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Database: PDB
Entry: 5XTB
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Original site: 5XTB 
HEADER    OXIDOREDUCTASE/ELECTRON TRANSPORT       18-JUN-17   5XTB              
TITLE     CRYO-EM STRUCTURE OF HUMAN RESPIRATORY COMPLEX I MATRIX ARM           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 1,            
COMPND   3 MITOCHONDRIAL;                                                       
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: UNP RESIDUES 27-457;                                       
COMPND   6 SYNONYM: COMPLEX I-51KD,CI-51KD,NADH DEHYDROGENASE FLAVOPROTEIN 1,   
COMPND   7 NADH-UBIQUINONE OXIDOREDUCTASE 51 KDA SUBUNIT;                       
COMPND   8 EC: 1.6.5.3,1.6.99.3;                                                
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 8,     
COMPND  11 MITOCHONDRIAL;                                                       
COMPND  12 CHAIN: B;                                                            
COMPND  13 SYNONYM: COMPLEX I-23KD,CI-23KD,NADH-UBIQUINONE OXIDOREDUCTASE 23 KDA
COMPND  14 SUBUNIT,TYKY SUBUNIT;                                                
COMPND  15 EC: 1.6.5.3,1.6.99.3;                                                
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 7,     
COMPND  18 MITOCHONDRIAL;                                                       
COMPND  19 CHAIN: C;                                                            
COMPND  20 FRAGMENT: UNP RESIDUES 58-213;                                       
COMPND  21 SYNONYM: COMPLEX I-20KD,CI-20KD,NADH-UBIQUINONE OXIDOREDUCTASE 20 KDA
COMPND  22 SUBUNIT,PSST SUBUNIT;                                                
COMPND  23 EC: 1.6.5.3,1.6.99.3;                                                
COMPND  24 MOL_ID: 4;                                                           
COMPND  25 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 
COMPND  26 6;                                                                   
COMPND  27 CHAIN: E;                                                            
COMPND  28 FRAGMENT: UNP RESIDUES 42-154;                                       
COMPND  29 SYNONYM: COMPLEX I-B14,CI-B14,LYR MOTIF-CONTAINING PROTEIN 6,NADH-   
COMPND  30 UBIQUINONE OXIDOREDUCTASE B14 SUBUNIT;                               
COMPND  31 MOL_ID: 5;                                                           
COMPND  32 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 
COMPND  33 2;                                                                   
COMPND  34 CHAIN: F;                                                            
COMPND  35 FRAGMENT: UNP RESIDUES 14-96;                                        
COMPND  36 SYNONYM: COMPLEX I-B8,CI-B8,NADH-UBIQUINONE OXIDOREDUCTASE B8        
COMPND  37 SUBUNIT;                                                             
COMPND  38 MOL_ID: 6;                                                           
COMPND  39 MOLECULE: ACYL CARRIER PROTEIN, MITOCHONDRIAL;                       
COMPND  40 CHAIN: G;                                                            
COMPND  41 SYNONYM: ACP,CI-SDAP,NADH-UBIQUINONE OXIDOREDUCTASE 9.6 KDA SUBUNIT; 
COMPND  42 MOL_ID: 7;                                                           
COMPND  43 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 
COMPND  44 5;                                                                   
COMPND  45 CHAIN: H;                                                            
COMPND  46 SYNONYM: COMPLEX I SUBUNIT B13,COMPLEX I-13KD-B,CI-13KD-B,NADH-      
COMPND  47 UBIQUINONE OXIDOREDUCTASE 13 KDA-B SUBUNIT;                          
COMPND  48 MOL_ID: 8;                                                           
COMPND  49 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 
COMPND  50 7;                                                                   
COMPND  51 CHAIN: I;                                                            
COMPND  52 FRAGMENT: UNP RESIDUES 4-113;                                        
COMPND  53 SYNONYM: COMPLEX I-B14.5A,CI-B14.5A,NADH-UBIQUINONE OXIDOREDUCTASE   
COMPND  54 SUBUNIT B14.5A;                                                      
COMPND  55 MOL_ID: 9;                                                           
COMPND  56 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 
COMPND  57 9, MITOCHONDRIAL;                                                    
COMPND  58 CHAIN: J;                                                            
COMPND  59 FRAGMENT: UNP RESIDUES 40-375;                                       
COMPND  60 SYNONYM: COMPLEX I-39KD,CI-39KD,NADH-UBIQUINONE OXIDOREDUCTASE 39 KDA
COMPND  61 SUBUNIT;                                                             
COMPND  62 MOL_ID: 10;                                                          
COMPND  63 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 3,            
COMPND  64 MITOCHONDRIAL;                                                       
COMPND  65 CHAIN: K;                                                            
COMPND  66 FRAGMENT: UNP RESIDUES 74-106;                                       
COMPND  67 SYNONYM: COMPLEX I-9KD,CI-9KD,NADH-UBIQUINONE OXIDOREDUCTASE 9 KDA   
COMPND  68 SUBUNIT,RENAL CARCINOMA ANTIGEN NY-REN-4;                            
COMPND  69 MOL_ID: 11;                                                          
COMPND  70 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 4,     
COMPND  71 MITOCHONDRIAL;                                                       
COMPND  72 CHAIN: L;                                                            
COMPND  73 FRAGMENT: UNP RESIDUES 58-175;                                       
COMPND  74 SYNONYM: COMPLEX I-18 KDA,CI-18 KDA,COMPLEX I-AQDQ,CI-AQDQ,NADH-     
COMPND  75 UBIQUINONE OXIDOREDUCTASE 18 KDA SUBUNIT;                            
COMPND  76 MOL_ID: 12;                                                          
COMPND  77 MOLECULE: NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT,             
COMPND  78 MITOCHONDRIAL;                                                       
COMPND  79 CHAIN: M;                                                            
COMPND  80 FRAGMENT: UNP RESIDUES 30-716;                                       
COMPND  81 SYNONYM: COMPLEX I-75KD,CI-75KD;                                     
COMPND  82 EC: 1.6.5.3,1.6.99.3;                                                
COMPND  83 MOL_ID: 13;                                                          
COMPND  84 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 
COMPND  85 12;                                                                  
COMPND  86 CHAIN: N;                                                            
COMPND  87 SYNONYM: 13 KDA DIFFERENTIATION-ASSOCIATED PROTEIN,COMPLEX I-B17.2,  
COMPND  88 CIB17.2,NADH-UBIQUINONE OXIDOREDUCTASE SUBUNIT B17.2;                
COMPND  89 MOL_ID: 14;                                                          
COMPND  90 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 2,            
COMPND  91 MITOCHONDRIAL;                                                       
COMPND  92 CHAIN: O;                                                            
COMPND  93 FRAGMENT: UNP RESIDUES 36-247;                                       
COMPND  94 SYNONYM: NADH-UBIQUINONE OXIDOREDUCTASE 24 KDA SUBUNIT;              
COMPND  95 EC: 1.6.5.3,1.6.99.3;                                                
COMPND  96 MOL_ID: 15;                                                          
COMPND  97 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 3,     
COMPND  98 MITOCHONDRIAL;                                                       
COMPND  99 CHAIN: P;                                                            
COMPND 100 FRAGMENT: UNP RESIDUES 43-250;                                       
COMPND 101 SYNONYM: COMPLEX I-30KD,CI-30KD,NADH-UBIQUINONE OXIDOREDUCTASE 30 KDA
COMPND 102 SUBUNIT;                                                             
COMPND 103 EC: 1.6.5.3,1.6.99.3;                                                
COMPND 104 MOL_ID: 16;                                                          
COMPND 105 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2,     
COMPND 106 MITOCHONDRIAL;                                                       
COMPND 107 CHAIN: Q;                                                            
COMPND 108 FRAGMENT: UNP RESIDUES 79-463;                                       
COMPND 109 SYNONYM: COMPLEX I-49KD,CI-49KD,NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA
COMPND 110 SUBUNIT;                                                             
COMPND 111 EC: 1.6.5.3,1.6.99.3;                                                
COMPND 112 MOL_ID: 17;                                                          
COMPND 113 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 6,     
COMPND 114 MITOCHONDRIAL;                                                       
COMPND 115 CHAIN: T;                                                            
COMPND 116 SYNONYM: COMPLEX I-13KD-A,CI-13KD-A,NADH-UBIQUINONE OXIDOREDUCTASE 13
COMPND 117 KDA-A SUBUNIT;                                                       
COMPND 118 MOL_ID: 18;                                                          
COMPND 119 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 
COMPND 120 13;                                                                  
COMPND 121 CHAIN: W;                                                            
COMPND 122 FRAGMENT: UNP RESIDUES 7-28;                                         
COMPND 123 SYNONYM: CELL DEATH REGULATORY PROTEIN GRIM-19,COMPLEX I-B16.6,CI-   
COMPND 124 B16.6,GENE ASSOCIATED WITH RETINOIC AND INTERFERON-INDUCED MORTALITY 
COMPND 125 19 PROTEIN,GENE ASSOCIATED WITH RETINOIC AND IFN-INDUCED MORTALITY 19
COMPND 126 PROTEIN,NADH-UBIQUINONE OXIDOREDUCTASE B16.6 SUBUNIT                 
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 MOL_ID: 14;                                                          
SOURCE  54 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  55 ORGANISM_COMMON: HUMAN;                                              
SOURCE  56 ORGANISM_TAXID: 9606;                                                
SOURCE  57 MOL_ID: 15;                                                          
SOURCE  58 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  59 ORGANISM_COMMON: HUMAN;                                              
SOURCE  60 ORGANISM_TAXID: 9606;                                                
SOURCE  61 MOL_ID: 16;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  63 ORGANISM_COMMON: HUMAN;                                              
SOURCE  64 ORGANISM_TAXID: 9606;                                                
SOURCE  65 MOL_ID: 17;                                                          
SOURCE  66 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  67 ORGANISM_COMMON: HUMAN;                                              
SOURCE  68 ORGANISM_TAXID: 9606;                                                
SOURCE  69 MOL_ID: 18;                                                          
SOURCE  70 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  71 ORGANISM_COMMON: HUMAN;                                              
SOURCE  72 ORGANISM_TAXID: 9606                                                 
KEYWDS    RESPIRATORY, OXIDOREDUCTASE-ELECTRON TRANSPORT COMPLEX                
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    J.GU,M.WU,M.YANG                                                      
REVDAT   3   06-DEC-17 5XTB    1       JRNL   REMARK                            
REVDAT   2   06-SEP-17 5XTB    1       JRNL                                     
REVDAT   1   30-AUG-17 5XTB    0                                                
JRNL        AUTH   R.GUO,S.ZONG,M.WU,J.GU,M.YANG                                
JRNL        TITL   ARCHITECTURE OF HUMAN MITOCHONDRIAL RESPIRATORY MEGACOMPLEX  
JRNL        TITL 2 I2III2IV2.                                                   
JRNL        REF    CELL                          V. 170  1247 2017              
JRNL        REFN                   ISSN 1097-4172                               
JRNL        PMID   28844695                                                     
JRNL        DOI    10.1016/J.CELL.2017.07.050                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : EMAN, AUTOEMATION, CTFFIND, COOT,         
REMARK   3                            RELION, RELION, RELION, RELION, PHENIX    
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 3.400                          
REMARK   3   NUMBER OF PARTICLES               : 167761                         
REMARK   3   CTF CORRECTION METHOD             : NONE                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 5XTB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300004145.                                   
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 RESPIRATORY COMPLEX I       
REMARK 245                                    MATRIX ARM                        
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.20                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.40                              
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                     : FEI FALCON II (4K X 4K)        
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 1.25                           
REMARK 245   ILLUMINATION MODE                 : OTHER                          
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTADECAMERIC                     
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, F, G, H, I, J, K,         
REMARK 350                    AND CHAINS: L, M, N, O, P, Q, T, W                
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA I    75                                                      
REMARK 465     LEU I    76                                                      
REMARK 465     VAL I    77                                                      
REMARK 465     SER I    78                                                      
REMARK 465     GLY I    79                                                      
REMARK 465     LYS I    80                                                      
REMARK 465     PRO I    81                                                      
REMARK 465     ALA I    82                                                      
REMARK 465     GLU I    83                                                      
REMARK 465     SER I    84                                                      
REMARK 465     SER I    85                                                      
REMARK 465     ALA I    86                                                      
REMARK 465     VAL I    87                                                      
REMARK 465     ALA I    88                                                      
REMARK 465     ALA I    89                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER G 112    CB   OG                                             
REMARK 470     ASP G 150    CG   OD1  OD2                                       
REMARK 470     LYS G 151    CG   CD   CE   NZ                                   
REMARK 470     LYS G 152    CG   CD   CE   NZ                                   
REMARK 470     ASP G 153    CG   OD1  OD2                                       
REMARK 470     CYS M 131    SG                                                  
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   SG   CYS M   176    FE4   SF4 M   802              1.38            
REMARK 500   SG   CYS M   176     S2   SF4 M   802              1.54            
REMARK 500   O    ILE J   206     OD2  ASP J   211              1.61            
REMARK 500   O    ASN J   171     CD2  LEU J   181              1.92            
REMARK 500   OD1  ASN E    70     O4   8Q1 E   201              1.95            
REMARK 500   OE2  GLU C   204     NH1  ARG C   206              1.98            
REMARK 500   OD2  ASP Q   140     OG   SER Q   143              2.02            
REMARK 500   OE1  GLU C   143     OH   TYR J    89              2.03            
REMARK 500   NH1  ARG H    45     OE2  GLU H    49              2.04            
REMARK 500   OG   SER P   134     OG   SER P   139              2.07            
REMARK 500   O    ILE Q   450     OG1  THR Q   453              2.07            
REMARK 500   O    THR B    81     NH2  ARG N    58              2.09            
REMARK 500   N    ASN A   244     O2P  FMN A   502              2.09            
REMARK 500   O    ASN E    70     O40  8Q1 E   201              2.10            
REMARK 500   O    ASP M   194     OG1  THR M   208              2.10            
REMARK 500   O    ARG Q   294     N    GLY Q   321              2.11            
REMARK 500   OD1  ASP O    54     OH   TYR O    60              2.11            
REMARK 500   O    ILE M   500     OG1  THR M   503              2.12            
REMARK 500   O    HIS M   460     OG   SER M   463              2.13            
REMARK 500   OG1  THR T    40     O    THR T    42              2.14            
REMARK 500   O    PHE L   137     ND2  ASN L   141              2.15            
REMARK 500   NH2  ARG J   270     O    ASP J   326              2.16            
REMARK 500   O    THR P    46     N    ARG Q   162              2.16            
REMARK 500   NH1  ARG L    75     OD2  ASP L   119              2.16            
REMARK 500   OH   TYR M   385     OD1  ASP M   527              2.17            
REMARK 500   OG   SER M   627     O    MET M   632              2.17            
REMARK 500   NZ   LYS I    33     O    THR I    35              2.17            
REMARK 500   NZ   LYS A    64     O    GLY O   244              2.18            
REMARK 500   O    GLU A   161     OH   TYR O   192              2.18            
REMARK 500   OE2  GLU P    85     NH1  ARG P   142              2.19            
REMARK 500   OG1  THR I    96     O    ALA I    98              2.19            
REMARK 500   OG   SER K    80     OG1  THR K    83              2.19            
REMARK 500   NH2  ARG E    37     OE2  GLU G   123              2.19            
REMARK 500   ND2  ASN O   182     OE1  GLU O   194              2.19            
REMARK 500   OE2  GLU M    54     NH2  ARG M    62              2.19            
REMARK 500   O    GLY J    77     NE2  GLN J   102              2.19            
REMARK 500   O    LEU I   106     N    SER I   108              2.19            
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 E  19   C   -  N   -  CA  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    PRO I  39   C   -  N   -  CA  ANGL. DEV. =  11.3 DEGREES          
REMARK 500    PRO Q 366   C   -  N   -  CA  ANGL. DEV. =  10.6 DEGREES          
REMARK 500    PRO W  11   C   -  N   -  CA  ANGL. DEV. = -10.1 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    LEU A  35      117.03   -173.02                                   
REMARK 500    ASP A  50      106.22     63.03                                   
REMARK 500    TYR A  63     -101.68     13.26                                   
REMARK 500    PRO A  73     -100.56    -59.12                                   
REMARK 500    ASP A  74      -88.52     52.23                                   
REMARK 500    PRO A  94      103.67    -50.65                                   
REMARK 500    MET A 102       41.92   -105.20                                   
REMARK 500    ASP A 134       57.04   -159.39                                   
REMARK 500    ILE A 182     -155.68   -117.31                                   
REMARK 500    ASN A 185      -39.21     62.52                                   
REMARK 500    ALA A 186      100.31     60.65                                   
REMARK 500    SER A 189      -28.43     71.60                                   
REMARK 500    ARG A 256      -79.49   -103.17                                   
REMARK 500    ASN A 270       48.18   -100.77                                   
REMARK 500    HIS A 281       97.81    -63.80                                   
REMARK 500    LYS A 302      -84.52   -117.67                                   
REMARK 500    SER A 323      -46.66   -133.70                                   
REMARK 500    ALA A 352       29.06     49.55                                   
REMARK 500    SER A 378       18.00   -159.08                                   
REMARK 500    CYS A 379      -84.62     36.27                                   
REMARK 500    GLN A 381      -76.85    -79.64                                   
REMARK 500    GLU A 420      -75.25    -55.60                                   
REMARK 500    ASN B  40     -115.84     54.38                                   
REMARK 500    MET B  41      -32.48     62.13                                   
REMARK 500    LEU B  59      -72.09    -99.17                                   
REMARK 500    TRP B  61      -34.54     72.99                                   
REMARK 500    THR B  62      -81.79     40.49                                   
REMARK 500    CYS B 121      103.54    -39.08                                   
REMARK 500    ALA B 164      -78.68    -73.40                                   
REMARK 500    PHE B 171      -30.49   -139.32                                   
REMARK 500    PHE B 173       40.23   -163.66                                   
REMARK 500    SER C  78       68.34   -157.61                                   
REMARK 500    PHE C  84       13.33   -173.24                                   
REMARK 500    ALA C  87     -149.76   -163.74                                   
REMARK 500    TYR C 101      -61.43   -108.89                                   
REMARK 500    ASP C 102       93.89     62.18                                   
REMARK 500    SER C 113      151.60     71.68                                   
REMARK 500    ARG C 115      -54.15   -126.01                                   
REMARK 500    ASP C 118      -74.39   -109.20                                   
REMARK 500    SER C 165      -83.01    -57.91                                   
REMARK 500    VAL C 167       58.53   -100.89                                   
REMARK 500    ARG C 168     -126.22     40.93                                   
REMARK 500    ILE E  20      -81.62    -56.36                                   
REMARK 500    PHE E  21      -71.75   -121.91                                   
REMARK 500    ASP E  24      160.22     67.13                                   
REMARK 500    TRP E  97     -158.66    -85.41                                   
REMARK 500    LYS E  98     -161.07     54.72                                   
REMARK 500    VAL E 124      -70.80    -72.10                                   
REMARK 500    ASP E 127     -167.91     57.83                                   
REMARK 500    ARG F  17      -45.28   -135.33                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     238 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 501  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 381   NE2                                                    
REMARK 620 2 SF4 A 501   S2  112.5                                              
REMARK 620 3 SF4 A 501   S3   67.7  89.9                                        
REMARK 620 4 SF4 A 501   S4  147.0  90.0  89.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 301  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 114   N                                                      
REMARK 620 2 SF4 B 301   S1  116.1                                              
REMARK 620 3 SF4 B 301   S3   90.0  90.5                                        
REMARK 620 4 SF4 B 301   S4  154.8  89.1  90.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 302  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY B 154   N                                                      
REMARK 620 2 SF4 B 302   S1  103.0                                              
REMARK 620 3 SF4 B 302   S2   96.5  89.4                                        
REMARK 620 4 SF4 B 302   S3  164.1  91.5  90.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 301  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  89   SG                                                     
REMARK 620 2 SF4 C 301   S1   86.5                                              
REMARK 620 3 SF4 C 301   S3   86.3  88.7                                        
REMARK 620 4 SF4 C 301   S4  176.4  90.6  91.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 M 801  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS M 124   NE2                                                    
REMARK 620 2 SF4 M 801   S1  117.5                                              
REMARK 620 3 SF4 M 801   S2  141.1  89.7                                        
REMARK 620 4 SF4 M 801   S4  113.8  91.8  90.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 M 801  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS M 137   SG                                                     
REMARK 620 2 SF4 M 801   S1  121.7                                              
REMARK 620 3 SF4 M 801   S2  101.5  89.7                                        
REMARK 620 4 SF4 M 801   S3  148.2  87.8  89.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 M 802  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS M 176   SG                                                     
REMARK 620 2 SF4 M 802   S2   40.8                                              
REMARK 620 3 SF4 M 802   S3   58.0  90.1                                        
REMARK 620 4 SF4 M 802   S4  112.2  89.6  90.3                                  
REMARK 620 5 CYS M 179   O   121.1  88.5 178.5  89.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES O 301  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS O 176   SG                                                     
REMARK 620 2 FES O 301   S1  102.4                                              
REMARK 620 3 FES O 301   S2   81.3  90.5                                        
REMARK 620 4 CYS O 180   SG   81.2 162.9  73.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8Q1 E 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP J 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 M 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 M 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FES M 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FES O 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-6771   RELATED DB: EMDB                              
DBREF  5XTB A   27   457  UNP    P49821   NDUV1_HUMAN     27    457             
DBREF  5XTB B   35   210  UNP    O00217   NDUS8_HUMAN     35    210             
DBREF  5XTB C   58   213  UNP    O75251   NDUS7_HUMAN     58    213             
DBREF  5XTB E   16   128  UNP    P56556   NDUA6_HUMAN     42    154             
DBREF  5XTB F   14    96  UNP    O43678   NDUA2_HUMAN     14     96             
DBREF  5XTB G   72   156  UNP    O14561   ACPM_HUMAN      72    156             
DBREF  5XTB H    5   116  UNP    Q16718   NDUA5_HUMAN      5    116             
DBREF  5XTB I    4   113  UNP    O95182   NDUA7_HUMAN      4    113             
DBREF  5XTB J   40   376  UNP    Q16795   NDUA9_HUMAN     40    376             
DBREF  5XTB K   74   106  UNP    P56181   NDUV3_HUMAN     74    106             
DBREF  5XTB L   58   175  UNP    O43181   NDUS4_HUMAN     58    175             
DBREF  5XTB M   30   716  UNP    P28331   NDUS1_HUMAN     30    716             
DBREF  5XTB N    2   144  UNP    Q9UI09   NDUAC_HUMAN      2    144             
DBREF  5XTB O   36   247  UNP    P19404   NDUV2_HUMAN     36    247             
DBREF  5XTB P   43   250  UNP    O75489   NDUS3_HUMAN     43    250             
DBREF  5XTB Q   79   463  UNP    O75306   NDUS2_HUMAN     79    463             
DBREF  5XTB T   29   123  UNP    O75380   NDUS6_HUMAN     29    123             
DBREF  5XTB W    7    28  UNP    Q9P0J0   NDUAD_HUMAN      7     28             
SEQRES   1 A  431  PRO LYS LYS THR SER PHE GLY SER LEU LYS ASP GLU ASP          
SEQRES   2 A  431  ARG ILE PHE THR ASN LEU TYR GLY ARG HIS ASP TRP ARG          
SEQRES   3 A  431  LEU LYS GLY SER LEU SER ARG GLY ASP TRP TYR LYS THR          
SEQRES   4 A  431  LYS GLU ILE LEU LEU LYS GLY PRO ASP TRP ILE LEU GLY          
SEQRES   5 A  431  GLU ILE LYS THR SER GLY LEU ARG GLY ARG GLY GLY ALA          
SEQRES   6 A  431  GLY PHE PRO THR GLY LEU LYS TRP SER PHE MET ASN LYS          
SEQRES   7 A  431  PRO SER ASP GLY ARG PRO LYS TYR LEU VAL VAL ASN ALA          
SEQRES   8 A  431  ASP GLU GLY GLU PRO GLY THR CYS LYS ASP ARG GLU ILE          
SEQRES   9 A  431  LEU ARG HIS ASP PRO HIS LYS LEU LEU GLU GLY CYS LEU          
SEQRES  10 A  431  VAL GLY GLY ARG ALA MET GLY ALA ARG ALA ALA TYR ILE          
SEQRES  11 A  431  TYR ILE ARG GLY GLU PHE TYR ASN GLU ALA SER ASN LEU          
SEQRES  12 A  431  GLN VAL ALA ILE ARG GLU ALA TYR GLU ALA GLY LEU ILE          
SEQRES  13 A  431  GLY LYS ASN ALA CYS GLY SER GLY TYR ASP PHE ASP VAL          
SEQRES  14 A  431  PHE VAL VAL ARG GLY ALA GLY ALA TYR ILE CYS GLY GLU          
SEQRES  15 A  431  GLU THR ALA LEU ILE GLU SER ILE GLU GLY LYS GLN GLY          
SEQRES  16 A  431  LYS PRO ARG LEU LYS PRO PRO PHE PRO ALA ASP VAL GLY          
SEQRES  17 A  431  VAL PHE GLY CYS PRO THR THR VAL ALA ASN VAL GLU THR          
SEQRES  18 A  431  VAL ALA VAL SER PRO THR ILE CYS ARG ARG GLY GLY THR          
SEQRES  19 A  431  TRP PHE ALA GLY PHE GLY ARG GLU ARG ASN SER GLY THR          
SEQRES  20 A  431  LYS LEU PHE ASN ILE SER GLY HIS VAL ASN HIS PRO CYS          
SEQRES  21 A  431  THR VAL GLU GLU GLU MET SER VAL PRO LEU LYS GLU LEU          
SEQRES  22 A  431  ILE GLU LYS HIS ALA GLY GLY VAL THR GLY GLY TRP ASP          
SEQRES  23 A  431  ASN LEU LEU ALA VAL ILE PRO GLY GLY SER SER THR PRO          
SEQRES  24 A  431  LEU ILE PRO LYS SER VAL CYS GLU THR VAL LEU MET ASP          
SEQRES  25 A  431  PHE ASP ALA LEU VAL GLN ALA GLN THR GLY LEU GLY THR          
SEQRES  26 A  431  ALA ALA VAL ILE VAL MET ASP ARG SER THR ASP ILE VAL          
SEQRES  27 A  431  LYS ALA ILE ALA ARG LEU ILE GLU PHE TYR LYS HIS GLU          
SEQRES  28 A  431  SER CYS GLY GLN CYS THR PRO CYS ARG GLU GLY VAL ASP          
SEQRES  29 A  431  TRP MET ASN LYS VAL MET ALA ARG PHE VAL ARG GLY ASP          
SEQRES  30 A  431  ALA ARG PRO ALA GLU ILE ASP SER LEU TRP GLU ILE SER          
SEQRES  31 A  431  LYS GLN ILE GLU GLY HIS THR ILE CYS ALA LEU GLY ASP          
SEQRES  32 A  431  GLY ALA ALA TRP PRO VAL GLN GLY LEU ILE ARG HIS PHE          
SEQRES  33 A  431  ARG PRO GLU LEU GLU GLU ARG MET GLN ARG PHE ALA GLN          
SEQRES  34 A  431  GLN HIS                                                      
SEQRES   1 B  176  THR TYR LYS TYR VAL ASN MET GLN ASP PRO GLU MET ASP          
SEQRES   2 B  176  MET LYS SER VAL THR ASP ARG ALA ALA ARG THR LEU LEU          
SEQRES   3 B  176  TRP THR GLU LEU PHE ARG GLY LEU GLY MET THR LEU SER          
SEQRES   4 B  176  TYR LEU PHE ARG GLU PRO ALA THR ILE ASN TYR PRO PHE          
SEQRES   5 B  176  GLU LYS GLY PRO LEU SER PRO ARG PHE ARG GLY GLU HIS          
SEQRES   6 B  176  ALA LEU ARG ARG TYR PRO SER GLY GLU GLU ARG CYS ILE          
SEQRES   7 B  176  ALA CYS LYS LEU CYS GLU ALA ILE CYS PRO ALA GLN ALA          
SEQRES   8 B  176  ILE THR ILE GLU ALA GLU PRO ARG ALA ASP GLY SER ARG          
SEQRES   9 B  176  ARG THR THR ARG TYR ASP ILE ASP MET THR LYS CYS ILE          
SEQRES  10 B  176  TYR CYS GLY PHE CYS GLN GLU ALA CYS PRO VAL ASP ALA          
SEQRES  11 B  176  ILE VAL GLU GLY PRO ASN PHE GLU PHE SER THR GLU THR          
SEQRES  12 B  176  HIS GLU GLU LEU LEU TYR ASN LYS GLU LYS LEU LEU ASN          
SEQRES  13 B  176  ASN GLY ASP LYS TRP GLU ALA GLU ILE ALA ALA ASN ILE          
SEQRES  14 B  176  GLN ALA ASP TYR LEU TYR ARG                                  
SEQRES   1 C  156  SER ARG GLY GLU TYR VAL VAL ALA LYS LEU ASP ASP LEU          
SEQRES   2 C  156  VAL ASN TRP ALA ARG ARG SER SER LEU TRP PRO MET THR          
SEQRES   3 C  156  PHE GLY LEU ALA CYS CYS ALA VAL GLU MET MET HIS MET          
SEQRES   4 C  156  ALA ALA PRO ARG TYR ASP MET ASP ARG PHE GLY VAL VAL          
SEQRES   5 C  156  PHE ARG ALA SER PRO ARG GLN SER ASP VAL MET ILE VAL          
SEQRES   6 C  156  ALA GLY THR LEU THR ASN LYS MET ALA PRO ALA LEU ARG          
SEQRES   7 C  156  LYS VAL TYR ASP GLN MET PRO GLU PRO ARG TYR VAL VAL          
SEQRES   8 C  156  SER MET GLY SER CYS ALA ASN GLY GLY GLY TYR TYR HIS          
SEQRES   9 C  156  TYR SER TYR SER VAL VAL ARG GLY CYS ASP ARG ILE VAL          
SEQRES  10 C  156  PRO VAL ASP ILE TYR ILE PRO GLY CYS PRO PRO THR ALA          
SEQRES  11 C  156  GLU ALA LEU LEU TYR GLY ILE LEU GLN LEU GLN ARG LYS          
SEQRES  12 C  156  ILE LYS ARG GLU ARG ARG LEU GLN ILE TRP TYR ARG ARG          
SEQRES   1 E  113  PHE VAL LYS PRO ILE PHE SER ARG ASP MET ASN GLU ALA          
SEQRES   2 E  113  LYS ARG ARG VAL ARG GLU LEU TYR ARG ALA TRP TYR ARG          
SEQRES   3 E  113  GLU VAL PRO ASN THR VAL HIS GLN PHE GLN LEU ASP ILE          
SEQRES   4 E  113  THR VAL LYS MET GLY ARG ASP LYS VAL ARG GLU MET PHE          
SEQRES   5 E  113  MET LYS ASN ALA HIS VAL THR ASP PRO ARG VAL VAL ASP          
SEQRES   6 E  113  LEU LEU VAL ILE LYS GLY LYS ILE GLU LEU GLU GLU THR          
SEQRES   7 E  113  ILE LYS VAL TRP LYS GLN ARG THR HIS VAL MET ARG PHE          
SEQRES   8 E  113  PHE HIS GLU THR GLU ALA PRO ARG PRO LYS ASP PHE LEU          
SEQRES   9 E  113  SER LYS PHE TYR VAL GLY HIS ASP PRO                          
SEQRES   1 F   83  LEU GLY LEU ARG GLU ILE ARG ILE HIS LEU CYS GLN ARG          
SEQRES   2 F   83  SER PRO GLY SER GLN GLY VAL ARG ASP PHE ILE GLU LYS          
SEQRES   3 F   83  ARG TYR VAL GLU LEU LYS LYS ALA ASN PRO ASP LEU PRO          
SEQRES   4 F   83  ILE LEU ILE ARG GLU CYS SER ASP VAL GLN PRO LYS LEU          
SEQRES   5 F   83  TRP ALA ARG TYR ALA PHE GLY GLN GLU THR ASN VAL PRO          
SEQRES   6 F   83  LEU ASN ASN PHE SER ALA ASP GLN VAL THR ARG ALA LEU          
SEQRES   7 F   83  GLU ASN VAL LEU SER                                          
SEQRES   1 G   85  PRO PRO LEU THR LEU GLU GLY ILE GLN ASP ARG VAL LEU          
SEQRES   2 G   85  TYR VAL LEU LYS LEU TYR ASP LYS ILE ASP PRO GLU LYS          
SEQRES   3 G   85  LEU SER VAL ASN SER HIS PHE MET LYS ASP LEU GLY LEU          
SEQRES   4 G   85  ASP SER LEU ASP GLN VAL GLU ILE ILE MET ALA MET GLU          
SEQRES   5 G   85  ASP GLU PHE GLY PHE GLU ILE PRO ASP ILE ASP ALA GLU          
SEQRES   6 G   85  LYS LEU MET CYS PRO GLN GLU ILE VAL ASP TYR ILE ALA          
SEQRES   7 G   85  ASP LYS LYS ASP VAL TYR GLU                                  
SEQRES   1 H  112  LEU LYS LYS THR THR GLY LEU VAL GLY LEU ALA VAL CYS          
SEQRES   2 H  112  ASN THR PRO HIS GLU ARG LEU ARG ILE LEU TYR THR LYS          
SEQRES   3 H  112  ILE LEU ASP VAL LEU GLU GLU ILE PRO LYS ASN ALA ALA          
SEQRES   4 H  112  TYR ARG LYS TYR THR GLU GLN ILE THR ASN GLU LYS LEU          
SEQRES   5 H  112  ALA MET VAL LYS ALA GLU PRO ASP VAL LYS LYS LEU GLU          
SEQRES   6 H  112  ASP GLN LEU GLN GLY GLY GLN LEU GLU GLU VAL ILE LEU          
SEQRES   7 H  112  GLN ALA GLU HIS GLU LEU ASN LEU ALA ARG LYS MET ARG          
SEQRES   8 H  112  GLU TRP LYS LEU TRP GLU PRO LEU VAL GLU GLU PRO PRO          
SEQRES   9 H  112  ALA ASP GLN TRP LYS TRP PRO ILE                              
SEQRES   1 I  110  ALA THR ARG LEU ILE GLN ARG LEU ARG ASN TRP ALA SER          
SEQRES   2 I  110  GLY HIS ASP LEU GLN GLY LYS LEU GLN LEU ARG TYR GLN          
SEQRES   3 I  110  GLU ILE SER LYS ARG THR GLN PRO PRO PRO LYS LEU PRO          
SEQRES   4 I  110  VAL GLY PRO SER HIS LYS LEU SER ASN ASN TYR TYR CYS          
SEQRES   5 I  110  THR ARG ASP GLY ARG ARG GLU SER VAL PRO PRO SER ILE          
SEQRES   6 I  110  ILE MET SER SER GLN LYS ALA LEU VAL SER GLY LYS PRO          
SEQRES   7 I  110  ALA GLU SER SER ALA VAL ALA ALA THR GLU LYS LYS ALA          
SEQRES   8 I  110  VAL THR PRO ALA PRO PRO ILE LYS ARG TRP GLU LEU SER          
SEQRES   9 I  110  SER ASP GLN PRO TYR LEU                                      
SEQRES   1 J  337  LEU MET PRO HIS GLY LYS GLY GLY ARG SER SER VAL SER          
SEQRES   2 J  337  GLY ILE VAL ALA THR VAL PHE GLY ALA THR GLY PHE LEU          
SEQRES   3 J  337  GLY ARG TYR VAL VAL ASN HIS LEU GLY ARG MET GLY SER          
SEQRES   4 J  337  GLN VAL ILE ILE PRO TYR ARG CYS ASP LYS TYR ASP ILE          
SEQRES   5 J  337  MET HIS LEU ARG PRO MET GLY ASP LEU GLY GLN LEU LEU          
SEQRES   6 J  337  PHE LEU GLU TRP ASP ALA ARG ASP LYS ASP SER ILE ARG          
SEQRES   7 J  337  ARG VAL VAL GLN HIS SER ASN VAL VAL ILE ASN LEU ILE          
SEQRES   8 J  337  GLY ARG ASP TRP GLU THR LYS ASN PHE ASP PHE GLU ASP          
SEQRES   9 J  337  VAL PHE VAL LYS ILE PRO GLN ALA ILE ALA GLN LEU SER          
SEQRES  10 J  337  LYS GLU ALA GLY VAL GLU LYS PHE ILE HIS VAL SER HIS          
SEQRES  11 J  337  LEU ASN ALA ASN ILE LYS SER SER SER ARG TYR LEU ARG          
SEQRES  12 J  337  ASN LYS ALA VAL GLY GLU LYS VAL VAL ARG ASP ALA PHE          
SEQRES  13 J  337  PRO GLU ALA ILE ILE VAL LYS PRO SER ASP ILE PHE GLY          
SEQRES  14 J  337  ARG GLU ASP ARG PHE LEU ASN SER PHE ALA SER MET HIS          
SEQRES  15 J  337  ARG PHE GLY PRO ILE PRO LEU GLY SER LEU GLY TRP LYS          
SEQRES  16 J  337  THR VAL LYS GLN PRO VAL TYR VAL VAL ASP VAL SER LYS          
SEQRES  17 J  337  GLY ILE VAL ASN ALA VAL LYS ASP PRO ASP ALA ASN GLY          
SEQRES  18 J  337  LYS SER PHE ALA PHE VAL GLY PRO SER ARG TYR LEU LEU          
SEQRES  19 J  337  PHE HIS LEU VAL LYS TYR ILE PHE ALA VAL ALA HIS ARG          
SEQRES  20 J  337  LEU PHE LEU PRO PHE PRO LEU PRO LEU PHE ALA TYR ARG          
SEQRES  21 J  337  TRP VAL ALA ARG VAL PHE GLU ILE SER PRO PHE GLU PRO          
SEQRES  22 J  337  TRP ILE THR ARG ASP LYS VAL GLU ARG MET HIS ILE THR          
SEQRES  23 J  337  ASP MET LYS LEU PRO HIS LEU PRO GLY LEU GLU ASP LEU          
SEQRES  24 J  337  GLY ILE GLN ALA THR PRO LEU GLU LEU LYS ALA ILE GLU          
SEQRES  25 J  337  VAL LEU ARG ARG HIS ARG THR TYR ARG TRP LEU SER ALA          
SEQRES  26 J  337  GLU ILE GLU ASP VAL LYS PRO ALA LYS THR VAL ASN              
SEQRES   1 K   33  LEU GLN HIS HIS ASP TYR SER THR TYR THR PHE LEU ASP          
SEQRES   2 K   33  LEU ASN LEU GLU LEU SER LYS PHE ARG MET PRO GLN PRO          
SEQRES   3 K   33  SER SER GLY ARG GLU SER PRO                                  
SEQRES   1 L  118  LYS LEU ASP ILE THR THR LEU THR GLY VAL PRO GLU GLU          
SEQRES   2 L  118  HIS ILE LYS THR ARG LYS VAL ARG ILE PHE VAL PRO ALA          
SEQRES   3 L  118  ARG ASN ASN MET GLN SER GLY VAL ASN ASN THR LYS LYS          
SEQRES   4 L  118  TRP LYS MET GLU PHE ASP THR ARG GLU ARG TRP GLU ASN          
SEQRES   5 L  118  PRO LEU MET GLY TRP ALA SER THR ALA ASP PRO LEU SER          
SEQRES   6 L  118  ASN MET VAL LEU THR PHE SER THR LYS GLU ASP ALA VAL          
SEQRES   7 L  118  SER PHE ALA GLU LYS ASN GLY TRP SER TYR ASP ILE GLU          
SEQRES   8 L  118  GLU ARG LYS VAL PRO LYS PRO LYS SER LYS SER TYR GLY          
SEQRES   9 L  118  ALA ASN PHE SER TRP ASN LYS ARG THR ARG VAL SER THR          
SEQRES  10 L  118  LYS                                                          
SEQRES   1 M  687  ASN LEU ILE GLU VAL PHE VAL ASP GLY GLN SER VAL MET          
SEQRES   2 M  687  VAL GLU PRO GLY THR THR VAL LEU GLN ALA CYS GLU LYS          
SEQRES   3 M  687  VAL GLY MET GLN ILE PRO ARG PHE CYS TYR HIS GLU ARG          
SEQRES   4 M  687  LEU SER VAL ALA GLY ASN CYS ARG MET CYS LEU VAL GLU          
SEQRES   5 M  687  ILE GLU LYS ALA PRO LYS VAL VAL ALA ALA CYS ALA MET          
SEQRES   6 M  687  PRO VAL MET LYS GLY TRP ASN ILE LEU THR ASN SER GLU          
SEQRES   7 M  687  LYS SER LYS LYS ALA ARG GLU GLY VAL MET GLU PHE LEU          
SEQRES   8 M  687  LEU ALA ASN HIS PRO LEU ASP CYS PRO ILE CYS ASP GLN          
SEQRES   9 M  687  GLY GLY GLU CYS ASP LEU GLN ASP GLN SER MET MET PHE          
SEQRES  10 M  687  GLY ASN ASP ARG SER ARG PHE LEU GLU GLY LYS ARG ALA          
SEQRES  11 M  687  VAL GLU ASP LYS ASN ILE GLY PRO LEU VAL LYS THR ILE          
SEQRES  12 M  687  MET THR ARG CYS ILE GLN CYS THR ARG CYS ILE ARG PHE          
SEQRES  13 M  687  ALA SER GLU ILE ALA GLY VAL ASP ASP LEU GLY THR THR          
SEQRES  14 M  687  GLY ARG GLY ASN ASP MET GLN VAL GLY THR TYR ILE GLU          
SEQRES  15 M  687  LYS MET PHE MET SER GLU LEU SER GLY ASN ILE ILE ASP          
SEQRES  16 M  687  ILE CYS PRO VAL GLY ALA LEU THR SER LYS PRO TYR ALA          
SEQRES  17 M  687  PHE THR ALA ARG PRO TRP GLU THR ARG LYS THR GLU SER          
SEQRES  18 M  687  ILE ASP VAL MET ASP ALA VAL GLY SER ASN ILE VAL VAL          
SEQRES  19 M  687  SER THR ARG THR GLY GLU VAL MET ARG ILE LEU PRO ARG          
SEQRES  20 M  687  MET HIS GLU ASP ILE ASN GLU GLU TRP ILE SER ASP LYS          
SEQRES  21 M  687  THR ARG PHE ALA TYR ASP GLY LEU LYS ARG GLN ARG LEU          
SEQRES  22 M  687  THR GLU PRO MET VAL ARG ASN GLU LYS GLY LEU LEU THR          
SEQRES  23 M  687  TYR THR SER TRP GLU ASP ALA LEU SER ARG VAL ALA GLY          
SEQRES  24 M  687  MET LEU GLN SER PHE GLN GLY LYS ASP VAL ALA ALA ILE          
SEQRES  25 M  687  ALA GLY GLY LEU VAL ASP ALA GLU ALA LEU VAL ALA LEU          
SEQRES  26 M  687  LYS ASP LEU LEU ASN ARG VAL ASP SER ASP THR LEU CYS          
SEQRES  27 M  687  THR GLU GLU VAL PHE PRO THR ALA GLY ALA GLY THR ASP          
SEQRES  28 M  687  LEU ARG SER ASN TYR LEU LEU ASN THR THR ILE ALA GLY          
SEQRES  29 M  687  VAL GLU GLU ALA ASP VAL VAL LEU LEU VAL GLY THR ASN          
SEQRES  30 M  687  PRO ARG PHE GLU ALA PRO LEU PHE ASN ALA ARG ILE ARG          
SEQRES  31 M  687  LYS SER TRP LEU HIS ASN ASP LEU LYS VAL ALA LEU ILE          
SEQRES  32 M  687  GLY SER PRO VAL ASP LEU THR TYR THR TYR ASP HIS LEU          
SEQRES  33 M  687  GLY ASP SER PRO LYS ILE LEU GLN ASP ILE ALA SER GLY          
SEQRES  34 M  687  SER HIS PRO PHE SER GLN VAL LEU LYS GLU ALA LYS LYS          
SEQRES  35 M  687  PRO MET VAL VAL LEU GLY SER SER ALA LEU GLN ARG ASN          
SEQRES  36 M  687  ASP GLY ALA ALA ILE LEU ALA ALA VAL SER SER ILE ALA          
SEQRES  37 M  687  GLN LYS ILE ARG MET THR SER GLY VAL THR GLY ASP TRP          
SEQRES  38 M  687  LYS VAL MET ASN ILE LEU HIS ARG ILE ALA SER GLN VAL          
SEQRES  39 M  687  ALA ALA LEU ASP LEU GLY TYR LYS PRO GLY VAL GLU ALA          
SEQRES  40 M  687  ILE ARG LYS ASN PRO PRO LYS VAL LEU PHE LEU LEU GLY          
SEQRES  41 M  687  ALA ASP GLY GLY CYS ILE THR ARG GLN ASP LEU PRO LYS          
SEQRES  42 M  687  ASP CYS PHE ILE ILE TYR GLN GLY HIS HIS GLY ASP VAL          
SEQRES  43 M  687  GLY ALA PRO ILE ALA ASP VAL ILE LEU PRO GLY ALA ALA          
SEQRES  44 M  687  TYR THR GLU LYS SER ALA THR TYR VAL ASN THR GLU GLY          
SEQRES  45 M  687  ARG ALA GLN GLN THR LYS VAL ALA VAL THR PRO PRO GLY          
SEQRES  46 M  687  LEU ALA ARG GLU ASP TRP LYS ILE ILE ARG ALA LEU SER          
SEQRES  47 M  687  GLU ILE ALA GLY MET THR LEU PRO TYR ASP THR LEU ASP          
SEQRES  48 M  687  GLN VAL ARG ASN ARG LEU GLU GLU VAL SER PRO ASN LEU          
SEQRES  49 M  687  VAL ARG TYR ASP ASP ILE GLU GLY ALA ASN TYR PHE GLN          
SEQRES  50 M  687  GLN ALA ASN GLU LEU SER LYS LEU VAL ASN GLN GLN LEU          
SEQRES  51 M  687  LEU ALA ASP PRO LEU VAL PRO PRO GLN LEU THR ILE LYS          
SEQRES  52 M  687  ASP PHE TYR MET THR ASP SER ILE SER ARG ALA SER GLN          
SEQRES  53 M  687  THR MET ALA LYS CYS VAL LYS ALA VAL THR GLU                  
SEQRES   1 N  143  GLU LEU VAL GLN VAL LEU LYS ARG GLY LEU GLN GLN ILE          
SEQRES   2 N  143  THR GLY HIS GLY GLY LEU ARG GLY TYR LEU ARG VAL PHE          
SEQRES   3 N  143  PHE ARG THR ASN ASP ALA LYS VAL GLY THR LEU VAL GLY          
SEQRES   4 N  143  GLU ASP LYS TYR GLY ASN LYS TYR TYR GLU ASP ASN LYS          
SEQRES   5 N  143  GLN PHE PHE GLY ARG HIS ARG TRP VAL VAL TYR THR THR          
SEQRES   6 N  143  GLU MET ASN GLY LYS ASN THR PHE TRP ASP VAL ASP GLY          
SEQRES   7 N  143  SER MET VAL PRO PRO GLU TRP HIS ARG TRP LEU HIS SER          
SEQRES   8 N  143  MET THR ASP ASP PRO PRO THR THR LYS PRO LEU THR ALA          
SEQRES   9 N  143  ARG LYS PHE ILE TRP THR ASN HIS LYS PHE ASN VAL THR          
SEQRES  10 N  143  GLY THR PRO GLU GLN TYR VAL PRO TYR SER THR THR ARG          
SEQRES  11 N  143  LYS LYS ILE GLN GLU TRP ILE PRO PRO SER THR PRO TYR          
SEQRES   1 O  212  GLY ALA LEU PHE VAL HIS ARG ASP THR PRO GLU ASN ASN          
SEQRES   2 O  212  PRO ASP THR PRO PHE ASP PHE THR PRO GLU ASN TYR LYS          
SEQRES   3 O  212  ARG ILE GLU ALA ILE VAL LYS ASN TYR PRO GLU GLY HIS          
SEQRES   4 O  212  LYS ALA ALA ALA VAL LEU PRO VAL LEU ASP LEU ALA GLN          
SEQRES   5 O  212  ARG GLN ASN GLY TRP LEU PRO ILE SER ALA MET ASN LYS          
SEQRES   6 O  212  VAL ALA GLU VAL LEU GLN VAL PRO PRO MET ARG VAL TYR          
SEQRES   7 O  212  GLU VAL ALA THR PHE TYR THR MET TYR ASN ARG LYS PRO          
SEQRES   8 O  212  VAL GLY LYS TYR HIS ILE GLN VAL CYS THR THR THR PRO          
SEQRES   9 O  212  CYS MET LEU ARG ASN SER ASP SER ILE LEU GLU ALA ILE          
SEQRES  10 O  212  GLN LYS LYS LEU GLY ILE LYS VAL GLY GLU THR THR PRO          
SEQRES  11 O  212  ASP LYS LEU PHE THR LEU ILE GLU VAL GLU CYS LEU GLY          
SEQRES  12 O  212  ALA CYS VAL ASN ALA PRO MET VAL GLN ILE ASN ASP ASN          
SEQRES  13 O  212  TYR TYR GLU ASP LEU THR ALA LYS ASP ILE GLU GLU ILE          
SEQRES  14 O  212  ILE ASP GLU LEU LYS ALA GLY LYS ILE PRO LYS PRO GLY          
SEQRES  15 O  212  PRO ARG SER GLY ARG PHE SER CYS GLU PRO ALA GLY GLY          
SEQRES  16 O  212  LEU THR SER LEU THR GLU PRO PRO LYS GLY PRO GLY PHE          
SEQRES  17 O  212  GLY VAL GLN ALA                                              
SEQRES   1 P  208  THR ARG PRO THR VAL ARG PRO ARG ASN ASP VAL ALA HIS          
SEQRES   2 P  208  LYS GLN LEU SER ALA PHE GLY GLU TYR VAL ALA GLU ILE          
SEQRES   3 P  208  LEU PRO LYS TYR VAL GLN GLN VAL GLN VAL SER CYS PHE          
SEQRES   4 P  208  ASN GLU LEU GLU VAL CYS ILE HIS PRO ASP GLY VAL ILE          
SEQRES   5 P  208  PRO VAL LEU THR PHE LEU ARG ASP HIS THR ASN ALA GLN          
SEQRES   6 P  208  PHE LYS SER LEU VAL ASP LEU THR ALA VAL ASP VAL PRO          
SEQRES   7 P  208  THR ARG GLN ASN ARG PHE GLU ILE VAL TYR ASN LEU LEU          
SEQRES   8 P  208  SER LEU ARG PHE ASN SER ARG ILE ARG VAL LYS THR TYR          
SEQRES   9 P  208  THR ASP GLU LEU THR PRO ILE GLU SER ALA VAL SER VAL          
SEQRES  10 P  208  PHE LYS ALA ALA ASN TRP TYR GLU ARG GLU ILE TRP ASP          
SEQRES  11 P  208  MET PHE GLY VAL PHE PHE ALA ASN HIS PRO ASP LEU ARG          
SEQRES  12 P  208  ARG ILE LEU THR ASP TYR GLY PHE GLU GLY HIS PRO PHE          
SEQRES  13 P  208  ARG LYS ASP PHE PRO LEU SER GLY TYR VAL GLU LEU ARG          
SEQRES  14 P  208  TYR ASP ASP GLU VAL LYS ARG VAL VAL ALA GLU PRO VAL          
SEQRES  15 P  208  GLU LEU ALA GLN GLU PHE ARG LYS PHE ASP LEU ASN SER          
SEQRES  16 P  208  PRO TRP GLU ALA PHE PRO VAL TYR ARG GLN PRO PRO GLU          
SEQRES   1 Q  385  ASN ILE THR LEU ASN PHE GLY PRO GLN HIS PRO ALA ALA          
SEQRES   2 Q  385  HIS GLY VAL LEU ARG LEU VAL MET GLU LEU SER GLY GLU          
SEQRES   3 Q  385  MET VAL ARG LYS CYS ASP PRO HIS ILE GLY LEU LEU HIS          
SEQRES   4 Q  385  ARG GLY THR GLU LYS LEU ILE GLU TYR LYS THR TYR LEU          
SEQRES   5 Q  385  GLN ALA LEU PRO TYR PHE ASP ARG LEU ASP TYR VAL SER          
SEQRES   6 Q  385  MET MET CYS ASN GLU GLN ALA TYR SER LEU ALA VAL GLU          
SEQRES   7 Q  385  LYS LEU LEU ASN ILE ARG PRO PRO PRO ARG ALA GLN TRP          
SEQRES   8 Q  385  ILE ARG VAL LEU PHE GLY GLU ILE THR ARG LEU LEU ASN          
SEQRES   9 Q  385  HIS ILE MET ALA VAL THR THR HIS ALA LEU ASP LEU GLY          
SEQRES  10 Q  385  ALA MET THR PRO PHE PHE TRP LEU PHE GLU GLU ARG GLU          
SEQRES  11 Q  385  LYS MET PHE GLU PHE TYR GLU ARG VAL SER GLY ALA ARG          
SEQRES  12 Q  385  MET HIS ALA ALA TYR ILE ARG PRO GLY GLY VAL HIS GLN          
SEQRES  13 Q  385  ASP LEU PRO LEU GLY LEU MET ASP ASP ILE TYR GLN PHE          
SEQRES  14 Q  385  SER LYS ASN PHE SER LEU ARG LEU ASP GLU LEU GLU GLU          
SEQRES  15 Q  385  LEU LEU THR ASN ASN ARG ILE TRP ARG ASN ARG THR ILE          
SEQRES  16 Q  385  ASP ILE GLY VAL VAL THR ALA GLU GLU ALA LEU ASN TYR          
SEQRES  17 Q  385  GLY PHE SER GLY VAL MET LEU ARG GLY SER GLY ILE GLN          
SEQRES  18 Q  385  TRP ASP LEU ARG LYS THR GLN PRO TYR ASP VAL TYR ASP          
SEQRES  19 Q  385  GLN VAL GLU PHE ASP VAL PRO VAL GLY SER ARG GLY ASP          
SEQRES  20 Q  385  CYS TYR ASP ARG TYR LEU CYS ARG VAL GLU GLU MET ARG          
SEQRES  21 Q  385  GLN SER LEU ARG ILE ILE ALA GLN CYS LEU ASN LYS MET          
SEQRES  22 Q  385  PRO PRO GLY GLU ILE LYS VAL ASP ASP ALA LYS VAL SER          
SEQRES  23 Q  385  PRO PRO LYS ARG ALA GLU MET LYS THR SER MET GLU SER          
SEQRES  24 Q  385  LEU ILE HIS HIS PHE LYS LEU TYR THR GLU GLY TYR GLN          
SEQRES  25 Q  385  VAL PRO PRO GLY ALA THR TYR THR ALA ILE GLU ALA PRO          
SEQRES  26 Q  385  LYS GLY GLU PHE GLY VAL TYR LEU VAL SER ASP GLY SER          
SEQRES  27 Q  385  SER ARG PRO TYR ARG CYS LYS ILE LYS ALA PRO GLY PHE          
SEQRES  28 Q  385  ALA HIS LEU ALA GLY LEU ASP LYS MET SER LYS GLY HIS          
SEQRES  29 Q  385  MET LEU ALA ASP VAL VAL ALA ILE ILE GLY THR GLN ASP          
SEQRES  30 Q  385  ILE VAL PHE GLY GLU VAL ASP ARG                              
SEQRES   1 T   95  GLY VAL ARG VAL SER PRO THR GLY GLU LYS VAL THR HIS          
SEQRES   2 T   95  THR GLY GLN VAL TYR ASP ASP LYS ASP TYR ARG ARG ILE          
SEQRES   3 T   95  ARG PHE VAL GLY ARG GLN LYS GLU VAL ASN GLU ASN PHE          
SEQRES   4 T   95  ALA ILE ASP LEU ILE ALA GLU GLN PRO VAL SER GLU VAL          
SEQRES   5 T   95  GLU THR ARG VAL ILE ALA CYS ASP GLY GLY GLY GLY ALA          
SEQRES   6 T   95  LEU GLY HIS PRO LYS VAL TYR ILE ASN LEU ASP LYS GLU          
SEQRES   7 T   95  THR LYS THR GLY THR CYS GLY TYR CYS GLY LEU GLN PHE          
SEQRES   8 T   95  ARG GLN HIS HIS                                              
SEQRES   1 W   22  LYS GLN ASP MET PRO PRO PRO GLY GLY TYR GLY PRO ILE          
SEQRES   2 W   22  ASP TYR LYS ARG ASN LEU PRO ARG ARG                          
HET    SF4  A 501       8                                                       
HET    FMN  A 502      31                                                       
HET    SF4  B 301       8                                                       
HET    SF4  B 302       8                                                       
HET    SF4  C 301       8                                                       
HET    8Q1  E 201      35                                                       
HET    NDP  J 401      48                                                       
HET    SF4  M 801       8                                                       
HET    SF4  M 802       8                                                       
HET    FES  M 803       4                                                       
HET    FES  O 301       4                                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     FMN FLAVIN MONONUCLEOTIDE                                            
HETNAM     8Q1 S-[2-({N-[(2R)-2-HYDROXY-3,3-DIMETHYL-4-(PHOSPHONOOXY)           
HETNAM   2 8Q1  BUTANOYL]-BETA-ALANYL}AMINO)ETHYL] DODECANETHIOATE              
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETSYN     FMN RIBOFLAVIN MONOPHOSPHATE                                         
HETSYN     8Q1 S-DODECANOYL-4'-PHOSPHOPANTETHEINE                               
FORMUL  19  SF4    6(FE4 S4)                                                    
FORMUL  20  FMN    C17 H21 N4 O9 P                                              
FORMUL  24  8Q1    C23 H45 N2 O8 P S                                            
FORMUL  25  NDP    C21 H30 N7 O17 P3                                            
FORMUL  28  FES    2(FE2 S2)                                                    
HELIX    1 AA1 ARG A   52  ARG A   59  1                                   8    
HELIX    2 AA2 ASP A   74  THR A   82  1                                   9    
HELIX    3 AA3 PRO A   94  PHE A  101  1                                   8    
HELIX    4 AA4 MET A  102  LYS A  104  5                                   3    
HELIX    5 AA5 CYS A  125  ASP A  134  1                                  10    
HELIX    6 AA6 ASP A  134  GLY A  150  1                                  17    
HELIX    7 AA7 TYR A  163  ALA A  179  1                                  17    
HELIX    8 AA8 ALA A  203  GLY A  207  5                                   5    
HELIX    9 AA9 GLU A  208  GLU A  217  1                                  10    
HELIX   10 AB1 GLY A  234  CYS A  238  5                                   5    
HELIX   11 AB2 VAL A  245  ARG A  257  1                                  13    
HELIX   12 AB3 GLY A  258  GLY A  264  1                                   7    
HELIX   13 AB4 PRO A  295  LYS A  302  1                                   8    
HELIX   14 AB5 GLY A  310  ASP A  312  5                                   3    
HELIX   15 AB6 LYS A  329  GLU A  333  1                                   5    
HELIX   16 AB7 ASP A  338  ALA A  345  1                                   8    
HELIX   17 AB8 LEU A  349  THR A  351  5                                   3    
HELIX   18 AB9 ILE A  363  GLU A  377  1                                  15    
HELIX   19 AC1 CYS A  382  GLY A  402  1                                  21    
HELIX   20 AC2 ALA A  407  GLU A  420  1                                  14    
HELIX   21 AC3 ALA A  426  GLN A  455  1                                  30    
HELIX   22 AC4 ASP B   47  TRP B   61  1                                  15    
HELIX   23 AC5 THR B   62  ARG B   77  1                                  16    
HELIX   24 AC6 LEU B  116  CYS B  121  1                                   6    
HELIX   25 AC7 GLY B  154  CYS B  160  1                                   7    
HELIX   26 AC8 THR B  177  GLU B  180  5                                   4    
HELIX   27 AC9 LYS B  185  TRP B  195  1                                  11    
HELIX   28 AD1 TRP B  195  TYR B  207  1                                  13    
HELIX   29 AD2 LEU B  208  ARG B  210  5                                   3    
HELIX   30 AD3 ARG C   59  SER C   77  1                                  19    
HELIX   31 AD4 CYS C   89  ALA C   97  1                                   9    
HELIX   32 AD5 ASP C  102  GLY C  107  5                                   6    
HELIX   33 AD6 MET C  130  MET C  141  1                                  12    
HELIX   34 AD7 MET C  150  GLY C  157  1                                   8    
HELIX   35 AD8 GLY C  158  HIS C  161  5                                   4    
HELIX   36 AD9 GLY C  169  ILE C  173  5                                   5    
HELIX   37 AE1 THR C  186  ARG C  203  1                                  18    
HELIX   38 AE2 ARG C  205  ARG C  212  1                                   8    
HELIX   39 AE3 ASP E   24  ARG E   41  1                                  18    
HELIX   40 AE4 GLU E   42  PHE E   50  1                                   9    
HELIX   41 AE5 THR E   55  PHE E   67  1                                  13    
HELIX   42 AE6 ASP E   75  LYS E   95  1                                  21    
HELIX   43 AE7 GLN E   99  ARG E  105  1                                   7    
HELIX   44 AE8 ASP E  117  GLY E  125  1                                   9    
HELIX   45 AE9 SER F   27  LYS F   39  1                                  13    
HELIX   46 AF1 ARG F   40  ASN F   48  1                                   9    
HELIX   47 AF2 ALA F   70  GLY F   72  5                                   3    
HELIX   48 AF3 SER F   83  VAL F   94  1                                  12    
HELIX   49 AF4 THR G   75  TYR G   90  1                                  16    
HELIX   50 AF5 ASP G  111  GLY G  127  1                                  17    
HELIX   51 AF6 ASP G  132  LEU G  138  1                                   7    
HELIX   52 AF7 CYS G  140  LYS G  152  1                                  13    
HELIX   53 AF8 THR H   19  GLU H   36  1                                  18    
HELIX   54 AF9 ALA H   42  GLU H   62  1                                  21    
HELIX   55 AG1 ASP H   64  LEU H   72  1                                   9    
HELIX   56 AG2 GLU H   79  ARG H   95  1                                  17    
HELIX   57 AG3 GLU H   96  LYS H   98  5                                   3    
HELIX   58 AG4 THR I    5  GLY I   17  1                                  13    
HELIX   59 AG5 TYR I   53  ASP I   58  1                                   6    
HELIX   60 AG6 GLY I   59  SER I   63  5                                   5    
HELIX   61 AG7 GLY J   63  MET J   76  1                                  14    
HELIX   62 AG8 LYS J   88  GLY J   98  5                                  11    
HELIX   63 AG9 ASP J   99  GLY J  101  5                                   3    
HELIX   64 AH1 LYS J  113  VAL J  120  1                                   8    
HELIX   65 AH2 ASP J  140  PHE J  145  1                                   6    
HELIX   66 AH3 VAL J  146  GLY J  160  1                                  15    
HELIX   67 AH4 SER J  178  PHE J  195  1                                  18    
HELIX   68 AH5 ASP J  211  GLY J  224  1                                  14    
HELIX   69 AH6 TYR J  241  ASP J  255  1                                  15    
HELIX   70 AH7 LEU J  272  HIS J  285  1                                  14    
HELIX   71 AH8 PRO J  294  GLU J  306  1                                  13    
HELIX   72 AH9 THR J  315  ILE J  324  1                                  10    
HELIX   73 AI1 GLY J  334  LEU J  338  5                                   5    
HELIX   74 AI2 PRO J  344  LEU J  347  5                                   4    
HELIX   75 AI3 LYS J  348  ARG J  354  1                                   7    
HELIX   76 AI4 THR J  358  SER J  363  1                                   6    
HELIX   77 AI5 ILE J  366  LYS J  370  5                                   5    
HELIX   78 AI6 TYR K   82  LEU K   91  1                                  10    
HELIX   79 AI7 SER K   92  ARG K   95  5                                   4    
HELIX   80 AI8 PRO L   68  ARG L   75  1                                   8    
HELIX   81 AI9 ASP L  119  ASN L  123  5                                   5    
HELIX   82 AJ1 THR L  130  GLY L  142  1                                  13    
HELIX   83 AJ2 TYR L  160  PHE L  164  5                                   5    
HELIX   84 AJ3 THR M   48  GLY M   57  1                                  10    
HELIX   85 AJ4 SER M  106  LEU M  121  1                                  16    
HELIX   86 AJ5 CYS M  137  PHE M  146  1                                  10    
HELIX   87 AJ6 THR M  180  SER M  187  1                                   8    
HELIX   88 AJ7 GLY M  220  CYS M  226  1                                   7    
HELIX   89 AJ8 ARG M  241  THR M  245  5                                   5    
HELIX   90 AJ9 SER M  287  PHE M  292  1                                   6    
HELIX   91 AK1 ALA M  293  ARG M  299  5                                   7    
HELIX   92 AK2 SER M  318  GLN M  331  1                                  14    
HELIX   93 AK3 ASP M  347  VAL M  361  1                                  15    
HELIX   94 AK4 GLY M  393  ALA M  397  5                                   5    
HELIX   95 AK5 ASN M  406  GLU M  410  5                                   5    
HELIX   96 AK6 ALA M  411  HIS M  424  1                                  14    
HELIX   97 AK7 ASP M  447  GLY M  458  1                                  12    
HELIX   98 AK8 HIS M  460  ALA M  469  1                                  10    
HELIX   99 AK9 GLY M  477  GLN M  482  5                                   6    
HELIX  100 AL1 ASP M  485  SER M  504  1                                  20    
HELIX  101 AL2 SER M  521  LEU M  528  1                                   8    
HELIX  102 AL3 VAL M  534  ARG M  538  5                                   5    
HELIX  103 AL4 VAL M  575  ALA M  580  1                                   6    
HELIX  104 AL5 GLU M  618  ALA M  630  1                                  13    
HELIX  105 AL6 THR M  638  GLU M  648  1                                  11    
HELIX  106 AL7 PRO M  651  ARG M  655  5                                   5    
HELIX  107 AL8 PHE M  665  LEU M  674  1                                  10    
HELIX  108 AL9 THR M  690  MET M  696  5                                   7    
HELIX  109 AM1 ASP M  698  SER M  704  1                                   7    
HELIX  110 AM2 SER M  704  GLU M  716  1                                  13    
HELIX  111 AM3 LEU N    3  GLY N   16  1                                  14    
HELIX  112 AM4 LEU N   20  THR N   30  1                                  11    
HELIX  113 AM5 GLU N   67  LYS N   71  5                                   5    
HELIX  114 AM6 PRO N   83  HIS N   91  1                                   9    
HELIX  115 AM7 THR O   56  TYR O   70  1                                  15    
HELIX  116 AM8 HIS O   74  ALA O   77  5                                   4    
HELIX  117 AM9 ALA O   78  GLN O   89  1                                  12    
HELIX  118 AN1 PRO O   94  LEU O  105  1                                  12    
HELIX  119 AN2 PRO O  108  TYR O  119  1                                  12    
HELIX  120 AN3 THR O  137  LEU O  142  1                                   6    
HELIX  121 AN4 ASN O  144  GLY O  157  1                                  14    
HELIX  122 AN5 THR O  197  LYS O  209  1                                  13    
HELIX  123 AN6 ASN P   51  LEU P   69  1                                  19    
HELIX  124 AN7 HIS P   89  ASP P   91  5                                   3    
HELIX  125 AN8 GLY P   92  ASP P  102  1                                  11    
HELIX  126 AN9 LYS P  161  ALA P  163  5                                   3    
HELIX  127 AO1 ASN P  164  MET P  173  1                                  10    
HELIX  128 AO2 GLY Q  119  TYR Q  126  1                                   8    
HELIX  129 AO3 THR Q  128  LEU Q  133  1                                   6    
HELIX  130 AO4 LEU Q  133  ARG Q  138  1                                   6    
HELIX  131 AO5 MET Q  144  LEU Q  159  1                                  16    
HELIX  132 AO6 PRO Q  164  LEU Q  194  1                                  31    
HELIX  133 AO7 MET Q  197  GLY Q  219  1                                  23    
HELIX  134 AO8 GLY Q  239  ASN Q  250  1                                  12    
HELIX  135 AO9 ASN Q  250  GLU Q  260  1                                  11    
HELIX  136 AP1 ASN Q  265  ILE Q  273  1                                   9    
HELIX  137 AP2 THR Q  279  GLY Q  287  1                                   9    
HELIX  138 AP3 GLY Q  290  GLY Q  295  1                                   6    
HELIX  139 AP4 ASP Q  309  GLN Q  313  5                                   5    
HELIX  140 AP5 ASP Q  325  LYS Q  350  1                                  26    
HELIX  141 AP6 LYS Q  367  LYS Q  372  1                                   6    
HELIX  142 AP7 SER Q  374  TYR Q  385  1                                  12    
HELIX  143 AP8 ALA Q  426  LYS Q  440  1                                  15    
HELIX  144 AP9 MET Q  443  GLN Q  454  1                                  12    
HELIX  145 AQ1 VAL Q  457  ASP Q  462  1                                   6    
HELIX  146 AQ2 ASP T   50  VAL T   57  5                                   8    
HELIX  147 AQ3 PHE T   67  GLN T   75  1                                   9    
SHEET    1 AA1 4 ASP A 194  ARG A 199  0                                        
SHEET    2 AA1 4 ALA A 153  ILE A 158  1  N  ILE A 156   O  VAL A 198           
SHEET    3 AA1 4 VAL A 114  ASN A 116  1  N  VAL A 115   O  TYR A 155           
SHEET    4 AA1 4 VAL A 242  ASN A 244  1  O  ALA A 243   N  ASN A 116           
SHEET    1 AA2 5 CYS A 286  GLU A 291  0                                        
SHEET    2 AA2 5 THR A 273  GLY A 280 -1  N  LYS A 274   O  GLU A 290           
SHEET    3 AA2 5 ALA A 353  ASP A 358  1  O  VAL A 356   N  SER A 279           
SHEET    4 AA2 5 LEU A 314  PRO A 319 -1  N  ILE A 318   O  ILE A 355           
SHEET    5 AA2 5 ILE A 327  PRO A 328 -1  O  ILE A 327   N  VAL A 317           
SHEET    1 AA3 2 TYR B  36  TYR B  38  0                                        
SHEET    2 AA3 2 VAL Q 318  VAL Q 320  1  O  VAL Q 318   N  LYS B  37           
SHEET    1 AA4 2 HIS B  99  LEU B 101  0                                        
SHEET    2 AA4 2 ILE B 165  GLU B 167 -1  O  VAL B 166   N  ALA B 100           
SHEET    1 AA5 2 ALA B 130  PRO B 132  0                                        
SHEET    2 AA5 2 ARG B 138  THR B 140 -1  O  ARG B 139   N  GLU B 131           
SHEET    1 AA6 2 ASP B 144  ASP B 146  0                                        
SHEET    2 AA6 2 LEU B 182  ASN B 184 -1  O  TYR B 183   N  ILE B 145           
SHEET    1 AA7 2 MET C 120  ILE C 121  0                                        
SHEET    2 AA7 2 VAL C 147  VAL C 148  1  O  VAL C 148   N  MET C 120           
SHEET    1 AA8 4 ILE F  53  ARG F  56  0                                        
SHEET    2 AA8 4 ILE F  19  HIS F  22  1  N  ILE F  21   O  LEU F  54           
SHEET    3 AA8 4 LYS F  64  ARG F  68 -1  O  TRP F  66   N  ARG F  20           
SHEET    4 AA8 4 GLU F  74  ASN F  76 -1  O  THR F  75   N  ALA F  67           
SHEET    1 AA9 3 VAL J  55  THR J  57  0                                        
SHEET    2 AA9 3 GLN J  79  TYR J  84  1  O  ILE J  81   N  ALA J  56           
SHEET    3 AA9 3 LEU J 103  GLU J 107  1  O  LEU J 106   N  TYR J  84           
SHEET    1 AB1 3 VAL J 125  VAL J 126  0                                        
SHEET    2 AB1 3 LYS J 163  VAL J 167  1  O  ILE J 165   N  VAL J 126           
SHEET    3 AB1 3 ILE J 199  VAL J 201  1  O  VAL J 201   N  HIS J 166           
SHEET    1 AB2 2 ILE J 226  GLY J 229  0                                        
SHEET    2 AB2 2 PRO J 290  LEU J 293  1  O  PHE J 291   N  ILE J 226           
SHEET    1 AB3 3 VAL L  77  PHE L  80  0                                        
SHEET    2 AB3 3 TRP L  97  PHE L 101 -1  O  LYS L  98   N  PHE L  80           
SHEET    3 AB3 3 VAL L 125  PHE L 128 -1  O  PHE L 128   N  TRP L  97           
SHEET    1 AB4 2 ARG L 106  GLU L 108  0                                        
SHEET    2 AB4 2 ALA L 115  THR L 117 -1  O  SER L 116   N  TRP L 107           
SHEET    1 AB5 3 SER M  40  VAL M  43  0                                        
SHEET    2 AB5 3 ILE M  32  VAL M  36 -1  N  VAL M  34   O  VAL M  41           
SHEET    3 AB5 3 ASN M 101  ILE M 102  1  O  ILE M 102   N  PHE M  35           
SHEET    1 AB6 2 LEU M  79  VAL M  80  0                                        
SHEET    2 AB6 2 VAL M  89  ALA M  90 -1  O  VAL M  89   N  VAL M  80           
SHEET    1 AB7 3 ARG M 246  ILE M 251  0                                        
SHEET    2 AB7 3 ASN M 260  ARG M 266 -1  O  ILE M 261   N  SER M 250           
SHEET    3 AB7 3 GLU M 269  PRO M 275 -1  O  GLU M 269   N  ARG M 266           
SHEET    1 AB8 2 MET M 306  ARG M 308  0                                        
SHEET    2 AB8 2 LEU M 314  TYR M 316 -1  O  THR M 315   N  VAL M 307           
SHEET    1 AB9 3 ALA M 340  ILE M 341  0                                        
SHEET    2 AB9 3 LEU M 545  PHE M 546  1  O  LEU M 545   N  ILE M 341           
SHEET    3 AB9 3 ILE M 567  TYR M 568  1  O  ILE M 567   N  PHE M 546           
SHEET    1 AC1 2 THR M 595  VAL M 597  0                                        
SHEET    2 AC1 2 ALA M 603  GLN M 605 -1  O  GLN M 604   N  TYR M 596           
SHEET    1 AC2 5 VAL P  76  VAL P  78  0                                        
SHEET    2 AC2 5 LEU P  84  CYS P  87 -1  O  GLU P  85   N  GLN P  77           
SHEET    3 AC2 5 SER P 139  LYS P 144  1  O  ARG P 142   N  VAL P  86           
SHEET    4 AC2 5 VAL P 129  SER P 134 -1  N  TYR P 130   O  VAL P 143           
SHEET    5 AC2 5 ASP P 113  THR P 115 -1  N  THR P 115   O  VAL P 129           
SHEET    1 AC3 2 VAL P 208  ASP P 213  0                                        
SHEET    2 AC3 2 ARG P 218  PRO P 223 -1  O  VAL P 220   N  ARG P 211           
SHEET    1 AC4 3 ILE Q  80  LEU Q  82  0                                        
SHEET    2 AC4 3 ARG Q  96  LEU Q 101 -1  O  LEU Q 101   N  ILE Q  80           
SHEET    3 AC4 3 LYS Q 108  HIS Q 112 -1  O  HIS Q 112   N  ARG Q  96           
SHEET    1 AC5 2 ILE Q 227  ARG Q 228  0                                        
SHEET    2 AC5 2 GLY Q 231  VAL Q 232 -1  O  GLY Q 231   N  ARG Q 228           
SHEET    1 AC6 3 GLY Q 394  ALA Q 402  0                                        
SHEET    2 AC6 3 GLY Q 405  SER Q 413 -1  O  SER Q 413   N  GLY Q 394           
SHEET    3 AC6 3 PRO Q 419  LYS Q 423 -1  O  TYR Q 420   N  VAL Q 412           
SHEET    1 AC7 2 SER T  78  GLU T  79  0                                        
SHEET    2 AC7 2 PHE T 119  ARG T 120  1  O  ARG T 120   N  SER T  78           
SHEET    1 AC8 2 ILE T  85  CYS T  87  0                                        
SHEET    2 AC8 2 VAL T  99  ILE T 101 -1  O  VAL T  99   N  CYS T  87           
LINK         NE2 GLN A 381                FE1  SF4 A 501     1555   1555  2.52  
LINK         N   CYS B 114                FE2  SF4 B 301     1555   1555  2.67  
LINK         N   GLY B 154                FE4  SF4 B 302     1555   1555  2.79  
LINK         SG  CYS C  89                FE2  SF4 C 301     1555   1555  2.59  
LINK         NE2 HIS M 124                FE3  SF4 M 801     1555   1555  2.14  
LINK         SG  CYS M 137                FE4  SF4 M 801     1555   1555  2.56  
LINK         SG  CYS M 176                FE1  SF4 M 802     1555   1555  2.24  
LINK         SG  CYS M 176                 S3  SF4 M 802     1555   1555  2.15  
LINK         O   ILE M 177                 N   CYS M 179     1555   1555  1.48  
LINK         O   CYS M 179                FE1  SF4 M 802     1555   1555  2.57  
LINK         SG  CYS O 176                FE2  FES O 301     1555   1555  2.52  
LINK         SG  CYS O 180                FE2  FES O 301     1555   1555  2.61  
CISPEP   1 TYR B   84    PRO B   85          0        -3.84                     
CISPEP   2 GLU C  143    PRO C  144          0        -0.88                     
CISPEP   3 CYS C  183    PRO C  184          0       -17.99                     
CISPEP   4 TRP H  114    PRO H  115          0         0.67                     
CISPEP   5 SER M  650    PRO M  651          0       -18.83                     
CISPEP   6 ASP M  682    PRO M  683          0        -7.63                     
CISPEP   7 GLY Q   85    PRO Q   86          0         0.37                     
SITE     1 AC1 10 ILE A 205  PRO A 223  SER A 378  CYS A 379                    
SITE     2 AC1 10 GLN A 381  CYS A 382  CYS A 385  THR A 423                    
SITE     3 AC1 10 ILE A 424  CYS A 425                                          
SITE     1 AC2 11 GLY A  87  ARG A  88  GLY A  89  ASN A 116                    
SITE     2 AC2 11 GLU A 119  GLY A 207  GLU A 208  GLU A 209                    
SITE     3 AC2 11 ALA A 243  ASN A 244  ALA A 426                               
SITE     1 AC3  8 CYS B 111  ALA B 113  CYS B 114  LYS B 115                    
SITE     2 AC3  8 CYS B 117  CYS B 160  ALA B 164  ILE B 165                    
SITE     1 AC4 11 HIS B  99  CYS B 121  PRO B 122  CYS B 150                    
SITE     2 AC4 11 ILE B 151  TYR B 152  CYS B 153  GLY B 154                    
SITE     3 AC4 11 PHE B 155  CYS B 156  GLU B 167                               
SITE     1 AC5  9 ALA C  87  CYS C  88  CYS C  89  GLY C 151                    
SITE     2 AC5  9 SER C 152  CYS C 153  CYS C 183  PRO C 184                    
SITE     3 AC5  9 HIS Q 223                                                     
SITE     1 AC6  9 MET E  25  TRP E  39  MET E  66  PHE E  67                    
SITE     2 AC6  9 ASN E  70  VAL E  79  LEU E  82  VAL E  83                    
SITE     3 AC6  9 SER G 112                                                     
SITE     1 AC7 18 GLY J  60  THR J  62  GLY J  63  PHE J  64                    
SITE     2 AC7 18 LEU J  65  ALA J 110  LEU J 129  ILE J 130                    
SITE     3 AC7 18 GLY J 131  ARG J 132  PHE J 145  SER J 168                    
SITE     4 AC7 18 HIS J 169  TYR J 180  LYS J 184  PRO J 203                    
SITE     5 AC7 18 ILE J 206  ARG J 212                                          
SITE     1 AC8  9 HIS M 124  ASP M 127  CYS M 128  CYS M 131                    
SITE     2 AC8  9 GLY M 134  CYS M 137  GLN M 140  VAL M 228                    
SITE     3 AC8  9 GLY M 229                                                     
SITE     1 AC9  9 CYS M 176  ILE M 177  CYS M 179  CYS M 182                    
SITE     2 AC9  9 CYS M 226  PRO M 227  VAL M 228  ALA M 230                    
SITE     3 AC9  9 LEU M 231                                                     
SITE     1 AD1  9 ARG M  62  CYS M  64  TYR M  65  ALA M  72                    
SITE     2 AD1  9 ASN M  74  CYS M  75  MET M  77  CYS M  78                    
SITE     3 AD1  9 CYS M  92                                                     
SITE     1 AD2  9 CYS O 135  THR O 137  PRO O 139  CYS O 140                    
SITE     2 AD2  9 CYS O 176  LEU O 177  GLY O 178  ALA O 179                    
SITE     3 AD2  9 CYS O 180                                                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1                      
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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