYS J   7  CYS J  10  CYS J  44  CYS J  45                    
SITE     1 AD1  4 CYS L  19  CYS L  22  CYS L  36  CYS L  39                    
SITE     1 AD2  5 CYS M  15  HIS M  18  CYS M  34  CYS M  37                    
SITE     2 AD2  5 LEU M  39                                                     
SITE     1 AD3  4 CYS Q 129  CYS Q 132  CYS Q 154  CYS Q 157                    
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           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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