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Database: PDB
Entry: 3IAM
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Original site: 3IAM 
HEADER    OXIDOREDUCTASE                          14-JUL-09   3IAM              
TITLE     CRYSTAL STRUCTURE OF THE HYDROPHILIC DOMAIN OF RESPIRATORY COMPLEX I  
TITLE    2 FROM THERMUS THERMOPHILUS, REDUCED, 2 MOL/ASU, WITH BOUND NADH       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1;                     
COMPND   3 CHAIN: 1, A;                                                         
COMPND   4 SYNONYM: NADH DEHYDROGENASE I CHAIN 1, NDH-1 SUBUNIT 1;              
COMPND   5 EC: 1.6.99.5;                                                        
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2;                     
COMPND   8 CHAIN: 2, B;                                                         
COMPND   9 SYNONYM: NADH DEHYDROGENASE I CHAIN 2, NDH-1 SUBUNIT 2;              
COMPND  10 EC: 1.6.99.5;                                                        
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3;                     
COMPND  13 CHAIN: 3, C;                                                         
COMPND  14 SYNONYM: NADH DEHYDROGENASE I CHAIN 3, NDH-1 SUBUNIT 3;              
COMPND  15 EC: 1.6.99.5;                                                        
COMPND  16 MOL_ID: 4;                                                           
COMPND  17 MOLECULE: NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4;                     
COMPND  18 CHAIN: 4, D;                                                         
COMPND  19 SYNONYM: NADH DEHYDROGENASE I CHAIN 4, NDH-1 SUBUNIT 4;              
COMPND  20 EC: 1.6.99.5;                                                        
COMPND  21 MOL_ID: 5;                                                           
COMPND  22 MOLECULE: NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5;                     
COMPND  23 CHAIN: 5, E;                                                         
COMPND  24 SYNONYM: NADH DEHYDROGENASE I CHAIN 5, NDH-1 SUBUNIT 5;              
COMPND  25 EC: 1.6.99.5;                                                        
COMPND  26 MOL_ID: 6;                                                           
COMPND  27 MOLECULE: NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6;                     
COMPND  28 CHAIN: 6, F;                                                         
COMPND  29 SYNONYM: NADH DEHYDROGENASE I SUBUNIT 6, NDH-1 SUBUNIT 6;            
COMPND  30 EC: 1.6.99.5;                                                        
COMPND  31 MOL_ID: 7;                                                           
COMPND  32 MOLECULE: NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9;                     
COMPND  33 CHAIN: 9, G;                                                         
COMPND  34 SYNONYM: NADH DEHYDROGENASE I SUBUNIT 9, NDH-1 SUBUNIT 9;            
COMPND  35 EC: 1.6.99.5;                                                        
COMPND  36 MOL_ID: 8;                                                           
COMPND  37 MOLECULE: NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15;                    
COMPND  38 CHAIN: 7, H;                                                         
COMPND  39 SYNONYM: NADH DEHYDROGENASE I CHAIN 15, NDH-1 SUBUNIT 15;            
COMPND  40 EC: 1.6.99.5                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE   3 ORGANISM_TAXID: 300852;                                              
SOURCE   4 STRAIN: HB8;                                                         
SOURCE   5 ATCC: 27634 / DSM 579;                                               
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE   8 ORGANISM_TAXID: 300852;                                              
SOURCE   9 STRAIN: HB8;                                                         
SOURCE  10 ATCC: 27634 / DSM 579;                                               
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  13 ORGANISM_TAXID: 300852;                                              
SOURCE  14 STRAIN: HB8;                                                         
SOURCE  15 ATCC: 27634 / DSM 579;                                               
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  18 ORGANISM_TAXID: 300852;                                              
SOURCE  19 STRAIN: HB8;                                                         
SOURCE  20 ATCC: 27634 / DSM 579;                                               
SOURCE  21 MOL_ID: 5;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  23 ORGANISM_TAXID: 300852;                                              
SOURCE  24 STRAIN: HB8;                                                         
SOURCE  25 ATCC: 27634 / DSM 579;                                               
SOURCE  26 MOL_ID: 6;                                                           
SOURCE  27 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  28 ORGANISM_TAXID: 300852;                                              
SOURCE  29 STRAIN: HB8;                                                         
SOURCE  30 ATCC: 27634 / DSM 579;                                               
SOURCE  31 MOL_ID: 7;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  33 ORGANISM_TAXID: 300852;                                              
SOURCE  34 STRAIN: HB8;                                                         
SOURCE  35 ATCC: 27634 / DSM 579;                                               
SOURCE  36 MOL_ID: 8;                                                           
SOURCE  37 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  38 ORGANISM_TAXID: 300852;                                              
SOURCE  39 STRAIN: HB8;                                                         
SOURCE  40 ATCC: 27634 / DSM 579                                                
KEYWDS    OXIDOREDUCTASE, ELECTRON TRANSPORT, RESPIRATORY CHAIN                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.A.SAZANOV,J.M.BERRISFORD                                            
REVDAT   3   13-JUL-11 3IAM    1       VERSN                                    
REVDAT   2   03-NOV-09 3IAM    1       JRNL                                     
REVDAT   1   15-SEP-09 3IAM    0                                                
JRNL        AUTH   J.M.BERRISFORD,L.A.SAZANOV                                   
JRNL        TITL   STRUCTURAL BASIS FOR THE MECHANISM OF RESPIRATORY COMPLEX I  
JRNL        REF    J.BIOL.CHEM.                  V. 284 29773 2009              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   19635800                                                     
JRNL        DOI    10.1074/JBC.M109.032144                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   L.A.SAZANOV,P.HINCHLIFFE                                     
REMARK   1  TITL   STRUCTURE OF THE HYDROPHILIC DOMAIN OF RESPIRATORY COMPLEX I 
REMARK   1  TITL 2 FROM THERMUS THERMOPHILUS                                    
REMARK   1  REF    SCIENCE                       V. 311  1430 2006              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1  PMID   16469879                                                     
REMARK   1  DOI    10.1126/SCIENCE.1123809                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.57                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 111667                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.232                           
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.940                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2215                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.5720 -  5.9170    0.88    15844   311  0.1760 0.2010        
REMARK   3     2  5.9170 -  4.7020    0.91    16268   296  0.1820 0.2130        
REMARK   3     3  4.7020 -  4.1100    0.93    16517   304  0.2000 0.2280        
REMARK   3     4  4.1100 -  3.7350    0.90    15899   322  0.2350 0.2670        
REMARK   3     5  3.7350 -  3.4670    0.89    15777   346  0.2770 0.3090        
REMARK   3     6  3.4670 -  3.2630    0.90    15859   320  0.3180 0.3450        
REMARK   3     7  3.2630 -  3.1000    0.89    15700   316  0.3570 0.3970        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.31                                          
REMARK   3   B_SOL              : 26.84                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.550            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.370           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 62.81                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 62.22                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.67800                                             
REMARK   3    B22 (A**2) : -3.91100                                             
REMARK   3    B33 (A**2) : 6.59400                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 3.52300                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009          38688                                  
REMARK   3   ANGLE     :  1.375          52756                                  
REMARK   3   CHIRALITY :  0.091           5672                                  
REMARK   3   PLANARITY :  0.006           6802                                  
REMARK   3   DIHEDRAL  : 21.416          14442                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 8                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain 3 and (resseq 1:55 or resseq 73:143   
REMARK   3                          or resseq 150:777 )                         
REMARK   3     SELECTION          : chain C and (resseq 1:55 or resseq 73:143   
REMARK   3                          or resseq 150:777 )                         
REMARK   3     ATOM PAIRS NUMBER  : 5881                                        
REMARK   3     RMSD               : 0.032                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain 1 and (resseq 2:438 )                 
REMARK   3     SELECTION          : chain A and (resseq 2:438 )                 
REMARK   3     ATOM PAIRS NUMBER  : 3417                                        
REMARK   3     RMSD               : 0.036                                       
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain 4 and (resseq 25:31 or resseq 39:     
REMARK   3                          409 )                                       
REMARK   3     SELECTION          : chain D and (resseq 25:31 or resseq 39:     
REMARK   3                          409 )                                       
REMARK   3     ATOM PAIRS NUMBER  : 3018                                        
REMARK   3     RMSD               : 0.032                                       
REMARK   3   NCS GROUP : 4                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain 5 and (resseq 1:196 )                 
REMARK   3     SELECTION          : chain E and (resseq 1:196 )                 
REMARK   3     ATOM PAIRS NUMBER  : 1608                                        
REMARK   3     RMSD               : 0.032                                       
REMARK   3   NCS GROUP : 5                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain 2 and (resseq 2:180 )                 
REMARK   3     SELECTION          : chain B and (resseq 2:180 )                 
REMARK   3     ATOM PAIRS NUMBER  : 1411                                        
REMARK   3     RMSD               : 0.034                                       
REMARK   3   NCS GROUP : 6                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain 9 and (resseq 26:179 )                
REMARK   3     SELECTION          : chain G and (resseq 26:179 )                
REMARK   3     ATOM PAIRS NUMBER  : 1194                                        
REMARK   3     RMSD               : 0.037                                       
REMARK   3   NCS GROUP : 7                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain 6 and (resseq 15:56 or resseq 74:     
REMARK   3                          175 )                                       
REMARK   3     SELECTION          : chain F and (resseq 15:56 or resseq 74:     
REMARK   3                          175 )                                       
REMARK   3     ATOM PAIRS NUMBER  : 1103                                        
REMARK   3     RMSD               : 0.035                                       
REMARK   3   NCS GROUP : 8                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain 7 and (resseq 3:129 )                 
REMARK   3     SELECTION          : chain H and (resseq 3:129 )                 
REMARK   3     ATOM PAIRS NUMBER  : 1031                                        
REMARK   3     RMSD               : 0.032                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NATIVE STRUCTURE FACTORS AND HL           
REMARK   3  COEFFICIENTS ARE FROM PHASING RUN IN SHARP ON NATIVE AND FE-PEAK    
REMARK   3  DATASETS                                                            
REMARK   4                                                                      
REMARK   4 3IAM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUL-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB054173.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97654                            
REMARK 200  MONOCHROMATOR                  : SI(311)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 111667                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.913                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.2                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.15100                            
REMARK 200  R SYM                      (I) : 0.15100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.58600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER AND SHARP                                      
REMARK 200 STARTING MODEL: PDB ENTRY 2FUG                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 0.05 M NACL, 0.1 M   
REMARK 280  MGCL2, 7% PEG4000, 3 MM NADH, 5 MM SODIUM DITHIONITE, VAPOR         
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 295K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       75.50750            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 39370 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 81540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -400.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 1, 2, 3, 4, 5, 6, 9, 7                
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 39170 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 81560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -379.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H                
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET 1     1                                                      
REMARK 465     MET 2     1                                                      
REMARK 465     VAL 2   181                                                      
REMARK 465     LYS 3    56                                                      
REMARK 465     LYS 3    57                                                      
REMARK 465     GLY 3    58                                                      
REMARK 465     PRO 3    59                                                      
REMARK 465     ASP 3    60                                                      
REMARK 465     GLY 3    61                                                      
REMARK 465     LYS 3    62                                                      
REMARK 465     PRO 3    63                                                      
REMARK 465     LEU 3    64                                                      
REMARK 465     LEU 3    65                                                      
REMARK 465     ASN 3    66                                                      
REMARK 465     GLU 3    67                                                      
REMARK 465     LYS 3    68                                                      
REMARK 465     GLY 3    69                                                      
REMARK 465     GLU 3    70                                                      
REMARK 465     PRO 3    71                                                      
REMARK 465     GLU 3    72                                                      
REMARK 465     TYR 3   144                                                      
REMARK 465     GLN 3   145                                                      
REMARK 465     LYS 3   146                                                      
REMARK 465     GLY 3   147                                                      
REMARK 465     PRO 3   148                                                      
REMARK 465     LEU 3   149                                                      
REMARK 465     PRO 3   778                                                      
REMARK 465     ALA 3   779                                                      
REMARK 465     GLY 3   780                                                      
REMARK 465     GLY 3   781                                                      
REMARK 465     GLU 3   782                                                      
REMARK 465     ALA 3   783                                                      
REMARK 465     MET 4     1                                                      
REMARK 465     ARG 4     2                                                      
REMARK 465     GLU 4     3                                                      
REMARK 465     GLU 4     4                                                      
REMARK 465     PHE 4     5                                                      
REMARK 465     LEU 4     6                                                      
REMARK 465     GLU 4     7                                                      
REMARK 465     GLU 4     8                                                      
REMARK 465     ILE 4     9                                                      
REMARK 465     PRO 4    10                                                      
REMARK 465     LEU 4    11                                                      
REMARK 465     ASP 4    12                                                      
REMARK 465     ALA 4    13                                                      
REMARK 465     PRO 4    14                                                      
REMARK 465     PRO 4    15                                                      
REMARK 465     GLU 4    16                                                      
REMARK 465     GLU 4    17                                                      
REMARK 465     ALA 4    18                                                      
REMARK 465     LYS 4    19                                                      
REMARK 465     GLU 4    20                                                      
REMARK 465     LEU 4    21                                                      
REMARK 465     ARG 4    22                                                      
REMARK 465     THR 4    23                                                      
REMARK 465     GLU 4    24                                                      
REMARK 465     PRO 4    32                                                      
REMARK 465     GLN 4    33                                                      
REMARK 465     HIS 4    34                                                      
REMARK 465     PRO 4    35                                                      
REMARK 465     SER 4    36                                                      
REMARK 465     THR 4    37                                                      
REMARK 465     HIS 4    38                                                      
REMARK 465     ALA 5   197                                                      
REMARK 465     ASP 5   198                                                      
REMARK 465     LEU 5   199                                                      
REMARK 465     LYS 5   200                                                      
REMARK 465     LYS 5   201                                                      
REMARK 465     ALA 5   202                                                      
REMARK 465     ARG 5   203                                                      
REMARK 465     GLU 5   204                                                      
REMARK 465     VAL 5   205                                                      
REMARK 465     LYS 5   206                                                      
REMARK 465     GLY 5   207                                                      
REMARK 465     MET 6     1                                                      
REMARK 465     ALA 6     2                                                      
REMARK 465     LEU 6     3                                                      
REMARK 465     LYS 6     4                                                      
REMARK 465     ASP 6     5                                                      
REMARK 465     LEU 6     6                                                      
REMARK 465     PHE 6     7                                                      
REMARK 465     GLU 6     8                                                      
REMARK 465     ARG 6     9                                                      
REMARK 465     ASP 6    10                                                      
REMARK 465     VAL 6    11                                                      
REMARK 465     GLN 6    12                                                      
REMARK 465     GLU 6    13                                                      
REMARK 465     LEU 6    14                                                      
REMARK 465     ARG 6    57                                                      
REMARK 465     ASN 6    58                                                      
REMARK 465     ASP 6    59                                                      
REMARK 465     LEU 6    60                                                      
REMARK 465     ALA 6    61                                                      
REMARK 465     ARG 6    62                                                      
REMARK 465     PHE 6    63                                                      
REMARK 465     GLY 6    64                                                      
REMARK 465     SER 6    65                                                      
REMARK 465     GLU 6    66                                                      
REMARK 465     VAL 6    67                                                      
REMARK 465     PHE 6    68                                                      
REMARK 465     ARG 6    69                                                      
REMARK 465     ALA 6    70                                                      
REMARK 465     SER 6    71                                                      
REMARK 465     PRO 6    72                                                      
REMARK 465     ARG 6    73                                                      
REMARK 465     TRP 6   176                                                      
REMARK 465     LYS 6   177                                                      
REMARK 465     ARG 6   178                                                      
REMARK 465     THR 6   179                                                      
REMARK 465     ARG 6   180                                                      
REMARK 465     GLY 6   181                                                      
REMARK 465     MET 9     1                                                      
REMARK 465     THR 9     2                                                      
REMARK 465     LEU 9     3                                                      
REMARK 465     LYS 9     4                                                      
REMARK 465     ALA 9     5                                                      
REMARK 465     LEU 9     6                                                      
REMARK 465     ALA 9     7                                                      
REMARK 465     GLN 9     8                                                      
REMARK 465     SER 9     9                                                      
REMARK 465     LEU 9    10                                                      
REMARK 465     GLY 9    11                                                      
REMARK 465     ILE 9    12                                                      
REMARK 465     THR 9    13                                                      
REMARK 465     LEU 9    14                                                      
REMARK 465     LYS 9    15                                                      
REMARK 465     TYR 9    16                                                      
REMARK 465     LEU 9    17                                                      
REMARK 465     PHE 9    18                                                      
REMARK 465     SER 9    19                                                      
REMARK 465     LYS 9    20                                                      
REMARK 465     PRO 9    21                                                      
REMARK 465     VAL 9    22                                                      
REMARK 465     THR 9    23                                                      
REMARK 465     VAL 9    24                                                      
REMARK 465     PRO 9    25                                                      
REMARK 465     GLY 9   180                                                      
REMARK 465     LYS 9   181                                                      
REMARK 465     ARG 9   182                                                      
REMARK 465     MET 7     1                                                      
REMARK 465     SER 7     2                                                      
REMARK 465     MET A     1                                                      
REMARK 465     MET B     1                                                      
REMARK 465     VAL B   181                                                      
REMARK 465     LYS C    56                                                      
REMARK 465     LYS C    57                                                      
REMARK 465     GLY C    58                                                      
REMARK 465     PRO C    59                                                      
REMARK 465     ASP C    60                                                      
REMARK 465     GLY C    61                                                      
REMARK 465     LYS C    62                                                      
REMARK 465     PRO C    63                                                      
REMARK 465     LEU C    64                                                      
REMARK 465     LEU C    65                                                      
REMARK 465     ASN C    66                                                      
REMARK 465     GLU C    67                                                      
REMARK 465     LYS C    68                                                      
REMARK 465     GLY C    69                                                      
REMARK 465     GLU C    70                                                      
REMARK 465     PRO C    71                                                      
REMARK 465     GLU C    72                                                      
REMARK 465     TYR C   144                                                      
REMARK 465     GLN C   145                                                      
REMARK 465     LYS C   146                                                      
REMARK 465     GLY C   147                                                      
REMARK 465     PRO C   148                                                      
REMARK 465     LEU C   149                                                      
REMARK 465     PRO C   778                                                      
REMARK 465     ALA C   779                                                      
REMARK 465     GLY C   780                                                      
REMARK 465     GLY C   781                                                      
REMARK 465     GLU C   782                                                      
REMARK 465     ALA C   783                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ARG D     2                                                      
REMARK 465     GLU D     3                                                      
REMARK 465     GLU D     4                                                      
REMARK 465     PHE D     5                                                      
REMARK 465     LEU D     6                                                      
REMARK 465     GLU D     7                                                      
REMARK 465     GLU D     8                                                      
REMARK 465     ILE D     9                                                      
REMARK 465     PRO D    10                                                      
REMARK 465     LEU D    11                                                      
REMARK 465     ASP D    12                                                      
REMARK 465     ALA D    13                                                      
REMARK 465     PRO D    14                                                      
REMARK 465     PRO D    15                                                      
REMARK 465     GLU D    16                                                      
REMARK 465     GLU D    17                                                      
REMARK 465     ALA D    18                                                      
REMARK 465     LYS D    19                                                      
REMARK 465     GLU D    20                                                      
REMARK 465     LEU D    21                                                      
REMARK 465     ARG D    22                                                      
REMARK 465     THR D    23                                                      
REMARK 465     GLU D    24                                                      
REMARK 465     PRO D    32                                                      
REMARK 465     GLN D    33                                                      
REMARK 465     HIS D    34                                                      
REMARK 465     PRO D    35                                                      
REMARK 465     SER D    36                                                      
REMARK 465     THR D    37                                                      
REMARK 465     HIS D    38                                                      
REMARK 465     ALA E   197                                                      
REMARK 465     ASP E   198                                                      
REMARK 465     LEU E   199                                                      
REMARK 465     LYS E   200                                                      
REMARK 465     LYS E   201                                                      
REMARK 465     ALA E   202                                                      
REMARK 465     ARG E   203                                                      
REMARK 465     GLU E   204                                                      
REMARK 465     VAL E   205                                                      
REMARK 465     LYS E   206                                                      
REMARK 465     GLY E   207                                                      
REMARK 465     MET F     1                                                      
REMARK 465     ALA F     2                                                      
REMARK 465     LEU F     3                                                      
REMARK 465     LYS F     4                                                      
REMARK 465     ASP F     5                                                      
REMARK 465     LEU F     6                                                      
REMARK 465     PHE F     7                                                      
REMARK 465     GLU F     8                                                      
REMARK 465     ARG F     9                                                      
REMARK 465     ASP F    10                                                      
REMARK 465     VAL F    11                                                      
REMARK 465     GLN F    12                                                      
REMARK 465     GLU F    13                                                      
REMARK 465     LEU F    14                                                      
REMARK 465     ARG F    57                                                      
REMARK 465     ASN F    58                                                      
REMARK 465     ASP F    59                                                      
REMARK 465     LEU F    60                                                      
REMARK 465     ALA F    61                                                      
REMARK 465     ARG F    62                                                      
REMARK 465     PHE F    63                                                      
REMARK 465     GLY F    64                                                      
REMARK 465     SER F    65                                                      
REMARK 465     GLU F    66                                                      
REMARK 465     VAL F    67                                                      
REMARK 465     PHE F    68                                                      
REMARK 465     ARG F    69                                                      
REMARK 465     ALA F    70                                                      
REMARK 465     SER F    71                                                      
REMARK 465     PRO F    72                                                      
REMARK 465     ARG F    73                                                      
REMARK 465     TRP F   176                                                      
REMARK 465     LYS F   177                                                      
REMARK 465     ARG F   178                                                      
REMARK 465     THR F   179                                                      
REMARK 465     ARG F   180                                                      
REMARK 465     GLY F   181                                                      
REMARK 465     MET G     1                                                      
REMARK 465     THR G     2                                                      
REMARK 465     LEU G     3                                                      
REMARK 465     LYS G     4                                                      
REMARK 465     ALA G     5                                                      
REMARK 465     LEU G     6                                                      
REMARK 465     ALA G     7                                                      
REMARK 465     GLN G     8                                                      
REMARK 465     SER G     9                                                      
REMARK 465     LEU G    10                                                      
REMARK 465     GLY G    11                                                      
REMARK 465     ILE G    12                                                      
REMARK 465     THR G    13                                                      
REMARK 465     LEU G    14                                                      
REMARK 465     LYS G    15                                                      
REMARK 465     TYR G    16                                                      
REMARK 465     LEU G    17                                                      
REMARK 465     PHE G    18                                                      
REMARK 465     SER G    19                                                      
REMARK 465     LYS G    20                                                      
REMARK 465     PRO G    21                                                      
REMARK 465     VAL G    22                                                      
REMARK 465     THR G    23                                                      
REMARK 465     VAL G    24                                                      
REMARK 465     PRO G    25                                                      
REMARK 465     GLY G   180                                                      
REMARK 465     LYS G   181                                                      
REMARK 465     ARG G   182                                                      
REMARK 465     MET H     1                                                      
REMARK 465     SER H     2                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    GLU 1   427     NH1  ARG 3   316     2545     2.12            
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 1 292   C   -  N   -  CA  ANGL. DEV. =  11.1 DEGREES          
REMARK 500    PRO 3 116   C   -  N   -  CA  ANGL. DEV. =  11.7 DEGREES          
REMARK 500    PRO 3 219   C   -  N   -  CA  ANGL. DEV. =  12.6 DEGREES          
REMARK 500    GLY 4  39   N   -  CA  -  C   ANGL. DEV. = -19.3 DEGREES          
REMARK 500    LEU 4 105   CA  -  CB  -  CG  ANGL. DEV. =  16.6 DEGREES          
REMARK 500    PRO 6  38   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    PRO A 292   C   -  N   -  CA  ANGL. DEV. =  10.8 DEGREES          
REMARK 500    PRO C 116   C   -  N   -  CA  ANGL. DEV. =  11.6 DEGREES          
REMARK 500    PRO C 219   C   -  N   -  CA  ANGL. DEV. =  12.4 DEGREES          
REMARK 500    GLY D  39   N   -  CA  -  C   ANGL. DEV. = -19.0 DEGREES          
REMARK 500    LEU D 105   CA  -  CB  -  CG  ANGL. DEV. =  16.5 DEGREES          
REMARK 500    PRO E 145   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    PRO F  38   C   -  N   -  CA  ANGL. DEV. =   9.1 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    PRO 1   4      -90.96   -113.52                                   
REMARK 500    SER 1   7       23.53   -143.99                                   
REMARK 500    THR 1  16      -55.66   -125.90                                   
REMARK 500    LEU 1  17      -70.90    -79.54                                   
REMARK 500    TYR 1  18        3.43    -69.46                                   
REMARK 500    HIS 1  35        6.54    -67.05                                   
REMARK 500    TYR 1  38       31.23    -72.34                                   
REMARK 500    GLU 1  47      -79.95    -99.03                                   
REMARK 500    PRO 1  71       93.43    -35.00                                   
REMARK 500    LYS 1  81      -75.16    -72.63                                   
REMARK 500    VAL 1 110       56.89   -155.95                                   
REMARK 500    ASP 1 166       40.12    -90.14                                   
REMARK 500    ALA 1 177       39.60   -162.32                                   
REMARK 500    ALA 1 179      105.75   -165.55                                   
REMARK 500    TYR 1 277      -71.40   -104.96                                   
REMARK 500    MET 1 311       85.59    -64.79                                   
REMARK 500    TYR 1 313       21.16    -68.73                                   
REMARK 500    GLU 1 314      -39.43   -151.40                                   
REMARK 500    SER 1 321     -144.74   -143.31                                   
REMARK 500    ARG 1 360      -85.21    -55.39                                   
REMARK 500    ARG 1 433       76.31   -112.90                                   
REMARK 500    PRO 2  74      130.50    -35.92                                   
REMARK 500    LEU 2  86      -64.82    -16.49                                   
REMARK 500    PRO 2 108      -93.81    -18.67                                   
REMARK 500    THR 2 112      158.18    -46.26                                   
REMARK 500    CYS 2 124      101.48     -7.97                                   
REMARK 500    SER 2 127       55.45   -144.29                                   
REMARK 500    THR 2 130       57.51   -114.94                                   
REMARK 500    ASN 2 137      -75.77   -118.76                                   
REMARK 500    HIS 2 174      -99.70    -88.68                                   
REMARK 500    VAL 3   6     -106.99    -67.30                                   
REMARK 500    VAL 3  13      141.23   -178.05                                   
REMARK 500    TYR 3  28     -169.99    -61.54                                   
REMARK 500    PRO 3  31      171.51    -41.45                                   
REMARK 500    LEU 3  32       99.63    175.10                                   
REMARK 500    PHE 3  33      -79.62   -117.49                                   
REMARK 500    SER 3  97      150.23    -44.38                                   
REMARK 500    LEU 3 117       42.27     97.47                                   
REMARK 500    CYS 3 119      -61.68    -28.84                                   
REMARK 500    THR 3 121       44.84    -96.19                                   
REMARK 500    LYS 3 124       25.72    -72.13                                   
REMARK 500    ALA 3 127       35.09    -91.73                                   
REMARK 500    GLU 3 141       76.73   -108.36                                   
REMARK 500    VAL 3 164     -157.83   -155.00                                   
REMARK 500    HIS 3 167       62.03     39.66                                   
REMARK 500    CYS 3 181      128.62    -38.38                                   
REMARK 500    ILE 3 203     -109.86   -111.36                                   
REMARK 500    PHE 3 216      -80.64     34.12                                   
REMARK 500    LEU 3 218       61.04     64.31                                   
REMARK 500    PHE 3 222       37.61   -144.38                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     336 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 1 439  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 1 353   SG                                                     
REMARK 620 2 SF4 1 439   S1  112.1                                              
REMARK 620 3 SF4 1 439   S2  114.6 108.5                                        
REMARK 620 4 SF4 1 439   S3  117.2  98.0 104.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 1 439  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 1 356   SG                                                     
REMARK 620 2 SF4 1 439   S2  119.1                                              
REMARK 620 3 SF4 1 439   S3  115.6 105.3                                        
REMARK 620 4 SF4 1 439   S4  109.4 102.9 102.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 1 439  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 1 359   SG                                                     
REMARK 620 2 SF4 1 439   S1  127.6                                              
REMARK 620 3 SF4 1 439   S3  105.3  97.7                                        
REMARK 620 4 SF4 1 439   S4  108.4 111.0 103.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 1 439  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 1 400   SG                                                     
REMARK 620 2 SF4 1 439   S1  117.1                                              
REMARK 620 3 SF4 1 439   S2  106.4 106.7                                        
REMARK 620 4 SF4 1 439   S4  113.2 109.7 102.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES 2 182  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 2  83   SG                                                     
REMARK 620 2 FES 2 182   S1  116.2                                              
REMARK 620 3 FES 2 182   S2  113.4  93.1                                        
REMARK 620 4 CYS 2  88   SG   99.9 115.4 120.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES 2 182  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 2 124   SG                                                     
REMARK 620 2 FES 2 182   S1  113.7                                              
REMARK 620 3 FES 2 182   S2  107.8  92.3                                        
REMARK 620 4 CYS 2 128   SG  112.6 110.5 118.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES 3 787  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 3  34   SG                                                     
REMARK 620 2 FES 3 787   S1  108.8                                              
REMARK 620 3 FES 3 787   S2  111.4  95.6                                        
REMARK 620 4 CYS 3  45   SG  114.1 112.9 112.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES 3 787  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 3  48   SG                                                     
REMARK 620 2 FES 3 787   S1  118.0                                              
REMARK 620 3 FES 3 787   S2  111.6  96.0                                        
REMARK 620 4 CYS 3  83   SG  101.9 113.0 117.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 3 784  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS 3 115   NE2                                                    
REMARK 620 2 SF4 3 784   S1  135.9                                              
REMARK 620 3 SF4 3 784   S2  114.1 102.7                                        
REMARK 620 4 SF4 3 784   S4   92.7 103.1 101.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 3 784  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 3 119   SG                                                     
REMARK 620 2 SF4 3 784   S1  109.7                                              
REMARK 620 3 SF4 3 784   S3  118.8 103.1                                        
REMARK 620 4 SF4 3 784   S4  112.6 102.1 108.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 3 784  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 3 122   SG                                                     
REMARK 620 2 SF4 3 784   S1  117.1                                              
REMARK 620 3 SF4 3 784   S2  117.9 103.5                                        
REMARK 620 4 SF4 3 784   S3  109.2 104.4 103.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 3 784  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 3 128   SG                                                     
REMARK 620 2 SF4 3 784   S2  116.2                                              
REMARK 620 3 SF4 3 784   S3  108.1 103.0                                        
REMARK 620 4 SF4 3 784   S4  118.6 102.2 107.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 3 785  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 3 181   SG                                                     
REMARK 620 2 SF4 3 785   S1  110.5                                              
REMARK 620 3 SF4 3 785   S3  119.1 100.2                                        
REMARK 620 4 SF4 3 785   S4  114.6 107.8 103.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 3 785  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 3 184   SG                                                     
REMARK 620 2 SF4 3 785   S2  106.8                                              
REMARK 620 3 SF4 3 785   S3  115.7 105.9                                        
REMARK 620 4 SF4 3 785   S4  124.5  98.6 102.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 3 785  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 3 187   SG                                                     
REMARK 620 2 SF4 3 785   S1  124.9                                              
REMARK 620 3 SF4 3 785   S2  105.5 106.5                                        
REMARK 620 4 SF4 3 785   S4  111.2 108.4  96.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 3 785  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 3 230   SG                                                     
REMARK 620 2 SF4 3 785   S1  117.4                                              
REMARK 620 3 SF4 3 785   S2  117.0 107.2                                        
REMARK 620 4 SF4 3 785   S3  109.8  97.8 105.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 3 786  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 3 256   SG                                                     
REMARK 620 2 SF4 3 786   S2  108.8                                              
REMARK 620 3 SF4 3 786   S3  118.2 108.4                                        
REMARK 620 4 SF4 3 786   S4  112.3 100.9 106.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 3 786  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 3 259   SG                                                     
REMARK 620 2 SF4 3 786   S1  114.0                                              
REMARK 620 3 SF4 3 786   S2  119.3 100.6                                        
REMARK 620 4 SF4 3 786   S3  110.5 100.7 109.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 3 786  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 3 263   SG                                                     
REMARK 620 2 SF4 3 786   S1  121.3                                              
REMARK 620 3 SF4 3 786   S2  102.9 100.4                                        
REMARK 620 4 SF4 3 786   S4  121.0 104.3 103.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 3 786  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 3 291   SG                                                     
REMARK 620 2 SF4 3 786   S1  122.5                                              
REMARK 620 3 SF4 3 786   S3  102.2 101.0                                        
REMARK 620 4 SF4 3 786   S4  119.0 102.8 107.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 6 182  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 6  45   SG                                                     
REMARK 620 2 SF4 6 182   S1  114.0                                              
REMARK 620 3 SF4 6 182   S2  119.7 106.5                                        
REMARK 620 4 SF4 6 182   S4  109.6 104.7 100.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 6 182  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 6 111   SG                                                     
REMARK 620 2 SF4 6 182   S2  116.0                                              
REMARK 620 3 SF4 6 182   S3  105.3 107.5                                        
REMARK 620 4 SF4 6 182   S4  121.2 101.3 104.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 6 182  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 6 140   SG                                                     
REMARK 620 2 SF4 6 182   S1  118.4                                              
REMARK 620 3 SF4 6 182   S2  111.1 104.5                                        
REMARK 620 4 SF4 6 182   S3  109.7 106.4 106.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 9 184  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 9  53   SG                                                     
REMARK 620 2 SF4 9 184   S1  112.2                                              
REMARK 620 3 SF4 9 184   S2  115.1 102.2                                        
REMARK 620 4 SF4 9 184   S4  119.5 105.2 100.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 9 184  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 9  56   SG                                                     
REMARK 620 2 SF4 9 184   S1  111.2                                              
REMARK 620 3 SF4 9 184   S2  125.6 100.4                                        
REMARK 620 4 SF4 9 184   S3  105.9 105.2 107.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 9 184  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 9  59   SG                                                     
REMARK 620 2 SF4 9 184   S1  113.5                                              
REMARK 620 3 SF4 9 184   S3  104.6 104.9                                        
REMARK 620 4 SF4 9 184   S4  126.0 103.6 101.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 9 183  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 9  63   SG                                                     
REMARK 620 2 SF4 9 183   S1  116.5                                              
REMARK 620 3 SF4 9 183   S2  112.2 102.5                                        
REMARK 620 4 SF4 9 183   S3  111.6 108.9 104.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 9 183  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 9  98   SG                                                     
REMARK 620 2 SF4 9 183   S1  116.5                                              
REMARK 620 3 SF4 9 183   S3  116.2 107.7                                        
REMARK 620 4 SF4 9 183   S4  105.3 110.0  99.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 9 183  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 9 101   SG                                                     
REMARK 620 2 SF4 9 183   S2  100.2                                              
REMARK 620 3 SF4 9 183   S3  118.3 104.9                                        
REMARK 620 4 SF4 9 183   S4  123.7 107.5 100.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 9 183  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 9 104   SG                                                     
REMARK 620 2 SF4 9 183   S1  116.9                                              
REMARK 620 3 SF4 9 183   S2  107.4 102.0                                        
REMARK 620 4 SF4 9 183   S4  112.7 109.5 107.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 9 184  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 9 108   SG                                                     
REMARK 620 2 SF4 9 184   S2  114.6                                              
REMARK 620 3 SF4 9 184   S3  103.5 108.7                                        
REMARK 620 4 SF4 9 184   S4  125.8 101.1 101.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 439  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 353   SG                                                     
REMARK 620 2 SF4 A 439   S1  114.0                                              
REMARK 620 3 SF4 A 439   S2  110.4 105.7                                        
REMARK 620 4 SF4 A 439   S3  118.5 101.7 105.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 439  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 356   SG                                                     
REMARK 620 2 SF4 A 439   S2  117.8                                              
REMARK 620 3 SF4 A 439   S3  109.4 105.8                                        
REMARK 620 4 SF4 A 439   S4  111.2 106.8 105.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 439  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 359   SG                                                     
REMARK 620 2 SF4 A 439   S1  129.2                                              
REMARK 620 3 SF4 A 439   S3  108.6 101.2                                        
REMARK 620 4 SF4 A 439   S4  105.9 104.1 106.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 439  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 400   SG                                                     
REMARK 620 2 SF4 A 439   S1  115.5                                              
REMARK 620 3 SF4 A 439   S2  113.7 106.0                                        
REMARK 620 4 SF4 A 439   S4  109.7 103.3 107.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 182  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  83   SG                                                     
REMARK 620 2 FES B 182   S1  110.9                                              
REMARK 620 3 FES B 182   S2  116.8  92.3                                        
REMARK 620 4 CYS B  88   SG  103.6 115.8 117.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 182  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 124   SG                                                     
REMARK 620 2 FES B 182   S1  116.8                                              
REMARK 620 3 FES B 182   S2  114.0  91.9                                        
REMARK 620 4 CYS B 128   SG  106.9 114.0 113.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES C 787  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  34   SG                                                     
REMARK 620 2 FES C 787   S1  112.3                                              
REMARK 620 3 FES C 787   S2  109.0  93.2                                        
REMARK 620 4 CYS C  45   SG  117.2 112.3 110.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES C 787  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  48   SG                                                     
REMARK 620 2 FES C 787   S1  119.1                                              
REMARK 620 3 FES C 787   S2  120.9  93.8                                        
REMARK 620 4 CYS C  83   SG   98.1 110.0 115.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 784  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 115   NE2                                                    
REMARK 620 2 SF4 C 784   S1  135.1                                              
REMARK 620 3 SF4 C 784   S2  110.6 105.2                                        
REMARK 620 4 SF4 C 784   S4   91.8 107.7 100.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 784  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 119   SG                                                     
REMARK 620 2 SF4 C 784   S1  116.5                                              
REMARK 620 3 SF4 C 784   S3  113.6 105.8                                        
REMARK 620 4 SF4 C 784   S4  110.4 108.1 101.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 784  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 122   SG                                                     
REMARK 620 2 SF4 C 784   S1  112.3                                              
REMARK 620 3 SF4 C 784   S2  118.5 104.8                                        
REMARK 620 4 SF4 C 784   S3  110.4 106.1 103.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 784  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 128   SG                                                     
REMARK 620 2 SF4 C 784   S2  121.4                                              
REMARK 620 3 SF4 C 784   S3  108.2 104.6                                        
REMARK 620 4 SF4 C 784   S4  117.3 101.0 102.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 785  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 181   SG                                                     
REMARK 620 2 SF4 C 785   S1  116.8                                              
REMARK 620 3 SF4 C 785   S3  112.1 105.1                                        
REMARK 620 4 SF4 C 785   S4  111.6 109.6 100.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 785  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 184   SG                                                     
REMARK 620 2 SF4 C 785   S2  107.1                                              
REMARK 620 3 SF4 C 785   S3  112.9 107.3                                        
REMARK 620 4 SF4 C 785   S4  126.1 100.8 100.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 785  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 187   SG                                                     
REMARK 620 2 SF4 C 785   S1  119.1                                              
REMARK 620 3 SF4 C 785   S2  108.8 105.9                                        
REMARK 620 4 SF4 C 785   S4  111.4 110.1  99.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 785  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 230   SG                                                     
REMARK 620 2 SF4 C 785   S1  116.4                                              
REMARK 620 3 SF4 C 785   S2  113.5 105.9                                        
REMARK 620 4 SF4 C 785   S3  109.8 104.5 106.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 786  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 256   SG                                                     
REMARK 620 2 SF4 C 786   S2  107.2                                              
REMARK 620 3 SF4 C 786   S3  116.4 104.9                                        
REMARK 620 4 SF4 C 786   S4  116.1 102.8 107.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 786  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 259   SG                                                     
REMARK 620 2 SF4 C 786   S1  108.5                                              
REMARK 620 3 SF4 C 786   S2  119.7 102.8                                        
REMARK 620 4 SF4 C 786   S3  113.3 105.0 106.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 786  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 263   SG                                                     
REMARK 620 2 SF4 C 786   S1  119.1                                              
REMARK 620 3 SF4 C 786   S2  114.7 103.0                                        
REMARK 620 4 SF4 C 786   S4  113.6 100.1 104.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 786  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 291   SG                                                     
REMARK 620 2 SF4 C 786   S1  121.0                                              
REMARK 620 3 SF4 C 786   S3  109.2 105.8                                        
REMARK 620 4 SF4 C 786   S4  112.6  99.3 108.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 F 182  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F  45   SG                                                     
REMARK 620 2 SF4 F 182   S1  110.6                                              
REMARK 620 3 SF4 F 182   S2  122.1 103.4                                        
REMARK 620 4 SF4 F 182   S4  111.1 104.7 103.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 F 182  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 111   SG                                                     
REMARK 620 2 SF4 F 182   S2  114.5                                              
REMARK 620 3 SF4 F 182   S3  104.4 106.4                                        
REMARK 620 4 SF4 F 182   S4  124.7 104.0 100.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 F 182  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 140   SG                                                     
REMARK 620 2 SF4 F 182   S1  113.0                                              
REMARK 620 3 SF4 F 182   S2  107.5 102.0                                        
REMARK 620 4 SF4 F 182   S3  118.4 108.6 105.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 G 184  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G  53   SG                                                     
REMARK 620 2 SF4 G 184   S1  110.0                                              
REMARK 620 3 SF4 G 184   S2  116.1 103.1                                        
REMARK 620 4 SF4 G 184   S4  120.2 102.3 103.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 G 184  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G  56   SG                                                     
REMARK 620 2 SF4 G 184   S1  119.1                                              
REMARK 620 3 SF4 G 184   S2  120.6 101.4                                        
REMARK 620 4 SF4 G 184   S3  102.1 106.1 106.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 G 184  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G  59   SG                                                     
REMARK 620 2 SF4 G 184   S1  114.0                                              
REMARK 620 3 SF4 G 184   S3  105.2 107.1                                        
REMARK 620 4 SF4 G 184   S4  123.2 102.2 103.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 G 183  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G  63   SG                                                     
REMARK 620 2 SF4 G 183   S1  122.0                                              
REMARK 620 3 SF4 G 183   S2  104.7 100.2                                        
REMARK 620 4 SF4 G 183   S3  116.1 107.4 103.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 G 183  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G  98   SG                                                     
REMARK 620 2 SF4 G 183   S1  110.8                                              
REMARK 620 3 SF4 G 183   S3  113.7 104.5                                        
REMARK 620 4 SF4 G 183   S4  116.3 108.4 102.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 G 183  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G 101   SG                                                     
REMARK 620 2 SF4 G 183   S2  103.6                                              
REMARK 620 3 SF4 G 183   S3  123.4 104.9                                        
REMARK 620 4 SF4 G 183   S4  115.6 105.3 102.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 G 183  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G 104   SG                                                     
REMARK 620 2 SF4 G 183   S1  117.6                                              
REMARK 620 3 SF4 G 183   S2  114.9 100.3                                        
REMARK 620 4 SF4 G 183   S4  109.2 108.1 105.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 G 184  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G 108   SG                                                     
REMARK 620 2 SF4 G 184   S2  112.6                                              
REMARK 620 3 SF4 G 184   S3  106.9 106.7                                        
REMARK 620 4 SF4 G 184   S4  123.4 102.5 103.4                                  
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 6 182                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 9 183                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 9 184                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 3 784                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 3 785                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 3 786                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES 3 787                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 1 439                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES 2 182                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN 1 440                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI 1 441                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 3 788                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 3 789                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 5 208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 1 442                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA 7 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 4 410                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 F 182                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 G 183                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 G 184                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C 784                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C 785                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C 786                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES C 787                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 439                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 182                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN A 440                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI A 441                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 788                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 789                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 442                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 204                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2FUG   RELATED DB: PDB                                   
REMARK 900 ORIGINAL CRYSTAL STRUCTURE OF THE HYDROPHILIC DOMAIN OF              
REMARK 900 RESPIRATORY COMPLEX I FROM THERMUS THERMOPHILUS, OXIDIZED,           
REMARK 900 4 MOL/ASU                                                            
REMARK 900 RELATED ID: 3I9V   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HYDROPHILIC DOMAIN OF RESPIRATORY           
REMARK 900 COMPLEX I FROM THERMUS THERMOPHILUS, OXIDIZED, 2 MOL/ASU             
REMARK 900 RELATED ID: 3IAS   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HYDROPHILIC DOMAIN OF RESPIRATORY           
REMARK 900 COMPLEX I FROM THERMUS THERMOPHILUS, OXIDIZED, 4 MOL/ASU,            
REMARK 900 RE-REFINED TO 3.15 ANGSTROM RESOLUTION                               
DBREF  3IAM 1    1   438  UNP    Q56222   NQO1_THET8       1    438             
DBREF  3IAM 2    1   181  UNP    Q56221   NQO2_THET8       1    181             
DBREF  3IAM 3    1   783  UNP    Q56223   NQO3_THET8       1    783             
DBREF  3IAM 4    1   409  UNP    Q56220   NQO4_THET8       1    409             
DBREF  3IAM 5    1   207  UNP    Q56219   NQO5_THET8       1    207             
DBREF  3IAM 6    1   181  UNP    Q56218   NQO6_THET8       1    181             
DBREF  3IAM 9    1   182  UNP    Q56224   NQO9_THET8       1    182             
DBREF  3IAM 7    1   129  UNP    Q5SKZ7   NQO15_THET8      1    129             
DBREF  3IAM A    1   438  UNP    Q56222   NQO1_THET8       1    438             
DBREF  3IAM B    1   181  UNP    Q56221   NQO2_THET8       1    181             
DBREF  3IAM C    1   783  UNP    Q56223   NQO3_THET8       1    783             
DBREF  3IAM D    1   409  UNP    Q56220   NQO4_THET8       1    409             
DBREF  3IAM E    1   207  UNP    Q56219   NQO5_THET8       1    207             
DBREF  3IAM F    1   181  UNP    Q56218   NQO6_THET8       1    181             
DBREF  3IAM G    1   182  UNP    Q56224   NQO9_THET8       1    182             
DBREF  3IAM H    1   129  UNP    Q5SKZ7   NQO15_THET8      1    129             
SEQRES   1 1  438  MET THR GLY PRO ILE LEU SER GLY LEU ASP PRO ARG PHE          
SEQRES   2 1  438  GLU ARG THR LEU TYR ALA HIS VAL GLY LYS GLU GLY SER          
SEQRES   3 1  438  TRP THR LEU ASP TYR TYR LEU ARG HIS GLY GLY TYR GLU          
SEQRES   4 1  438  THR ALA LYS ARG VAL LEU LYS GLU LYS THR PRO ASP GLU          
SEQRES   5 1  438  VAL ILE GLU GLU VAL LYS ARG SER GLY LEU ARG GLY ARG          
SEQRES   6 1  438  GLY GLY ALA GLY PHE PRO THR GLY LEU LYS TRP SER PHE          
SEQRES   7 1  438  MET PRO LYS ASP ASP GLY LYS GLN HIS TYR LEU ILE CYS          
SEQRES   8 1  438  ASN ALA ASP GLU SER GLU PRO GLY SER PHE LYS ASP ARG          
SEQRES   9 1  438  TYR ILE LEU GLU ASP VAL PRO HIS LEU LEU ILE GLU GLY          
SEQRES  10 1  438  MET ILE LEU ALA GLY TYR ALA ILE ARG ALA THR VAL GLY          
SEQRES  11 1  438  TYR ILE TYR VAL ARG GLY GLU TYR ARG ARG ALA ALA ASP          
SEQRES  12 1  438  ARG LEU GLU GLN ALA ILE LYS GLU ALA ARG ALA ARG GLY          
SEQRES  13 1  438  TYR LEU GLY LYS ASN LEU PHE GLY THR ASP PHE SER PHE          
SEQRES  14 1  438  ASP LEU HIS VAL HIS ARG GLY ALA GLY ALA TYR ILE CYS          
SEQRES  15 1  438  GLY GLU GLU THR ALA LEU MET ASN SER LEU GLU GLY LEU          
SEQRES  16 1  438  ARG ALA ASN PRO ARG LEU LYS PRO PRO PHE PRO ALA GLN          
SEQRES  17 1  438  SER GLY LEU TRP GLY LYS PRO THR THR ILE ASN ASN VAL          
SEQRES  18 1  438  GLU THR LEU ALA SER VAL VAL PRO ILE MET GLU ARG GLY          
SEQRES  19 1  438  ALA ASP TRP PHE ALA GLN MET GLY THR GLU GLN SER LYS          
SEQRES  20 1  438  GLY MET LYS LEU TYR GLN ILE SER GLY PRO VAL LYS ARG          
SEQRES  21 1  438  PRO GLY VAL TYR GLU LEU PRO MET GLY THR THR PHE ARG          
SEQRES  22 1  438  GLU LEU ILE TYR GLU TRP ALA GLY GLY PRO LEU GLU PRO          
SEQRES  23 1  438  ILE GLN ALA ILE ILE PRO GLY GLY SER SER THR PRO PRO          
SEQRES  24 1  438  LEU PRO PHE THR GLU GLU VAL LEU ASP THR PRO MET SER          
SEQRES  25 1  438  TYR GLU HIS LEU GLN ALA LYS GLY SER MET LEU GLY THR          
SEQRES  26 1  438  GLY GLY VAL ILE LEU ILE PRO GLU ARG VAL SER MET VAL          
SEQRES  27 1  438  ASP ALA MET TRP ASN LEU THR ARG PHE TYR ALA HIS GLU          
SEQRES  28 1  438  SER CYS GLY LYS CYS THR PRO CYS ARG GLU GLY VAL ALA          
SEQRES  29 1  438  GLY PHE MET VAL ASN LEU PHE ALA LYS ILE GLY THR GLY          
SEQRES  30 1  438  GLN GLY GLU GLU LYS ASP VAL GLU ASN LEU GLU ALA LEU          
SEQRES  31 1  438  LEU PRO LEU ILE GLU GLY ARG SER PHE CYS PRO LEU ALA          
SEQRES  32 1  438  ASP ALA ALA VAL TRP PRO VAL LYS GLY SER LEU ARG HIS          
SEQRES  33 1  438  PHE LYS ASP GLN TYR LEU ALA LEU ALA ARG GLU LYS ARG          
SEQRES  34 1  438  PRO VAL PRO ARG PRO SER LEU TRP ARG                          
SEQRES   1 2  181  MET GLY PHE PHE ASP ASP LYS GLN ASP PHE LEU GLU GLU          
SEQRES   2 2  181  THR PHE ALA LYS TYR PRO PRO GLU GLY ARG ARG ALA ALA          
SEQRES   3 2  181  ILE MET PRO LEU LEU ARG ARG VAL GLN GLN GLU GLU GLY          
SEQRES   4 2  181  TRP ILE ARG PRO GLU ARG ILE GLU GLU ILE ALA ARG LEU          
SEQRES   5 2  181  VAL GLY THR THR PRO THR GLU VAL MET GLY VAL ALA SER          
SEQRES   6 2  181  PHE TYR SER TYR TYR GLN PHE VAL PRO THR GLY LYS TYR          
SEQRES   7 2  181  HIS LEU GLN VAL CYS ALA THR LEU SER CYS LYS LEU ALA          
SEQRES   8 2  181  GLY ALA GLU GLU LEU TRP ASP TYR LEU THR GLU THR LEU          
SEQRES   9 2  181  GLY ILE GLY PRO GLY GLU VAL THR PRO ASP GLY LEU PHE          
SEQRES  10 2  181  SER VAL GLN LYS VAL GLU CYS LEU GLY SER CYS HIS THR          
SEQRES  11 2  181  ALA PRO VAL ILE GLN VAL ASN ASP GLU PRO TYR VAL GLU          
SEQRES  12 2  181  CYS VAL THR ARG ALA ARG LEU GLU ALA LEU LEU ALA GLY          
SEQRES  13 2  181  LEU ARG ALA GLY LYS ARG LEU GLU GLU ILE GLU LEU PRO          
SEQRES  14 2  181  GLY LYS CYS GLY HIS HIS VAL HIS GLU VAL GLU VAL              
SEQRES   1 3  783  MET VAL ARG VAL LYS VAL ASN ASP ARG ILE VAL GLU VAL          
SEQRES   2 3  783  PRO PRO GLY THR SER VAL MET ASP ALA VAL PHE HIS ALA          
SEQRES   3 3  783  GLY TYR ASP VAL PRO LEU PHE CYS SER GLU LYS HIS LEU          
SEQRES   4 3  783  SER PRO ILE GLY ALA CYS ARG MET CYS LEU VAL ARG ILE          
SEQRES   5 3  783  GLY LEU PRO LYS LYS GLY PRO ASP GLY LYS PRO LEU LEU          
SEQRES   6 3  783  ASN GLU LYS GLY GLU PRO GLU ILE GLN TRP GLN PRO LYS          
SEQRES   7 3  783  LEU ALA ALA SER CYS VAL THR ALA VAL ALA ASP GLY MET          
SEQRES   8 3  783  VAL VAL ASP THR LEU SER ASP VAL VAL ARG GLU ALA GLN          
SEQRES   9 3  783  ALA GLY MET VAL GLU PHE THR LEU LEU ASN HIS PRO LEU          
SEQRES  10 3  783  ASP CYS PRO THR CYS ASP LYS GLY GLY ALA CYS GLU LEU          
SEQRES  11 3  783  GLN ASP ARG THR VAL GLU TYR GLY LEU TYR GLU LYS TYR          
SEQRES  12 3  783  TYR GLN LYS GLY PRO LEU GLU LEU PRO VAL TYR THR ARG          
SEQRES  13 3  783  PHE GLU PHE THR ARG ARG HIS VAL ASP LYS HIS HIS PRO          
SEQRES  14 3  783  LEU SER PRO PHE VAL ILE LEU ASP ARG GLU ARG CYS ILE          
SEQRES  15 3  783  HIS CYS LYS ARG CYS VAL ARG TYR PHE GLU GLU VAL PRO          
SEQRES  16 3  783  GLY ASP GLU VAL LEU ASP PHE ILE GLU ARG GLY VAL HIS          
SEQRES  17 3  783  THR PHE ILE GLY THR MET ASP PHE GLY LEU PRO SER GLY          
SEQRES  18 3  783  PHE SER GLY ASN ILE THR ASP ILE CYS PRO VAL GLY ALA          
SEQRES  19 3  783  LEU LEU ASP LEU THR ALA ARG PHE ARG ALA ARG ASN TRP          
SEQRES  20 3  783  GLU MET GLU GLU THR PRO THR THR CYS ALA LEU CYS PRO          
SEQRES  21 3  783  VAL GLY CYS GLY ILE THR ALA ASP THR ARG SER GLY GLU          
SEQRES  22 3  783  LEU LEU ARG ILE ARG ALA ARG GLU VAL PRO GLU VAL ASN          
SEQRES  23 3  783  GLU ILE TRP ILE CYS ASP ALA GLY ARG PHE GLY HIS GLU          
SEQRES  24 3  783  TRP ALA ASP GLN ASN ARG LEU LYS THR PRO LEU VAL ARG          
SEQRES  25 3  783  LYS GLU GLY ARG LEU VAL GLU ALA THR TRP GLU GLU ALA          
SEQRES  26 3  783  PHE LEU ALA LEU LYS GLU GLY LEU LYS GLU ALA ARG GLY          
SEQRES  27 3  783  GLU GLU VAL GLY LEU TYR LEU ALA HIS ASP ALA THR LEU          
SEQRES  28 3  783  GLU GLU GLY LEU LEU ALA SER GLU LEU ALA LYS ALA LEU          
SEQRES  29 3  783  LYS THR PRO HIS LEU ASP PHE GLN GLY ARG THR ALA ALA          
SEQRES  30 3  783  PRO ALA SER LEU PHE PRO PRO ALA SER LEU GLU ASP LEU          
SEQRES  31 3  783  LEU GLN ALA ASP PHE ALA LEU VAL LEU GLY ASP PRO THR          
SEQRES  32 3  783  GLU GLU ALA PRO ILE LEU HIS LEU ARG LEU SER GLU PHE          
SEQRES  33 3  783  VAL ARG ASP LEU LYS PRO PRO HIS ARG TYR ASN HIS GLY          
SEQRES  34 3  783  THR PRO PHE ALA ASP LEU GLN ILE LYS GLU ARG MET PRO          
SEQRES  35 3  783  ARG ARG THR ASP LYS MET ALA LEU PHE ALA PRO TYR ARG          
SEQRES  36 3  783  ALA PRO LEU MET LYS TRP ALA ALA ILE HIS GLU VAL HIS          
SEQRES  37 3  783  ARG PRO GLY GLU GLU ARG GLU ILE LEU LEU ALA LEU LEU          
SEQRES  38 3  783  GLY ASP LYS GLU GLY SER GLU MET VAL ALA LYS ALA LYS          
SEQRES  39 3  783  GLU ALA TRP GLU LYS ALA LYS ASN PRO VAL LEU ILE LEU          
SEQRES  40 3  783  GLY ALA GLY VAL LEU GLN ASP THR VAL ALA ALA GLU ARG          
SEQRES  41 3  783  ALA ARG LEU LEU ALA GLU ARG LYS GLY ALA LYS VAL LEU          
SEQRES  42 3  783  ALA MET THR PRO ALA ALA ASN ALA ARG GLY LEU GLU ALA          
SEQRES  43 3  783  MET GLY VAL LEU PRO GLY ALA LYS GLY ALA SER TRP ASP          
SEQRES  44 3  783  GLU PRO GLY ALA LEU TYR ALA TYR TYR GLY PHE VAL PRO          
SEQRES  45 3  783  PRO GLU GLU ALA LEU LYS GLY LYS ARG PHE VAL VAL MET          
SEQRES  46 3  783  HIS LEU SER HIS LEU HIS PRO LEU ALA GLU ARG TYR ALA          
SEQRES  47 3  783  HIS VAL VAL LEU PRO ALA PRO THR PHE TYR GLU LYS ARG          
SEQRES  48 3  783  GLY HIS LEU VAL ASN LEU GLU GLY ARG VAL LEU PRO LEU          
SEQRES  49 3  783  SER PRO ALA PRO ILE GLU ASN GLY GLU ALA GLU GLY ALA          
SEQRES  50 3  783  LEU GLN VAL LEU ALA LEU LEU ALA GLU ALA LEU GLY VAL          
SEQRES  51 3  783  ARG PRO PRO PHE ARG LEU HIS LEU GLU ALA GLN LYS ALA          
SEQRES  52 3  783  LEU LYS ALA ARG LYS VAL PRO GLU ALA MET GLY ARG LEU          
SEQRES  53 3  783  SER PHE ARG LEU LYS GLU LEU ARG PRO LYS GLU ARG LYS          
SEQRES  54 3  783  GLY ALA PHE TYR LEU ARG PRO THR MET TRP LYS ALA HIS          
SEQRES  55 3  783  GLN ALA VAL GLY LYS ALA GLN GLU ALA ALA ARG ALA GLU          
SEQRES  56 3  783  LEU TRP ALA HIS PRO GLU THR ALA ARG ALA GLU ALA LEU          
SEQRES  57 3  783  PRO GLU GLY ALA GLN VAL ALA VAL GLU THR PRO PHE GLY          
SEQRES  58 3  783  ARG VAL GLU ALA ARG VAL VAL HIS ARG GLU ASP VAL PRO          
SEQRES  59 3  783  LYS GLY HIS LEU TYR LEU SER ALA LEU GLY PRO ALA ALA          
SEQRES  60 3  783  GLY LEU ARG VAL GLU GLY ARG VAL LEU VAL PRO ALA GLY          
SEQRES  61 3  783  GLY GLU ALA                                                  
SEQRES   1 4  409  MET ARG GLU GLU PHE LEU GLU GLU ILE PRO LEU ASP ALA          
SEQRES   2 4  409  PRO PRO GLU GLU ALA LYS GLU LEU ARG THR GLU VAL MET          
SEQRES   3 4  409  THR LEU ASN VAL GLY PRO GLN HIS PRO SER THR HIS GLY          
SEQRES   4 4  409  VAL LEU ARG LEU MET VAL THR LEU SER GLY GLU GLU VAL          
SEQRES   5 4  409  LEU GLU VAL VAL PRO HIS ILE GLY TYR LEU HIS THR GLY          
SEQRES   6 4  409  PHE GLU LYS THR MET GLU HIS ARG THR TYR LEU GLN ASN          
SEQRES   7 4  409  ILE THR TYR THR PRO ARG MET ASP TYR LEU HIS SER PHE          
SEQRES   8 4  409  ALA HIS ASP LEU ALA TYR ALA LEU ALA VAL GLU LYS LEU          
SEQRES   9 4  409  LEU GLY ALA VAL VAL PRO PRO ARG ALA GLU THR ILE ARG          
SEQRES  10 4  409  VAL ILE LEU ASN GLU LEU SER ARG LEU ALA SER HIS LEU          
SEQRES  11 4  409  VAL PHE LEU GLY THR GLY LEU LEU ASP LEU GLY ALA LEU          
SEQRES  12 4  409  THR PRO PHE PHE TYR ALA PHE ARG GLU ARG GLU THR ILE          
SEQRES  13 4  409  LEU ASP LEU PHE GLU TRP VAL THR GLY GLN ARG PHE HIS          
SEQRES  14 4  409  HIS ASN TYR ILE ARG ILE GLY GLY VAL LYS GLU ASP LEU          
SEQRES  15 4  409  PRO GLU GLU PHE VAL PRO GLU LEU LYS LYS LEU LEU GLU          
SEQRES  16 4  409  VAL LEU PRO HIS ARG ILE ASP GLU TYR GLU ALA LEU PHE          
SEQRES  17 4  409  ALA GLU SER PRO ILE PHE TYR GLU ARG ALA ARG GLY VAL          
SEQRES  18 4  409  GLY VAL ILE PRO PRO GLU VAL ALA ILE ASP LEU GLY LEU          
SEQRES  19 4  409  THR GLY GLY SER LEU ARG ALA SER GLY VAL ASN TYR ASP          
SEQRES  20 4  409  VAL ARG LYS ALA TYR PRO TYR SER GLY TYR GLU THR TYR          
SEQRES  21 4  409  THR PHE ASP VAL PRO LEU GLY GLU ARG GLY ASP VAL PHE          
SEQRES  22 4  409  ASP ARG MET LEU VAL ARG ILE ARG GLU MET ARG GLU SER          
SEQRES  23 4  409  VAL LYS ILE ILE LYS GLN ALA LEU GLU ARG LEU GLU PRO          
SEQRES  24 4  409  GLY PRO VAL ARG ASP PRO ASN PRO GLN ILE THR PRO PRO          
SEQRES  25 4  409  PRO ARG HIS LEU LEU GLU THR SER MET GLU ALA VAL ILE          
SEQRES  26 4  409  TYR HIS PHE LYS HIS TYR THR GLU GLY PHE HIS PRO PRO          
SEQRES  27 4  409  LYS GLY GLU VAL TYR VAL PRO THR GLU SER ALA ARG GLY          
SEQRES  28 4  409  GLU LEU GLY TYR TYR ILE VAL SER ASP GLY GLY SER MET          
SEQRES  29 4  409  PRO TYR ARG VAL LYS VAL ARG ALA PRO SER PHE VAL ASN          
SEQRES  30 4  409  LEU GLN SER LEU PRO TYR ALA CYS LYS GLY GLU GLN VAL          
SEQRES  31 4  409  PRO ASP MET VAL ALA ILE ILE ALA SER LEU ASP PRO VAL          
SEQRES  32 4  409  MET GLY ASP VAL ASP ARG                                      
SEQRES   1 5  207  MET ARG LEU GLU ARG VAL LEU GLU GLU ALA ARG ALA LYS          
SEQRES   2 5  207  GLY TYR PRO ILE GLU ASP ASN GLY LEU GLY ASN LEU TRP          
SEQRES   3 5  207  VAL VAL LEU PRO ARG GLU ARG PHE LYS GLU GLU MET ALA          
SEQRES   4 5  207  HIS TYR LYS ALA MET GLY PHE ASN PHE LEU ALA ASP ILE          
SEQRES   5 5  207  VAL GLY LEU ASP TYR LEU THR TYR PRO ASP PRO ARG PRO          
SEQRES   6 5  207  GLU ARG PHE ALA VAL VAL TYR GLU LEU VAL SER LEU PRO          
SEQRES   7 5  207  GLY TRP LYS ASP GLY ASP GLY SER ARG PHE PHE VAL ARG          
SEQRES   8 5  207  VAL TYR VAL PRO GLU GLU ASP PRO ARG LEU PRO THR VAL          
SEQRES   9 5  207  THR ASP LEU TRP GLY SER ALA ASN PHE LEU GLU ARG GLU          
SEQRES  10 5  207  VAL TYR ASP LEU PHE GLY ILE VAL PHE GLU GLY HIS PRO          
SEQRES  11 5  207  ASP LEU ARG LYS ILE LEU THR PRO GLU ASP LEU GLU GLY          
SEQRES  12 5  207  HIS PRO LEU ARG LYS ASP TYR PRO LEU GLY GLU THR PRO          
SEQRES  13 5  207  THR LEU PHE ARG GLU GLY ARG TYR ILE ILE PRO ALA GLU          
SEQRES  14 5  207  PHE ARG ALA ALA LEU THR GLY LYS ASP PRO GLY LEU THR          
SEQRES  15 5  207  PHE TYR LYS GLY GLY SER ARG LYS GLY TYR ARG SER LEU          
SEQRES  16 5  207  TRP ALA ASP LEU LYS LYS ALA ARG GLU VAL LYS GLY              
SEQRES   1 6  181  MET ALA LEU LYS ASP LEU PHE GLU ARG ASP VAL GLN GLU          
SEQRES   2 6  181  LEU GLU ARG GLU GLY ILE LEU PHE THR THR LEU GLU LYS          
SEQRES   3 6  181  LEU VAL ALA TRP GLY ARG SER ASN SER LEU TRP PRO ALA          
SEQRES   4 6  181  THR PHE GLY LEU ALA CYS CYS ALA ILE GLU MET MET ALA          
SEQRES   5 6  181  SER THR ASP ALA ARG ASN ASP LEU ALA ARG PHE GLY SER          
SEQRES   6 6  181  GLU VAL PHE ARG ALA SER PRO ARG GLN ALA ASP VAL MET          
SEQRES   7 6  181  ILE VAL ALA GLY ARG LEU SER LYS LYS MET ALA PRO VAL          
SEQRES   8 6  181  MET ARG ARG VAL TRP GLU GLN MET PRO ASP PRO LYS TRP          
SEQRES   9 6  181  VAL ILE SER MET GLY ALA CYS ALA SER SER GLY GLY MET          
SEQRES  10 6  181  PHE ASN ASN TYR ALA ILE VAL GLN ASN VAL ASP SER VAL          
SEQRES  11 6  181  VAL PRO VAL ASP VAL TYR VAL PRO GLY CYS PRO PRO ARG          
SEQRES  12 6  181  PRO GLU ALA LEU ILE TYR ALA VAL MET GLN LEU GLN LYS          
SEQRES  13 6  181  LYS VAL ARG GLY GLN ALA TYR ASN GLU ARG GLY GLU ARG          
SEQRES  14 6  181  LEU PRO PRO VAL ALA ALA TRP LYS ARG THR ARG GLY              
SEQRES   1 9  182  MET THR LEU LYS ALA LEU ALA GLN SER LEU GLY ILE THR          
SEQRES   2 9  182  LEU LYS TYR LEU PHE SER LYS PRO VAL THR VAL PRO TYR          
SEQRES   3 9  182  PRO ASP ALA PRO VAL ALA LEU LYS PRO ARG PHE HIS GLY          
SEQRES   4 9  182  ARG HIS VAL LEU THR ARG HIS PRO ASN GLY LEU GLU LYS          
SEQRES   5 9  182  CYS ILE GLY CYS SER LEU CYS ALA ALA ALA CYS PRO ALA          
SEQRES   6 9  182  TYR ALA ILE TYR VAL GLU PRO ALA GLU ASN ASP PRO GLU          
SEQRES   7 9  182  ASN PRO VAL SER ALA GLY GLU ARG TYR ALA LYS VAL TYR          
SEQRES   8 9  182  GLU ILE ASN MET LEU ARG CYS ILE PHE CYS GLY LEU CYS          
SEQRES   9 9  182  GLU GLU ALA CYS PRO THR GLY ALA ILE VAL LEU GLY TYR          
SEQRES  10 9  182  ASP PHE GLU MET ALA ASP TYR GLU TYR SER ASP LEU VAL          
SEQRES  11 9  182  TYR GLY LYS GLU ASP MET LEU VAL ASP VAL VAL GLY THR          
SEQRES  12 9  182  LYS PRO GLN ARG ARG GLU ALA LYS ARG THR GLY LYS PRO          
SEQRES  13 9  182  VAL LYS VAL GLY TYR VAL VAL PRO TYR VAL ARG PRO GLU          
SEQRES  14 9  182  LEU GLU GLY PHE LYS ALA PRO THR GLU GLY GLY LYS ARG          
SEQRES   1 7  129  MET SER ALA SER SER GLU ARG GLU LEU TYR GLU ALA TRP          
SEQRES   2 7  129  VAL GLU LEU LEU SER TRP MET ARG GLU TYR ALA GLN ALA          
SEQRES   3 7  129  LYS GLY VAL ARG PHE GLU LYS GLU ALA ASP PHE PRO ASP          
SEQRES   4 7  129  PHE ILE TYR ARG MET GLU ARG PRO TYR ASP LEU PRO THR          
SEQRES   5 7  129  THR ILE MET THR ALA SER LEU SER ASP GLY LEU GLY GLU          
SEQRES   6 7  129  PRO PHE LEU LEU ALA ASP VAL SER PRO ARG HIS ALA LYS          
SEQRES   7 7  129  LEU LYS ARG ILE GLY LEU ARG LEU PRO ARG ALA HIS ILE          
SEQRES   8 7  129  HIS LEU HIS ALA HIS TYR GLU PRO GLY LYS GLY LEU VAL          
SEQRES   9 7  129  THR GLY LYS ILE PRO LEU THR LYS GLU ARG PHE PHE ALA          
SEQRES  10 7  129  LEU ALA ASP ARG ALA ARG GLU ALA LEU ALA PHE ALA              
SEQRES   1 A  438  MET THR GLY PRO ILE LEU SER GLY LEU ASP PRO ARG PHE          
SEQRES   2 A  438  GLU ARG THR LEU TYR ALA HIS VAL GLY LYS GLU GLY SER          
SEQRES   3 A  438  TRP THR LEU ASP TYR TYR LEU ARG HIS GLY GLY TYR GLU          
SEQRES   4 A  438  THR ALA LYS ARG VAL LEU LYS GLU LYS THR PRO ASP GLU          
SEQRES   5 A  438  VAL ILE GLU GLU VAL LYS ARG SER GLY LEU ARG GLY ARG          
SEQRES   6 A  438  GLY GLY ALA GLY PHE PRO THR GLY LEU LYS TRP SER PHE          
SEQRES   7 A  438  MET PRO LYS ASP ASP GLY LYS GLN HIS TYR LEU ILE CYS          
SEQRES   8 A  438  ASN ALA ASP GLU SER GLU PRO GLY SER PHE LYS ASP ARG          
SEQRES   9 A  438  TYR ILE LEU GLU ASP VAL PRO HIS LEU LEU ILE GLU GLY          
SEQRES  10 A  438  MET ILE LEU ALA GLY TYR ALA ILE ARG ALA THR VAL GLY          
SEQRES  11 A  438  TYR ILE TYR VAL ARG GLY GLU TYR ARG ARG ALA ALA ASP          
SEQRES  12 A  438  ARG LEU GLU GLN ALA ILE LYS GLU ALA ARG ALA ARG GLY          
SEQRES  13 A  438  TYR LEU GLY LYS ASN LEU PHE GLY THR ASP PHE SER PHE          
SEQRES  14 A  438  ASP LEU HIS VAL HIS ARG GLY ALA GLY ALA TYR ILE CYS          
SEQRES  15 A  438  GLY GLU GLU THR ALA LEU MET ASN SER LEU GLU GLY LEU          
SEQRES  16 A  438  ARG ALA ASN PRO ARG LEU LYS PRO PRO PHE PRO ALA GLN          
SEQRES  17 A  438  SER GLY LEU TRP GLY LYS PRO THR THR ILE ASN ASN VAL          
SEQRES  18 A  438  GLU THR LEU ALA SER VAL VAL PRO ILE MET GLU ARG GLY          
SEQRES  19 A  438  ALA ASP TRP PHE ALA GLN MET GLY THR GLU GLN SER LYS          
SEQRES  20 A  438  GLY MET LYS LEU TYR GLN ILE SER GLY PRO VAL LYS ARG          
SEQRES  21 A  438  PRO GLY VAL TYR GLU LEU PRO MET GLY THR THR PHE ARG          
SEQRES  22 A  438  GLU LEU ILE TYR GLU TRP ALA GLY GLY PRO LEU GLU PRO          
SEQRES  23 A  438  ILE GLN ALA ILE ILE PRO GLY GLY SER SER THR PRO PRO          
SEQRES  24 A  438  LEU PRO PHE THR GLU GLU VAL LEU ASP THR PRO MET SER          
SEQRES  25 A  438  TYR GLU HIS LEU GLN ALA LYS GLY SER MET LEU GLY THR          
SEQRES  26 A  438  GLY GLY VAL ILE LEU ILE PRO GLU ARG VAL SER MET VAL          
SEQRES  27 A  438  ASP ALA MET TRP ASN LEU THR ARG PHE TYR ALA HIS GLU          
SEQRES  28 A  438  SER CYS GLY LYS CYS THR PRO CYS ARG GLU GLY VAL ALA          
SEQRES  29 A  438  GLY PHE MET VAL ASN LEU PHE ALA LYS ILE GLY THR GLY          
SEQRES  30 A  438  GLN GLY GLU GLU LYS ASP VAL GLU ASN LEU GLU ALA LEU          
SEQRES  31 A  438  LEU PRO LEU ILE GLU GLY ARG SER PHE CYS PRO LEU ALA          
SEQRES  32 A  438  ASP ALA ALA VAL TRP PRO VAL LYS GLY SER LEU ARG HIS          
SEQRES  33 A  438  PHE LYS ASP GLN TYR LEU ALA LEU ALA ARG GLU LYS ARG          
SEQRES  34 A  438  PRO VAL PRO ARG PRO SER LEU TRP ARG                          
SEQRES   1 B  181  MET GLY PHE PHE ASP ASP LYS GLN ASP PHE LEU GLU GLU          
SEQRES   2 B  181  THR PHE ALA LYS TYR PRO PRO GLU GLY ARG ARG ALA ALA          
SEQRES   3 B  181  ILE MET PRO LEU LEU ARG ARG VAL GLN GLN GLU GLU GLY          
SEQRES   4 B  181  TRP ILE ARG PRO GLU ARG ILE GLU GLU ILE ALA ARG LEU          
SEQRES   5 B  181  VAL GLY THR THR PRO THR GLU VAL MET GLY VAL ALA SER          
SEQRES   6 B  181  PHE TYR SER TYR TYR GLN PHE VAL PRO THR GLY LYS TYR          
SEQRES   7 B  181  HIS LEU GLN VAL CYS ALA THR LEU SER CYS LYS LEU ALA          
SEQRES   8 B  181  GLY ALA GLU GLU LEU TRP ASP TYR LEU THR GLU THR LEU          
SEQRES   9 B  181  GLY ILE GLY PRO GLY GLU VAL THR PRO ASP GLY LEU PHE          
SEQRES  10 B  181  SER VAL GLN LYS VAL GLU CYS LEU GLY SER CYS HIS THR          
SEQRES  11 B  181  ALA PRO VAL ILE GLN VAL ASN ASP GLU PRO TYR VAL GLU          
SEQRES  12 B  181  CYS VAL THR ARG ALA ARG LEU GLU ALA LEU LEU ALA GLY          
SEQRES  13 B  181  LEU ARG ALA GLY LYS ARG LEU GLU GLU ILE GLU LEU PRO          
SEQRES  14 B  181  GLY LYS CYS GLY HIS HIS VAL HIS GLU VAL GLU VAL              
SEQRES   1 C  783  MET VAL ARG VAL LYS VAL ASN ASP ARG ILE VAL GLU VAL          
SEQRES   2 C  783  PRO PRO GLY THR SER VAL MET ASP ALA VAL PHE HIS ALA          
SEQRES   3 C  783  GLY TYR ASP VAL PRO LEU PHE CYS SER GLU LYS HIS LEU          
SEQRES   4 C  783  SER PRO ILE GLY ALA CYS ARG MET CYS LEU VAL ARG ILE          
SEQRES   5 C  783  GLY LEU PRO LYS LYS GLY PRO ASP GLY LYS PRO LEU LEU          
SEQRES   6 C  783  ASN GLU LYS GLY GLU PRO GLU ILE GLN TRP GLN PRO LYS          
SEQRES   7 C  783  LEU ALA ALA SER CYS VAL THR ALA VAL ALA ASP GLY MET          
SEQRES   8 C  783  VAL VAL ASP THR LEU SER ASP VAL VAL ARG GLU ALA GLN          
SEQRES   9 C  783  ALA GLY MET VAL GLU PHE THR LEU LEU ASN HIS PRO LEU          
SEQRES  10 C  783  ASP CYS PRO THR CYS ASP LYS GLY GLY ALA CYS GLU LEU          
SEQRES  11 C  783  GLN ASP ARG THR VAL GLU TYR GLY LEU TYR GLU LYS TYR          
SEQRES  12 C  783  TYR GLN LYS GLY PRO LEU GLU LEU PRO VAL TYR THR ARG          
SEQRES  13 C  783  PHE GLU PHE THR ARG ARG HIS VAL ASP LYS HIS HIS PRO          
SEQRES  14 C  783  LEU SER PRO PHE VAL ILE LEU ASP ARG GLU ARG CYS ILE          
SEQRES  15 C  783  HIS CYS LYS ARG CYS VAL ARG TYR PHE GLU GLU VAL PRO          
SEQRES  16 C  783  GLY ASP GLU VAL LEU ASP PHE ILE GLU ARG GLY VAL HIS          
SEQRES  17 C  783  THR PHE ILE GLY THR MET ASP PHE GLY LEU PRO SER GLY          
SEQRES  18 C  783  PHE SER GLY ASN ILE THR ASP ILE CYS PRO VAL GLY ALA          
SEQRES  19 C  783  LEU LEU ASP LEU THR ALA ARG PHE ARG ALA ARG ASN TRP          
SEQRES  20 C  783  GLU MET GLU GLU THR PRO THR THR CYS ALA LEU CYS PRO          
SEQRES  21 C  783  VAL GLY CYS GLY ILE THR ALA ASP THR ARG SER GLY GLU          
SEQRES  22 C  783  LEU LEU ARG ILE ARG ALA ARG GLU VAL PRO GLU VAL ASN          
SEQRES  23 C  783  GLU ILE TRP ILE CYS ASP ALA GLY ARG PHE GLY HIS GLU          
SEQRES  24 C  783  TRP ALA ASP GLN ASN ARG LEU LYS THR PRO LEU VAL ARG          
SEQRES  25 C  783  LYS GLU GLY ARG LEU VAL GLU ALA THR TRP GLU GLU ALA          
SEQRES  26 C  783  PHE LEU ALA LEU LYS GLU GLY LEU LYS GLU ALA ARG GLY          
SEQRES  27 C  783  GLU GLU VAL GLY LEU TYR LEU ALA HIS ASP ALA THR LEU          
SEQRES  28 C  783  GLU GLU GLY LEU LEU ALA SER GLU LEU ALA LYS ALA LEU          
SEQRES  29 C  783  LYS THR PRO HIS LEU ASP PHE GLN GLY ARG THR ALA ALA          
SEQRES  30 C  783  PRO ALA SER LEU PHE PRO PRO ALA SER LEU GLU ASP LEU          
SEQRES  31 C  783  LEU GLN ALA ASP PHE ALA LEU VAL LEU GLY ASP PRO THR          
SEQRES  32 C  783  GLU GLU ALA PRO ILE LEU HIS LEU ARG LEU SER GLU PHE          
SEQRES  33 C  783  VAL ARG ASP LEU LYS PRO PRO HIS ARG TYR ASN HIS GLY          
SEQRES  34 C  783  THR PRO PHE ALA ASP LEU GLN ILE LYS GLU ARG MET PRO          
SEQRES  35 C  783  ARG ARG THR ASP LYS MET ALA LEU PHE ALA PRO TYR ARG          
SEQRES  36 C  783  ALA PRO LEU MET LYS TRP ALA ALA ILE HIS GLU VAL HIS          
SEQRES  37 C  783  ARG PRO GLY GLU GLU ARG GLU ILE LEU LEU ALA LEU LEU          
SEQRES  38 C  783  GLY ASP LYS GLU GLY SER GLU MET VAL ALA LYS ALA LYS          
SEQRES  39 C  783  GLU ALA TRP GLU LYS ALA LYS ASN PRO VAL LEU ILE LEU          
SEQRES  40 C  783  GLY ALA GLY VAL LEU GLN ASP THR VAL ALA ALA GLU ARG          
SEQRES  41 C  783  ALA ARG LEU LEU ALA GLU ARG LYS GLY ALA LYS VAL LEU          
SEQRES  42 C  783  ALA MET THR PRO ALA ALA ASN ALA ARG GLY LEU GLU ALA          
SEQRES  43 C  783  MET GLY VAL LEU PRO GLY ALA LYS GLY ALA SER TRP ASP          
SEQRES  44 C  783  GLU PRO GLY ALA LEU TYR ALA TYR TYR GLY PHE VAL PRO          
SEQRES  45 C  783  PRO GLU GLU ALA LEU LYS GLY LYS ARG PHE VAL VAL MET          
SEQRES  46 C  783  HIS LEU SER HIS LEU HIS PRO LEU ALA GLU ARG TYR ALA          
SEQRES  47 C  783  HIS VAL VAL LEU PRO ALA PRO THR PHE TYR GLU LYS ARG          
SEQRES  48 C  783  GLY HIS LEU VAL ASN LEU GLU GLY ARG VAL LEU PRO LEU          
SEQRES  49 C  783  SER PRO ALA PRO ILE GLU ASN GLY GLU ALA GLU GLY ALA          
SEQRES  50 C  783  LEU GLN VAL LEU ALA LEU LEU ALA GLU ALA LEU GLY VAL          
SEQRES  51 C  783  ARG PRO PRO PHE ARG LEU HIS LEU GLU ALA GLN LYS ALA          
SEQRES  52 C  783  LEU LYS ALA ARG LYS VAL PRO GLU ALA MET GLY ARG LEU          
SEQRES  53 C  783  SER PHE ARG LEU LYS GLU LEU ARG PRO LYS GLU ARG LYS          
SEQRES  54 C  783  GLY ALA PHE TYR LEU ARG PRO THR MET TRP LYS ALA HIS          
SEQRES  55 C  783  GLN ALA VAL GLY LYS ALA GLN GLU ALA ALA ARG ALA GLU          
SEQRES  56 C  783  LEU TRP ALA HIS PRO GLU THR ALA ARG ALA GLU ALA LEU          
SEQRES  57 C  783  PRO GLU GLY ALA GLN VAL ALA VAL GLU THR PRO PHE GLY          
SEQRES  58 C  783  ARG VAL GLU ALA ARG VAL VAL HIS ARG GLU ASP VAL PRO          
SEQRES  59 C  783  LYS GLY HIS LEU TYR LEU SER ALA LEU GLY PRO ALA ALA          
SEQRES  60 C  783  GLY LEU ARG VAL GLU GLY ARG VAL LEU VAL PRO ALA GLY          
SEQRES  61 C  783  GLY GLU ALA                                                  
SEQRES   1 D  409  MET ARG GLU GLU PHE LEU GLU GLU ILE PRO LEU ASP ALA          
SEQRES   2 D  409  PRO PRO GLU GLU ALA LYS GLU LEU ARG THR GLU VAL MET          
SEQRES   3 D  409  THR LEU ASN VAL GLY PRO GLN HIS PRO SER THR HIS GLY          
SEQRES   4 D  409  VAL LEU ARG LEU MET VAL THR LEU SER GLY GLU GLU VAL          
SEQRES   5 D  409  LEU GLU VAL VAL PRO HIS ILE GLY TYR LEU HIS THR GLY          
SEQRES   6 D  409  PHE GLU LYS THR MET GLU HIS ARG THR TYR LEU GLN ASN          
SEQRES   7 D  409  ILE THR TYR THR PRO ARG MET ASP TYR LEU HIS SER PHE          
SEQRES   8 D  409  ALA HIS ASP LEU ALA TYR ALA LEU ALA VAL GLU LYS LEU          
SEQRES   9 D  409  LEU GLY ALA VAL VAL PRO PRO ARG ALA GLU THR ILE ARG          
SEQRES  10 D  409  VAL ILE LEU ASN GLU LEU SER ARG LEU ALA SER HIS LEU          
SEQRES  11 D  409  VAL PHE LEU GLY THR GLY LEU LEU ASP LEU GLY ALA LEU          
SEQRES  12 D  409  THR PRO PHE PHE TYR ALA PHE ARG GLU ARG GLU THR ILE          
SEQRES  13 D  409  LEU ASP LEU PHE GLU TRP VAL THR GLY GLN ARG PHE HIS          
SEQRES  14 D  409  HIS ASN TYR ILE ARG ILE GLY GLY VAL LYS GLU ASP LEU          
SEQRES  15 D  409  PRO GLU GLU PHE VAL PRO GLU LEU LYS LYS LEU LEU GLU          
SEQRES  16 D  409  VAL LEU PRO HIS ARG ILE ASP GLU TYR GLU ALA LEU PHE          
SEQRES  17 D  409  ALA GLU SER PRO ILE PHE TYR GLU ARG ALA ARG GLY VAL          
SEQRES  18 D  409  GLY VAL ILE PRO PRO GLU VAL ALA ILE ASP LEU GLY LEU          
SEQRES  19 D  409  THR GLY GLY SER LEU ARG ALA SER GLY VAL ASN TYR ASP          
SEQRES  20 D  409  VAL ARG LYS ALA TYR PRO TYR SER GLY TYR GLU THR TYR          
SEQRES  21 D  409  THR PHE ASP VAL PRO LEU GLY GLU ARG GLY ASP VAL PHE          
SEQRES  22 D  409  ASP ARG MET LEU VAL ARG ILE ARG GLU MET ARG GLU SER          
SEQRES  23 D  409  VAL LYS ILE ILE LYS GLN ALA LEU GLU ARG LEU GLU PRO          
SEQRES  24 D  409  GLY PRO VAL ARG ASP PRO ASN PRO GLN ILE THR PRO PRO          
SEQRES  25 D  409  PRO ARG HIS LEU LEU GLU THR SER MET GLU ALA VAL ILE          
SEQRES  26 D  409  TYR HIS PHE LYS HIS TYR THR GLU GLY PHE HIS PRO PRO          
SEQRES  27 D  409  LYS GLY GLU VAL TYR VAL PRO THR GLU SER ALA ARG GLY          
SEQRES  28 D  409  GLU LEU GLY TYR TYR ILE VAL SER ASP GLY GLY SER MET          
SEQRES  29 D  409  PRO TYR ARG VAL LYS VAL ARG ALA PRO SER PHE VAL ASN          
SEQRES  30 D  409  LEU GLN SER LEU PRO TYR ALA CYS LYS GLY GLU GLN VAL          
SEQRES  31 D  409  PRO ASP MET VAL ALA ILE ILE ALA SER LEU ASP PRO VAL          
SEQRES  32 D  409  MET GLY ASP VAL ASP ARG                                      
SEQRES   1 E  207  MET ARG LEU GLU ARG VAL LEU GLU GLU ALA ARG ALA LYS          
SEQRES   2 E  207  GLY TYR PRO ILE GLU ASP ASN GLY LEU GLY ASN LEU TRP          
SEQRES   3 E  207  VAL VAL LEU PRO ARG GLU ARG PHE LYS GLU GLU MET ALA          
SEQRES   4 E  207  HIS TYR LYS ALA MET GLY PHE ASN PHE LEU ALA ASP ILE          
SEQRES   5 E  207  VAL GLY LEU ASP TYR LEU THR TYR PRO ASP PRO ARG PRO          
SEQRES   6 E  207  GLU ARG PHE ALA VAL VAL TYR GLU LEU VAL SER LEU PRO          
SEQRES   7 E  207  GLY TRP LYS ASP GLY ASP GLY SER ARG PHE PHE VAL ARG          
SEQRES   8 E  207  VAL TYR VAL PRO GLU GLU ASP PRO ARG LEU PRO THR VAL          
SEQRES   9 E  207  THR ASP LEU TRP GLY SER ALA ASN PHE LEU GLU ARG GLU          
SEQRES  10 E  207  VAL TYR ASP LEU PHE GLY ILE VAL PHE GLU GLY HIS PRO          
SEQRES  11 E  207  ASP LEU ARG LYS ILE LEU THR PRO GLU ASP LEU GLU GLY          
SEQRES  12 E  207  HIS PRO LEU ARG LYS ASP TYR PRO LEU GLY GLU THR PRO          
SEQRES  13 E  207  THR LEU PHE ARG GLU GLY ARG TYR ILE ILE PRO ALA GLU          
SEQRES  14 E  207  PHE ARG ALA ALA LEU THR GLY LYS ASP PRO GLY LEU THR          
SEQRES  15 E  207  PHE TYR LYS GLY GLY SER ARG LYS GLY TYR ARG SER LEU          
SEQRES  16 E  207  TRP ALA ASP LEU LYS LYS ALA ARG GLU VAL LYS GLY              
SEQRES   1 F  181  MET ALA LEU LYS ASP LEU PHE GLU ARG ASP VAL GLN GLU          
SEQRES   2 F  181  LEU GLU ARG GLU GLY ILE LEU PHE THR THR LEU GLU LYS          
SEQRES   3 F  181  LEU VAL ALA TRP GLY ARG SER ASN SER LEU TRP PRO ALA          
SEQRES   4 F  181  THR PHE GLY LEU ALA CYS CYS ALA ILE GLU MET MET ALA          
SEQRES   5 F  181  SER THR ASP ALA ARG ASN ASP LEU ALA ARG PHE GLY SER          
SEQRES   6 F  181  GLU VAL PHE ARG ALA SER PRO ARG GLN ALA ASP VAL MET          
SEQRES   7 F  181  ILE VAL ALA GLY ARG LEU SER LYS LYS MET ALA PRO VAL          
SEQRES   8 F  181  MET ARG ARG VAL TRP GLU GLN MET PRO ASP PRO LYS TRP          
SEQRES   9 F  181  VAL ILE SER MET GLY ALA CYS ALA SER SER GLY GLY MET          
SEQRES  10 F  181  PHE ASN ASN TYR ALA ILE VAL GLN ASN VAL ASP SER VAL          
SEQRES  11 F  181  VAL PRO VAL ASP VAL TYR VAL PRO GLY CYS PRO PRO ARG          
SEQRES  12 F  181  PRO GLU ALA LEU ILE TYR ALA VAL MET GLN LEU GLN LYS          
SEQRES  13 F  181  LYS VAL ARG GLY GLN ALA TYR ASN GLU ARG GLY GLU ARG          
SEQRES  14 F  181  LEU PRO PRO VAL ALA ALA TRP LYS ARG THR ARG GLY              
SEQRES   1 G  182  MET THR LEU LYS ALA LEU ALA GLN SER LEU GLY ILE THR          
SEQRES   2 G  182  LEU LYS TYR LEU PHE SER LYS PRO VAL THR VAL PRO TYR          
SEQRES   3 G  182  PRO ASP ALA PRO VAL ALA LEU LYS PRO ARG PHE HIS GLY          
SEQRES   4 G  182  ARG HIS VAL LEU THR ARG HIS PRO ASN GLY LEU GLU LYS          
SEQRES   5 G  182  CYS ILE GLY CYS SER LEU CYS ALA ALA ALA CYS PRO ALA          
SEQRES   6 G  182  TYR ALA ILE TYR VAL GLU PRO ALA GLU ASN ASP PRO GLU          
SEQRES   7 G  182  ASN PRO VAL SER ALA GLY GLU ARG TYR ALA LYS VAL TYR          
SEQRES   8 G  182  GLU ILE ASN MET LEU ARG CYS ILE PHE CYS GLY LEU CYS          
SEQRES   9 G  182  GLU GLU ALA CYS PRO THR GLY ALA ILE VAL LEU GLY TYR          
SEQRES  10 G  182  ASP PHE GLU MET ALA ASP TYR GLU TYR SER ASP LEU VAL          
SEQRES  11 G  182  TYR GLY LYS GLU ASP MET LEU VAL ASP VAL VAL GLY THR          
SEQRES  12 G  182  LYS PRO GLN ARG ARG GLU ALA LYS ARG THR GLY LYS PRO          
SEQRES  13 G  182  VAL LYS VAL GLY TYR VAL VAL PRO TYR VAL ARG PRO GLU          
SEQRES  14 G  182  LEU GLU GLY PHE LYS ALA PRO THR GLU GLY GLY LYS ARG          
SEQRES   1 H  129  MET SER ALA SER SER GLU ARG GLU LEU TYR GLU ALA TRP          
SEQRES   2 H  129  VAL GLU LEU LEU SER TRP MET ARG GLU TYR ALA GLN ALA          
SEQRES   3 H  129  LYS GLY VAL ARG PHE GLU LYS GLU ALA ASP PHE PRO ASP          
SEQRES   4 H  129  PHE ILE TYR ARG MET GLU ARG PRO TYR ASP LEU PRO THR          
SEQRES   5 H  129  THR ILE MET THR ALA SER LEU SER ASP GLY LEU GLY GLU          
SEQRES   6 H  129  PRO PHE LEU LEU ALA ASP VAL SER PRO ARG HIS ALA LYS          
SEQRES   7 H  129  LEU LYS ARG ILE GLY LEU ARG LEU PRO ARG ALA HIS ILE          
SEQRES   8 H  129  HIS LEU HIS ALA HIS TYR GLU PRO GLY LYS GLY LEU VAL          
SEQRES   9 H  129  THR GLY LYS ILE PRO LEU THR LYS GLU ARG PHE PHE ALA          
SEQRES  10 H  129  LEU ALA ASP ARG ALA ARG GLU ALA LEU ALA PHE ALA              
HET    SF4  6 182       8                                                       
HET    SF4  9 183       8                                                       
HET    SF4  9 184       8                                                       
HET    SF4  3 784       8                                                       
HET    SF4  3 785       8                                                       
HET    SF4  3 786       8                                                       
HET    FES  3 787       4                                                       
HET    SF4  1 439       8                                                       
HET    FES  2 182       4                                                       
HET    FMN  1 440      31                                                       
HET    NAI  1 441      44                                                       
HET     MG  3 788       1                                                       
HET     MG  3 789       1                                                       
HET     MG  5 208       1                                                       
HET     MG  1 442       1                                                       
HET     CA  7 204       1                                                       
HET     MG  4 410       1                                                       
HET     MG  2 206       1                                                       
HET    SF4  F 182       8                                                       
HET    SF4  G 183       8                                                       
HET    SF4  G 184       8                                                       
HET    SF4  C 784       8                                                       
HET    SF4  C 785       8                                                       
HET    SF4  C 786       8                                                       
HET    FES  C 787       4                                                       
HET    SF4  A 439       8                                                       
HET    FES  B 182       4                                                       
HET    FMN  A 440      31                                                       
HET    NAI  A 441      44                                                       
HET     MG  C 788       1                                                       
HET     MG  C 789       1                                                       
HET     MG  E 208       1                                                       
HET     MG  A 442       1                                                       
HET     CA  H 204       1                                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     FMN FLAVIN MONONUCLEOTIDE                                            
HETNAM     NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE                     
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CA CALCIUM ION                                                      
HETSYN     FMN RIBOFLAVIN MONOPHOSPHATE                                         
HETSYN     NAI NADH                                                             
FORMUL  17  SF4    14(FE4 S4)                                                   
FORMUL  23  FES    4(FE2 S2)                                                    
FORMUL  26  FMN    2(C17 H21 N4 O9 P)                                           
FORMUL  27  NAI    2(C21 H29 N7 O14 P2)                                         
FORMUL  28   MG    10(MG 2+)                                                    
FORMUL  32   CA    2(CA 2+)                                                     
HELIX    1   1 LEU 1   17  VAL 1   21  5                                   5    
HELIX    2   2 THR 1   28  HIS 1   35  1                                   8    
HELIX    3   3 TYR 1   38  GLU 1   47  1                                  10    
HELIX    4   4 THR 1   49  GLY 1   61  1                                  13    
HELIX    5   5 PRO 1   71  SER 1   77  1                                   7    
HELIX    6   6 ASP 1  103  VAL 1  110  1                                   8    
HELIX    7   7 VAL 1  110  ILE 1  125  1                                  16    
HELIX    8   8 ARG 1  139  ARG 1  155  1                                  17    
HELIX    9   9 ASN 1  161  THR 1  165  5                                   5    
HELIX   10  10 ALA 1  179  GLY 1  183  5                                   5    
HELIX   11  11 GLU 1  184  GLU 1  193  1                                  10    
HELIX   12  12 GLY 1  210  LYS 1  214  5                                   5    
HELIX   13  13 VAL 1  221  ARG 1  233  1                                  13    
HELIX   14  14 ARG 1  233  GLN 1  240  1                                   8    
HELIX   15  15 THR 1  271  TYR 1  277  1                                   7    
HELIX   16  16 THR 1  303  ASP 1  308  1                                   6    
HELIX   17  17 LEU 1  316  GLY 1  320  5                                   5    
HELIX   18  18 SER 1  336  SER 1  352  1                                  17    
HELIX   19  19 CYS 1  356  GLY 1  365  1                                  10    
HELIX   20  20 GLY 1  365  GLY 1  375  1                                  11    
HELIX   21  21 GLU 1  380  GLU 1  395  1                                  16    
HELIX   22  22 PRO 1  401  GLU 1  427  1                                  27    
HELIX   23  23 LYS 2    7  ALA 2   16  1                                  10    
HELIX   24  24 GLY 2   22  ALA 2   25  5                                   4    
HELIX   25  25 ALA 2   26  GLY 2   39  1                                  14    
HELIX   26  26 ARG 2   42  GLY 2   54  1                                  13    
HELIX   27  27 THR 2   56  SER 2   65  1                                  10    
HELIX   28  28 THR 2   85  GLY 2   92  1                                   8    
HELIX   29  29 GLY 2   92  GLY 2  105  1                                  14    
HELIX   30  30 SER 2  127  ALA 2  131  5                                   5    
HELIX   31  31 THR 2  146  GLY 2  160  1                                  15    
HELIX   32  32 ARG 2  162  ILE 2  166  5                                   5    
HELIX   33  33 SER 3   18  GLY 3   27  1                                  10    
HELIX   34  34 SER 3   97  LEU 3  113  1                                  17    
HELIX   35  35 ASP 3  118  CYS 3  122  5                                   5    
HELIX   36  36 CYS 3  128  GLY 3  138  1                                  11    
HELIX   37  37 LYS 3  185  VAL 3  194  1                                  10    
HELIX   38  38 ARG 3  205  THR 3  209  5                                   5    
HELIX   39  39 PHE 3  222  GLY 3  224  5                                   3    
HELIX   40  40 ASN 3  225  CYS 3  230  1                                   6    
HELIX   41  41 THR 3  239  ARG 3  241  5                                   3    
HELIX   42  42 ARG 3  245  MET 3  249  5                                   5    
HELIX   43  43 CYS 3  291  GLY 3  297  1                                   7    
HELIX   44  44 HIS 3  298  GLN 3  303  1                                   6    
HELIX   45  45 THR 3  321  GLY 3  332  1                                  12    
HELIX   46  46 THR 3  350  LEU 3  364  1                                  15    
HELIX   47  47 PRO 3  378  PHE 3  382  5                                   5    
HELIX   48  48 GLU 3  388  ALA 3  393  1                                   6    
HELIX   49  49 ASP 3  401  ALA 3  406  1                                   6    
HELIX   50  50 PRO 3  407  ARG 3  418  1                                  12    
HELIX   51  51 ALA 3  456  TRP 3  461  5                                   6    
HELIX   52  52 GLU 3  472  GLY 3  482  1                                  11    
HELIX   53  53 SER 3  487  ALA 3  500  1                                  14    
HELIX   54  54 GLY 3  508  GLN 3  513  1                                   6    
HELIX   55  55 ASP 3  514  LYS 3  528  1                                  15    
HELIX   56  56 ASN 3  540  GLU 3  545  1                                   6    
HELIX   57  57 ALA 3  546  GLY 3  548  5                                   3    
HELIX   58  58 PRO 3  573  LEU 3  577  5                                   5    
HELIX   59  59 LEU 3  593  ALA 3  598  1                                   6    
HELIX   60  60 THR 3  606  LYS 3  610  5                                   5    
HELIX   61  61 GLY 3  636  ALA 3  647  1                                  12    
HELIX   62  62 LEU 3  656  LYS 3  668  1                                  13    
HELIX   63  63 LYS 3  700  ALA 3  704  5                                   5    
HELIX   64  64 HIS 3  719  ALA 3  725  1                                   7    
HELIX   65  65 GLY 4   65  MET 4   70  1                                   6    
HELIX   66  66 GLU 4   71  ARG 4   73  5                                   3    
HELIX   67  67 GLN 4   77  MET 4   85  5                                   9    
HELIX   68  68 HIS 4   89  LEU 4  105  1                                  17    
HELIX   69  69 PRO 4  110  LEU 4  138  1                                  29    
HELIX   70  70 ALA 4  142  GLY 4  165  1                                  24    
HELIX   71  71 GLU 4  185  LEU 4  193  1                                   9    
HELIX   72  72 VAL 4  196  GLU 4  210  1                                  15    
HELIX   73  73 ILE 4  213  ARG 4  219  1                                   7    
HELIX   74  74 PRO 4  225  GLY 4  233  1                                   9    
HELIX   75  75 LEU 4  239  GLY 4  243  5                                   5    
HELIX   76  76 ASP 4  247  TYR 4  252  1                                   6    
HELIX   77  77 GLY 4  256  TYR 4  260  5                                   5    
HELIX   78  78 ASP 4  271  LEU 4  297  1                                  27    
HELIX   79  79 PRO 4  313  LEU 4  317  5                                   5    
HELIX   80  80 SER 4  320  THR 4  332  1                                  13    
HELIX   81  81 ALA 4  372  ASN 4  377  1                                   6    
HELIX   82  82 SER 4  380  CYS 4  385  1                                   6    
HELIX   83  83 VAL 4  390  MET 4  393  5                                   4    
HELIX   84  84 VAL 4  394  SER 4  399  1                                   6    
HELIX   85  85 VAL 4  403  ARG 4  409  1                                   7    
HELIX   86  86 LEU 5    3  LYS 5   13  1                                  11    
HELIX   87  87 PRO 5   30  GLY 5   45  1                                  16    
HELIX   88  88 SER 5  110  PHE 5  122  1                                  13    
HELIX   89  89 ILE 5  166  ARG 5  171  1                                   6    
HELIX   90  90 GLY 5  186  LYS 5  190  5                                   5    
HELIX   91  91 GLY 6   18  SER 6   35  1                                  18    
HELIX   92  92 CYS 6   45  MET 6   51  1                                   7    
HELIX   93  93 MET 6   88  GLN 6   98  1                                  11    
HELIX   94  94 GLY 6  109  SER 6  114  1                                   6    
HELIX   95  95 ASN 6  126  VAL 6  130  5                                   5    
HELIX   96  96 ARG 6  143  ARG 6  159  1                                  17    
HELIX   97  97 SER 9   57  CYS 9   63  1                                   7    
HELIX   98  98 GLY 9  102  CYS 9  108  1                                   7    
HELIX   99  99 GLU 9  125  ASP 9  128  5                                   4    
HELIX  100 100 LYS 9  133  LEU 9  137  1                                   5    
HELIX  101 101 THR 9  143  ALA 9  150  1                                   8    
HELIX  102 102 SER 7    4  LYS 7   27  1                                  24    
HELIX  103 103 PHE 7   37  TYR 7   42  1                                   6    
HELIX  104 104 THR 7  111  ALA 7  127  1                                  17    
HELIX  105 105 LEU A   17  VAL A   21  5                                   5    
HELIX  106 106 THR A   28  HIS A   35  1                                   8    
HELIX  107 107 TYR A   38  GLU A   47  1                                  10    
HELIX  108 108 THR A   49  GLY A   61  1                                  13    
HELIX  109 109 PRO A   71  SER A   77  1                                   7    
HELIX  110 110 ASP A  103  VAL A  110  1                                   8    
HELIX  111 111 VAL A  110  ILE A  125  1                                  16    
HELIX  112 112 ARG A  139  ARG A  155  1                                  17    
HELIX  113 113 ASN A  161  THR A  165  5                                   5    
HELIX  114 114 ALA A  179  GLY A  183  5                                   5    
HELIX  115 115 GLU A  184  GLU A  193  1                                  10    
HELIX  116 116 GLY A  210  LYS A  214  5                                   5    
HELIX  117 117 VAL A  221  ARG A  233  1                                  13    
HELIX  118 118 ARG A  233  GLN A  240  1                                   8    
HELIX  119 119 THR A  271  TYR A  277  1                                   7    
HELIX  120 120 THR A  303  ASP A  308  1                                   6    
HELIX  121 121 LEU A  316  GLY A  320  5                                   5    
HELIX  122 122 SER A  336  SER A  352  1                                  17    
HELIX  123 123 CYS A  356  GLY A  365  1                                  10    
HELIX  124 124 GLY A  365  GLY A  375  1                                  11    
HELIX  125 125 GLU A  380  GLU A  395  1                                  16    
HELIX  126 126 PRO A  401  GLU A  427  1                                  27    
HELIX  127 127 LYS B    7  ALA B   16  1                                  10    
HELIX  128 128 GLY B   22  ALA B   25  5                                   4    
HELIX  129 129 ALA B   26  GLY B   39  1                                  14    
HELIX  130 130 ARG B   42  GLY B   54  1                                  13    
HELIX  131 131 THR B   56  SER B   65  1                                  10    
HELIX  132 132 THR B   85  GLY B   92  1                                   8    
HELIX  133 133 GLY B   92  GLY B  105  1                                  14    
HELIX  134 134 SER B  127  ALA B  131  5                                   5    
HELIX  135 135 THR B  146  GLY B  160  1                                  15    
HELIX  136 136 ARG B  162  ILE B  166  5                                   5    
HELIX  137 137 SER C   18  GLY C   27  1                                  10    
HELIX  138 138 SER C   97  LEU C  113  1                                  17    
HELIX  139 139 ASP C  118  CYS C  122  5                                   5    
HELIX  140 140 CYS C  128  GLY C  138  1                                  11    
HELIX  141 141 LYS C  185  VAL C  194  1                                  10    
HELIX  142 142 ARG C  205  THR C  209  5                                   5    
HELIX  143 143 PHE C  222  GLY C  224  5                                   3    
HELIX  144 144 ASN C  225  CYS C  230  1                                   6    
HELIX  145 145 THR C  239  ARG C  241  5                                   3    
HELIX  146 146 ARG C  245  MET C  249  5                                   5    
HELIX  147 147 CYS C  291  GLY C  297  1                                   7    
HELIX  148 148 HIS C  298  GLN C  303  1                                   6    
HELIX  149 149 THR C  321  GLY C  332  1                                  12    
HELIX  150 150 THR C  350  LEU C  364  1                                  15    
HELIX  151 151 PRO C  378  PHE C  382  5                                   5    
HELIX  152 152 GLU C  388  ALA C  393  1                                   6    
HELIX  153 153 ASP C  401  ALA C  406  1                                   6    
HELIX  154 154 PRO C  407  ARG C  418  1                                  12    
HELIX  155 155 ALA C  456  TRP C  461  5                                   6    
HELIX  156 156 GLU C  472  GLY C  482  1                                  11    
HELIX  157 157 SER C  487  ALA C  500  1                                  14    
HELIX  158 158 GLY C  508  GLN C  513  1                                   6    
HELIX  159 159 ASP C  514  LYS C  528  1                                  15    
HELIX  160 160 ASN C  540  GLU C  545  1                                   6    
HELIX  161 161 ALA C  546  GLY C  548  5                                   3    
HELIX  162 162 PRO C  573  LEU C  577  5                                   5    
HELIX  163 163 LEU C  593  ALA C  598  1                                   6    
HELIX  164 164 THR C  606  LYS C  610  5                                   5    
HELIX  165 165 GLY C  636  ALA C  647  1                                  12    
HELIX  166 166 LEU C  656  LYS C  668  1                                  13    
HELIX  167 167 LYS C  700  ALA C  704  5                                   5    
HELIX  168 168 HIS C  719  ALA C  725  1                                   7    
HELIX  169 169 GLY D   65  MET D   70  1                                   6    
HELIX  170 170 GLU D   71  ARG D   73  5                                   3    
HELIX  171 171 GLN D   77  MET D   85  5                                   9    
HELIX  172 172 HIS D   89  LEU D  105  1                                  17    
HELIX  173 173 PRO D  110  LEU D  138  1                                  29    
HELIX  174 174 LEU D  143  GLY D  165  1                                  23    
HELIX  175 175 PHE D  186  LEU D  193  1                                   8    
HELIX  176 176 VAL D  196  GLU D  210  1                                  15    
HELIX  177 177 ILE D  213  ARG D  219  1                                   7    
HELIX  178 178 PRO D  225  GLY D  233  1                                   9    
HELIX  179 179 LEU D  239  GLY D  243  5                                   5    
HELIX  180 180 ASP D  247  TYR D  252  1                                   6    
HELIX  181 181 GLY D  256  TYR D  260  5                                   5    
HELIX  182 182 ASP D  271  LEU D  297  1                                  27    
HELIX  183 183 PRO D  313  LEU D  317  5                                   5    
HELIX  184 184 SER D  320  THR D  332  1                                  13    
HELIX  185 185 ALA D  372  ASN D  377  1                                   6    
HELIX  186 186 SER D  380  CYS D  385  1                                   6    
HELIX  187 187 VAL D  390  MET D  393  5                                   4    
HELIX  188 188 VAL D  394  SER D  399  1                                   6    
HELIX  189 189 VAL D  403  ARG D  409  1                                   7    
HELIX  190 190 LEU E    3  LYS E   13  1                                  11    
HELIX  191 191 PRO E   30  GLY E   45  1                                  16    
HELIX  192 192 SER E  110  PHE E  122  1                                  13    
HELIX  193 193 ARG E  160  GLY E  162  5                                   3    
HELIX  194 194 ILE E  166  ARG E  171  1                                   6    
HELIX  195 195 GLY E  186  LYS E  190  5                                   5    
HELIX  196 196 GLY F   18  SER F   35  1                                  18    
HELIX  197 197 CYS F   45  MET F   51  1                                   7    
HELIX  198 198 MET F   88  GLN F   98  1                                  11    
HELIX  199 199 GLY F  109  SER F  114  1                                   6    
HELIX  200 200 ASN F  126  VAL F  130  5                                   5    
HELIX  201 201 ARG F  143  ARG F  159  1                                  17    
HELIX  202 202 LEU G   58  CYS G   63  1                                   6    
HELIX  203 203 GLY G  102  CYS G  108  1                                   7    
HELIX  204 204 GLU G  125  ASP G  128  5                                   4    
HELIX  205 205 LYS G  133  LEU G  137  1                                   5    
HELIX  206 206 THR G  143  ALA G  150  1                                   8    
HELIX  207 207 ARG G  167  GLU G  171  5                                   5    
HELIX  208 208 SER H    4  LYS H   27  1                                  24    
HELIX  209 209 PHE H   37  TYR H   42  1                                   6    
HELIX  210 210 PRO H   87  HIS H   90  5                                   4    
HELIX  211 211 THR H  111  ALA H  127  1                                  17    
SHEET    1   A 4 ASP 1 170  HIS 1 174  0                                        
SHEET    2   A 4 VAL 1 129  VAL 1 134  1  N  ILE 1 132   O  HIS 1 172           
SHEET    3   A 4 TYR 1  88  ALA 1  93  1  N  CYS 1  91   O  TYR 1 131           
SHEET    4   A 4 THR 1 216  ASN 1 220  1  O  ASN 1 219   N  ASN 1  92           
SHEET    1   B 5 GLY 1 262  PRO 1 267  0                                        
SHEET    2   B 5 MET 1 249  SER 1 255 -1  N  TYR 1 252   O  TYR 1 264           
SHEET    3   B 5 GLY 1 327  PRO 1 332  1  O  VAL 1 328   N  GLN 1 253           
SHEET    4   B 5 ILE 1 287  ILE 1 291 -1  N  GLN 1 288   O  ILE 1 331           
SHEET    5   B 5 LEU 1 300  PRO 1 301 -1  O  LEU 1 300   N  ILE 1 290           
SHEET    1   C 4 PHE 2 117  VAL 2 122  0                                        
SHEET    2   C 4 TYR 2  78  CYS 2  83  1  N  VAL 2  82   O  VAL 2 122           
SHEET    3   C 4 VAL 2 133  GLN 2 135 -1  O  GLN 2 135   N  GLN 2  81           
SHEET    4   C 4 VAL 2 142  GLU 2 143 -1  O  VAL 2 142   N  ILE 2 134           
SHEET    1   D 2 VAL 3   2  LYS 3   5  0                                        
SHEET    2   D 2 ILE 3  10  VAL 3  13 -1  O  VAL 3  11   N  VAL 3   4           
SHEET    1   E 3 ALA 3  80  ALA 3  81  0                                        
SHEET    2   E 3 LEU 3  49  GLY 3  53 -1  N  VAL 3  50   O  ALA 3  80           
SHEET    3   E 3 VAL 3  92  ASP 3  94 -1  O  VAL 3  92   N  GLY 3  53           
SHEET    1   F 3 HIS 3 168  PRO 3 169  0                                        
SHEET    2   F 3 VAL 3 174  LEU 3 176 -1  O  LEU 3 176   N  HIS 3 168           
SHEET    3   F 3 LEU 3 235  ASP 3 237 -1  O  LEU 3 236   N  ILE 3 175           
SHEET    1   G 2 ASP 3 201  PHE 3 202  0                                        
SHEET    2   G 2 ILE 3 211  GLY 3 212 -1  O  GLY 3 212   N  ASP 3 201           
SHEET    1   H 3 GLU 3 250  THR 3 254  0                                        
SHEET    2   H 3 ILE 3 265  THR 3 269 -1  O  ALA 3 267   N  THR 3 252           
SHEET    3   H 3 LEU 3 274  ALA 3 279 -1  O  ARG 3 276   N  ASP 3 268           
SHEET    1   I 7 LEU 3 317  GLU 3 319  0                                        
SHEET    2   I 7 LEU 3 310  ARG 3 312 -1  N  VAL 3 311   O  VAL 3 318           
SHEET    3   I 7 VAL 3 600  PRO 3 603 -1  O  VAL 3 601   N  LEU 3 310           
SHEET    4   I 7 PHE 3 582  LEU 3 587  1  N  MET 3 585   O  LEU 3 602           
SHEET    5   I 7 TYR 3 565  TYR 3 568  1  N  TYR 3 568   O  HIS 3 586           
SHEET    6   I 7 VAL 3 341  LEU 3 345  1  N  GLY 3 342   O  TYR 3 567           
SHEET    7   I 7 LEU 3 369  PHE 3 371  1  O  ASP 3 370   N  LEU 3 343           
SHEET    1   J 5 ILE 3 464  GLU 3 466  0                                        
SHEET    2   J 5 MET 3 448  PHE 3 451  1  N  LEU 3 450   O  ILE 3 464           
SHEET    3   J 5 ALA 3 396  LEU 3 399  1  N  ALA 3 396   O  ALA 3 449           
SHEET    4   J 5 VAL 3 504  LEU 3 507  1  O  ILE 3 506   N  LEU 3 397           
SHEET    5   J 5 VAL 3 532  ALA 3 534  1  O  LEU 3 533   N  LEU 3 505           
SHEET    1   K 2 GLY 3 612  VAL 3 615  0                                        
SHEET    2   K 2 VAL 3 621  LEU 3 624 -1  O  LEU 3 624   N  GLY 3 612           
SHEET    1   L 7 ARG 3 770  VAL 3 771  0                                        
SHEET    2   L 7 PHE 3 692  PRO 3 696 -1  N  PHE 3 692   O  VAL 3 771           
SHEET    3   L 7 LEU 3 758  ALA 3 762  1  O  LEU 3 760   N  TYR 3 693           
SHEET    4   L 7 ALA 3 714  ALA 3 718 -1  N  TRP 3 717   O  TYR 3 759           
SHEET    5   L 7 GLY 3 741  HIS 3 749  1  O  VAL 3 748   N  LEU 3 716           
SHEET    6   L 7 GLN 3 733  THR 3 738 -1  N  VAL 3 736   O  VAL 3 743           
SHEET    7   L 7 ARG 3 774  VAL 3 775 -1  O  ARG 3 774   N  GLU 3 737           
SHEET    1   M 3 LEU 4  28  VAL 4  30  0                                        
SHEET    2   M 3 ARG 4  42  THR 4  46 -1  O  LEU 4  43   N  VAL 4  30           
SHEET    3   M 3 GLU 4  54  HIS 4  58 -1  O  HIS 4  58   N  ARG 4  42           
SHEET    1   N 3 GLY 4 340  SER 4 348  0                                        
SHEET    2   N 3 GLY 4 351  SER 4 359 -1  O  SER 4 359   N  GLY 4 340           
SHEET    3   N 3 ARG 4 367  VAL 4 370 -1  O  LYS 4 369   N  TYR 4 356           
SHEET    1   O 2 ILE 5  17  ASP 5  19  0                                        
SHEET    2   O 2 LEU 5  25  VAL 5  27 -1  O  TRP 5  26   N  GLU 5  18           
SHEET    1   P 3 PHE 5  48  ASP 5  56  0                                        
SHEET    2   P 3 PHE 5  68  VAL 5  75 -1  O  ALA 5  69   N  LEU 5  55           
SHEET    3   P 3 ARG 5  87  VAL 5  94 -1  O  VAL 5  90   N  TYR 5  72           
SHEET    1   Q 2 THR 5 157  LEU 5 158  0                                        
SHEET    2   Q 2 TYR 5 164  ILE 5 165 -1  O  ILE 5 165   N  THR 5 157           
SHEET    1   R 4 PHE 6  41  GLY 6  42  0                                        
SHEET    2   R 4 MET 6  78  ALA 6  81  1  O  ILE 6  79   N  PHE 6  41           
SHEET    3   R 4 VAL 6 105  MET 6 108  1  O  ILE 6 106   N  VAL 6  80           
SHEET    4   R 4 VAL 6 135  VAL 6 137  1  O  VAL 6 135   N  SER 6 107           
SHEET    1   S 2 VAL 9  31  ALA 9  32  0                                        
SHEET    2   S 2 TYR 9 161  VAL 9 162  1  O  VAL 9 162   N  VAL 9  31           
SHEET    1   T 2 VAL 9  42  LEU 9  43  0                                        
SHEET    2   T 2 ILE 9 113  VAL 9 114 -1  O  VAL 9 114   N  VAL 9  42           
SHEET    1   U 3 ILE 9  68  GLU 9  74  0                                        
SHEET    2   U 3 ARG 9  86  ASN 9  94 -1  O  TYR 9  87   N  ALA 9  73           
SHEET    3   U 3 VAL 9 130  GLY 9 132 -1  O  TYR 9 131   N  ILE 9  93           
SHEET    1   V 7 PHE 7  31  ASP 7  36  0                                        
SHEET    2   V 7 ILE 7  54  SER 7  60 -1  O  THR 7  56   N  GLU 7  34           
SHEET    3   V 7 PRO 7  66  VAL 7  72 -1  O  PHE 7  67   N  LEU 7  59           
SHEET    4   V 7 ILE 7  82  LEU 7  86 -1  O  GLY 7  83   N  ASP 7  71           
SHEET    5   V 7 ILE 7  91  GLU 7  98 -1  O  ALA 7  95   N  ILE 7  82           
SHEET    6   V 7 GLY 7 102  THR 7 105 -1  O  VAL 7 104   N  HIS 7  96           
SHEET    7   V 7 ILE 7 108  PRO 7 109 -1  O  ILE 7 108   N  THR 7 105           
SHEET    1   W 4 ASP A 170  HIS A 174  0                                        
SHEET    2   W 4 VAL A 129  VAL A 134  1  N  ILE A 132   O  HIS A 172           
SHEET    3   W 4 TYR A  88  ALA A  93  1  N  CYS A  91   O  TYR A 131           
SHEET    4   W 4 THR A 216  ASN A 220  1  O  ASN A 219   N  ASN A  92           
SHEET    1   X 5 GLY A 262  PRO A 267  0                                        
SHEET    2   X 5 MET A 249  SER A 255 -1  N  TYR A 252   O  TYR A 264           
SHEET    3   X 5 GLY A 327  PRO A 332  1  O  VAL A 328   N  GLN A 253           
SHEET    4   X 5 ILE A 287  ILE A 291 -1  N  GLN A 288   O  ILE A 331           
SHEET    5   X 5 LEU A 300  PRO A 301 -1  O  LEU A 300   N  ILE A 290           
SHEET    1   Y 3 PHE B 117  VAL B 122  0                                        
SHEET    2   Y 3 TYR B  78  CYS B  83  1  N  VAL B  82   O  VAL B 122           
SHEET    3   Y 3 ILE B 134  GLN B 135 -1  O  GLN B 135   N  GLN B  81           
SHEET    1   Z 2 VAL C   2  LYS C   5  0                                        
SHEET    2   Z 2 ILE C  10  VAL C  13 -1  O  VAL C  11   N  VAL C   4           
SHEET    1  AA 3 ALA C  80  ALA C  81  0                                        
SHEET    2  AA 3 LEU C  49  GLY C  53 -1  N  VAL C  50   O  ALA C  80           
SHEET    3  AA 3 VAL C  92  ASP C  94 -1  O  VAL C  92   N  GLY C  53           
SHEET    1  AB 3 HIS C 168  PRO C 169  0                                        
SHEET    2  AB 3 VAL C 174  LEU C 176 -1  O  LEU C 176   N  HIS C 168           
SHEET    3  AB 3 LEU C 235  ASP C 237 -1  O  LEU C 236   N  ILE C 175           
SHEET    1  AC 2 ASP C 201  PHE C 202  0                                        
SHEET    2  AC 2 ILE C 211  GLY C 212 -1  O  GLY C 212   N  ASP C 201           
SHEET    1  AD 3 THR C 252  THR C 254  0                                        
SHEET    2  AD 3 ILE C 265  THR C 269 -1  O  ALA C 267   N  THR C 252           
SHEET    3  AD 3 LEU C 274  ALA C 279 -1  O  ARG C 276   N  ASP C 268           
SHEET    1  AE 7 LEU C 317  GLU C 319  0                                        
SHEET    2  AE 7 LEU C 310  ARG C 312 -1  N  VAL C 311   O  VAL C 318           
SHEET    3  AE 7 VAL C 600  PRO C 603 -1  O  VAL C 601   N  LEU C 310           
SHEET    4  AE 7 PHE C 582  LEU C 587  1  N  MET C 585   O  LEU C 602           
SHEET    5  AE 7 TYR C 565  TYR C 568  1  N  TYR C 568   O  HIS C 586           
SHEET    6  AE 7 VAL C 341  LEU C 345  1  N  GLY C 342   O  TYR C 567           
SHEET    7  AE 7 LEU C 369  PHE C 371  1  O  ASP C 370   N  LEU C 343           
SHEET    1  AF 5 ILE C 464  GLU C 466  0                                        
SHEET    2  AF 5 MET C 448  PHE C 451  1  N  LEU C 450   O  GLU C 466           
SHEET    3  AF 5 ALA C 396  LEU C 399  1  N  ALA C 396   O  ALA C 449           
SHEET    4  AF 5 VAL C 504  LEU C 507  1  O  ILE C 506   N  LEU C 397           
SHEET    5  AF 5 VAL C 532  ALA C 534  1  O  LEU C 533   N  LEU C 505           
SHEET    1  AG 2 GLY C 612  VAL C 615  0                                        
SHEET    2  AG 2 VAL C 621  LEU C 624 -1  O  LEU C 624   N  GLY C 612           
SHEET    1  AH 7 ARG C 770  VAL C 771  0                                        
SHEET    2  AH 7 PHE C 692  PRO C 696 -1  N  PHE C 692   O  VAL C 771           
SHEET    3  AH 7 LEU C 758  ALA C 762  1  O  LEU C 760   N  TYR C 693           
SHEET    4  AH 7 ALA C 714  ALA C 718 -1  N  TRP C 717   O  TYR C 759           
SHEET    5  AH 7 VAL C 743  HIS C 749  1  O  VAL C 748   N  LEU C 716           
SHEET    6  AH 7 GLN C 733  GLU C 737 -1  N  VAL C 736   O  VAL C 743           
SHEET    7  AH 7 ARG C 774  VAL C 775 -1  O  ARG C 774   N  GLU C 737           
SHEET    1  AI 3 LEU D  28  VAL D  30  0                                        
SHEET    2  AI 3 ARG D  42  THR D  46 -1  O  LEU D  43   N  VAL D  30           
SHEET    3  AI 3 GLU D  54  HIS D  58 -1  O  HIS D  58   N  ARG D  42           
SHEET    1  AJ 3 GLY D 340  SER D 348  0                                        
SHEET    2  AJ 3 GLY D 351  SER D 359 -1  O  SER D 359   N  GLY D 340           
SHEET    3  AJ 3 ARG D 367  VAL D 370 -1  O  LYS D 369   N  TYR D 356           
SHEET    1  AK 3 PHE E  48  ASP E  56  0                                        
SHEET    2  AK 3 PHE E  68  VAL E  75 -1  O  ALA E  69   N  LEU E  55           
SHEET    3  AK 3 ARG E  87  VAL E  94 -1  O  VAL E  90   N  TYR E  72           
SHEET    1  AL 2 THR E 157  LEU E 158  0                                        
SHEET    2  AL 2 TYR E 164  ILE E 165 -1  O  ILE E 165   N  THR E 157           
SHEET    1  AM 4 PHE F  41  GLY F  42  0                                        
SHEET    2  AM 4 MET F  78  ALA F  81  1  O  ILE F  79   N  PHE F  41           
SHEET    3  AM 4 VAL F 105  MET F 108  1  O  ILE F 106   N  VAL F  80           
SHEET    4  AM 4 VAL F 135  VAL F 137  1  O  VAL F 135   N  SER F 107           
SHEET    1  AN 2 VAL G  31  ALA G  32  0                                        
SHEET    2  AN 2 TYR G 161  VAL G 162  1  O  VAL G 162   N  VAL G  31           
SHEET    1  AO 2 VAL G  42  LEU G  43  0                                        
SHEET    2  AO 2 ILE G 113  VAL G 114 -1  O  VAL G 114   N  VAL G  42           
SHEET    1  AP 3 ILE G  68  GLU G  74  0                                        
SHEET    2  AP 3 ARG G  86  ASN G  94 -1  O  TYR G  87   N  ALA G  73           
SHEET    3  AP 3 VAL G 130  GLY G 132 -1  O  TYR G 131   N  ILE G  93           
SHEET    1  AQ 7 PHE H  31  ASP H  36  0                                        
SHEET    2  AQ 7 ILE H  54  SER H  60 -1  O  THR H  56   N  GLU H  34           
SHEET    3  AQ 7 PRO H  66  VAL H  72 -1  O  ALA H  70   N  ALA H  57           
SHEET    4  AQ 7 ILE H  82  LEU H  86 -1  O  GLY H  83   N  ASP H  71           
SHEET    5  AQ 7 ILE H  91  GLU H  98 -1  O  ALA H  95   N  ILE H  82           
SHEET    6  AQ 7 GLY H 102  THR H 105 -1  O  VAL H 104   N  HIS H  96           
SHEET    7  AQ 7 ILE H 108  PRO H 109 -1  O  ILE H 108   N  THR H 105           
SSBOND   1 CYS 2  144    CYS 2  172                          1555   1555  2.05  
SSBOND   2 CYS B  144    CYS B  172                          1555   1555  2.05  
LINK         NE2 HIS 1  35                MG    MG 1 442     1555   1555  2.16  
LINK         SG  CYS 1 353                FE4  SF4 1 439     1555   1555  2.25  
LINK         SG  CYS 1 356                FE1  SF4 1 439     1555   1555  2.26  
LINK         SG  CYS 1 359                FE2  SF4 1 439     1555   1555  2.24  
LINK         SG  CYS 1 400                FE3  SF4 1 439     1555   1555  2.25  
LINK         SG  CYS 2  83                FE1  FES 2 182     1555   1555  2.31  
LINK         SG  CYS 2  88                FE1  FES 2 182     1555   1555  2.31  
LINK         SG  CYS 2 124                FE2  FES 2 182     1555   1555  2.32  
LINK         SG  CYS 2 128                FE2  FES 2 182     1555   1555  2.28  
LINK         SG  CYS 3  34                FE1  FES 3 787     1555   1555  2.32  
LINK         SG  CYS 3  45                FE1  FES 3 787     1555   1555  2.29  
LINK         SG  CYS 3  48                FE2  FES 3 787     1555   1555  2.30  
LINK         SG  CYS 3  83                FE2  FES 3 787     1555   1555  2.26  
LINK         NE2 HIS 3 115                FE3  SF4 3 784     1555   1555  2.11  
LINK         SG  CYS 3 119                FE2  SF4 3 784     1555   1555  2.27  
LINK         SG  CYS 3 122                FE4  SF4 3 784     1555   1555  2.28  
LINK         SG  CYS 3 128                FE1  SF4 3 784     1555   1555  2.30  
LINK         SG  CYS 3 181                FE2  SF4 3 785     1555   1555  2.26  
LINK         SG  CYS 3 184                FE1  SF4 3 785     1555   1555  2.29  
LINK         SG  CYS 3 187                FE3  SF4 3 785     1555   1555  2.28  
LINK         SG  CYS 3 230                FE4  SF4 3 785     1555   1555  2.25  
LINK         SG  CYS 3 256                FE1  SF4 3 786     1555   1555  2.34  
LINK         SG  CYS 3 259                FE4  SF4 3 786     1555   1555  2.31  
LINK         SG  CYS 3 263                FE3  SF4 3 786     1555   1555  2.22  
LINK         SG  CYS 3 291                FE2  SF4 3 786     1555   1555  2.21  
LINK         OD1 ASP 3 302                MG    MG 3 788     1555   1555  2.07  
LINK         NE2 HIS 5 144                MG    MG 5 208     1555   1555  2.38  
LINK         SG  CYS 6  45                FE3  SF4 6 182     1555   1555  2.26  
LINK         SG  CYS 6 111                FE1  SF4 6 182     1555   1555  2.28  
LINK         SG  CYS 6 140                FE4  SF4 6 182     1555   1555  2.26  
LINK         SG  CYS 9  53                FE3  SF4 9 184     1555   1555  2.26  
LINK         SG  CYS 9  56                FE4  SF4 9 184     1555   1555  2.28  
LINK         SG  CYS 9  59                FE2  SF4 9 184     1555   1555  2.25  
LINK         SG  CYS 9  63                FE4  SF4 9 183     1555   1555  2.26  
LINK         SG  CYS 9  98                FE2  SF4 9 183     1555   1555  2.31  
LINK         SG  CYS 9 101                FE1  SF4 9 183     1555   1555  2.29  
LINK         SG  CYS 9 104                FE3  SF4 9 183     1555   1555  2.25  
LINK         SG  CYS 9 108                FE1  SF4 9 184     1555   1555  2.28  
LINK         O   GLY 7  64                CA    CA 7 204     1555   1555  2.58  
LINK         SG  CYS A 353                FE4  SF4 A 439     1555   1555  2.25  
LINK         SG  CYS A 356                FE1  SF4 A 439     1555   1555  2.27  
LINK         SG  CYS A 359                FE2  SF4 A 439     1555   1555  2.23  
LINK         SG  CYS A 400                FE3  SF4 A 439     1555   1555  2.29  
LINK         SG  CYS B  83                FE1  FES B 182     1555   1555  2.29  
LINK         SG  CYS B  88                FE1  FES B 182     1555   1555  2.29  
LINK         SG  CYS B 124                FE2  FES B 182     1555   1555  2.30  
LINK         SG  CYS B 128                FE2  FES B 182     1555   1555  2.32  
LINK         SG  CYS C  34                FE1  FES C 787     1555   1555  2.28  
LINK         SG  CYS C  45                FE1  FES C 787     1555   1555  2.30  
LINK         SG  CYS C  48                FE2  FES C 787     1555   1555  2.27  
LINK         SG  CYS C  83                FE2  FES C 787     1555   1555  2.30  
LINK         NE2 HIS C 115                FE3  SF4 C 784     1555   1555  2.19  
LINK         SG  CYS C 119                FE2  SF4 C 784     1555   1555  2.28  
LINK         SG  CYS C 122                FE4  SF4 C 784     1555   1555  2.29  
LINK         SG  CYS C 128                FE1  SF4 C 784     1555   1555  2.23  
LINK         SG  CYS C 181                FE2  SF4 C 785     1555   1555  2.28  
LINK         SG  CYS C 184                FE1  SF4 C 785     1555   1555  2.29  
LINK         SG  CYS C 187                FE3  SF4 C 785     1555   1555  2.29  
LINK         SG  CYS C 230                FE4  SF4 C 785     1555   1555  2.31  
LINK         SG  CYS C 256                FE1  SF4 C 786     1555   1555  2.29  
LINK         SG  CYS C 259                FE4  SF4 C 786     1555   1555  2.28  
LINK         SG  CYS C 263                FE3  SF4 C 786     1555   1555  2.22  
LINK         SG  CYS C 291                FE2  SF4 C 786     1555   1555  2.25  
LINK         OD1 ASP C 302                MG    MG C 788     1555   1555  2.30  
LINK         SG  CYS F  45                FE3  SF4 F 182     1555   1555  2.26  
LINK         SG  CYS F 111                FE1  SF4 F 182     1555   1555  2.25  
LINK         SG  CYS F 140                FE4  SF4 F 182     1555   1555  2.25  
LINK         SG  CYS G  53                FE3  SF4 G 184     1555   1555  2.25  
LINK         SG  CYS G  56                FE4  SF4 G 184     1555   1555  2.26  
LINK         SG  CYS G  59                FE2  SF4 G 184     1555   1555  2.25  
LINK         SG  CYS G  63                FE4  SF4 G 183     1555   1555  2.24  
LINK         SG  CYS G  98                FE2  SF4 G 183     1555   1555  2.31  
LINK         SG  CYS G 101                FE1  SF4 G 183     1555   1555  2.31  
LINK         SG  CYS G 104                FE3  SF4 G 183     1555   1555  2.24  
LINK         SG  CYS G 108                FE1  SF4 G 184     1555   1555  2.29  
LINK         O   GLY H  64                CA    CA H 204     1555   1555  2.80  
CISPEP   1 ALA 2  131    PRO 2  132          0        -2.69                     
CISPEP   2 CYS 6  140    PRO 6  141          0        -5.61                     
CISPEP   3 ALA B  131    PRO B  132          0        -0.87                     
CISPEP   4 CYS F  140    PRO F  141          0        -8.28                     
SITE     1 AC1 10 ARG 4  84  HIS 4 169  CYS 6  45  CYS 6  46                    
SITE     2 AC1 10 GLY 6  82  ARG 6  83  ALA 6 110  CYS 6 111                    
SITE     3 AC1 10 CYS 6 140  PRO 6 141                                          
SITE     1 AC2  9 HIS 9  41  CYS 9  63  ILE 9  68  CYS 9  98                    
SITE     2 AC2  9 ILE 9  99  PHE 9 100  CYS 9 101  GLY 9 102                    
SITE     3 AC2  9 CYS 9 104                                                     
SITE     1 AC3  8 CYS 9  53  ILE 9  54  CYS 9  56  SER 9  57                    
SITE     2 AC3  8 CYS 9  59  CYS 9 108  THR 9 110  ALA 9 112                    
SITE     1 AC4  7 HIS 3 115  CYS 3 119  CYS 3 122  CYS 3 128                    
SITE     2 AC4  7 LEU 3 130  VAL 3 232  GLY 3 233                               
SITE     1 AC5  8 CYS 3 181  ILE 3 182  CYS 3 184  ARG 3 186                    
SITE     2 AC5  8 CYS 3 187  CYS 3 230  VAL 3 232  ALA 3 234                    
SITE     1 AC6  9 CYS 3 256  CYS 3 259  VAL 3 261  GLY 3 262                    
SITE     2 AC6  9 CYS 3 263  ILE 3 290  CYS 3 291  PRO 3 407                    
SITE     3 AC6  9 ILE 3 408                                                     
SITE     1 AC7  8 CYS 3  34  SER 3  35  GLY 3  43  ALA 3  44                    
SITE     2 AC7  8 CYS 3  45  ARG 3  46  CYS 3  48  CYS 3  83                    
SITE     1 AC8  9 PRO 1 199  SER 1 352  CYS 1 353  LYS 1 355                    
SITE     2 AC8  9 CYS 1 356  CYS 1 359  SER 1 398  PHE 1 399                    
SITE     3 AC8  9 CYS 1 400                                                     
SITE     1 AC9  8 CYS 2  83  SER 2  87  CYS 2  88  CYS 2 124                    
SITE     2 AC9  8 LEU 2 125  GLY 2 126  SER 2 127  CYS 2 128                    
SITE     1 BC1 16 GLY 1  64  ARG 1  65  GLY 1  66  LYS 1  75                    
SITE     2 BC1 16 ASN 1  92  ASP 1  94  SER 1  96  GLY 1 183                    
SITE     3 BC1 16 GLU 1 184  GLU 1 185  ILE 1 218  ASN 1 219                    
SITE     4 BC1 16 ASN 1 220  THR 1 223  PRO 1 401  NAI 1 441                    
SITE     1 BC2 14 GLY 1  66  GLY 1  67  ALA 1  68  PHE 1  70                    
SITE     2 BC2 14 LYS 1  75  PHE 1  78  GLU 1  97  TYR 1 180                    
SITE     3 BC2 14 GLU 1 185  LYS 1 202  PHE 1 205  THR 1 325                    
SITE     4 BC2 14 PRO 1 401  FMN 1 440                                          
SITE     1 BC3  2 LEU 3 274  ASP 3 302                                          
SITE     1 BC4  2 HIS 3 167  GLU 7  32                                          
SITE     1 BC5  1 HIS 5 144                                                     
SITE     1 BC6  2 HIS 1  35  GLU D 210                                          
SITE     1 BC7  6 ASP 3 165  HIS 3 168  GLU 7  32  GLU 7  34                    
SITE     2 BC7  6 SER 7  60  GLY 7  64                                          
SITE     1 BC8  4 VAL 4 223  ALA 4 384  LYS 4 386  GLU 4 388                    
SITE     1 BC9  3 HIS 1 350  SER 2  68  GLU 2 123                               
SITE     1 CC1 10 ARG D  84  HIS D 169  CYS F  45  CYS F  46                    
SITE     2 CC1 10 GLY F  82  ARG F  83  ALA F 110  CYS F 111                    
SITE     3 CC1 10 CYS F 140  PRO F 141                                          
SITE     1 CC2  9 HIS G  41  CYS G  63  ILE G  68  CYS G  98                    
SITE     2 CC2  9 ILE G  99  PHE G 100  CYS G 101  GLY G 102                    
SITE     3 CC2  9 CYS G 104                                                     
SITE     1 CC3  8 CYS G  53  ILE G  54  CYS G  56  SER G  57                    
SITE     2 CC3  8 CYS G  59  CYS G 108  THR G 110  ALA G 112                    
SITE     1 CC4  7 HIS C 115  CYS C 119  CYS C 122  CYS C 128                    
SITE     2 CC4  7 LEU C 130  VAL C 232  GLY C 233                               
SITE     1 CC5  8 CYS C 181  ILE C 182  CYS C 184  CYS C 187                    
SITE     2 CC5  8 CYS C 230  VAL C 232  ALA C 234  LEU C 235                    
SITE     1 CC6  7 CYS C 256  LEU C 258  CYS C 259  VAL C 261                    
SITE     2 CC6  7 GLY C 262  CYS C 263  CYS C 291                               
SITE     1 CC7  8 CYS C  34  SER C  35  GLY C  43  ALA C  44                    
SITE     2 CC7  8 CYS C  45  ARG C  46  CYS C  48  CYS C  83                    
SITE     1 CC8  9 PRO A 199  SER A 352  CYS A 353  LYS A 355                    
SITE     2 CC8  9 CYS A 356  CYS A 359  PHE A 399  CYS A 400                    
SITE     3 CC8  9 ALA A 403                                                     
SITE     1 CC9  9 CYS B  83  THR B  85  SER B  87  CYS B  88                    
SITE     2 CC9  9 CYS B 124  LEU B 125  GLY B 126  SER B 127                    
SITE     3 CC9  9 CYS B 128                                                     
SITE     1 DC1 15 GLY A  64  GLY A  66  LYS A  75  ASN A  92                    
SITE     2 DC1 15 ASP A  94  SER A  96  GLY A 183  GLU A 184                    
SITE     3 DC1 15 GLU A 185  ILE A 218  ASN A 219  ASN A 220                    
SITE     4 DC1 15 THR A 223  PRO A 401  NAI A 441                               
SITE     1 DC2 13 GLY A  66  GLY A  67  ALA A  68  PHE A  70                    
SITE     2 DC2 13 LYS A  75  SER A  96  GLU A  97  TYR A 180                    
SITE     3 DC2 13 GLU A 185  LYS A 202  PHE A 205  THR A 325                    
SITE     4 DC2 13 FMN A 440                                                     
SITE     1 DC3  2 LEU C 274  ASP C 302                                          
SITE     1 DC4  2 HIS C 167  GLU H  32                                          
SITE     1 DC5  1 HIS E 144                                                     
SITE     1 DC6  2 GLU 4 210  HIS A  35                                          
SITE     1 DC7  5 ASP C 165  HIS C 168  GLU H  32  GLU H  34                    
SITE     2 DC7  5 GLY H  64                                                     
CRYST1  109.002  151.015  216.624  90.00  93.07  90.00 P 1 21 1      4          
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      0.009174  0.000000  0.000492        0.00000                         
SCALE2      0.000000  0.006622  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004623        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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