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Database: PDB
Entry: 5EXR
LinkDB: 5EXR
Original site: 5EXR 
HEADER    REPLICATION                             24-NOV-15   5EXR              
TITLE     CRYSTAL STRUCTURE OF HUMAN PRIMOSOME                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA PRIMASE SMALL SUBUNIT;                                 
COMPND   3 CHAIN: A, E;                                                         
COMPND   4 SYNONYM: DNA PRIMASE 49 KDA SUBUNIT,P49;                             
COMPND   5 EC: 2.7.7.-;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA PRIMASE LARGE SUBUNIT;                                 
COMPND   9 CHAIN: B, F;                                                         
COMPND  10 SYNONYM: DNA PRIMASE 58 KDA SUBUNIT,P58;                             
COMPND  11 EC: 2.7.7.-;                                                         
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: DNA POLYMERASE ALPHA CATALYTIC SUBUNIT;                    
COMPND  15 CHAIN: C, G;                                                         
COMPND  16 SYNONYM: DNA POLYMERASE ALPHA CATALYTIC SUBUNIT P180;                
COMPND  17 EC: 2.7.7.7;                                                         
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MUTATION: YES;                                                       
COMPND  20 MOL_ID: 4;                                                           
COMPND  21 MOLECULE: DNA POLYMERASE ALPHA SUBUNIT B;                            
COMPND  22 CHAIN: D, H;                                                         
COMPND  23 SYNONYM: DNA POLYMERASE ALPHA 70 KDA SUBUNIT;                        
COMPND  24 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PRIM1;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: PRIM2, PRIM2A;                                                 
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: POLA1, POLA;                                                   
SOURCE  20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  24 ORGANISM_COMMON: HUMAN;                                              
SOURCE  25 ORGANISM_TAXID: 9606;                                                
SOURCE  26 GENE: POLA2;                                                         
SOURCE  27 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    HUMAN PRIMOSOME, COMPLEX, PRIMASE, DNA POLYMERASE ALPHA, PRIMER, DNA  
KEYWDS   2 REPLICATION, DNA, RNA, REPLICASE, REPLICATION                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.H.TAHIROV,A.G.BARANOVSKIY,N.D.BABAYEVA                              
REVDAT   6   25-DEC-19 5EXR    1       REMARK                                   
REVDAT   5   01-NOV-17 5EXR    1       REMARK                                   
REVDAT   4   20-SEP-17 5EXR    1       JRNL   REMARK                            
REVDAT   3   01-JUN-16 5EXR    1       JRNL                                     
REVDAT   2   30-MAR-16 5EXR    1       JRNL                                     
REVDAT   1   23-MAR-16 5EXR    0                                                
JRNL        AUTH   A.G.BARANOVSKIY,N.D.BABAYEVA,Y.ZHANG,J.GU,Y.SUWA,Y.I.PAVLOV, 
JRNL        AUTH 2 T.H.TAHIROV                                                  
JRNL        TITL   MECHANISM OF CONCERTED RNA-DNA PRIMER SYNTHESIS BY THE HUMAN 
JRNL        TITL 2 PRIMOSOME.                                                   
JRNL        REF    J.BIOL.CHEM.                  V. 291 10006 2016              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   26975377                                                     
JRNL        DOI    10.1074/JBC.M116.717405                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 6416908.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 68.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 64105                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.268                           
REMARK   3   FREE R VALUE                     : 0.326                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3215                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.83                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 52.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 7661                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3770                       
REMARK   3   BIN FREE R VALUE                    : 0.3910                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 389                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 37636                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.91000                                              
REMARK   3    B22 (A**2) : -5.74000                                             
REMARK   3    B33 (A**2) : 3.83000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.94000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.53                            
REMARK   3   ESD FROM SIGMAA              (A) : 1.15                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.63                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 1.19                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.800                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.190                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 3.970 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 6.670 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.760 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 7.410 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.40                                                 
REMARK   3   BSOL        : 161.8                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : SF4.PAR                                        
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : SF4:PROTEIN.TOP                                
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : SF4.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5EXR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000215669.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 74238                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -1.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 80.5                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.930                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS 1.1                                               
REMARK 200 STARTING MODEL: 4QCL, 4Q5V, 4RR2, 4Y97                               
REMARK 200                                                                      
REMARK 200 REMARK: THIN PLATE IN FORM OF PARALLELOGRAM                          
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM SULPHATE, 50 MM TRIS HCL   
REMARK 280  PH 8.5, 2 MM TCEP PH 7.5, 11.2% W/V PEG 4,000, 3% V/V ETHANOL,      
REMARK 280  0.5% V/V POLYPROPYLENE GLYCOL P400 AND 0.2 MM EDTA, 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      105.08200            
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 300 REMARK: TETRAMER ACCORDING TO ELECTROPHORESIS                        
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     LYS A   284                                                      
REMARK 465     ASN A   285                                                      
REMARK 465     ASP A   286                                                      
REMARK 465     LYS A   287                                                      
REMARK 465     TYR A   288                                                      
REMARK 465     SER A   361                                                      
REMARK 465     THR A   362                                                      
REMARK 465     ASN A   363                                                      
REMARK 465     GLU A   364                                                      
REMARK 465     GLU A   365                                                      
REMARK 465     GLU A   366                                                      
REMARK 465     LYS A   367                                                      
REMARK 465     GLU A   368                                                      
REMARK 465     GLU A   369                                                      
REMARK 465     ASN A   370                                                      
REMARK 465     GLU A   371                                                      
REMARK 465     ALA A   372                                                      
REMARK 465     GLU A   373                                                      
REMARK 465     SER A   374                                                      
REMARK 465     ASP A   375                                                      
REMARK 465     VAL A   376                                                      
REMARK 465     LYS A   377                                                      
REMARK 465     HIS A   378                                                      
REMARK 465     LYS A   413                                                      
REMARK 465     SER A   414                                                      
REMARK 465     ASP A   415                                                      
REMARK 465     LEU A   416                                                      
REMARK 465     GLN A   417                                                      
REMARK 465     LYS A   418                                                      
REMARK 465     ASP A   419                                                      
REMARK 465     PHE A   420                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     PHE B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     TRP B     8                                                      
REMARK 465     ARG B     9                                                      
REMARK 465     LYS B    10                                                      
REMARK 465     LEU B    11                                                      
REMARK 465     ARG B    12                                                      
REMARK 465     LEU B    13                                                      
REMARK 465     ALA B    14                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     ASP B    16                                                      
REMARK 465     GLN B    17                                                      
REMARK 465     ARG B    18                                                      
REMARK 465     ASN B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     SER B    21                                                      
REMARK 465     ASN B   456                                                      
REMARK 465     GLY B   457                                                      
REMARK 465     GLY B   458                                                      
REMARK 465     LYS B   459                                                      
REMARK 465     ASP B   460                                                      
REMARK 465     ILE B   461                                                      
REMARK 465     LYS B   462                                                      
REMARK 465     LYS B   463                                                      
REMARK 465     GLU B   464                                                      
REMARK 465     PRO B   465                                                      
REMARK 465     ILE B   466                                                      
REMARK 465     GLN B   467                                                      
REMARK 465     PRO B   468                                                      
REMARK 465     GLU B   469                                                      
REMARK 465     THR B   470                                                      
REMARK 465     PRO B   471                                                      
REMARK 465     GLN B   472                                                      
REMARK 465     PRO B   473                                                      
REMARK 465     LYS B   474                                                      
REMARK 465     PRO B   475                                                      
REMARK 465     SER B   476                                                      
REMARK 465     VAL B   477                                                      
REMARK 465     GLN B   478                                                      
REMARK 465     LYS B   479                                                      
REMARK 465     THR B   480                                                      
REMARK 465     LYS B   481                                                      
REMARK 465     ASP B   482                                                      
REMARK 465     ALA B   483                                                      
REMARK 465     SER B   484                                                      
REMARK 465     SER B   485                                                      
REMARK 465     ALA B   486                                                      
REMARK 465     LEU B   487                                                      
REMARK 465     ALA B   488                                                      
REMARK 465     SER B   489                                                      
REMARK 465     LEU B   490                                                      
REMARK 465     ASN B   491                                                      
REMARK 465     SER B   492                                                      
REMARK 465     SER B   493                                                      
REMARK 465     LEU B   494                                                      
REMARK 465     GLU B   495                                                      
REMARK 465     MET B   496                                                      
REMARK 465     ASP B   497                                                      
REMARK 465     MET B   498                                                      
REMARK 465     GLU B   499                                                      
REMARK 465     GLY B   500                                                      
REMARK 465     LEU B   501                                                      
REMARK 465     GLU B   502                                                      
REMARK 465     ASP B   503                                                      
REMARK 465     TYR B   504                                                      
REMARK 465     PHE B   505                                                      
REMARK 465     SER B   506                                                      
REMARK 465     GLU B   507                                                      
REMARK 465     ASP B   508                                                      
REMARK 465     SER B   509                                                      
REMARK 465     ALA C   335                                                      
REMARK 465     ASP C   336                                                      
REMARK 465     GLU C   337                                                      
REMARK 465     LEU C   673                                                      
REMARK 465     GLY C   674                                                      
REMARK 465     GLY C   675                                                      
REMARK 465     ARG C   676                                                      
REMARK 465     SER C   677                                                      
REMARK 465     GLY C   678                                                      
REMARK 465     PHE C   679                                                      
REMARK 465     PHE C   809                                                      
REMARK 465     ARG C   810                                                      
REMARK 465     LYS C   811                                                      
REMARK 465     PRO C   812                                                      
REMARK 465     GLN C   813                                                      
REMARK 465     GLN C   814                                                      
REMARK 465     LYS C   815                                                      
REMARK 465     LEU C   816                                                      
REMARK 465     GLY C   817                                                      
REMARK 465     ASP C   818                                                      
REMARK 465     GLU C   819                                                      
REMARK 465     ASP C   820                                                      
REMARK 465     GLU C   821                                                      
REMARK 465     GLU C   822                                                      
REMARK 465     ILE C   823                                                      
REMARK 465     ASP C   824                                                      
REMARK 465     GLY C   825                                                      
REMARK 465     ASP C   826                                                      
REMARK 465     THR C   827                                                      
REMARK 465     ASN C   828                                                      
REMARK 465     LYS C   829                                                      
REMARK 465     TYR C   830                                                      
REMARK 465     LYS C   831                                                      
REMARK 465     LYS C   832                                                      
REMARK 465     GLY C   833                                                      
REMARK 465     ARG C   834                                                      
REMARK 465     LYS C   835                                                      
REMARK 465     LYS C   836                                                      
REMARK 465     ALA C   837                                                      
REMARK 465     ALA C   838                                                      
REMARK 465     TYR C   839                                                      
REMARK 465     ALA C   840                                                      
REMARK 465     GLY C   841                                                      
REMARK 465     ALA C   883                                                      
REMARK 465     SER C   884                                                      
REMARK 465     GLU C   885                                                      
REMARK 465     ALA C   886                                                      
REMARK 465     GLN C   887                                                      
REMARK 465     LYS C   888                                                      
REMARK 465     VAL C   889                                                      
REMARK 465     THR C   890                                                      
REMARK 465     GLU C   891                                                      
REMARK 465     ASP C   892                                                      
REMARK 465     GLY C   893                                                      
REMARK 465     GLU C   894                                                      
REMARK 465     GLN C   895                                                      
REMARK 465     GLU C   896                                                      
REMARK 465     GLN C   897                                                      
REMARK 465     ALA C  1259                                                      
REMARK 465     LEU C  1260                                                      
REMARK 465     LEU C  1261                                                      
REMARK 465     GLY C  1262                                                      
REMARK 465     GLY C  1263                                                      
REMARK 465     PRO C  1264                                                      
REMARK 465     ALA C  1265                                                      
REMARK 465     GLY C  1457                                                      
REMARK 465     CYS C  1458                                                      
REMARK 465     ALA C  1459                                                      
REMARK 465     VAL C  1460                                                      
REMARK 465     LYS C  1461                                                      
REMARK 465     SER C  1462                                                      
REMARK 465     SER D     2                                                      
REMARK 465     ALA D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     ALA D     5                                                      
REMARK 465     GLN D     6                                                      
REMARK 465     GLN D     7                                                      
REMARK 465     LEU D     8                                                      
REMARK 465     ALA D     9                                                      
REMARK 465     GLU D    10                                                      
REMARK 465     GLU D    11                                                      
REMARK 465     LEU D    12                                                      
REMARK 465     GLN D    13                                                      
REMARK 465     ILE D    14                                                      
REMARK 465     PHE D    15                                                      
REMARK 465     GLY D    16                                                      
REMARK 465     LEU D    17                                                      
REMARK 465     ASP D    18                                                      
REMARK 465     CYS D    19                                                      
REMARK 465     GLU D    20                                                      
REMARK 465     GLU D    21                                                      
REMARK 465     ALA D    22                                                      
REMARK 465     LEU D    23                                                      
REMARK 465     ILE D    24                                                      
REMARK 465     GLU D    25                                                      
REMARK 465     LYS D    26                                                      
REMARK 465     LEU D    27                                                      
REMARK 465     VAL D    28                                                      
REMARK 465     GLU D    29                                                      
REMARK 465     LEU D    30                                                      
REMARK 465     CYS D    31                                                      
REMARK 465     VAL D    32                                                      
REMARK 465     GLN D    33                                                      
REMARK 465     TYR D    34                                                      
REMARK 465     GLY D    35                                                      
REMARK 465     GLN D    36                                                      
REMARK 465     ASN D    37                                                      
REMARK 465     GLU D    38                                                      
REMARK 465     GLU D    39                                                      
REMARK 465     GLY D    40                                                      
REMARK 465     MET D    41                                                      
REMARK 465     VAL D    42                                                      
REMARK 465     GLY D    43                                                      
REMARK 465     GLU D    44                                                      
REMARK 465     LEU D    45                                                      
REMARK 465     ILE D    46                                                      
REMARK 465     ALA D    47                                                      
REMARK 465     PHE D    48                                                      
REMARK 465     CYS D    49                                                      
REMARK 465     THR D    50                                                      
REMARK 465     SER D    51                                                      
REMARK 465     THR D    52                                                      
REMARK 465     HIS D    53                                                      
REMARK 465     LYS D    54                                                      
REMARK 465     VAL D    55                                                      
REMARK 465     GLY D    56                                                      
REMARK 465     LEU D    57                                                      
REMARK 465     THR D    58                                                      
REMARK 465     SER D    59                                                      
REMARK 465     GLU D    60                                                      
REMARK 465     ILE D    61                                                      
REMARK 465     LEU D    62                                                      
REMARK 465     ASN D    63                                                      
REMARK 465     SER D    64                                                      
REMARK 465     PHE D    65                                                      
REMARK 465     GLU D    66                                                      
REMARK 465     HIS D    67                                                      
REMARK 465     GLU D    68                                                      
REMARK 465     PHE D    69                                                      
REMARK 465     LEU D    70                                                      
REMARK 465     SER D    71                                                      
REMARK 465     LYS D    72                                                      
REMARK 465     ARG D    73                                                      
REMARK 465     LEU D    74                                                      
REMARK 465     SER D    75                                                      
REMARK 465     LYS D    76                                                      
REMARK 465     ALA D    77                                                      
REMARK 465     ARG D    78                                                      
REMARK 465     HIS D    79                                                      
REMARK 465     SER D    80                                                      
REMARK 465     THR D    81                                                      
REMARK 465     CYS D    82                                                      
REMARK 465     LYS D    83                                                      
REMARK 465     ASP D    84                                                      
REMARK 465     SER D    85                                                      
REMARK 465     GLY D    86                                                      
REMARK 465     HIS D    87                                                      
REMARK 465     ALA D    88                                                      
REMARK 465     GLY D    89                                                      
REMARK 465     ALA D    90                                                      
REMARK 465     ARG D    91                                                      
REMARK 465     ASP D    92                                                      
REMARK 465     ILE D    93                                                      
REMARK 465     VAL D    94                                                      
REMARK 465     SER D    95                                                      
REMARK 465     ILE D    96                                                      
REMARK 465     GLN D    97                                                      
REMARK 465     GLU D    98                                                      
REMARK 465     LEU D    99                                                      
REMARK 465     ILE D   100                                                      
REMARK 465     GLU D   101                                                      
REMARK 465     VAL D   102                                                      
REMARK 465     GLU D   103                                                      
REMARK 465     GLU D   104                                                      
REMARK 465     GLU D   105                                                      
REMARK 465     GLU D   106                                                      
REMARK 465     GLU D   107                                                      
REMARK 465     ILE D   108                                                      
REMARK 465     LEU D   109                                                      
REMARK 465     LEU D   110                                                      
REMARK 465     ASN D   111                                                      
REMARK 465     SER D   112                                                      
REMARK 465     TYR D   113                                                      
REMARK 465     THR D   114                                                      
REMARK 465     THR D   115                                                      
REMARK 465     PRO D   116                                                      
REMARK 465     SER D   117                                                      
REMARK 465     LYS D   118                                                      
REMARK 465     GLY D   119                                                      
REMARK 465     SER D   120                                                      
REMARK 465     GLN D   121                                                      
REMARK 465     LYS D   122                                                      
REMARK 465     ARG D   123                                                      
REMARK 465     ALA D   124                                                      
REMARK 465     ILE D   125                                                      
REMARK 465     SER D   126                                                      
REMARK 465     THR D   127                                                      
REMARK 465     PRO D   128                                                      
REMARK 465     GLU D   129                                                      
REMARK 465     THR D   130                                                      
REMARK 465     PRO D   131                                                      
REMARK 465     LEU D   132                                                      
REMARK 465     THR D   133                                                      
REMARK 465     LYS D   134                                                      
REMARK 465     ARG D   135                                                      
REMARK 465     SER D   136                                                      
REMARK 465     VAL D   137                                                      
REMARK 465     SER D   138                                                      
REMARK 465     THR D   139                                                      
REMARK 465     ARG D   140                                                      
REMARK 465     SER D   141                                                      
REMARK 465     PRO D   142                                                      
REMARK 465     HIS D   143                                                      
REMARK 465     GLN D   144                                                      
REMARK 465     LEU D   145                                                      
REMARK 465     LEU D   146                                                      
REMARK 465     SER D   147                                                      
REMARK 465     PRO D   148                                                      
REMARK 465     SER D   149                                                      
REMARK 465     SER D   150                                                      
REMARK 465     PHE D   151                                                      
REMARK 465     SER D   152                                                      
REMARK 465     PRO D   153                                                      
REMARK 465     SER D   154                                                      
REMARK 465     LYS E   284                                                      
REMARK 465     ASN E   285                                                      
REMARK 465     ASP E   286                                                      
REMARK 465     LYS E   287                                                      
REMARK 465     TYR E   288                                                      
REMARK 465     SER E   361                                                      
REMARK 465     THR E   362                                                      
REMARK 465     ASN E   363                                                      
REMARK 465     GLU E   364                                                      
REMARK 465     GLU E   365                                                      
REMARK 465     GLU E   366                                                      
REMARK 465     LYS E   367                                                      
REMARK 465     GLU E   368                                                      
REMARK 465     GLU E   369                                                      
REMARK 465     ASN E   370                                                      
REMARK 465     GLU E   371                                                      
REMARK 465     ALA E   372                                                      
REMARK 465     GLU E   373                                                      
REMARK 465     SER E   374                                                      
REMARK 465     ASP E   375                                                      
REMARK 465     VAL E   376                                                      
REMARK 465     LYS E   377                                                      
REMARK 465     HIS E   378                                                      
REMARK 465     LYS E   413                                                      
REMARK 465     SER E   414                                                      
REMARK 465     ASP E   415                                                      
REMARK 465     LEU E   416                                                      
REMARK 465     GLN E   417                                                      
REMARK 465     LYS E   418                                                      
REMARK 465     ASP E   419                                                      
REMARK 465     PHE E   420                                                      
REMARK 465     MET F     1                                                      
REMARK 465     GLU F     2                                                      
REMARK 465     PHE F     3                                                      
REMARK 465     SER F     4                                                      
REMARK 465     GLY F     5                                                      
REMARK 465     ARG F     6                                                      
REMARK 465     LYS F     7                                                      
REMARK 465     TRP F     8                                                      
REMARK 465     ARG F     9                                                      
REMARK 465     LYS F    10                                                      
REMARK 465     LEU F    11                                                      
REMARK 465     ARG F    12                                                      
REMARK 465     LEU F    13                                                      
REMARK 465     ALA F    14                                                      
REMARK 465     GLY F    15                                                      
REMARK 465     ASP F    16                                                      
REMARK 465     GLN F    17                                                      
REMARK 465     ARG F    18                                                      
REMARK 465     ASN F    19                                                      
REMARK 465     ALA F    20                                                      
REMARK 465     SER F    21                                                      
REMARK 465     ASN F   456                                                      
REMARK 465     GLY F   457                                                      
REMARK 465     GLY F   458                                                      
REMARK 465     LYS F   459                                                      
REMARK 465     ASP F   460                                                      
REMARK 465     ILE F   461                                                      
REMARK 465     LYS F   462                                                      
REMARK 465     LYS F   463                                                      
REMARK 465     GLU F   464                                                      
REMARK 465     PRO F   465                                                      
REMARK 465     ILE F   466                                                      
REMARK 465     GLN F   467                                                      
REMARK 465     PRO F   468                                                      
REMARK 465     GLU F   469                                                      
REMARK 465     THR F   470                                                      
REMARK 465     PRO F   471                                                      
REMARK 465     GLN F   472                                                      
REMARK 465     PRO F   473                                                      
REMARK 465     LYS F   474                                                      
REMARK 465     PRO F   475                                                      
REMARK 465     SER F   476                                                      
REMARK 465     VAL F   477                                                      
REMARK 465     GLN F   478                                                      
REMARK 465     LYS F   479                                                      
REMARK 465     THR F   480                                                      
REMARK 465     LYS F   481                                                      
REMARK 465     ASP F   482                                                      
REMARK 465     ALA F   483                                                      
REMARK 465     SER F   484                                                      
REMARK 465     SER F   485                                                      
REMARK 465     ALA F   486                                                      
REMARK 465     LEU F   487                                                      
REMARK 465     ALA F   488                                                      
REMARK 465     SER F   489                                                      
REMARK 465     LEU F   490                                                      
REMARK 465     ASN F   491                                                      
REMARK 465     SER F   492                                                      
REMARK 465     SER F   493                                                      
REMARK 465     LEU F   494                                                      
REMARK 465     GLU F   495                                                      
REMARK 465     MET F   496                                                      
REMARK 465     ASP F   497                                                      
REMARK 465     MET F   498                                                      
REMARK 465     GLU F   499                                                      
REMARK 465     GLY F   500                                                      
REMARK 465     LEU F   501                                                      
REMARK 465     GLU F   502                                                      
REMARK 465     ASP F   503                                                      
REMARK 465     TYR F   504                                                      
REMARK 465     PHE F   505                                                      
REMARK 465     SER F   506                                                      
REMARK 465     GLU F   507                                                      
REMARK 465     ASP F   508                                                      
REMARK 465     SER F   509                                                      
REMARK 465     ALA G   335                                                      
REMARK 465     ASP G   336                                                      
REMARK 465     GLU G   337                                                      
REMARK 465     LEU G   673                                                      
REMARK 465     GLY G   674                                                      
REMARK 465     GLY G   675                                                      
REMARK 465     ARG G   676                                                      
REMARK 465     SER G   677                                                      
REMARK 465     GLY G   678                                                      
REMARK 465     PHE G   679                                                      
REMARK 465     PHE G   809                                                      
REMARK 465     ARG G   810                                                      
REMARK 465     LYS G   811                                                      
REMARK 465     PRO G   812                                                      
REMARK 465     GLN G   813                                                      
REMARK 465     GLN G   814                                                      
REMARK 465     LYS G   815                                                      
REMARK 465     LEU G   816                                                      
REMARK 465     GLY G   817                                                      
REMARK 465     ASP G   818                                                      
REMARK 465     GLU G   819                                                      
REMARK 465     ASP G   820                                                      
REMARK 465     GLU G   821                                                      
REMARK 465     GLU G   822                                                      
REMARK 465     ILE G   823                                                      
REMARK 465     ASP G   824                                                      
REMARK 465     GLY G   825                                                      
REMARK 465     ASP G   826                                                      
REMARK 465     THR G   827                                                      
REMARK 465     ASN G   828                                                      
REMARK 465     LYS G   829                                                      
REMARK 465     TYR G   830                                                      
REMARK 465     LYS G   831                                                      
REMARK 465     LYS G   832                                                      
REMARK 465     GLY G   833                                                      
REMARK 465     ARG G   834                                                      
REMARK 465     LYS G   835                                                      
REMARK 465     LYS G   836                                                      
REMARK 465     ALA G   837                                                      
REMARK 465     ALA G   838                                                      
REMARK 465     TYR G   839                                                      
REMARK 465     ALA G   840                                                      
REMARK 465     GLY G   841                                                      
REMARK 465     ALA G   883                                                      
REMARK 465     SER G   884                                                      
REMARK 465     GLU G   885                                                      
REMARK 465     ALA G   886                                                      
REMARK 465     GLN G   887                                                      
REMARK 465     LYS G   888                                                      
REMARK 465     VAL G   889                                                      
REMARK 465     THR G   890                                                      
REMARK 465     GLU G   891                                                      
REMARK 465     ASP G   892                                                      
REMARK 465     GLY G   893                                                      
REMARK 465     GLU G   894                                                      
REMARK 465     GLN G   895                                                      
REMARK 465     GLU G   896                                                      
REMARK 465     GLN G   897                                                      
REMARK 465     ALA G  1259                                                      
REMARK 465     LEU G  1260                                                      
REMARK 465     LEU G  1261                                                      
REMARK 465     GLY G  1262                                                      
REMARK 465     GLY G  1263                                                      
REMARK 465     PRO G  1264                                                      
REMARK 465     ALA G  1265                                                      
REMARK 465     GLY G  1457                                                      
REMARK 465     CYS G  1458                                                      
REMARK 465     ALA G  1459                                                      
REMARK 465     VAL G  1460                                                      
REMARK 465     LYS G  1461                                                      
REMARK 465     SER G  1462                                                      
REMARK 465     SER H     2                                                      
REMARK 465     ALA H     3                                                      
REMARK 465     SER H     4                                                      
REMARK 465     ALA H     5                                                      
REMARK 465     GLN H     6                                                      
REMARK 465     GLN H     7                                                      
REMARK 465     LEU H     8                                                      
REMARK 465     ALA H     9                                                      
REMARK 465     GLU H    10                                                      
REMARK 465     GLU H    11                                                      
REMARK 465     LEU H    12                                                      
REMARK 465     GLN H    13                                                      
REMARK 465     ILE H    14                                                      
REMARK 465     PHE H    15                                                      
REMARK 465     GLY H    16                                                      
REMARK 465     LEU H    17                                                      
REMARK 465     ASP H    18                                                      
REMARK 465     CYS H    19                                                      
REMARK 465     GLU H    20                                                      
REMARK 465     GLU H    21                                                      
REMARK 465     ALA H    22                                                      
REMARK 465     LEU H    23                                                      
REMARK 465     ILE H    24                                                      
REMARK 465     GLU H    25                                                      
REMARK 465     LYS H    26                                                      
REMARK 465     LEU H    27                                                      
REMARK 465     VAL H    28                                                      
REMARK 465     GLU H    29                                                      
REMARK 465     LEU H    30                                                      
REMARK 465     CYS H    31                                                      
REMARK 465     VAL H    32                                                      
REMARK 465     GLN H    33                                                      
REMARK 465     TYR H    34                                                      
REMARK 465     GLY H    35                                                      
REMARK 465     GLN H    36                                                      
REMARK 465     ASN H    37                                                      
REMARK 465     GLU H    38                                                      
REMARK 465     GLU H    39                                                      
REMARK 465     GLY H    40                                                      
REMARK 465     MET H    41                                                      
REMARK 465     VAL H    42                                                      
REMARK 465     GLY H    43                                                      
REMARK 465     GLU H    44                                                      
REMARK 465     LEU H    45                                                      
REMARK 465     ILE H    46                                                      
REMARK 465     ALA H    47                                                      
REMARK 465     PHE H    48                                                      
REMARK 465     CYS H    49                                                      
REMARK 465     THR H    50                                                      
REMARK 465     SER H    51                                                      
REMARK 465     THR H    52                                                      
REMARK 465     HIS H    53                                                      
REMARK 465     LYS H    54                                                      
REMARK 465     VAL H    55                                                      
REMARK 465     GLY H    56                                                      
REMARK 465     LEU H    57                                                      
REMARK 465     THR H    58                                                      
REMARK 465     SER H    59                                                      
REMARK 465     GLU H    60                                                      
REMARK 465     ILE H    61                                                      
REMARK 465     LEU H    62                                                      
REMARK 465     ASN H    63                                                      
REMARK 465     SER H    64                                                      
REMARK 465     PHE H    65                                                      
REMARK 465     GLU H    66                                                      
REMARK 465     HIS H    67                                                      
REMARK 465     GLU H    68                                                      
REMARK 465     PHE H    69                                                      
REMARK 465     LEU H    70                                                      
REMARK 465     SER H    71                                                      
REMARK 465     LYS H    72                                                      
REMARK 465     ARG H    73                                                      
REMARK 465     LEU H    74                                                      
REMARK 465     SER H    75                                                      
REMARK 465     LYS H    76                                                      
REMARK 465     ALA H    77                                                      
REMARK 465     ARG H    78                                                      
REMARK 465     HIS H    79                                                      
REMARK 465     SER H    80                                                      
REMARK 465     THR H    81                                                      
REMARK 465     CYS H    82                                                      
REMARK 465     LYS H    83                                                      
REMARK 465     ASP H    84                                                      
REMARK 465     SER H    85                                                      
REMARK 465     GLY H    86                                                      
REMARK 465     HIS H    87                                                      
REMARK 465     ALA H    88                                                      
REMARK 465     GLY H    89                                                      
REMARK 465     ALA H    90                                                      
REMARK 465     ARG H    91                                                      
REMARK 465     ASP H    92                                                      
REMARK 465     ILE H    93                                                      
REMARK 465     VAL H    94                                                      
REMARK 465     SER H    95                                                      
REMARK 465     ILE H    96                                                      
REMARK 465     GLN H    97                                                      
REMARK 465     GLU H    98                                                      
REMARK 465     LEU H    99                                                      
REMARK 465     ILE H   100                                                      
REMARK 465     GLU H   101                                                      
REMARK 465     VAL H   102                                                      
REMARK 465     GLU H   103                                                      
REMARK 465     GLU H   104                                                      
REMARK 465     GLU H   105                                                      
REMARK 465     GLU H   106                                                      
REMARK 465     GLU H   107                                                      
REMARK 465     ILE H   108                                                      
REMARK 465     LEU H   109                                                      
REMARK 465     LEU H   110                                                      
REMARK 465     ASN H   111                                                      
REMARK 465     SER H   112                                                      
REMARK 465     TYR H   113                                                      
REMARK 465     THR H   114                                                      
REMARK 465     THR H   115                                                      
REMARK 465     PRO H   116                                                      
REMARK 465     SER H   117                                                      
REMARK 465     LYS H   118                                                      
REMARK 465     GLY H   119                                                      
REMARK 465     SER H   120                                                      
REMARK 465     GLN H   121                                                      
REMARK 465     LYS H   122                                                      
REMARK 465     ARG H   123                                                      
REMARK 465     ALA H   124                                                      
REMARK 465     ILE H   125                                                      
REMARK 465     SER H   126                                                      
REMARK 465     THR H   127                                                      
REMARK 465     PRO H   128                                                      
REMARK 465     GLU H   129                                                      
REMARK 465     THR H   130                                                      
REMARK 465     PRO H   131                                                      
REMARK 465     LEU H   132                                                      
REMARK 465     THR H   133                                                      
REMARK 465     LYS H   134                                                      
REMARK 465     ARG H   135                                                      
REMARK 465     SER H   136                                                      
REMARK 465     VAL H   137                                                      
REMARK 465     SER H   138                                                      
REMARK 465     THR H   139                                                      
REMARK 465     ARG H   140                                                      
REMARK 465     SER H   141                                                      
REMARK 465     PRO H   142                                                      
REMARK 465     HIS H   143                                                      
REMARK 465     GLN H   144                                                      
REMARK 465     LEU H   145                                                      
REMARK 465     LEU H   146                                                      
REMARK 465     SER H   147                                                      
REMARK 465     PRO H   148                                                      
REMARK 465     SER H   149                                                      
REMARK 465     SER H   150                                                      
REMARK 465     PHE H   151                                                      
REMARK 465     SER H   152                                                      
REMARK 465     PRO H   153                                                      
REMARK 465     SER H   154                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG1  THR B   258     N    ASP B   261              2.04            
REMARK 500   O    SER C   587     OH   TYR C   732              2.12            
REMARK 500   OH   TYR B    29     OD2  ASP B    99              2.13            
REMARK 500   OG1  THR D   356     OD2  ASP D   358              2.15            
REMARK 500   O    GLU D   411     N    THR D   413              2.16            
REMARK 500   O    PRO G   631     NH1  ARG G   688              2.16            
REMARK 500   O    LEU H   176     NE2  GLN H   178              2.16            
REMARK 500   O    GLU H   411     N    THR H   413              2.18            
REMARK 500   OG   SER G   375     OD2  ASP G   630              2.18            
REMARK 500   O    PHE B   143     OG   SER B   147              2.18            
REMARK 500   OG1  THR H   351     OD2  ASP H   353              2.19            
REMARK 500   O    SER G  1444     N    TYR G  1446              2.19            
REMARK 500   ND2  ASN C   774     OG1  THR C   779              2.19            
REMARK 500   O    SER C  1444     N    TYR C  1446              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A   6   C   -  N   -  CA  ANGL. DEV. =  11.0 DEGREES          
REMARK 500    PRO B  32   C   -  N   -  CA  ANGL. DEV. =  12.6 DEGREES          
REMARK 500    LEU B 368   CA  -  CB  -  CG  ANGL. DEV. = -16.4 DEGREES          
REMARK 500    HIS C 553   N   -  CA  -  C   ANGL. DEV. =  16.6 DEGREES          
REMARK 500    PRO C 578   C   -  N   -  CA  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    LEU C 742   CA  -  CB  -  CG  ANGL. DEV. = -14.5 DEGREES          
REMARK 500    PRO C1143   C   -  N   -  CA  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    CYS C1348   CA  -  CB  -  SG  ANGL. DEV. =   7.9 DEGREES          
REMARK 500    SER C1447   N   -  CA  -  C   ANGL. DEV. = -16.2 DEGREES          
REMARK 500    LEU D 202   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    PRO D 514   C   -  N   -  CA  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    PRO D 514   C   -  N   -  CD  ANGL. DEV. = -16.6 DEGREES          
REMARK 500    PRO E   6   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    PRO F  32   C   -  N   -  CA  ANGL. DEV. =  12.3 DEGREES          
REMARK 500    LEU F 368   CA  -  CB  -  CG  ANGL. DEV. = -17.8 DEGREES          
REMARK 500    HIS G 553   N   -  CA  -  C   ANGL. DEV. =  16.8 DEGREES          
REMARK 500    PRO G 578   C   -  N   -  CA  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    PRO G 724   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    PRO G1143   C   -  N   -  CA  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    PRO G1143   C   -  N   -  CD  ANGL. DEV. = -15.4 DEGREES          
REMARK 500    PRO G1351   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    LEU G1405   CA  -  CB  -  CG  ANGL. DEV. = -14.1 DEGREES          
REMARK 500    LEU H 202   CA  -  CB  -  CG  ANGL. DEV. =  14.9 DEGREES          
REMARK 500    CYS H 346   CA  -  CB  -  SG  ANGL. DEV. =   7.2 DEGREES          
REMARK 500    PRO H 514   C   -  N   -  CA  ANGL. DEV. =  16.2 DEGREES          
REMARK 500    PRO H 514   C   -  N   -  CD  ANGL. DEV. = -14.7 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 A   6        8.29    -66.51                                   
REMARK 500    ARG A  28      -35.95    -36.80                                   
REMARK 500    LYS A  37      -91.24    -17.84                                   
REMARK 500    LEU A  49     -143.16    -91.08                                   
REMARK 500    ASP A  51       -6.73     76.01                                   
REMARK 500    ASP A  52       15.42     93.63                                   
REMARK 500    ARG A  56      -71.61   -133.78                                   
REMARK 500    TYR A  57       57.99    -65.84                                   
REMARK 500    ASN A  74       62.23     26.36                                   
REMARK 500    ASN A  89        1.78    -66.00                                   
REMARK 500    GLU A 105      170.71    -58.87                                   
REMARK 500    ALA A 145      -71.82    -53.39                                   
REMARK 500    LEU A 146      -36.50    -31.23                                   
REMARK 500    ARG A 162      -40.79   -153.03                                   
REMARK 500    ARG A 163       42.84   -150.02                                   
REMARK 500    GLN A 196       69.78    -67.24                                   
REMARK 500    ASP A 197       65.99     65.17                                   
REMARK 500    HIS A 209      157.13    -47.75                                   
REMARK 500    PHE A 223      -78.31    -25.51                                   
REMARK 500    TYR A 226      -62.01    -93.08                                   
REMARK 500    ALA A 245       -3.56    -58.92                                   
REMARK 500    GLU A 249      -38.21    -30.74                                   
REMARK 500    HIS A 252      -76.41    -38.93                                   
REMARK 500    ASP A 253      -47.02    -28.82                                   
REMARK 500    LYS A 274      -74.94    -87.11                                   
REMARK 500    GLN A 299       -4.25    -51.70                                   
REMARK 500    PRO A 303      150.12    -47.30                                   
REMARK 500    LEU A 336       -6.49    -57.46                                   
REMARK 500    ALA A 359       33.99    -92.85                                   
REMARK 500    ARG A 381       34.74   -149.32                                   
REMARK 500    LEU A 410      -71.98    -83.76                                   
REMARK 500    LEU A 411        4.24    -52.66                                   
REMARK 500    PRO B  23     -128.24    -90.51                                   
REMARK 500    HIS B  24       38.38    -73.57                                   
REMARK 500    TYR B  29       78.92    -56.44                                   
REMARK 500    GLN B  31      106.12     61.95                                   
REMARK 500    GLU B  35     -141.64    -58.84                                   
REMARK 500    ASN B  36      149.23    179.10                                   
REMARK 500    LEU B  39       -7.39    -56.26                                   
REMARK 500    TYR B  63     -151.62   -128.83                                   
REMARK 500    TYR B  70      -70.20    -60.73                                   
REMARK 500    SER B  72      -79.68    -54.30                                   
REMARK 500    LEU B  78      -38.02    -38.13                                   
REMARK 500    ARG B  79      -74.31    -70.57                                   
REMARK 500    LYS B  82       64.26     63.99                                   
REMARK 500    SER B  84      100.57    173.13                                   
REMARK 500    TYR B  85     -117.82   -166.12                                   
REMARK 500    ASN B  88      171.82    176.44                                   
REMARK 500    LEU B  89      100.96    -57.00                                   
REMARK 500    GLU B  90      -57.53     35.63                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     661 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR B 110         0.08    SIDE CHAIN                              
REMARK 500    TYR B 309         0.06    SIDE CHAIN                              
REMARK 500    TYR C 740         0.08    SIDE CHAIN                              
REMARK 500    TYR D 349         0.07    SIDE CHAIN                              
REMARK 500    TYR F 110         0.11    SIDE CHAIN                              
REMARK 500    TYR G 452         0.07    SIDE CHAIN                              
REMARK 500    TYR H 442         0.07    SIDE CHAIN                              
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                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 121   SG                                                     
REMARK 620 2 CYS A 122   SG  116.0                                              
REMARK 620 3 CYS A 128   SG  130.5  88.9                                        
REMARK 620 4 CYS A 131   SG   85.8  90.6 138.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 601  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 287   SG                                                     
REMARK 620 2 SF4 B 601   S1   85.3                                              
REMARK 620 3 SF4 B 601   S2  168.5  83.3                                        
REMARK 620 4 SF4 B 601   S3   95.7  89.8  85.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 601  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 367   SG                                                     
REMARK 620 2 SF4 B 601   S2  105.7                                              
REMARK 620 3 SF4 B 601   S3   98.5  83.8                                        
REMARK 620 4 SF4 B 601   S4  157.0  91.6  98.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C1283   SG                                                     
REMARK 620 2 CYS C1286   SG  115.0                                              
REMARK 620 3 CYS C1310   SG   96.9 108.7                                        
REMARK 620 4 CYS C1315   SG  114.1  99.8 123.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C1348   SG                                                     
REMARK 620 2 CYS C1353   SG   79.2                                              
REMARK 620 3 CYS C1371   SG  130.4 103.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E 121   SG                                                     
REMARK 620 2 CYS E 122   SG   92.0                                              
REMARK 620 3 CYS E 128   SG  126.9 126.1                                        
REMARK 620 4 CYS E 131   SG  106.7  75.0 117.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 F 601  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 287   SG                                                     
REMARK 620 2 SF4 F 601   S1   82.6                                              
REMARK 620 3 SF4 F 601   S2  162.3  81.5                                        
REMARK 620 4 SF4 F 601   S3   87.5  89.9  84.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 F 601  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 367   SG                                                     
REMARK 620 2 SF4 F 601   S2   75.0                                              
REMARK 620 3 SF4 F 601   S3  107.9  82.7                                        
REMARK 620 4 SF4 F 601   S4  147.8  91.4  98.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G1501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G1286   SG                                                     
REMARK 620 2 CYS G1310   SG  127.5                                              
REMARK 620 3 CYS G1315   SG  120.9 110.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G1502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G1348   SG                                                     
REMARK 620 2 CYS G1353   SG   84.1                                              
REMARK 620 3 CYS G1371   SG  133.6 101.3                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN E 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 F 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 1501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 1502                 
DBREF  5EXR A    1   420  UNP    P49642   PRI1_HUMAN       1    420             
DBREF  5EXR B    1   509  UNP    P49643   PRI2_HUMAN       1    509             
DBREF  5EXR C  335  1462  UNP    P09884   DPOLA_HUMAN    335   1462             
DBREF  5EXR D    2   598  UNP    Q14181   DPOA2_HUMAN      2    598             
DBREF  5EXR E    1   420  UNP    P49642   PRI1_HUMAN       1    420             
DBREF  5EXR F    1   509  UNP    P49643   PRI2_HUMAN       1    509             
DBREF  5EXR G  335  1462  UNP    P09884   DPOLA_HUMAN    335   1462             
DBREF  5EXR H    2   598  UNP    Q14181   DPOA2_HUMAN      2    598             
SEQADV 5EXR ALA C  516  UNP  P09884    VAL   516 ENGINEERED MUTATION            
SEQADV 5EXR ALA G  516  UNP  P09884    VAL   516 ENGINEERED MUTATION            
SEQRES   1 A  420  MET GLU THR PHE ASP PRO THR GLU LEU PRO GLU LEU LEU          
SEQRES   2 A  420  LYS LEU TYR TYR ARG ARG LEU PHE PRO TYR SER GLN TYR          
SEQRES   3 A  420  TYR ARG TRP LEU ASN TYR GLY GLY VAL ILE LYS ASN TYR          
SEQRES   4 A  420  PHE GLN HIS ARG GLU PHE SER PHE THR LEU LYS ASP ASP          
SEQRES   5 A  420  ILE TYR ILE ARG TYR GLN SER PHE ASN ASN GLN SER ASP          
SEQRES   6 A  420  LEU GLU LYS GLU MET GLN LYS MET ASN PRO TYR LYS ILE          
SEQRES   7 A  420  ASP ILE GLY ALA VAL TYR SER HIS ARG PRO ASN GLN HIS          
SEQRES   8 A  420  ASN THR VAL LYS LEU GLY ALA PHE GLN ALA GLN GLU LYS          
SEQRES   9 A  420  GLU LEU VAL PHE ASP ILE ASP MET THR ASP TYR ASP ASP          
SEQRES  10 A  420  VAL ARG ARG CYS CYS SER SER ALA ASP ILE CYS PRO LYS          
SEQRES  11 A  420  CYS TRP THR LEU MET THR MET ALA ILE ARG ILE ILE ASP          
SEQRES  12 A  420  ARG ALA LEU LYS GLU ASP PHE GLY PHE LYS HIS ARG LEU          
SEQRES  13 A  420  TRP VAL TYR SER GLY ARG ARG GLY VAL HIS CYS TRP VAL          
SEQRES  14 A  420  CYS ASP GLU SER VAL ARG LYS LEU SER SER ALA VAL ARG          
SEQRES  15 A  420  SER GLY ILE VAL GLU TYR LEU SER LEU VAL LYS GLY GLY          
SEQRES  16 A  420  GLN ASP VAL LYS LYS LYS VAL HIS LEU SER GLU LYS ILE          
SEQRES  17 A  420  HIS PRO PHE ILE ARG LYS SER ILE ASN ILE ILE LYS LYS          
SEQRES  18 A  420  TYR PHE GLU GLU TYR ALA LEU VAL ASN GLN ASP ILE LEU          
SEQRES  19 A  420  GLU ASN LYS GLU SER TRP ASP LYS ILE LEU ALA LEU VAL          
SEQRES  20 A  420  PRO GLU THR ILE HIS ASP GLU LEU GLN GLN SER PHE GLN          
SEQRES  21 A  420  LYS SER HIS ASN SER LEU GLN ARG TRP GLU HIS LEU LYS          
SEQRES  22 A  420  LYS VAL ALA SER ARG TYR GLN ASN ASN ILE LYS ASN ASP          
SEQRES  23 A  420  LYS TYR GLY PRO TRP LEU GLU TRP GLU ILE MET LEU GLN          
SEQRES  24 A  420  TYR CYS PHE PRO ARG LEU ASP ILE ASN VAL SER LYS GLY          
SEQRES  25 A  420  ILE ASN HIS LEU LEU LYS SER PRO PHE SER VAL HIS PRO          
SEQRES  26 A  420  LYS THR GLY ARG ILE SER VAL PRO ILE ASP LEU GLN LYS          
SEQRES  27 A  420  VAL ASP GLN PHE ASP PRO PHE THR VAL PRO THR ILE SER          
SEQRES  28 A  420  PHE ILE CYS ARG GLU LEU ASP ALA ILE SER THR ASN GLU          
SEQRES  29 A  420  GLU GLU LYS GLU GLU ASN GLU ALA GLU SER ASP VAL LYS          
SEQRES  30 A  420  HIS ARG THR ARG ASP TYR LYS LYS THR SER LEU ALA PRO          
SEQRES  31 A  420  TYR VAL LYS VAL PHE GLU HIS PHE LEU GLU ASN LEU ASP          
SEQRES  32 A  420  LYS SER ARG LYS GLY GLU LEU LEU LYS LYS SER ASP LEU          
SEQRES  33 A  420  GLN LYS ASP PHE                                              
SEQRES   1 B  509  MET GLU PHE SER GLY ARG LYS TRP ARG LYS LEU ARG LEU          
SEQRES   2 B  509  ALA GLY ASP GLN ARG ASN ALA SER TYR PRO HIS CYS LEU          
SEQRES   3 B  509  GLN PHE TYR LEU GLN PRO PRO SER GLU ASN ILE SER LEU          
SEQRES   4 B  509  ILE GLU PHE GLU ASN LEU ALA ILE ASP ARG VAL LYS LEU          
SEQRES   5 B  509  LEU LYS SER VAL GLU ASN LEU GLY VAL SER TYR VAL LYS          
SEQRES   6 B  509  GLY THR GLU GLN TYR GLN SER LYS LEU GLU SER GLU LEU          
SEQRES   7 B  509  ARG LYS LEU LYS PHE SER TYR ARG GLU ASN LEU GLU ASP          
SEQRES   8 B  509  GLU TYR GLU PRO ARG ARG ARG ASP HIS ILE SER HIS PHE          
SEQRES   9 B  509  ILE LEU ARG LEU ALA TYR CYS GLN SER GLU GLU LEU ARG          
SEQRES  10 B  509  ARG TRP PHE ILE GLN GLN GLU MET ASP LEU LEU ARG PHE          
SEQRES  11 B  509  ARG PHE SER ILE LEU PRO LYS ASP LYS ILE GLN ASP PHE          
SEQRES  12 B  509  LEU LYS ASP SER GLN LEU GLN PHE GLU ALA ILE SER ASP          
SEQRES  13 B  509  GLU GLU LYS THR LEU ARG GLU GLN GLU ILE VAL ALA SER          
SEQRES  14 B  509  SER PRO SER LEU SER GLY LEU LYS LEU GLY PHE GLU SER          
SEQRES  15 B  509  ILE TYR LYS ILE PRO PHE ALA ASP ALA LEU ASP LEU PHE          
SEQRES  16 B  509  ARG GLY ARG LYS VAL TYR LEU GLU ASP GLY PHE ALA TYR          
SEQRES  17 B  509  VAL PRO LEU LYS ASP ILE VAL ALA ILE ILE LEU ASN GLU          
SEQRES  18 B  509  PHE ARG ALA LYS LEU SER LYS ALA LEU ALA LEU THR ALA          
SEQRES  19 B  509  ARG SER LEU PRO ALA VAL GLN SER ASP GLU ARG LEU GLN          
SEQRES  20 B  509  PRO LEU LEU ASN HIS LEU SER HIS SER TYR THR GLY GLN          
SEQRES  21 B  509  ASP TYR SER THR GLN GLY ASN VAL GLY LYS ILE SER LEU          
SEQRES  22 B  509  ASP GLN ILE ASP LEU LEU SER THR LYS SER PHE PRO PRO          
SEQRES  23 B  509  CYS MET ARG GLN LEU HIS LYS ALA LEU ARG GLU ASN HIS          
SEQRES  24 B  509  HIS LEU ARG HIS GLY GLY ARG MET GLN TYR GLY LEU PHE          
SEQRES  25 B  509  LEU LYS GLY ILE GLY LEU THR LEU GLU GLN ALA LEU GLN          
SEQRES  26 B  509  PHE TRP LYS GLN GLU PHE ILE LYS GLY LYS MET ASP PRO          
SEQRES  27 B  509  ASP LYS PHE ASP LYS GLY TYR SER TYR ASN ILE ARG HIS          
SEQRES  28 B  509  SER PHE GLY LYS GLU GLY LYS ARG THR ASP TYR THR PRO          
SEQRES  29 B  509  PHE SER CYS LEU LYS ILE ILE LEU SER ASN PRO PRO SER          
SEQRES  30 B  509  GLN GLY ASP TYR HIS GLY CYS PRO PHE ARG HIS SER ASP          
SEQRES  31 B  509  PRO GLU LEU LEU LYS GLN LYS LEU GLN SER TYR LYS ILE          
SEQRES  32 B  509  SER PRO GLY GLY ILE SER GLN ILE LEU ASP LEU VAL LYS          
SEQRES  33 B  509  GLY THR HIS TYR GLN VAL ALA CYS GLN LYS TYR PHE GLU          
SEQRES  34 B  509  MET ILE HIS ASN VAL ASP ASP CYS GLY PHE SER LEU ASN          
SEQRES  35 B  509  HIS PRO ASN GLN PHE PHE CYS GLU SER GLN ARG ILE LEU          
SEQRES  36 B  509  ASN GLY GLY LYS ASP ILE LYS LYS GLU PRO ILE GLN PRO          
SEQRES  37 B  509  GLU THR PRO GLN PRO LYS PRO SER VAL GLN LYS THR LYS          
SEQRES  38 B  509  ASP ALA SER SER ALA LEU ALA SER LEU ASN SER SER LEU          
SEQRES  39 B  509  GLU MET ASP MET GLU GLY LEU GLU ASP TYR PHE SER GLU          
SEQRES  40 B  509  ASP SER                                                      
SEQRES   1 C 1128  ALA ASP GLU GLU GLN VAL PHE HIS PHE TYR TRP LEU ASP          
SEQRES   2 C 1128  ALA TYR GLU ASP GLN TYR ASN GLN PRO GLY VAL VAL PHE          
SEQRES   3 C 1128  LEU PHE GLY LYS VAL TRP ILE GLU SER ALA GLU THR HIS          
SEQRES   4 C 1128  VAL SER CYS CYS VAL MET VAL LYS ASN ILE GLU ARG THR          
SEQRES   5 C 1128  LEU TYR PHE LEU PRO ARG GLU MET LYS ILE ASP LEU ASN          
SEQRES   6 C 1128  THR GLY LYS GLU THR GLY THR PRO ILE SER MET LYS ASP          
SEQRES   7 C 1128  VAL TYR GLU GLU PHE ASP GLU LYS ILE ALA THR LYS TYR          
SEQRES   8 C 1128  LYS ILE MET LYS PHE LYS SER LYS PRO VAL GLU LYS ASN          
SEQRES   9 C 1128  TYR ALA PHE GLU ILE PRO ASP VAL PRO GLU LYS SER GLU          
SEQRES  10 C 1128  TYR LEU GLU VAL LYS TYR SER ALA GLU MET PRO GLN LEU          
SEQRES  11 C 1128  PRO GLN ASP LEU LYS GLY GLU THR PHE SER HIS VAL PHE          
SEQRES  12 C 1128  GLY THR ASN THR SER SER LEU GLU LEU PHE LEU MET ASN          
SEQRES  13 C 1128  ARG LYS ILE LYS GLY PRO CYS TRP LEU GLU VAL LYS SER          
SEQRES  14 C 1128  PRO GLN LEU LEU ASN GLN PRO VAL SER TRP CYS LYS ALA          
SEQRES  15 C 1128  GLU ALA MET ALA LEU LYS PRO ASP LEU VAL ASN VAL ILE          
SEQRES  16 C 1128  LYS ASP VAL SER PRO PRO PRO LEU VAL VAL MET ALA PHE          
SEQRES  17 C 1128  SER MET LYS THR MET GLN ASN ALA LYS ASN HIS GLN ASN          
SEQRES  18 C 1128  GLU ILE ILE ALA MET ALA ALA LEU VAL HIS HIS SER PHE          
SEQRES  19 C 1128  ALA LEU ASP LYS ALA ALA PRO LYS PRO PRO PHE GLN SER          
SEQRES  20 C 1128  HIS PHE CYS VAL VAL SER LYS PRO LYS ASP CYS ILE PHE          
SEQRES  21 C 1128  PRO TYR ALA PHE LYS GLU VAL ILE GLU LYS LYS ASN VAL          
SEQRES  22 C 1128  LYS VAL GLU VAL ALA ALA THR GLU ARG THR LEU LEU GLY          
SEQRES  23 C 1128  PHE PHE LEU ALA LYS VAL HIS LYS ILE ASP PRO ASP ILE          
SEQRES  24 C 1128  ILE VAL GLY HIS ASN ILE TYR GLY PHE GLU LEU GLU VAL          
SEQRES  25 C 1128  LEU LEU GLN ARG ILE ASN VAL CYS LYS ALA PRO HIS TRP          
SEQRES  26 C 1128  SER LYS ILE GLY ARG LEU LYS ARG SER ASN MET PRO LYS          
SEQRES  27 C 1128  LEU GLY GLY ARG SER GLY PHE GLY GLU ARG ASN ALA THR          
SEQRES  28 C 1128  CYS GLY ARG MET ILE CYS ASP VAL GLU ILE SER ALA LYS          
SEQRES  29 C 1128  GLU LEU ILE ARG CYS LYS SER TYR HIS LEU SER GLU LEU          
SEQRES  30 C 1128  VAL GLN GLN ILE LEU LYS THR GLU ARG VAL VAL ILE PRO          
SEQRES  31 C 1128  MET GLU ASN ILE GLN ASN MET TYR SER GLU SER SER GLN          
SEQRES  32 C 1128  LEU LEU TYR LEU LEU GLU HIS THR TRP LYS ASP ALA LYS          
SEQRES  33 C 1128  PHE ILE LEU GLN ILE MET CYS GLU LEU ASN VAL LEU PRO          
SEQRES  34 C 1128  LEU ALA LEU GLN ILE THR ASN ILE ALA GLY ASN ILE MET          
SEQRES  35 C 1128  SER ARG THR LEU MET GLY GLY ARG SER GLU ARG ASN GLU          
SEQRES  36 C 1128  PHE LEU LEU LEU HIS ALA PHE TYR GLU ASN ASN TYR ILE          
SEQRES  37 C 1128  VAL PRO ASP LYS GLN ILE PHE ARG LYS PRO GLN GLN LYS          
SEQRES  38 C 1128  LEU GLY ASP GLU ASP GLU GLU ILE ASP GLY ASP THR ASN          
SEQRES  39 C 1128  LYS TYR LYS LYS GLY ARG LYS LYS ALA ALA TYR ALA GLY          
SEQRES  40 C 1128  GLY LEU VAL LEU ASP PRO LYS VAL GLY PHE TYR ASP LYS          
SEQRES  41 C 1128  PHE ILE LEU LEU LEU ASP PHE ASN SER LEU TYR PRO SER          
SEQRES  42 C 1128  ILE ILE GLN GLU PHE ASN ILE CYS PHE THR THR VAL GLN          
SEQRES  43 C 1128  ARG VAL ALA SER GLU ALA GLN LYS VAL THR GLU ASP GLY          
SEQRES  44 C 1128  GLU GLN GLU GLN ILE PRO GLU LEU PRO ASP PRO SER LEU          
SEQRES  45 C 1128  GLU MET GLY ILE LEU PRO ARG GLU ILE ARG LYS LEU VAL          
SEQRES  46 C 1128  GLU ARG ARG LYS GLN VAL LYS GLN LEU MET LYS GLN GLN          
SEQRES  47 C 1128  ASP LEU ASN PRO ASP LEU ILE LEU GLN TYR ASP ILE ARG          
SEQRES  48 C 1128  GLN LYS ALA LEU LYS LEU THR ALA ASN SER MET TYR GLY          
SEQRES  49 C 1128  CYS LEU GLY PHE SER TYR SER ARG PHE TYR ALA LYS PRO          
SEQRES  50 C 1128  LEU ALA ALA LEU VAL THR TYR LYS GLY ARG GLU ILE LEU          
SEQRES  51 C 1128  MET HIS THR LYS GLU MET VAL GLN LYS MET ASN LEU GLU          
SEQRES  52 C 1128  VAL ILE TYR GLY ASP THR ASP SER ILE MET ILE ASN THR          
SEQRES  53 C 1128  ASN SER THR ASN LEU GLU GLU VAL PHE LYS LEU GLY ASN          
SEQRES  54 C 1128  LYS VAL LYS SER GLU VAL ASN LYS LEU TYR LYS LEU LEU          
SEQRES  55 C 1128  GLU ILE ASP ILE ASP GLY VAL PHE LYS SER LEU LEU LEU          
SEQRES  56 C 1128  LEU LYS LYS LYS LYS TYR ALA ALA LEU VAL VAL GLU PRO          
SEQRES  57 C 1128  THR SER ASP GLY ASN TYR VAL THR LYS GLN GLU LEU LYS          
SEQRES  58 C 1128  GLY LEU ASP ILE VAL ARG ARG ASP TRP CYS ASP LEU ALA          
SEQRES  59 C 1128  LYS ASP THR GLY ASN PHE VAL ILE GLY GLN ILE LEU SER          
SEQRES  60 C 1128  ASP GLN SER ARG ASP THR ILE VAL GLU ASN ILE GLN LYS          
SEQRES  61 C 1128  ARG LEU ILE GLU ILE GLY GLU ASN VAL LEU ASN GLY SER          
SEQRES  62 C 1128  VAL PRO VAL SER GLN PHE GLU ILE ASN LYS ALA LEU THR          
SEQRES  63 C 1128  LYS ASP PRO GLN ASP TYR PRO ASP LYS LYS SER LEU PRO          
SEQRES  64 C 1128  HIS VAL HIS VAL ALA LEU TRP ILE ASN SER GLN GLY GLY          
SEQRES  65 C 1128  ARG LYS VAL LYS ALA GLY ASP THR VAL SER TYR VAL ILE          
SEQRES  66 C 1128  CYS GLN ASP GLY SER ASN LEU THR ALA SER GLN ARG ALA          
SEQRES  67 C 1128  TYR ALA PRO GLU GLN LEU GLN LYS GLN ASP ASN LEU THR          
SEQRES  68 C 1128  ILE ASP THR GLN TYR TYR LEU ALA GLN GLN ILE HIS PRO          
SEQRES  69 C 1128  VAL VAL ALA ARG ILE CYS GLU PRO ILE ASP GLY ILE ASP          
SEQRES  70 C 1128  ALA VAL LEU ILE ALA THR TRP LEU GLY LEU ASP PRO THR          
SEQRES  71 C 1128  GLN PHE ARG VAL HIS HIS TYR HIS LYS ASP GLU GLU ASN          
SEQRES  72 C 1128  ASP ALA LEU LEU GLY GLY PRO ALA GLN LEU THR ASP GLU          
SEQRES  73 C 1128  GLU LYS TYR ARG ASP CYS GLU ARG PHE LYS CYS PRO CYS          
SEQRES  74 C 1128  PRO THR CYS GLY THR GLU ASN ILE TYR ASP ASN VAL PHE          
SEQRES  75 C 1128  ASP GLY SER GLY THR ASP MET GLU PRO SER LEU TYR ARG          
SEQRES  76 C 1128  CYS SER ASN ILE ASP CYS LYS ALA SER PRO LEU THR PHE          
SEQRES  77 C 1128  THR VAL GLN LEU SER ASN LYS LEU ILE MET ASP ILE ARG          
SEQRES  78 C 1128  ARG PHE ILE LYS LYS TYR TYR ASP GLY TRP LEU ILE CYS          
SEQRES  79 C 1128  GLU GLU PRO THR CYS ARG ASN ARG THR ARG HIS LEU PRO          
SEQRES  80 C 1128  LEU GLN PHE SER ARG THR GLY PRO LEU CYS PRO ALA CYS          
SEQRES  81 C 1128  MET LYS ALA THR LEU GLN PRO GLU TYR SER ASP LYS SER          
SEQRES  82 C 1128  LEU TYR THR GLN LEU CYS PHE TYR ARG TYR ILE PHE ASP          
SEQRES  83 C 1128  ALA GLU CYS ALA LEU GLU LYS LEU THR THR ASP HIS GLU          
SEQRES  84 C 1128  LYS ASP LYS LEU LYS LYS GLN PHE PHE THR PRO LYS VAL          
SEQRES  85 C 1128  LEU GLN ASP TYR ARG LYS LEU LYS ASN THR ALA GLU GLN          
SEQRES  86 C 1128  PHE LEU SER ARG SER GLY TYR SER GLU VAL ASN LEU SER          
SEQRES  87 C 1128  LYS LEU PHE ALA GLY CYS ALA VAL LYS SER                      
SEQRES   1 D  597  SER ALA SER ALA GLN GLN LEU ALA GLU GLU LEU GLN ILE          
SEQRES   2 D  597  PHE GLY LEU ASP CYS GLU GLU ALA LEU ILE GLU LYS LEU          
SEQRES   3 D  597  VAL GLU LEU CYS VAL GLN TYR GLY GLN ASN GLU GLU GLY          
SEQRES   4 D  597  MET VAL GLY GLU LEU ILE ALA PHE CYS THR SER THR HIS          
SEQRES   5 D  597  LYS VAL GLY LEU THR SER GLU ILE LEU ASN SER PHE GLU          
SEQRES   6 D  597  HIS GLU PHE LEU SER LYS ARG LEU SER LYS ALA ARG HIS          
SEQRES   7 D  597  SER THR CYS LYS ASP SER GLY HIS ALA GLY ALA ARG ASP          
SEQRES   8 D  597  ILE VAL SER ILE GLN GLU LEU ILE GLU VAL GLU GLU GLU          
SEQRES   9 D  597  GLU GLU ILE LEU LEU ASN SER TYR THR THR PRO SER LYS          
SEQRES  10 D  597  GLY SER GLN LYS ARG ALA ILE SER THR PRO GLU THR PRO          
SEQRES  11 D  597  LEU THR LYS ARG SER VAL SER THR ARG SER PRO HIS GLN          
SEQRES  12 D  597  LEU LEU SER PRO SER SER PHE SER PRO SER ALA THR PRO          
SEQRES  13 D  597  SER GLN LYS TYR ASN SER ARG SER ASN ARG GLY GLU VAL          
SEQRES  14 D  597  VAL THR SER PHE GLY LEU ALA GLN GLY VAL SER TRP SER          
SEQRES  15 D  597  GLY ARG GLY GLY ALA GLY ASN ILE SER LEU LYS VAL LEU          
SEQRES  16 D  597  GLY CYS PRO GLU ALA LEU THR GLY SER TYR LYS SER MET          
SEQRES  17 D  597  PHE GLN LYS LEU PRO ASP ILE ARG GLU VAL LEU THR CYS          
SEQRES  18 D  597  LYS ILE GLU GLU LEU GLY SER GLU LEU LYS GLU HIS TYR          
SEQRES  19 D  597  LYS ILE GLU ALA PHE THR PRO LEU LEU ALA PRO ALA GLN          
SEQRES  20 D  597  GLU PRO VAL THR LEU LEU GLY GLN ILE GLY CYS ASP SER          
SEQRES  21 D  597  ASN GLY LYS LEU ASN ASN LYS SER VAL ILE LEU GLU GLY          
SEQRES  22 D  597  ASP ARG GLU HIS SER SER GLY ALA GLN ILE PRO VAL ASP          
SEQRES  23 D  597  LEU SER GLU LEU LYS GLU TYR SER LEU PHE PRO GLY GLN          
SEQRES  24 D  597  VAL VAL ILE MET GLU GLY ILE ASN THR THR GLY ARG LYS          
SEQRES  25 D  597  LEU VAL ALA THR LYS LEU TYR GLU GLY VAL PRO LEU PRO          
SEQRES  26 D  597  PHE TYR GLN PRO THR GLU GLU ASP ALA ASP PHE GLU GLN          
SEQRES  27 D  597  SER MET VAL LEU VAL ALA CYS GLY PRO TYR THR THR SER          
SEQRES  28 D  597  ASP SER ILE THR TYR ASP PRO LEU LEU ASP LEU ILE ALA          
SEQRES  29 D  597  VAL ILE ASN HIS ASP ARG PRO ASP VAL CYS ILE LEU PHE          
SEQRES  30 D  597  GLY PRO PHE LEU ASP ALA LYS HIS GLU GLN VAL GLU ASN          
SEQRES  31 D  597  CYS LEU LEU THR SER PRO PHE GLU ASP ILE PHE LYS GLN          
SEQRES  32 D  597  CYS LEU ARG THR ILE ILE GLU GLY THR ARG SER SER GLY          
SEQRES  33 D  597  SER HIS LEU VAL PHE VAL PRO SER LEU ARG ASP VAL HIS          
SEQRES  34 D  597  HIS GLU PRO VAL TYR PRO GLN PRO PRO PHE SER TYR SER          
SEQRES  35 D  597  ASP LEU SER ARG GLU ASP LYS LYS GLN VAL GLN PHE VAL          
SEQRES  36 D  597  SER GLU PRO CYS SER LEU SER ILE ASN GLY VAL ILE PHE          
SEQRES  37 D  597  GLY LEU THR SER THR ASP LEU LEU PHE HIS LEU GLY ALA          
SEQRES  38 D  597  GLU GLU ILE SER SER SER SER GLY THR SER ASP ARG PHE          
SEQRES  39 D  597  SER ARG ILE LEU LYS HIS ILE LEU THR GLN ARG SER TYR          
SEQRES  40 D  597  TYR PRO LEU TYR PRO PRO GLN GLU ASP MET ALA ILE ASP          
SEQRES  41 D  597  TYR GLU SER PHE TYR VAL TYR ALA GLN LEU PRO VAL THR          
SEQRES  42 D  597  PRO ASP VAL LEU ILE ILE PRO SER GLU LEU ARG TYR PHE          
SEQRES  43 D  597  VAL LYS ASP VAL LEU GLY CYS VAL CYS VAL ASN PRO GLY          
SEQRES  44 D  597  ARG LEU THR LYS GLY GLN VAL GLY GLY THR PHE ALA ARG          
SEQRES  45 D  597  LEU TYR LEU ARG ARG PRO ALA ALA ASP GLY ALA GLU ARG          
SEQRES  46 D  597  GLN SER PRO CYS ILE ALA VAL GLN VAL VAL ARG ILE              
SEQRES   1 E  420  MET GLU THR PHE ASP PRO THR GLU LEU PRO GLU LEU LEU          
SEQRES   2 E  420  LYS LEU TYR TYR ARG ARG LEU PHE PRO TYR SER GLN TYR          
SEQRES   3 E  420  TYR ARG TRP LEU ASN TYR GLY GLY VAL ILE LYS ASN TYR          
SEQRES   4 E  420  PHE GLN HIS ARG GLU PHE SER PHE THR LEU LYS ASP ASP          
SEQRES   5 E  420  ILE TYR ILE ARG TYR GLN SER PHE ASN ASN GLN SER ASP          
SEQRES   6 E  420  LEU GLU LYS GLU MET GLN LYS MET ASN PRO TYR LYS ILE          
SEQRES   7 E  420  ASP ILE GLY ALA VAL TYR SER HIS ARG PRO ASN GLN HIS          
SEQRES   8 E  420  ASN THR VAL LYS LEU GLY ALA PHE GLN ALA GLN GLU LYS          
SEQRES   9 E  420  GLU LEU VAL PHE ASP ILE ASP MET THR ASP TYR ASP ASP          
SEQRES  10 E  420  VAL ARG ARG CYS CYS SER SER ALA ASP ILE CYS PRO LYS          
SEQRES  11 E  420  CYS TRP THR LEU MET THR MET ALA ILE ARG ILE ILE ASP          
SEQRES  12 E  420  ARG ALA LEU LYS GLU ASP PHE GLY PHE LYS HIS ARG LEU          
SEQRES  13 E  420  TRP VAL TYR SER GLY ARG ARG GLY VAL HIS CYS TRP VAL          
SEQRES  14 E  420  CYS ASP GLU SER VAL ARG LYS LEU SER SER ALA VAL ARG          
SEQRES  15 E  420  SER GLY ILE VAL GLU TYR LEU SER LEU VAL LYS GLY GLY          
SEQRES  16 E  420  GLN ASP VAL LYS LYS LYS VAL HIS LEU SER GLU LYS ILE          
SEQRES  17 E  420  HIS PRO PHE ILE ARG LYS SER ILE ASN ILE ILE LYS LYS          
SEQRES  18 E  420  TYR PHE GLU GLU TYR ALA LEU VAL ASN GLN ASP ILE LEU          
SEQRES  19 E  420  GLU ASN LYS GLU SER TRP ASP LYS ILE LEU ALA LEU VAL          
SEQRES  20 E  420  PRO GLU THR ILE HIS ASP GLU LEU GLN GLN SER PHE GLN          
SEQRES  21 E  420  LYS SER HIS ASN SER LEU GLN ARG TRP GLU HIS LEU LYS          
SEQRES  22 E  420  LYS VAL ALA SER ARG TYR GLN ASN ASN ILE LYS ASN ASP          
SEQRES  23 E  420  LYS TYR GLY PRO TRP LEU GLU TRP GLU ILE MET LEU GLN          
SEQRES  24 E  420  TYR CYS PHE PRO ARG LEU ASP ILE ASN VAL SER LYS GLY          
SEQRES  25 E  420  ILE ASN HIS LEU LEU LYS SER PRO PHE SER VAL HIS PRO          
SEQRES  26 E  420  LYS THR GLY ARG ILE SER VAL PRO ILE ASP LEU GLN LYS          
SEQRES  27 E  420  VAL ASP GLN PHE ASP PRO PHE THR VAL PRO THR ILE SER          
SEQRES  28 E  420  PHE ILE CYS ARG GLU LEU ASP ALA ILE SER THR ASN GLU          
SEQRES  29 E  420  GLU GLU LYS GLU GLU ASN GLU ALA GLU SER ASP VAL LYS          
SEQRES  30 E  420  HIS ARG THR ARG ASP TYR LYS LYS THR SER LEU ALA PRO          
SEQRES  31 E  420  TYR VAL LYS VAL PHE GLU HIS PHE LEU GLU ASN LEU ASP          
SEQRES  32 E  420  LYS SER ARG LYS GLY GLU LEU LEU LYS LYS SER ASP LEU          
SEQRES  33 E  420  GLN LYS ASP PHE                                              
SEQRES   1 F  509  MET GLU PHE SER GLY ARG LYS TRP ARG LYS LEU ARG LEU          
SEQRES   2 F  509  ALA GLY ASP GLN ARG ASN ALA SER TYR PRO HIS CYS LEU          
SEQRES   3 F  509  GLN PHE TYR LEU GLN PRO PRO SER GLU ASN ILE SER LEU          
SEQRES   4 F  509  ILE GLU PHE GLU ASN LEU ALA ILE ASP ARG VAL LYS LEU          
SEQRES   5 F  509  LEU LYS SER VAL GLU ASN LEU GLY VAL SER TYR VAL LYS          
SEQRES   6 F  509  GLY THR GLU GLN TYR GLN SER LYS LEU GLU SER GLU LEU          
SEQRES   7 F  509  ARG LYS LEU LYS PHE SER TYR ARG GLU ASN LEU GLU ASP          
SEQRES   8 F  509  GLU TYR GLU PRO ARG ARG ARG ASP HIS ILE SER HIS PHE          
SEQRES   9 F  509  ILE LEU ARG LEU ALA TYR CYS GLN SER GLU GLU LEU ARG          
SEQRES  10 F  509  ARG TRP PHE ILE GLN GLN GLU MET ASP LEU LEU ARG PHE          
SEQRES  11 F  509  ARG PHE SER ILE LEU PRO LYS ASP LYS ILE GLN ASP PHE          
SEQRES  12 F  509  LEU LYS ASP SER GLN LEU GLN PHE GLU ALA ILE SER ASP          
SEQRES  13 F  509  GLU GLU LYS THR LEU ARG GLU GLN GLU ILE VAL ALA SER          
SEQRES  14 F  509  SER PRO SER LEU SER GLY LEU LYS LEU GLY PHE GLU SER          
SEQRES  15 F  509  ILE TYR LYS ILE PRO PHE ALA ASP ALA LEU ASP LEU PHE          
SEQRES  16 F  509  ARG GLY ARG LYS VAL TYR LEU GLU ASP GLY PHE ALA TYR          
SEQRES  17 F  509  VAL PRO LEU LYS ASP ILE VAL ALA ILE ILE LEU ASN GLU          
SEQRES  18 F  509  PHE ARG ALA LYS LEU SER LYS ALA LEU ALA LEU THR ALA          
SEQRES  19 F  509  ARG SER LEU PRO ALA VAL GLN SER ASP GLU ARG LEU GLN          
SEQRES  20 F  509  PRO LEU LEU ASN HIS LEU SER HIS SER TYR THR GLY GLN          
SEQRES  21 F  509  ASP TYR SER THR GLN GLY ASN VAL GLY LYS ILE SER LEU          
SEQRES  22 F  509  ASP GLN ILE ASP LEU LEU SER THR LYS SER PHE PRO PRO          
SEQRES  23 F  509  CYS MET ARG GLN LEU HIS LYS ALA LEU ARG GLU ASN HIS          
SEQRES  24 F  509  HIS LEU ARG HIS GLY GLY ARG MET GLN TYR GLY LEU PHE          
SEQRES  25 F  509  LEU LYS GLY ILE GLY LEU THR LEU GLU GLN ALA LEU GLN          
SEQRES  26 F  509  PHE TRP LYS GLN GLU PHE ILE LYS GLY LYS MET ASP PRO          
SEQRES  27 F  509  ASP LYS PHE ASP LYS GLY TYR SER TYR ASN ILE ARG HIS          
SEQRES  28 F  509  SER PHE GLY LYS GLU GLY LYS ARG THR ASP TYR THR PRO          
SEQRES  29 F  509  PHE SER CYS LEU LYS ILE ILE LEU SER ASN PRO PRO SER          
SEQRES  30 F  509  GLN GLY ASP TYR HIS GLY CYS PRO PHE ARG HIS SER ASP          
SEQRES  31 F  509  PRO GLU LEU LEU LYS GLN LYS LEU GLN SER TYR LYS ILE          
SEQRES  32 F  509  SER PRO GLY GLY ILE SER GLN ILE LEU ASP LEU VAL LYS          
SEQRES  33 F  509  GLY THR HIS TYR GLN VAL ALA CYS GLN LYS TYR PHE GLU          
SEQRES  34 F  509  MET ILE HIS ASN VAL ASP ASP CYS GLY PHE SER LEU ASN          
SEQRES  35 F  509  HIS PRO ASN GLN PHE PHE CYS GLU SER GLN ARG ILE LEU          
SEQRES  36 F  509  ASN GLY GLY LYS ASP ILE LYS LYS GLU PRO ILE GLN PRO          
SEQRES  37 F  509  GLU THR PRO GLN PRO LYS PRO SER VAL GLN LYS THR LYS          
SEQRES  38 F  509  ASP ALA SER SER ALA LEU ALA SER LEU ASN SER SER LEU          
SEQRES  39 F  509  GLU MET ASP MET GLU GLY LEU GLU ASP TYR PHE SER GLU          
SEQRES  40 F  509  ASP SER                                                      
SEQRES   1 G 1128  ALA ASP GLU GLU GLN VAL PHE HIS PHE TYR TRP LEU ASP          
SEQRES   2 G 1128  ALA TYR GLU ASP GLN TYR ASN GLN PRO GLY VAL VAL PHE          
SEQRES   3 G 1128  LEU PHE GLY LYS VAL TRP ILE GLU SER ALA GLU THR HIS          
SEQRES   4 G 1128  VAL SER CYS CYS VAL MET VAL LYS ASN ILE GLU ARG THR          
SEQRES   5 G 1128  LEU TYR PHE LEU PRO ARG GLU MET LYS ILE ASP LEU ASN          
SEQRES   6 G 1128  THR GLY LYS GLU THR GLY THR PRO ILE SER MET LYS ASP          
SEQRES   7 G 1128  VAL TYR GLU GLU PHE ASP GLU LYS ILE ALA THR LYS TYR          
SEQRES   8 G 1128  LYS ILE MET LYS PHE LYS SER LYS PRO VAL GLU LYS ASN          
SEQRES   9 G 1128  TYR ALA PHE GLU ILE PRO ASP VAL PRO GLU LYS SER GLU          
SEQRES  10 G 1128  TYR LEU GLU VAL LYS TYR SER ALA GLU MET PRO GLN LEU          
SEQRES  11 G 1128  PRO GLN ASP LEU LYS GLY GLU THR PHE SER HIS VAL PHE          
SEQRES  12 G 1128  GLY THR ASN THR SER SER LEU GLU LEU PHE LEU MET ASN          
SEQRES  13 G 1128  ARG LYS ILE LYS GLY PRO CYS TRP LEU GLU VAL LYS SER          
SEQRES  14 G 1128  PRO GLN LEU LEU ASN GLN PRO VAL SER TRP CYS LYS ALA          
SEQRES  15 G 1128  GLU ALA MET ALA LEU LYS PRO ASP LEU VAL ASN VAL ILE          
SEQRES  16 G 1128  LYS ASP VAL SER PRO PRO PRO LEU VAL VAL MET ALA PHE          
SEQRES  17 G 1128  SER MET LYS THR MET GLN ASN ALA LYS ASN HIS GLN ASN          
SEQRES  18 G 1128  GLU ILE ILE ALA MET ALA ALA LEU VAL HIS HIS SER PHE          
SEQRES  19 G 1128  ALA LEU ASP LYS ALA ALA PRO LYS PRO PRO PHE GLN SER          
SEQRES  20 G 1128  HIS PHE CYS VAL VAL SER LYS PRO LYS ASP CYS ILE PHE          
SEQRES  21 G 1128  PRO TYR ALA PHE LYS GLU VAL ILE GLU LYS LYS ASN VAL          
SEQRES  22 G 1128  LYS VAL GLU VAL ALA ALA THR GLU ARG THR LEU LEU GLY          
SEQRES  23 G 1128  PHE PHE LEU ALA LYS VAL HIS LYS ILE ASP PRO ASP ILE          
SEQRES  24 G 1128  ILE VAL GLY HIS ASN ILE TYR GLY PHE GLU LEU GLU VAL          
SEQRES  25 G 1128  LEU LEU GLN ARG ILE ASN VAL CYS LYS ALA PRO HIS TRP          
SEQRES  26 G 1128  SER LYS ILE GLY ARG LEU LYS ARG SER ASN MET PRO LYS          
SEQRES  27 G 1128  LEU GLY GLY ARG SER GLY PHE GLY GLU ARG ASN ALA THR          
SEQRES  28 G 1128  CYS GLY ARG MET ILE CYS ASP VAL GLU ILE SER ALA LYS          
SEQRES  29 G 1128  GLU LEU ILE ARG CYS LYS SER TYR HIS LEU SER GLU LEU          
SEQRES  30 G 1128  VAL GLN GLN ILE LEU LYS THR GLU ARG VAL VAL ILE PRO          
SEQRES  31 G 1128  MET GLU ASN ILE GLN ASN MET TYR SER GLU SER SER GLN          
SEQRES  32 G 1128  LEU LEU TYR LEU LEU GLU HIS THR TRP LYS ASP ALA LYS          
SEQRES  33 G 1128  PHE ILE LEU GLN ILE MET CYS GLU LEU ASN VAL LEU PRO          
SEQRES  34 G 1128  LEU ALA LEU GLN ILE THR ASN ILE ALA GLY ASN ILE MET          
SEQRES  35 G 1128  SER ARG THR LEU MET GLY GLY ARG SER GLU ARG ASN GLU          
SEQRES  36 G 1128  PHE LEU LEU LEU HIS ALA PHE TYR GLU ASN ASN TYR ILE          
SEQRES  37 G 1128  VAL PRO ASP LYS GLN ILE PHE ARG LYS PRO GLN GLN LYS          
SEQRES  38 G 1128  LEU GLY ASP GLU ASP GLU GLU ILE ASP GLY ASP THR ASN          
SEQRES  39 G 1128  LYS TYR LYS LYS GLY ARG LYS LYS ALA ALA TYR ALA GLY          
SEQRES  40 G 1128  GLY LEU VAL LEU ASP PRO LYS VAL GLY PHE TYR ASP LYS          
SEQRES  41 G 1128  PHE ILE LEU LEU LEU ASP PHE ASN SER LEU TYR PRO SER          
SEQRES  42 G 1128  ILE ILE GLN GLU PHE ASN ILE CYS PHE THR THR VAL GLN          
SEQRES  43 G 1128  ARG VAL ALA SER GLU ALA GLN LYS VAL THR GLU ASP GLY          
SEQRES  44 G 1128  GLU GLN GLU GLN ILE PRO GLU LEU PRO ASP PRO SER LEU          
SEQRES  45 G 1128  GLU MET GLY ILE LEU PRO ARG GLU ILE ARG LYS LEU VAL          
SEQRES  46 G 1128  GLU ARG ARG LYS GLN VAL LYS GLN LEU MET LYS GLN GLN          
SEQRES  47 G 1128  ASP LEU ASN PRO ASP LEU ILE LEU GLN TYR ASP ILE ARG          
SEQRES  48 G 1128  GLN LYS ALA LEU LYS LEU THR ALA ASN SER MET TYR GLY          
SEQRES  49 G 1128  CYS LEU GLY PHE SER TYR SER ARG PHE TYR ALA LYS PRO          
SEQRES  50 G 1128  LEU ALA ALA LEU VAL THR TYR LYS GLY ARG GLU ILE LEU          
SEQRES  51 G 1128  MET HIS THR LYS GLU MET VAL GLN LYS MET ASN LEU GLU          
SEQRES  52 G 1128  VAL ILE TYR GLY ASP THR ASP SER ILE MET ILE ASN THR          
SEQRES  53 G 1128  ASN SER THR ASN LEU GLU GLU VAL PHE LYS LEU GLY ASN          
SEQRES  54 G 1128  LYS VAL LYS SER GLU VAL ASN LYS LEU TYR LYS LEU LEU          
SEQRES  55 G 1128  GLU ILE ASP ILE ASP GLY VAL PHE LYS SER LEU LEU LEU          
SEQRES  56 G 1128  LEU LYS LYS LYS LYS TYR ALA ALA LEU VAL VAL GLU PRO          
SEQRES  57 G 1128  THR SER ASP GLY ASN TYR VAL THR LYS GLN GLU LEU LYS          
SEQRES  58 G 1128  GLY LEU ASP ILE VAL ARG ARG ASP TRP CYS ASP LEU ALA          
SEQRES  59 G 1128  LYS ASP THR GLY ASN PHE VAL ILE GLY GLN ILE LEU SER          
SEQRES  60 G 1128  ASP GLN SER ARG ASP THR ILE VAL GLU ASN ILE GLN LYS          
SEQRES  61 G 1128  ARG LEU ILE GLU ILE GLY GLU ASN VAL LEU ASN GLY SER          
SEQRES  62 G 1128  VAL PRO VAL SER GLN PHE GLU ILE ASN LYS ALA LEU THR          
SEQRES  63 G 1128  LYS ASP PRO GLN ASP TYR PRO ASP LYS LYS SER LEU PRO          
SEQRES  64 G 1128  HIS VAL HIS VAL ALA LEU TRP ILE ASN SER GLN GLY GLY          
SEQRES  65 G 1128  ARG LYS VAL LYS ALA GLY ASP THR VAL SER TYR VAL ILE          
SEQRES  66 G 1128  CYS GLN ASP GLY SER ASN LEU THR ALA SER GLN ARG ALA          
SEQRES  67 G 1128  TYR ALA PRO GLU GLN LEU GLN LYS GLN ASP ASN LEU THR          
SEQRES  68 G 1128  ILE ASP THR GLN TYR TYR LEU ALA GLN GLN ILE HIS PRO          
SEQRES  69 G 1128  VAL VAL ALA ARG ILE CYS GLU PRO ILE ASP GLY ILE ASP          
SEQRES  70 G 1128  ALA VAL LEU ILE ALA THR TRP LEU GLY LEU ASP PRO THR          
SEQRES  71 G 1128  GLN PHE ARG VAL HIS HIS TYR HIS LYS ASP GLU GLU ASN          
SEQRES  72 G 1128  ASP ALA LEU LEU GLY GLY PRO ALA GLN LEU THR ASP GLU          
SEQRES  73 G 1128  GLU LYS TYR ARG ASP CYS GLU ARG PHE LYS CYS PRO CYS          
SEQRES  74 G 1128  PRO THR CYS GLY THR GLU ASN ILE TYR ASP ASN VAL PHE          
SEQRES  75 G 1128  ASP GLY SER GLY THR ASP MET GLU PRO SER LEU TYR ARG          
SEQRES  76 G 1128  CYS SER ASN ILE ASP CYS LYS ALA SER PRO LEU THR PHE          
SEQRES  77 G 1128  THR VAL GLN LEU SER ASN LYS LEU ILE MET ASP ILE ARG          
SEQRES  78 G 1128  ARG PHE ILE LYS LYS TYR TYR ASP GLY TRP LEU ILE CYS          
SEQRES  79 G 1128  GLU GLU PRO THR CYS ARG ASN ARG THR ARG HIS LEU PRO          
SEQRES  80 G 1128  LEU GLN PHE SER ARG THR GLY PRO LEU CYS PRO ALA CYS          
SEQRES  81 G 1128  MET LYS ALA THR LEU GLN PRO GLU TYR SER ASP LYS SER          
SEQRES  82 G 1128  LEU TYR THR GLN LEU CYS PHE TYR ARG TYR ILE PHE ASP          
SEQRES  83 G 1128  ALA GLU CYS ALA LEU GLU LYS LEU THR THR ASP HIS GLU          
SEQRES  84 G 1128  LYS ASP LYS LEU LYS LYS GLN PHE PHE THR PRO LYS VAL          
SEQRES  85 G 1128  LEU GLN ASP TYR ARG LYS LEU LYS ASN THR ALA GLU GLN          
SEQRES  86 G 1128  PHE LEU SER ARG SER GLY TYR SER GLU VAL ASN LEU SER          
SEQRES  87 G 1128  LYS LEU PHE ALA GLY CYS ALA VAL LYS SER                      
SEQRES   1 H  597  SER ALA SER ALA GLN GLN LEU ALA GLU GLU LEU GLN ILE          
SEQRES   2 H  597  PHE GLY LEU ASP CYS GLU GLU ALA LEU ILE GLU LYS LEU          
SEQRES   3 H  597  VAL GLU LEU CYS VAL GLN TYR GLY GLN ASN GLU GLU GLY          
SEQRES   4 H  597  MET VAL GLY GLU LEU ILE ALA PHE CYS THR SER THR HIS          
SEQRES   5 H  597  LYS VAL GLY LEU THR SER GLU ILE LEU ASN SER PHE GLU          
SEQRES   6 H  597  HIS GLU PHE LEU SER LYS ARG LEU SER LYS ALA ARG HIS          
SEQRES   7 H  597  SER THR CYS LYS ASP SER GLY HIS ALA GLY ALA ARG ASP          
SEQRES   8 H  597  ILE VAL SER ILE GLN GLU LEU ILE GLU VAL GLU GLU GLU          
SEQRES   9 H  597  GLU GLU ILE LEU LEU ASN SER TYR THR THR PRO SER LYS          
SEQRES  10 H  597  GLY SER GLN LYS ARG ALA ILE SER THR PRO GLU THR PRO          
SEQRES  11 H  597  LEU THR LYS ARG SER VAL SER THR ARG SER PRO HIS GLN          
SEQRES  12 H  597  LEU LEU SER PRO SER SER PHE SER PRO SER ALA THR PRO          
SEQRES  13 H  597  SER GLN LYS TYR ASN SER ARG SER ASN ARG GLY GLU VAL          
SEQRES  14 H  597  VAL THR SER PHE GLY LEU ALA GLN GLY VAL SER TRP SER          
SEQRES  15 H  597  GLY ARG GLY GLY ALA GLY ASN ILE SER LEU LYS VAL LEU          
SEQRES  16 H  597  GLY CYS PRO GLU ALA LEU THR GLY SER TYR LYS SER MET          
SEQRES  17 H  597  PHE GLN LYS LEU PRO ASP ILE ARG GLU VAL LEU THR CYS          
SEQRES  18 H  597  LYS ILE GLU GLU LEU GLY SER GLU LEU LYS GLU HIS TYR          
SEQRES  19 H  597  LYS ILE GLU ALA PHE THR PRO LEU LEU ALA PRO ALA GLN          
SEQRES  20 H  597  GLU PRO VAL THR LEU LEU GLY GLN ILE GLY CYS ASP SER          
SEQRES  21 H  597  ASN GLY LYS LEU ASN ASN LYS SER VAL ILE LEU GLU GLY          
SEQRES  22 H  597  ASP ARG GLU HIS SER SER GLY ALA GLN ILE PRO VAL ASP          
SEQRES  23 H  597  LEU SER GLU LEU LYS GLU TYR SER LEU PHE PRO GLY GLN          
SEQRES  24 H  597  VAL VAL ILE MET GLU GLY ILE ASN THR THR GLY ARG LYS          
SEQRES  25 H  597  LEU VAL ALA THR LYS LEU TYR GLU GLY VAL PRO LEU PRO          
SEQRES  26 H  597  PHE TYR GLN PRO THR GLU GLU ASP ALA ASP PHE GLU GLN          
SEQRES  27 H  597  SER MET VAL LEU VAL ALA CYS GLY PRO TYR THR THR SER          
SEQRES  28 H  597  ASP SER ILE THR TYR ASP PRO LEU LEU ASP LEU ILE ALA          
SEQRES  29 H  597  VAL ILE ASN HIS ASP ARG PRO ASP VAL CYS ILE LEU PHE          
SEQRES  30 H  597  GLY PRO PHE LEU ASP ALA LYS HIS GLU GLN VAL GLU ASN          
SEQRES  31 H  597  CYS LEU LEU THR SER PRO PHE GLU ASP ILE PHE LYS GLN          
SEQRES  32 H  597  CYS LEU ARG THR ILE ILE GLU GLY THR ARG SER SER GLY          
SEQRES  33 H  597  SER HIS LEU VAL PHE VAL PRO SER LEU ARG ASP VAL HIS          
SEQRES  34 H  597  HIS GLU PRO VAL TYR PRO GLN PRO PRO PHE SER TYR SER          
SEQRES  35 H  597  ASP LEU SER ARG GLU ASP LYS LYS GLN VAL GLN PHE VAL          
SEQRES  36 H  597  SER GLU PRO CYS SER LEU SER ILE ASN GLY VAL ILE PHE          
SEQRES  37 H  597  GLY LEU THR SER THR ASP LEU LEU PHE HIS LEU GLY ALA          
SEQRES  38 H  597  GLU GLU ILE SER SER SER SER GLY THR SER ASP ARG PHE          
SEQRES  39 H  597  SER ARG ILE LEU LYS HIS ILE LEU THR GLN ARG SER TYR          
SEQRES  40 H  597  TYR PRO LEU TYR PRO PRO GLN GLU ASP MET ALA ILE ASP          
SEQRES  41 H  597  TYR GLU SER PHE TYR VAL TYR ALA GLN LEU PRO VAL THR          
SEQRES  42 H  597  PRO ASP VAL LEU ILE ILE PRO SER GLU LEU ARG TYR PHE          
SEQRES  43 H  597  VAL LYS ASP VAL LEU GLY CYS VAL CYS VAL ASN PRO GLY          
SEQRES  44 H  597  ARG LEU THR LYS GLY GLN VAL GLY GLY THR PHE ALA ARG          
SEQRES  45 H  597  LEU TYR LEU ARG ARG PRO ALA ALA ASP GLY ALA GLU ARG          
SEQRES  46 H  597  GLN SER PRO CYS ILE ALA VAL GLN VAL VAL ARG ILE              
HET     ZN  A 501       1                                                       
HET    SF4  B 601       8                                                       
HET     ZN  C1501       1                                                       
HET     ZN  C1502       1                                                       
HET     ZN  E 501       1                                                       
HET    SF4  F 601       8                                                       
HET     ZN  G1501       1                                                       
HET     ZN  G1502       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
FORMUL   9   ZN    6(ZN 2+)                                                     
FORMUL  10  SF4    2(FE4 S4)                                                    
HELIX    1 AA1 GLU A    8  LEU A   20  1                                  13    
HELIX    2 AA2 PRO A   22  TYR A   32  1                                  11    
HELIX    3 AA3 GLY A   33  VAL A   35  5                                   3    
HELIX    4 AA4 LYS A   50  ASP A   52  5                                   3    
HELIX    5 AA5 ASN A   62  LYS A   72  1                                  11    
HELIX    6 AA6 ARG A   87  HIS A   91  5                                   5    
HELIX    7 AA7 CYS A  128  CYS A  131  5                                   4    
HELIX    8 AA8 TRP A  132  ASP A  149  1                                  18    
HELIX    9 AA9 ASP A  171  LYS A  176  1                                   6    
HELIX   10 AB1 SER A  178  LEU A  189  1                                  12    
HELIX   11 AB2 HIS A  209  ILE A  219  1                                  11    
HELIX   12 AB3 TYR A  222  ALA A  227  1                                   6    
HELIX   13 AB4 ASN A  236  ALA A  245  1                                  10    
HELIX   14 AB5 LEU A  246  VAL A  247  5                                   2    
HELIX   15 AB6 PRO A  248  THR A  250  5                                   3    
HELIX   16 AB7 ILE A  251  LYS A  261  1                                  11    
HELIX   17 AB8 ASN A  264  ILE A  283  1                                  20    
HELIX   18 AB9 TRP A  291  PHE A  302  1                                  12    
HELIX   19 AC1 ASP A  306  GLY A  312  1                                   7    
HELIX   20 AC2 ASP A  335  VAL A  339  5                                   5    
HELIX   21 AC3 THR A  349  GLU A  356  1                                   8    
HELIX   22 AC4 LEU A  388  LYS A  412  1                                  25    
HELIX   23 AC5 LEU B   39  TYR B   63  1                                  25    
HELIX   24 AC6 THR B   67  LEU B   81  1                                  15    
HELIX   25 AC7 TYR B   93  LEU B  106  1                                  14    
HELIX   26 AC8 ARG B  107  GLN B  112  5                                   6    
HELIX   27 AC9 SER B  113  GLU B  124  1                                  12    
HELIX   28 AD1 GLU B  124  ILE B  134  1                                  11    
HELIX   29 AD2 ASP B  138  SER B  147  1                                  10    
HELIX   30 AD3 SER B  155  ARG B  162  1                                   8    
HELIX   31 AD4 ARG B  162  SER B  170  1                                   9    
HELIX   32 AD5 ALA B  191  ARG B  196  1                                   6    
HELIX   33 AD6 PRO B  210  ARG B  235  1                                  26    
HELIX   34 AD7 LEU B  246  ASN B  251  1                                   6    
HELIX   35 AD8 GLN B  275  SER B  283  1                                   9    
HELIX   36 AD9 PRO B  285  ASN B  298  1                                  14    
HELIX   37 AE1 ARG B  302  ILE B  316  1                                  15    
HELIX   38 AE2 THR B  319  ILE B  332  1                                  14    
HELIX   39 AE3 ASP B  337  TYR B  345  1                                   9    
HELIX   40 AE4 TYR B  345  GLY B  354  1                                  10    
HELIX   41 AE5 SER B  366  SER B  373  1                                   8    
HELIX   42 AE6 CYS B  384  SER B  389  1                                   6    
HELIX   43 AE7 ASP B  390  TYR B  401  1                                  12    
HELIX   44 AE8 SER B  404  LYS B  416  1                                  13    
HELIX   45 AE9 HIS B  419  ASN B  433  1                                  15    
HELIX   46 AF1 HIS B  443  ILE B  454  1                                  12    
HELIX   47 AF2 GLU C  368  GLU C  371  5                                   4    
HELIX   48 AF3 SER C  409  ILE C  421  1                                  13    
HELIX   49 AF4 ALA C  422  LYS C  426  5                                   5    
HELIX   50 AF5 SER C  482  ARG C  491  1                                  10    
HELIX   51 AF6 LYS C  522  VAL C  526  5                                   5    
HELIX   52 AF7 ALA C  597  LYS C  605  1                                   9    
HELIX   53 AF8 THR C  614  ASP C  630  1                                  17    
HELIX   54 AF9 PHE C  642  CYS C  654  1                                  13    
HELIX   55 AG1 HIS C  658  GLY C  663  5                                   6    
HELIX   56 AG2 VAL C  693  GLU C  699  1                                   7    
HELIX   57 AG3 HIS C  707  ILE C  715  1                                   9    
HELIX   58 AG4 ILE C  728  TYR C  732  5                                   5    
HELIX   59 AG5 GLU C  734  LEU C  759  1                                  26    
HELIX   60 AG6 ASN C  760  GLY C  773  1                                  14    
HELIX   61 AG7 ILE C  775  GLY C  782  1                                   8    
HELIX   62 AG8 GLY C  783  ASN C  799  1                                  17    
HELIX   63 AG9 SER C  863  PHE C  872  1                                  10    
HELIX   64 AH1 LEU C  911  MET C  929  1                                  19    
HELIX   65 AH2 ASP C  937  CYS C  959  1                                  23    
HELIX   66 AH3 ALA C  969  LYS C  993  1                                  25    
HELIX   67 AH4 ASN C 1014  TYR C 1033  1                                  20    
HELIX   68 AH5 CYS C 1085  LEU C 1100  1                                  16    
HELIX   69 AH6 SER C 1104  GLY C 1126  1                                  23    
HELIX   70 AH7 PRO C 1129  GLU C 1134  5                                   6    
HELIX   71 AH8 ASP C 1142  TYR C 1146  5                                   5    
HELIX   72 AH9 ASP C 1148  SER C 1151  5                                   4    
HELIX   73 AI1 LEU C 1152  GLY C 1165  1                                  14    
HELIX   74 AI2 THR C 1187  GLN C 1190  5                                   4    
HELIX   75 AI3 ALA C 1194  LYS C 1200  1                                   7    
HELIX   76 AI4 ASP C 1207  GLN C 1215  1                                   9    
HELIX   77 AI5 GLN C 1215  GLU C 1225  1                                  11    
HELIX   78 AI6 ASP C 1231  LEU C 1239  1                                   9    
HELIX   79 AI7 ASP C 1242  HIS C 1250  1                                   9    
HELIX   80 AI8 THR C 1268  TYR C 1273  1                                   6    
HELIX   81 AI9 SER C 1318  THR C 1321  5                                   4    
HELIX   82 AJ1 PHE C 1322  GLY C 1344  1                                  23    
HELIX   83 AJ2 SER C 1384  PHE C 1399  1                                  16    
HELIX   84 AJ3 ASP C 1400  GLU C 1406  1                                   7    
HELIX   85 AJ4 THR C 1410  PHE C 1421  1                                  12    
HELIX   86 AJ5 THR C 1423  SER C 1444  1                                  22    
HELIX   87 AJ6 LEU C 1451  ALA C 1456  1                                   6    
HELIX   88 AJ7 SER D  158  SER D  163  1                                   6    
HELIX   89 AJ8 LYS D  212  TYR D  235  1                                  24    
HELIX   90 AJ9 ASP D  275  SER D  280  1                                   6    
HELIX   91 AK1 GLU D  332  ASP D  336  5                                   5    
HELIX   92 AK2 TYR D  357  ARG D  371  1                                  15    
HELIX   93 AK3 HIS D  386  ASN D  391  1                                   6    
HELIX   94 AK4 PRO D  397  GLY D  412  1                                  16    
HELIX   95 AK5 GLU D  448  GLN D  452  1                                   5    
HELIX   96 AK6 ASP D  475  GLY D  481  1                                   7    
HELIX   97 AK7 ASP D  493  ARG D  506  1                                  14    
HELIX   98 AK8 ASP D  521  ALA D  529  1                                   9    
HELIX   99 AK9 GLU E    8  LEU E   20  1                                  13    
HELIX  100 AL1 PRO E   22  TYR E   32  1                                  11    
HELIX  101 AL2 GLY E   33  VAL E   35  5                                   3    
HELIX  102 AL3 LYS E   50  ASP E   52  5                                   3    
HELIX  103 AL4 ASN E   62  LYS E   72  1                                  11    
HELIX  104 AL5 ARG E   87  HIS E   91  5                                   5    
HELIX  105 AL6 THR E  113  ASP E  116  5                                   4    
HELIX  106 AL7 TRP E  132  ASP E  149  1                                  18    
HELIX  107 AL8 ASP E  171  LYS E  176  1                                   6    
HELIX  108 AL9 SER E  178  SER E  190  1                                  13    
HELIX  109 AM1 HIS E  209  ALA E  227  1                                  19    
HELIX  110 AM2 ASN E  236  ALA E  245  1                                  10    
HELIX  111 AM3 ILE E  251  LYS E  261  1                                  11    
HELIX  112 AM4 ASN E  264  ILE E  283  1                                  20    
HELIX  113 AM5 TRP E  291  PHE E  302  1                                  12    
HELIX  114 AM6 ASP E  306  GLY E  312  1                                   7    
HELIX  115 AM7 THR E  349  GLU E  356  1                                   8    
HELIX  116 AM8 LEU E  388  LEU E  410  1                                  23    
HELIX  117 AM9 LEU F   39  TYR F   63  1                                  25    
HELIX  118 AN1 THR F   67  LEU F   81  1                                  15    
HELIX  119 AN2 TYR F   93  LEU F  106  1                                  14    
HELIX  120 AN3 ARG F  107  GLN F  112  5                                   6    
HELIX  121 AN4 SER F  113  GLU F  124  1                                  12    
HELIX  122 AN5 MET F  125  ILE F  134  1                                  10    
HELIX  123 AN6 ASP F  138  SER F  147  1                                  10    
HELIX  124 AN7 SER F  155  ARG F  162  1                                   8    
HELIX  125 AN8 ARG F  162  SER F  170  1                                   9    
HELIX  126 AN9 ALA F  191  ARG F  196  1                                   6    
HELIX  127 AO1 PRO F  210  SER F  236  1                                  27    
HELIX  128 AO2 LEU F  246  ASN F  251  1                                   6    
HELIX  129 AO3 GLN F  275  SER F  283  1                                   9    
HELIX  130 AO4 PRO F  285  ASN F  298  1                                  14    
HELIX  131 AO5 ARG F  302  ILE F  316  1                                  15    
HELIX  132 AO6 THR F  319  ILE F  332  1                                  14    
HELIX  133 AO7 ASP F  337  TYR F  345  1                                   9    
HELIX  134 AO8 TYR F  345  GLY F  354  1                                  10    
HELIX  135 AO9 SER F  366  SER F  373  1                                   8    
HELIX  136 AP1 CYS F  384  SER F  389  1                                   6    
HELIX  137 AP2 ASP F  390  TYR F  401  1                                  12    
HELIX  138 AP3 SER F  404  LYS F  416  1                                  13    
HELIX  139 AP4 HIS F  419  ASN F  433  1                                  15    
HELIX  140 AP5 HIS F  443  ILE F  454  1                                  12    
HELIX  141 AP6 GLU G  368  GLU G  371  5                                   4    
HELIX  142 AP7 SER G  409  ILE G  421  1                                  13    
HELIX  143 AP8 ALA G  422  LYS G  426  5                                   5    
HELIX  144 AP9 SER G  482  ARG G  491  1                                  10    
HELIX  145 AQ1 LYS G  522  VAL G  526  5                                   5    
HELIX  146 AQ2 ALA G  597  LYS G  605  1                                   9    
HELIX  147 AQ3 THR G  614  ASP G  630  1                                  17    
HELIX  148 AQ4 PHE G  642  CYS G  654  1                                  13    
HELIX  149 AQ5 HIS G  658  GLY G  663  5                                   6    
HELIX  150 AQ6 VAL G  693  GLU G  699  1                                   7    
HELIX  151 AQ7 HIS G  707  ILE G  715  1                                   9    
HELIX  152 AQ8 ILE G  728  TYR G  732  5                                   5    
HELIX  153 AQ9 GLU G  734  LEU G  759  1                                  26    
HELIX  154 AR1 ASN G  760  GLY G  773  1                                  14    
HELIX  155 AR2 ILE G  775  GLY G  782  1                                   8    
HELIX  156 AR3 GLY G  783  ASN G  799  1                                  17    
HELIX  157 AR4 SER G  863  PHE G  872  1                                  10    
HELIX  158 AR5 GLY G  909  MET G  929  1                                  21    
HELIX  159 AR6 ASP G  937  CYS G  959  1                                  23    
HELIX  160 AR7 ALA G  969  LYS G  993  1                                  25    
HELIX  161 AR8 ASN G 1014  TYR G 1033  1                                  20    
HELIX  162 AR9 CYS G 1085  LEU G 1100  1                                  16    
HELIX  163 AS1 SER G 1104  GLY G 1126  1                                  23    
HELIX  164 AS2 PRO G 1129  GLU G 1134  5                                   6    
HELIX  165 AS3 ASP G 1148  SER G 1151  5                                   4    
HELIX  166 AS4 LEU G 1152  GLY G 1165  1                                  14    
HELIX  167 AS5 THR G 1187  GLN G 1190  5                                   4    
HELIX  168 AS6 ALA G 1194  LYS G 1200  1                                   7    
HELIX  169 AS7 ASP G 1207  GLN G 1215  1                                   9    
HELIX  170 AS8 GLN G 1215  GLU G 1225  1                                  11    
HELIX  171 AS9 ASP G 1231  LEU G 1239  1                                   9    
HELIX  172 AT1 ASP G 1242  HIS G 1250  1                                   9    
HELIX  173 AT2 THR G 1268  TYR G 1273  1                                   6    
HELIX  174 AT3 SER G 1318  THR G 1321  5                                   4    
HELIX  175 AT4 PHE G 1322  GLY G 1344  1                                  23    
HELIX  176 AT5 SER G 1384  PHE G 1399  1                                  16    
HELIX  177 AT6 ASP G 1400  GLU G 1406  1                                   7    
HELIX  178 AT7 THR G 1410  PHE G 1421  1                                  12    
HELIX  179 AT8 THR G 1423  SER G 1444  1                                  22    
HELIX  180 AT9 LEU G 1451  ALA G 1456  1                                   6    
HELIX  181 AU1 SER H  158  SER H  163  1                                   6    
HELIX  182 AU2 LYS H  212  TYR H  235  1                                  24    
HELIX  183 AU3 ASP H  275  SER H  280  1                                   6    
HELIX  184 AU4 GLU H  332  ASP H  336  5                                   5    
HELIX  185 AU5 TYR H  357  ARG H  371  1                                  15    
HELIX  186 AU6 HIS H  386  ASN H  391  1                                   6    
HELIX  187 AU7 PRO H  397  THR H  413  1                                  17    
HELIX  188 AU8 GLU H  448  GLN H  452  1                                   5    
HELIX  189 AU9 ASP H  475  GLY H  481  1                                   7    
HELIX  190 AV1 ALA H  482  GLU H  484  5                                   3    
HELIX  191 AV2 ASP H  493  ARG H  506  1                                  14    
HELIX  192 AV3 ASP H  521  ALA H  529  1                                   9    
SHEET    1 AA1 4 TYR A  54  GLN A  58  0                                        
SHEET    2 AA1 4 ARG A  43  THR A  48 -1  N  PHE A  47   O  ILE A  55           
SHEET    3 AA1 4 LYS A  77  TYR A  84 -1  O  GLY A  81   N  GLU A  44           
SHEET    4 AA1 4 ALA A 101  GLU A 103 -1  O  GLU A 103   N  VAL A  83           
SHEET    1 AA2 4 TYR A  54  GLN A  58  0                                        
SHEET    2 AA2 4 ARG A  43  THR A  48 -1  N  PHE A  47   O  ILE A  55           
SHEET    3 AA2 4 LYS A  77  TYR A  84 -1  O  GLY A  81   N  GLU A  44           
SHEET    4 AA2 4 LEU A 317  LYS A 318 -1  O  LEU A 317   N  ILE A  80           
SHEET    1 AA3 3 LEU A 106  ASP A 111  0                                        
SHEET    2 AA3 3 GLY A 164  VAL A 169 -1  O  VAL A 165   N  ILE A 110           
SHEET    3 AA3 3 ARG A 155  TYR A 159 -1  N  LEU A 156   O  TRP A 168           
SHEET    1 AA4 2 ASN B  36  SER B  38  0                                        
SHEET    2 AA4 2 GLU C1448  ASN C1450 -1  O  VAL C1449   N  ILE B  37           
SHEET    1 AA5 4 GLU B 152  ALA B 153  0                                        
SHEET    2 AA5 4 TYR B 184  PRO B 187 -1  O  LYS B 185   N  GLU B 152           
SHEET    3 AA5 4 PHE B 206  VAL B 209 -1  O  ALA B 207   N  ILE B 186           
SHEET    4 AA5 4 TYR B 201  LEU B 202 -1  N  TYR B 201   O  TYR B 208           
SHEET    1 AA6 5 TRP C 498  LYS C 502  0                                        
SHEET    2 AA6 5 VAL C 340  ASP C 351 -1  N  PHE C 341   O  VAL C 501           
SHEET    3 AA6 5 GLN C 355  TRP C 366 -1  O  PHE C 360   N  TYR C 349           
SHEET    4 AA6 5 HIS C 373  LYS C 381 -1  O  VAL C 378   N  LEU C 361           
SHEET    5 AA6 5 GLU C 517  ALA C 520  1  O  ALA C 520   N  MET C 379           
SHEET    1 AA7 4 LYS C 431  ASN C 438  0                                        
SHEET    2 AA7 4 LYS C 449  TYR C 457 -1  O  LYS C 456   N  LYS C 431           
SHEET    3 AA7 4 ARG C 385  PRO C 391 -1  N  LEU C 387   O  VAL C 455           
SHEET    4 AA7 4 PHE C 473  PHE C 477 -1  O  HIS C 475   N  LEU C 390           
SHEET    1 AA8 2 MET C 394  ASP C 397  0                                        
SHEET    2 AA8 2 LYS C 402  PRO C 407 -1  O  LYS C 402   N  ASP C 397           
SHEET    1 AA9 5 VAL C 585  VAL C 586  0                                        
SHEET    2 AA9 5 ASN C 555  PHE C 568 -1  N  MET C 560   O  VAL C 585           
SHEET    3 AA9 5 LEU C 537  GLN C 548 -1  N  LEU C 537   O  PHE C 568           
SHEET    4 AA9 5 ILE C 633  GLY C 636  1  O  VAL C 635   N  MET C 540           
SHEET    5 AA9 5 MET C 689  ASP C 692  1  O  MET C 689   N  ILE C 634           
SHEET    1 AB1 4 GLY C 850  TYR C 852  0                                        
SHEET    2 AB1 4 PHE C1044  LYS C1051 -1  O  LEU C1049   N  GLY C 850           
SHEET    3 AB1 4 LYS C1054  VAL C1060 -1  O  ALA C1056   N  LEU C1048           
SHEET    4 AB1 4 THR C1070  LYS C1075 -1  O  LYS C1071   N  VAL C1059           
SHEET    1 AB2 4 TYR C1000  ASP C1002  0                                        
SHEET    2 AB2 4 SER C1005  MET C1007 -1  N  SER C1005   O  ASP C1002           
SHEET    3 AB2 4 LEU C 859  PHE C 861 -1  N  LEU C 859   O  ILE C1006           
SHEET    4 AB2 4 ILE C1038  ASP C1039 -1  O  ASP C1039   N  ASP C 860           
SHEET    1 AB3 3 ILE C1135  ALA C1138  0                                        
SHEET    2 AB3 3 THR C1174  GLN C1181 -1  O  TYR C1177   N  ILE C1135           
SHEET    3 AB3 3 ALA C1192  TYR C1193 -1  O  TYR C1193   N  VAL C1178           
SHEET    1 AB4 3 ILE C1135  ALA C1138  0                                        
SHEET    2 AB4 3 THR C1174  GLN C1181 -1  O  TYR C1177   N  ILE C1135           
SHEET    3 AB4 3 THR C1205  ILE C1206 -1  O  THR C1205   N  GLN C1181           
SHEET    1 AB5 2 PHE C1279  PRO C1282  0                                        
SHEET    2 AB5 2 GLU C1289  TYR C1292 -1  O  TYR C1292   N  PHE C1279           
SHEET    1 AB6 2 PHE C1296  ASP C1297  0                                        
SHEET    2 AB6 2 GLU C1304  PRO C1305 -1  O  GLU C1304   N  ASP C1297           
SHEET    1 AB7 3 ARG C1356  THR C1357  0                                        
SHEET    2 AB7 3 LEU C1346  CYS C1348 -1  N  LEU C1346   O  THR C1357           
SHEET    3 AB7 3 LEU C1379  PRO C1381 -1  O  GLN C1380   N  ILE C1347           
SHEET    1 AB8 7 VAL D 170  PHE D 174  0                                        
SHEET    2 AB8 7 CYS D 590  ARG D 597 -1  O  VAL D 593   N  PHE D 174           
SHEET    3 AB8 7 THR D 570  LEU D 576 -1  N  PHE D 571   O  VAL D 596           
SHEET    4 AB8 7 SER D 340  CYS D 346 -1  N  SER D 340   O  LEU D 576           
SHEET    5 AB8 7 VAL D 374  PHE D 378  1  O  VAL D 374   N  LEU D 343           
SHEET    6 AB8 7 HIS D 419  VAL D 423  1  O  VAL D 423   N  LEU D 377           
SHEET    7 AB8 7 VAL D 453  PHE D 455  1  O  GLN D 454   N  LEU D 420           
SHEET    1 AB9 6 LEU D 193  LEU D 196  0                                        
SHEET    2 AB9 6 CYS D 460  ILE D 464 -1  O  SER D 463   N  LYS D 194           
SHEET    3 AB9 6 ILE D 468  LEU D 471 -1  O  LEU D 471   N  CYS D 460           
SHEET    4 AB9 6 VAL D 537  ILE D 539  1  N  VAL D 537   O  ILE D 468           
SHEET    5 AB9 6 CYS D 554  ASN D 558  1  O  VAL D 557   N  LEU D 538           
SHEET    6 AB9 6 PHE D 547  VAL D 551 -1  N  VAL D 551   O  CYS D 554           
SHEET    1 AC1 6 VAL D 251  GLN D 256  0                                        
SHEET    2 AC1 6 ILE D 271  GLY D 274 -1  O  GLU D 273   N  GLN D 256           
SHEET    3 AC1 6 GLN D 283  ASP D 287 -1  O  ILE D 284   N  LEU D 272           
SHEET    4 AC1 6 LEU D 314  LEU D 319  1  O  LEU D 314   N  ASP D 287           
SHEET    5 AC1 6 VAL D 301  ILE D 307 -1  N  GLU D 305   O  THR D 317           
SHEET    6 AC1 6 VAL D 251  GLN D 256 -1  N  VAL D 251   O  GLY D 306           
SHEET    1 AC2 2 SER D 295  LEU D 296  0                                        
SHEET    2 AC2 2 ILE D 485  SER D 486 -1  O  ILE D 485   N  LEU D 296           
SHEET    1 AC3 2 THR D 563  LYS D 564  0                                        
SHEET    2 AC3 2 VAL D 567  GLY D 568 -1  O  VAL D 567   N  LYS D 564           
SHEET    1 AC4 4 TYR E  54  GLN E  58  0                                        
SHEET    2 AC4 4 ARG E  43  THR E  48 -1  N  PHE E  47   O  ILE E  55           
SHEET    3 AC4 4 LYS E  77  TYR E  84 -1  O  ALA E  82   N  GLU E  44           
SHEET    4 AC4 4 ALA E 101  GLU E 103 -1  O  GLU E 103   N  VAL E  83           
SHEET    1 AC5 4 TYR E  54  GLN E  58  0                                        
SHEET    2 AC5 4 ARG E  43  THR E  48 -1  N  PHE E  47   O  ILE E  55           
SHEET    3 AC5 4 LYS E  77  TYR E  84 -1  O  ALA E  82   N  GLU E  44           
SHEET    4 AC5 4 LEU E 317  LYS E 318 -1  O  LEU E 317   N  ILE E  80           
SHEET    1 AC6 3 LEU E 106  ASP E 111  0                                        
SHEET    2 AC6 3 GLY E 164  VAL E 169 -1  O  VAL E 165   N  ILE E 110           
SHEET    3 AC6 3 ARG E 155  TYR E 159 -1  N  LEU E 156   O  TRP E 168           
SHEET    1 AC7 2 ASN F  36  SER F  38  0                                        
SHEET    2 AC7 2 GLU G1448  ASN G1450 -1  O  VAL G1449   N  ILE F  37           
SHEET    1 AC8 4 GLU F 152  ALA F 153  0                                        
SHEET    2 AC8 4 TYR F 184  PRO F 187 -1  O  LYS F 185   N  GLU F 152           
SHEET    3 AC8 4 PHE F 206  VAL F 209 -1  O  ALA F 207   N  ILE F 186           
SHEET    4 AC8 4 TYR F 201  LEU F 202 -1  N  TYR F 201   O  TYR F 208           
SHEET    1 AC9 5 TRP G 498  LYS G 502  0                                        
SHEET    2 AC9 5 VAL G 340  ASP G 351 -1  N  PHE G 341   O  VAL G 501           
SHEET    3 AC9 5 GLN G 355  TRP G 366 -1  O  PHE G 360   N  TYR G 349           
SHEET    4 AC9 5 HIS G 373  LYS G 381 -1  O  VAL G 378   N  LEU G 361           
SHEET    5 AC9 5 GLU G 517  ALA G 520  1  O  ALA G 520   N  MET G 379           
SHEET    1 AD1 4 LYS G 431  ASN G 438  0                                        
SHEET    2 AD1 4 LYS G 449  TYR G 457 -1  O  LYS G 456   N  LYS G 431           
SHEET    3 AD1 4 ARG G 385  PRO G 391 -1  N  LEU G 387   O  VAL G 455           
SHEET    4 AD1 4 PHE G 473  PHE G 477 -1  O  HIS G 475   N  LEU G 390           
SHEET    1 AD2 2 MET G 394  ASP G 397  0                                        
SHEET    2 AD2 2 LYS G 402  PRO G 407 -1  O  LYS G 402   N  ASP G 397           
SHEET    1 AD3 4 ASN G 555  PHE G 568  0                                        
SHEET    2 AD3 4 LEU G 537  GLN G 548 -1  N  LEU G 537   O  PHE G 568           
SHEET    3 AD3 4 ILE G 633  GLY G 636  1  O  VAL G 635   N  MET G 540           
SHEET    4 AD3 4 MET G 689  ASP G 692  1  O  MET G 689   N  ILE G 634           
SHEET    1 AD4 4 GLY G 850  TYR G 852  0                                        
SHEET    2 AD4 4 PHE G1044  LYS G1051 -1  O  LEU G1049   N  GLY G 850           
SHEET    3 AD4 4 LYS G1054  VAL G1060 -1  O  LEU G1058   N  LYS G1045           
SHEET    4 AD4 4 THR G1070  LYS G1075 -1  O  LYS G1071   N  VAL G1059           
SHEET    1 AD5 4 TYR G1000  ASP G1002  0                                        
SHEET    2 AD5 4 SER G1005  MET G1007 -1  N  SER G1005   O  ASP G1002           
SHEET    3 AD5 4 LEU G 859  PHE G 861 -1  N  LEU G 859   O  ILE G1006           
SHEET    4 AD5 4 ILE G1038  ASP G1039 -1  O  ASP G1039   N  ASP G 860           
SHEET    1 AD6 3 ILE G1135  ALA G1138  0                                        
SHEET    2 AD6 3 THR G1174  ILE G1179 -1  O  TYR G1177   N  ILE G1135           
SHEET    3 AD6 3 ALA G1192  TYR G1193 -1  O  TYR G1193   N  VAL G1178           
SHEET    1 AD7 2 PHE G1279  PRO G1282  0                                        
SHEET    2 AD7 2 GLU G1289  TYR G1292 -1  O  TYR G1292   N  PHE G1279           
SHEET    1 AD8 2 PHE G1296  ASP G1297  0                                        
SHEET    2 AD8 2 GLU G1304  PRO G1305 -1  O  GLU G1304   N  ASP G1297           
SHEET    1 AD9 3 ARG G1356  THR G1357  0                                        
SHEET    2 AD9 3 LEU G1346  CYS G1348 -1  N  LEU G1346   O  THR G1357           
SHEET    3 AD9 3 LEU G1379  PRO G1381 -1  O  GLN G1380   N  ILE G1347           
SHEET    1 AE1 7 VAL H 170  PHE H 174  0                                        
SHEET    2 AE1 7 CYS H 590  ARG H 597 -1  O  VAL H 593   N  PHE H 174           
SHEET    3 AE1 7 THR H 570  LEU H 576 -1  N  PHE H 571   O  VAL H 596           
SHEET    4 AE1 7 SER H 340  CYS H 346 -1  N  SER H 340   O  LEU H 576           
SHEET    5 AE1 7 VAL H 374  PHE H 378  1  O  VAL H 374   N  LEU H 343           
SHEET    6 AE1 7 HIS H 419  VAL H 423  1  O  VAL H 423   N  LEU H 377           
SHEET    7 AE1 7 VAL H 453  PHE H 455  1  O  GLN H 454   N  LEU H 420           
SHEET    1 AE2 6 LEU H 193  LEU H 196  0                                        
SHEET    2 AE2 6 CYS H 460  ILE H 464 -1  O  SER H 463   N  LYS H 194           
SHEET    3 AE2 6 ILE H 468  LEU H 471 -1  O  LEU H 471   N  CYS H 460           
SHEET    4 AE2 6 VAL H 537  ILE H 539  1  N  VAL H 537   O  ILE H 468           
SHEET    5 AE2 6 CYS H 554  ASN H 558  1  O  VAL H 557   N  LEU H 538           
SHEET    6 AE2 6 PHE H 547  VAL H 551 -1  N  VAL H 551   O  CYS H 554           
SHEET    1 AE3 6 VAL H 251  GLN H 256  0                                        
SHEET    2 AE3 6 ILE H 271  GLY H 274 -1  O  GLU H 273   N  GLN H 256           
SHEET    3 AE3 6 GLN H 283  ASP H 287 -1  O  ILE H 284   N  LEU H 272           
SHEET    4 AE3 6 LEU H 314  LEU H 319  1  O  LEU H 314   N  ASP H 287           
SHEET    5 AE3 6 VAL H 301  ILE H 307 -1  N  GLU H 305   O  THR H 317           
SHEET    6 AE3 6 VAL H 251  GLN H 256 -1  N  VAL H 251   O  GLY H 306           
SHEET    1 AE4 2 SER H 295  LEU H 296  0                                        
SHEET    2 AE4 2 ILE H 485  SER H 486 -1  O  ILE H 485   N  LEU H 296           
SHEET    1 AE5 2 THR H 563  LYS H 564  0                                        
SHEET    2 AE5 2 VAL H 567  GLY H 568 -1  O  VAL H 567   N  LYS H 564           
SSBOND   1 CYS C 1348    CYS C 1353                          1555   1555  2.92  
SSBOND   2 CYS E  122    CYS E  131                          1555   1555  2.79  
SSBOND   3 CYS G 1348    CYS G 1353                          1555   1555  2.98  
LINK         SG  CYS A 121                ZN    ZN A 501     1555   1555  2.32  
LINK         SG  CYS A 122                ZN    ZN A 501     1555   1555  2.28  
LINK         SG  CYS A 128                ZN    ZN A 501     1555   1555  2.27  
LINK         SG  CYS A 131                ZN    ZN A 501     1555   1555  2.34  
LINK         SG  CYS B 287                FE4  SF4 B 601     1555   1555  2.21  
LINK         SG  CYS B 367                FE1  SF4 B 601     1555   1555  2.42  
LINK         SG  CYS C1283                ZN    ZN C1501     1555   1555  2.48  
LINK         SG  CYS C1286                ZN    ZN C1501     1555   1555  2.38  
LINK         SG  CYS C1310                ZN    ZN C1501     1555   1555  2.24  
LINK         SG  CYS C1315                ZN    ZN C1501     1555   1555  2.36  
LINK         SG  CYS C1348                ZN    ZN C1502     1555   1555  2.20  
LINK         SG  CYS C1353                ZN    ZN C1502     1555   1555  2.37  
LINK         SG  CYS C1371                ZN    ZN C1502     1555   1555  2.31  
LINK         SG  CYS E 121                ZN    ZN E 501     1555   1555  2.33  
LINK         SG  CYS E 122                ZN    ZN E 501     1555   1555  2.29  
LINK         SG  CYS E 128                ZN    ZN E 501     1555   1555  2.30  
LINK         SG  CYS E 131                ZN    ZN E 501     1555   1555  2.29  
LINK         SG  CYS F 287                FE4  SF4 F 601     1555   1555  2.24  
LINK         SG  CYS F 367                FE1  SF4 F 601     1555   1555  2.37  
LINK         SG  CYS G1286                ZN    ZN G1501     1555   1555  2.34  
LINK         SG  CYS G1310                ZN    ZN G1501     1555   1555  2.12  
LINK         SG  CYS G1315                ZN    ZN G1501     1555   1555  2.76  
LINK         SG  CYS G1348                ZN    ZN G1502     1555   1555  2.01  
LINK         SG  CYS G1353                ZN    ZN G1502     1555   1555  2.42  
LINK         SG  CYS G1371                ZN    ZN G1502     1555   1555  2.44  
CISPEP   1 LYS C  576    PRO C  577          0        -0.62                     
CISPEP   2 GLY D  347    PRO D  348          0        -0.95                     
CISPEP   3 GLY D  379    PRO D  380          0         2.16                     
CISPEP   4 TYR D  435    PRO D  436          0        -0.38                     
CISPEP   5 GLU D  458    PRO D  459          0         0.03                     
CISPEP   6 TYR D  512    PRO D  513          0         0.79                     
CISPEP   7 LYS G  576    PRO G  577          0        -0.44                     
CISPEP   8 GLY H  347    PRO H  348          0        -0.11                     
CISPEP   9 GLY H  379    PRO H  380          0        -0.50                     
CISPEP  10 TYR H  435    PRO H  436          0        -0.92                     
CISPEP  11 GLU H  458    PRO H  459          0        -0.34                     
CISPEP  12 TYR H  512    PRO H  513          0        -0.59                     
SITE     1 AC1  4 CYS A 121  CYS A 122  CYS A 128  CYS A 131                    
SITE     1 AC2  7 PRO B 285  CYS B 287  CYS B 367  CYS B 384                    
SITE     2 AC2  7 GLN B 421  CYS B 424  PRO B 444                               
SITE     1 AC3  4 CYS C1283  CYS C1286  CYS C1310  CYS C1315                    
SITE     1 AC4  4 CYS C1348  CYS C1353  CYS C1371  ALA C1377                    
SITE     1 AC5  4 CYS E 121  CYS E 122  CYS E 128  CYS E 131                    
SITE     1 AC6  7 PRO F 285  PRO F 286  CYS F 287  CYS F 367                    
SITE     2 AC6  7 CYS F 384  CYS F 424  PRO F 444                               
SITE     1 AC7  5 CYS G1283  CYS G1286  CYS G1310  ASN G1312                    
SITE     2 AC7  5 CYS G1315                                                     
SITE     1 AC8  5 CYS G1348  CYS G1353  CYS G1371  CYS G1374                    
SITE     2 AC8  5 ALA G1377                                                     
CRYST1  113.096  210.164  172.565  90.00  93.56  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      0.008842  0.000000  0.000551        0.00000                         
SCALE2      0.000000  0.004758  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005806        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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