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Database: PDB
Entry: 5IYD
LinkDB: 5IYD
Original site: 5IYD 
HEADER    TRANSCRIPTION, TRANSFERASE/DNA/RNA      24-MAR-16   5IYD              
TITLE     HUMAN CORE-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: SCP-X;                                                     
COMPND 127 CHAIN: X;                                                            
COMPND 128 ENGINEERED: YES;                                                     
COMPND 129 MOL_ID: 22;                                                          
COMPND 130 MOLECULE: SCP-Y;                                                     
COMPND 131 CHAIN: Y;                                                            
COMPND 132 ENGINEERED: YES;                                                     
COMPND 133 MOL_ID: 23;                                                          
COMPND 134 MOLECULE: RNA;                                                       
COMPND 135 CHAIN: Z;                                                            
COMPND 136 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 SYNTHETIC: YES;                                                      
SOURCE 107 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 108 ORGANISM_COMMON: HUMAN;                                              
SOURCE 109 ORGANISM_TAXID: 9606;                                                
SOURCE 110 MOL_ID: 22;                                                          
SOURCE 111 SYNTHETIC: YES;                                                      
SOURCE 112 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 113 ORGANISM_COMMON: HUMAN;                                              
SOURCE 114 ORGANISM_TAXID: 9606;                                                
SOURCE 115 MOL_ID: 23;                                                          
SOURCE 116 SYNTHETIC: YES;                                                      
SOURCE 117 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 118 ORGANISM_COMMON: HUMAN;                                              
SOURCE 119 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 5IYD    1       REMARK                                   
REVDAT   4   13-SEP-17 5IYD    1       JRNL                                     
REVDAT   3   22-JUN-16 5IYD    1       JRNL                                     
REVDAT   2   25-MAY-16 5IYD    1       JRNL                                     
REVDAT   1   18-MAY-16 5IYD    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.    3.90 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)  : 3.900                          
REMARK   3   NUMBER OF PARTICLES               : 99929                          
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 5IYD 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_1000219640.                                   
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 CORE-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: 23-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, 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   C    VAL Q   131    ZN     ZN Q   501              0.53            
REMARK 500   SG   CYS A   111    ZN     ZN A  2004              0.65            
REMARK 500   CB   CYS I    17    ZN     ZN I   201              0.75            
REMARK 500   OE1  GLN B    90     CG   LEU T   141              0.91            
REMARK 500   CA   CYS I    17    ZN     ZN I   201              0.93            
REMARK 500   N    ALA M    21    ZN     ZN M   401              1.03            
REMARK 500   CA   VAL J    14    ZN     ZN J   101              1.05            
REMARK 500   CZ   PHE Q   180     CA   ASP R   213              1.05            
REMARK 500   N    VAL J    14    ZN     ZN J   101              1.10            
REMARK 500   CD2  LEU T   141     NE2  GLN T   143              1.15            
REMARK 500   O    VAL Q   131    ZN     ZN Q   501              1.19            
REMARK 500   CA   ALA M    21    ZN     ZN M   401              1.22            
REMARK 500   C    GLN C     6     CD   PRO C     7              1.23            
REMARK 500   O    GLY P   160     N    VAL P   162              1.26            
REMARK 500   CA   CYS A    71    ZN     ZN A  2003              1.34            
REMARK 500   O    GLU L    38    ZN     ZN L   101              1.34            
REMARK 500   O    SER T   142     N    GLN T   144              1.43            
REMARK 500   N    CYS Q   132    ZN     ZN Q   501              1.44            
REMARK 500   O    ASN A   206     N    ASP A   208              1.45            
REMARK 500   CD2  LEU T   141     CD   GLN T   143              1.45            
REMARK 500   CB   ALA I   116    ZN     ZN I   202              1.46            
REMARK 500   CB   CYS A    71    ZN     ZN A  2003              1.51            
REMARK 500   C    HIS I    84     CD   PRO I    85              1.52            
REMARK 500   CZ   PHE Q   180     CB   ASP R   213              1.52            
REMARK 500   CB   VAL J    14    ZN     ZN J   101              1.52            
REMARK 500   CD1  PHE Q    25     CD1  LEU R   219              1.57            
REMARK 500   OE1  GLN B    90     CB   LEU T   141              1.57            
REMARK 500   O    PRO I    85     O    CYS I    86              1.62            
REMARK 500   CZ   PHE A   458     CB   MET A   501              1.63            
REMARK 500   CE2  PHE Q   180     CB   ASP R   213              1.63            
REMARK 500   CD2  LEU T   141     OE1  GLN T   143              1.64            
REMARK 500   C    ARG R   194     CD   PRO R   195              1.67            
REMARK 500   C    GLU L    38    ZN     ZN L   101              1.68            
REMARK 500   C    GLU P   206     CD   PRO P   207              1.68            
REMARK 500   O    VAL I    62     N    GLU I    64              1.71            
REMARK 500   O    ALA B    74     OG   SER B    75              1.72            
REMARK 500   O    THR B   883     N    ARG B   885              1.74            
REMARK 500   OD2  ASP M    94     O    GLY M    97              1.75            
REMARK 500   O    GLN A   273     O    ASP A   274              1.77            
REMARK 500   OE1  GLN B    90     CD2  LEU T   141              1.77            
REMARK 500   O    SER A   622     N    GLY A   624              1.77            
REMARK 500   O    VAL R   225     OE1  GLU R   230              1.78            
REMARK 500   OG   SER A  1290     O    SER B   250              1.79            
REMARK 500   OH   TYR Q   105     OE1  GLU R   234              1.80            
REMARK 500   CD1  ILE Q   184     OD2  ASP R   213              1.80            
REMARK 500   CE1  PHE Q    25     CD1  LEU R   219              1.82            
REMARK 500   O    LYS M   178     CB   LYS T   154              1.83            
REMARK 500   CD   GLN B    90     CG   LEU T   141              1.83            
REMARK 500   CB   SER A  1290     CB   SER B   250              1.84            
REMARK 500   OD2  ASP A   425     CD1  LEU M    39              1.85            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     106 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     -0.106                       
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    MET A 501   CA  -  CB  -  CG  ANGL. DEV. =  13.7 DEGREES          
REMARK 500    PRO A 610   C   -  N   -  CD  ANGL. DEV. = -25.6 DEGREES          
REMARK 500    ASP A 614   N   -  CA  -  C   ANGL. DEV. =  18.6 DEGREES          
REMARK 500    SER A 622   N   -  CA  -  C   ANGL. DEV. = -24.9 DEGREES          
REMARK 500    PRO A 623   C   -  N   -  CD  ANGL. DEV. = -27.9 DEGREES          
REMARK 500    VAL A1307   N   -  CA  -  C   ANGL. DEV. =  18.4 DEGREES          
REMARK 500    GLU B 112   OE1 -  CD  -  OE2 ANGL. DEV. = -10.0 DEGREES          
REMARK 500    LEU B 479   CB  -  CG  -  CD2 ANGL. DEV. = -11.9 DEGREES          
REMARK 500    PRO C   7   C   -  N   -  CD  ANGL. DEV. = -76.8 DEGREES          
REMARK 500    ASN C 137   N   -  CA  -  C   ANGL. DEV. = -21.6 DEGREES          
REMARK 500    PRO E  48   C   -  N   -  CD  ANGL. DEV. = -46.4 DEGREES          
REMARK 500    LEU H 148   CA  -  CB  -  CG  ANGL. DEV. =  14.8 DEGREES          
REMARK 500    PRO I  85   C   -  N   -  CA  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    PRO I  85   C   -  N   -  CD  ANGL. DEV. = -63.3 DEGREES          
REMARK 500    ALA I 104   N   -  CA  -  C   ANGL. DEV. = -18.6 DEGREES          
REMARK 500    PRO J  64   C   -  N   -  CD  ANGL. DEV. = -21.0 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    PRO P 207   C   -  N   -  CD  ANGL. DEV. = -55.3 DEGREES          
REMARK 500    ARG R  88   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    PRO R 195   C   -  N   -  CD  ANGL. DEV. = -55.7 DEGREES          
REMARK 500    THR R 224   N   -  CA  -  C   ANGL. DEV. =  19.4 DEGREES          
REMARK 500     DG X  28   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DT X  33   O4' -  C1' -  N1  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DT X  37   O4' -  C1' -  N1  ANGL. DEV. =   4.5 DEGREES          
REMARK 500     DT X  38   O4' -  C1' -  N1  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DT X  49   O4' -  C1' -  N1  ANGL. DEV. =   2.8 DEGREES          
REMARK 500     DG X  52   O4' -  C1' -  N9  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DG Y  39   O4' -  C1' -  N9  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DG Y  43   O4' -  C1' -  N9  ANGL. DEV. =   2.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  12       34.85     33.76                                   
REMARK 500    ASP A  29      -74.83    -66.49                                   
REMARK 500    GLU A  38      -76.11     60.89                                   
REMARK 500    ILE A  41      -15.72    -48.03                                   
REMARK 500    THR A  47      -95.51   -131.78                                   
REMARK 500    GLU A  48       -9.38     77.16                                   
REMARK 500    ARG A  51      -47.62   -132.45                                   
REMARK 500    LEU A  54     -170.59     57.82                                   
REMARK 500    ASP A  59       74.73     43.04                                   
REMARK 500    ARG A  61      -19.65   -167.85                                   
REMARK 500    GLN A  62     -148.49    -76.12                                   
REMARK 500    ILE A  65     -157.76   -128.27                                   
REMARK 500    GLU A  66       37.90     71.05                                   
REMARK 500    ARG A  70      119.39     62.09                                   
REMARK 500    CYS A  71       80.51   -166.51                                   
REMARK 500    GLN A  72     -122.42     62.19                                   
REMARK 500    ALA A  75     -128.26     49.62                                   
REMARK 500    ASN A  77     -159.15   -160.58                                   
REMARK 500    PHE A 113      -42.92     70.87                                   
REMARK 500    SER A 115       -6.09     64.13                                   
REMARK 500    LYS A 132       50.04    -45.27                                   
REMARK 500    SER A 133       -8.80     73.02                                   
REMARK 500    LYS A 134      -30.50     57.56                                   
REMARK 500    ILE A 153       34.27    123.31                                   
REMARK 500    CYS A 154      133.78     -9.81                                   
REMARK 500    GLU A 155     -143.28   -135.30                                   
REMARK 500    CYS A 184       90.86     46.91                                   
REMARK 500    HIS A 204      -66.77    105.72                                   
REMARK 500    GLU A 207      -58.95     35.17                                   
REMARK 500    ASP A 208      -60.19     25.79                                   
REMARK 500    GLN A 210     -168.23     33.38                                   
REMARK 500    LYS A 212       -1.46    116.40                                   
REMARK 500    ARG A 261       75.67   -108.23                                   
REMARK 500    PRO A 262        9.51    -54.29                                   
REMARK 500    VAL A 264      -14.25    -30.01                                   
REMARK 500    VAL A 265      -79.81     38.44                                   
REMARK 500    MET A 266       81.96     41.71                                   
REMARK 500    GLN A 267     -134.81     55.78                                   
REMARK 500    ASP A 274      162.98     -8.31                                   
REMARK 500    ASN A 296     -151.66    -92.10                                   
REMARK 500    LEU A 354      -47.23   -156.84                                   
REMARK 500    PHE A 361       65.34     61.72                                   
REMARK 500    LYS A 434      108.45   -168.63                                   
REMARK 500    ASP A 452       58.87    -68.15                                   
REMARK 500    ASN A 459     -166.73   -160.41                                   
REMARK 500    LYS A 466      -32.82    -31.76                                   
REMARK 500    TRP A 479     -174.02     70.22                                   
REMARK 500    ASP A 495     -153.34   -122.91                                   
REMARK 500    ASP A 497        4.12    -63.11                                   
REMARK 500    ILE A 525      -55.94   -122.74                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     442 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 TYR A 1308     MET A 1309                  137.37                    
REMARK 500 ILE H   99     GLU H  100                  -85.62                    
REMARK 500 ALA Q  125     SER Q  126                 -141.55                    
REMARK 500 PHE R  139     LYS R  140                  -33.84                    
REMARK 500 ASN T  123     TYR T  124                  140.40                    
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    GLN P 242         0.07    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         10.05                                           
REMARK 500    LEU B 873         11.12                                           
REMARK 500    SER I 101         10.44                                           
REMARK 500    LEU R 109        -11.45                                           
REMARK 500    PHE R 139        -12.28                                           
REMARK 500    GLU R 215        -10.82                                           
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 I 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN I 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN J 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN L 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN M 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
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-8138   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-8134   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-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: 5IY9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5IYB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5IYC   RELATED DB: PDB                                   
DBREF  5IYD A    1  1970  UNP    P24928   RPB1_HUMAN       1   1970             
DBREF  5IYD B    1  1174  UNP    P30876   RPB2_HUMAN       1   1174             
DBREF  5IYD C    1   275  UNP    P19387   RPB3_HUMAN       1    275             
DBREF  5IYD D    1   142  UNP    O15514   RPB4_HUMAN       1    142             
DBREF  5IYD E    1   210  UNP    P19388   RPAB1_HUMAN      1    210             
DBREF  5IYD F    1   127  UNP    P61218   RPAB2_HUMAN      1    127             
DBREF  5IYD G    1   172  UNP    P62487   RPB7_HUMAN       1    172             
DBREF  5IYD H    1   150  UNP    P52434   RPAB3_HUMAN      1    150             
DBREF  5IYD I    1   125  UNP    P36954   RPB9_HUMAN       1    125             
DBREF  5IYD J    1    67  UNP    P62875   RPAB5_HUMAN      1     67             
DBREF  5IYD K    1   117  UNP    P52435   RPB11_HUMAN      1    117             
DBREF  5IYD L    1    58  UNP    P53803   RPAB4_HUMAN      1     58             
DBREF  5IYD M    1   316  UNP    Q00403   TF2B_HUMAN       1    316             
DBREF  5IYD N    1   376  UNP    P52655   TF2AA_HUMAN      1    376             
DBREF  5IYD O    1   109  UNP    P52657   T2AG_HUMAN       1    109             
DBREF  5IYD P    1   339  UNP    P20226   TBP_HUMAN        1    339             
DBREF  5IYD Q    1   439  UNP    P29083   T2EA_HUMAN       1    439             
DBREF  5IYD R    1   291  UNP    P29084   T2EB_HUMAN       1    291             
DBREF  5IYD S    1   517  UNP    P35269   T2FA_HUMAN       1    517             
DBREF  5IYD T    1   249  UNP    P13984   T2FB_HUMAN       1    249             
DBREF  5IYD X    1    80  PDB    5IYD     5IYD             1     80             
DBREF  5IYD Y   14    93  PDB    5IYD     5IYD            14     93             
DBREF  5IYD Z    1     6  PDB    5IYD     5IYD             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 X   80   DG  DA  DA  DG  DG  DG  DC  DG  DC  DC  DT  DA  DT          
SEQRES   2 X   80   DA  DA  DA  DA  DG  DG  DG  DG  DG  DT  DG  DG  DG          
SEQRES   3 X   80   DG  DG  DC  DG  DT  DT  DT  DT  DT  DT  DT  DT  DT          
SEQRES   4 X   80   DT  DT  DT  DT  DT  DT  DT  DT  DT  DT  DT  DC  DG          
SEQRES   5 X   80   DA  DA  DC  DA  DC  DT  DC  DG  DA  DG  DC  DC  DG          
SEQRES   6 X   80   DA  DG  DC  DA  DG  DA  DC  DG  DT  DG  DC  DC  DT          
SEQRES   7 X   80   DA  DC                                                      
SEQRES   1 Y   80   DG  DT  DA  DG  DG  DC  DA  DC  DG  DT  DC  DT  DG          
SEQRES   2 Y   80   DC  DT  DC  DG  DG  DC  DT  DC  DG  DA  DG  DT  DG          
SEQRES   3 Y   80   DT  DT  DC  DG  DA  DT  DC  DG  DC  DG  DA  DC  DT          
SEQRES   4 Y   80   DG  DA  DG  DG  DA  DC  DG  DA  DA  DC  DG  DC  DG          
SEQRES   5 Y   80   DC  DC  DC  DC  DC  DA  DC  DC  DC  DC  DC  DT  DT          
SEQRES   6 Y   80   DT  DT  DA  DT  DA  DG  DG  DC  DG  DC  DC  DC  DT          
SEQRES   7 Y   80   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  A2005       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  24   MG    2(MG 2+)                                                     
FORMUL  26   ZN    11(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  ASN A  152  1                                  17    
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 TYR C  208  GLU C  213  5                                   6    
HELIX  116 AM8 ARG C  240  SER C  269  1                                  30    
HELIX  117 AM9 ASP D   16  LEU D   20  5                                   5    
HELIX  118 AN1 PRO D   23  THR D   28  1                                   6    
HELIX  119 AN2 LEU D   33  GLU D   52  1                                  20    
HELIX  120 AN3 SER D   58  PHE D   71  1                                  14    
HELIX  121 AN4 ASN D   76  GLN D   89  1                                  14    
HELIX  122 AN5 HIS D   93  CYS D  104  1                                  12    
HELIX  123 AN6 THR D  107  ILE D  115  1                                   9    
HELIX  124 AN7 PRO D  116  ARG D  121  5                                   6    
HELIX  125 AN8 GLU D  123  ARG D  138  1                                  16    
HELIX  126 AN9 ASP E    2  GLY E   25  1                                  24    
HELIX  127 AO1 THR E   29  ASP E   34  1                                   6    
HELIX  128 AO2 THR E   36  SER E   44  1                                   9    
HELIX  129 AO3 PRO E   53  LEU E   58  1                                   6    
HELIX  130 AO4 GLY E   83  ASN E   98  1                                  16    
HELIX  131 AO5 THR E  111  ALA E  122  1                                  12    
HELIX  132 AO6 GLN E  132  LEU E  136  1                                   5    
HELIX  133 AO7 ASN E  138  HIS E  142  5                                   5    
HELIX  134 AO8 THR E  152  LYS E  164  1                                  13    
HELIX  135 AO9 ARG E  166  LEU E  170  5                                   5    
HELIX  136 AP1 ASP E  177  GLY E  184  1                                   8    
HELIX  137 AP2 THR F   58  ALA F   74  1                                  17    
HELIX  138 AP3 ASP F   88  ARG F  100  1                                  13    
HELIX  139 AP4 HIS G   14  PHE G   18  5                                   5    
HELIX  140 AP5 ASN G   21  GLU G   35  1                                  15    
HELIX  141 AP6 ILE I   69  ASP I   75  5                                   7    
HELIX  142 AP7 VAL J   14  ASN J   16  5                                   3    
HELIX  143 AP8 LYS J   17  GLU J   28  1                                  12    
HELIX  144 AP9 THR J   30  LEU J   38  1                                   9    
HELIX  145 AQ1 ARG J   42  HIS J   52  1                                  11    
HELIX  146 AQ2 LEU J   55  LEU J   60  1                                   6    
HELIX  147 AQ3 PRO K    5  PHE K   10  5                                   6    
HELIX  148 AQ4 ASP K   39  ASP K   53  1                                  15    
HELIX  149 AQ5 SER K   82  ASP K  111  1                                  30    
HELIX  150 AQ6 ASP M   47  TRP M   52  1                                   6    
HELIX  151 AQ7 SER M  108  SER M  110  5                                   3    
HELIX  152 AQ8 ASP M  111  ILE M  128  1                                  18    
HELIX  153 AQ9 PRO M  131  LYS M  149  1                                  19    
HELIX  154 AR1 ALA M  155  GLU M  171  1                                  17    
HELIX  155 AR2 THR M  176  SER M  184  1                                   9    
HELIX  156 AR3 SER M  187  LEU M  202  1                                  16    
HELIX  157 AR4 THR M  211  LEU M  222  1                                  12    
HELIX  158 AR5 PRO M  225  LEU M  242  1                                  18    
HELIX  159 AR6 SER M  249  ALA M  264  1                                  16    
HELIX  160 AR7 THR M  270  GLY M  279  1                                  10    
HELIX  161 AR8 ALA M  281  TYR M  293  1                                  13    
HELIX  162 AR9 ARG M  295  PHE M  300  1                                   6    
HELIX  163 AS1 PRO M  309  LEU M  313  5                                   5    
HELIX  164 AS2 VAL N   10  GLY N   33  1                                  24    
HELIX  165 AS3 ASP N   35  MET N   51  1                                  17    
HELIX  166 AS4 PRO N  313  ASP N  318  5                                   6    
HELIX  167 AS5 TYR O    3  ASN O    8  5                                   6    
HELIX  168 AS6 THR O    9  SER O   25  1                                  17    
HELIX  169 AS7 THR O   29  ARG O   51  1                                  23    
HELIX  170 AS8 THR P  153  GLU P  157  5                                   5    
HELIX  171 AS9 ASP P  179  ALA P  187  1                                   9    
HELIX  172 AT1 ARG P  205  ARG P  208  5                                   4    
HELIX  173 AT2 SER P  226  LYS P  243  1                                  18    
HELIX  174 AT3 ARG P  269  HIS P  277  1                                   9    
HELIX  175 AT4 VAL P  317  PHE P  335  1                                  19    
HELIX  176 AT5 ALA Q   12  TYR Q   26  1                                  15    
HELIX  177 AT6 GLY Q   27  ARG Q   39  1                                  13    
HELIX  178 AT7 LYS Q   44  LYS Q   53  1                                  10    
HELIX  179 AT8 ASP Q   55  ASP Q   69  1                                  15    
HELIX  180 AT9 VAL Q  102  ARG Q  119  1                                  18    
HELIX  181 AU1 THR Q  137  LEU Q  144  1                                   8    
HELIX  182 AU2 ARG Q  174  TYR Q  188  1                                  15    
HELIX  183 AU3 TYR Q  188  GLU Q  202  1                                  15    
HELIX  184 AU4 GLY R   76  GLY R   92  1                                  17    
HELIX  185 AU5 THR R   98  THR R  106  1                                   9    
HELIX  186 AU6 GLY R  112  GLU R  122  1                                  11    
HELIX  187 AU7 GLU R  122  ASN R  127  1                                   6    
HELIX  188 AU8 LEU R  151  ASP R  156  1                                   6    
HELIX  189 AU9 LEU R  167  ALA R  174  1                                   8    
HELIX  190 AV1 PRO R  176  LEU R  185  1                                  10    
HELIX  191 AV2 GLU R  215  VAL R  223  1                                   9    
HELIX  192 AV3 ASP R  229  ARG R  239  1                                  11    
HELIX  193 AV4 ALA S   34  LYS S   36  5                                   3    
HELIX  194 AV5 ASN S   38  TRP S   42  5                                   5    
HELIX  195 AV6 ALA S  160  ARG S  167  1                                   8    
HELIX  196 AV7 HIS S  173  ARG S  180  1                                   8    
HELIX  197 AV8 LEU T    9  ASN T   15  1                                   7    
HELIX  198 AV9 LYS T   25  LYS T   33  1                                   9    
HELIX  199 AW1 ASN T  123  SER T  136  1                                  14    
HELIX  200 AW2 ASN T  158  LYS T  169  1                                  12    
HELIX  201 AW3 ASP T  179  HIS T  194  1                                  16    
HELIX  202 AW4 LEU T  199  LYS T  207  1                                   9    
HELIX  203 AW5 PRO T  209  GLY T  221  1                                  13    
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  ILE A 457   O  HIS A 504           
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 A1333   N  GLN A1313           
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  GLU C  24   N  THR C   8           
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           
SSBOND   1 CYS A   71    CYS A   81                          1555   1555  2.95  
CISPEP   1 GLN A  461    PRO A  462          0        -0.68                     
CISPEP   2 LYS A  581    PRO A  582          0        10.81                     
SITE     1 AC1  4 ASP A 497  GLY A 498  ASP A 499    C Z   6                    
SITE     1 AC2  5 ASP A 495  PHE A 496  ASP A 497  GLU B 791                    
SITE     2 AC2  5 ASP B 792                                                     
SITE     1 AC3  5 ARG A  61  GLN A  62  ARG A  70  CYS A  71                    
SITE     2 AC3  5 GLN A  72                                                     
SITE     1 AC4  4 CYS A 111  PHE A 112  CYS A 114  CYS A 154                    
SITE     1 AC5  3 ALA B1126  CYS B1137  ARG B1138                               
SITE     1 AC6  4 PHE I  16  CYS I  17  GLN I  18  ASN I  22                    
SITE     1 AC7  3 CYS I  89  HIS I  91  ALA I 116                               
SITE     1 AC8  4 ARG J   6  ILE J  13  VAL J  14  GLY J  15                    
SITE     1 AC9  3 GLU L  38  CYS L  39  LYS M 226                               
SITE     1 AD1  4 PRO M  19  ASP M  20  ALA M  21  ILE M  22                    
SITE     1 AD2  4 PRO Q 130  VAL Q 131  CYS Q 132  SER Q 133                    
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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