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Database: PDB
Entry: 2E1Q
LinkDB: 2E1Q
Original site: 2E1Q 
HEADER    OXIDOREDUCTASE                          27-OCT-06   2E1Q              
TITLE     CRYSTAL STRUCTURE OF HUMAN XANTHINE OXIDOREDUCTASE MUTANT, GLU803VAL  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: XANTHINE DEHYDROGENASE/OXIDASE;                            
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: XANTHINE DEHYDROGENASE, XD, XANTHINE OXIDASE, XO, XANTHINE  
COMPND   5 OXIDOREDUCTASE;                                                      
COMPND   6 EC: 1.17.1.4, 1.17.3.2;                                              
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: TP1000;                                    
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTRC99A                                   
KEYWDS    XANTHINE OXIDASE, MOLYBDENUM COFACTOR, FAD, OXIDOREDUCTASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.YAMAGUCHI,T.MATSUMURA,K.ICHIDA,K.OKAMOTO,T.NISHINO                  
REVDAT   3   13-JUL-11 2E1Q    1       VERSN                                    
REVDAT   2   24-FEB-09 2E1Q    1       VERSN                                    
REVDAT   1   18-SEP-07 2E1Q    0                                                
JRNL        AUTH   Y.YAMAGUCHI,T.MATSUMURA,K.ICHIDA,K.OKAMOTO,T.NISHINO         
JRNL        TITL   HUMAN XANTHINE OXIDASE CHANGES ITS SUBSTRATE SPECIFICITY TO  
JRNL        TITL 2 ALDEHYDE OXIDASE TYPE UPON MUTATION OF AMINO ACID RESIDUES   
JRNL        TITL 3 IN THE ACTIVE SITE: ROLES OF ACTIVE SITE RESIDUES IN BINDING 
JRNL        TITL 4 AND ACTIVATION OF PURINE SUBSTRATE                           
JRNL        REF    J.BIOCHEM.(TOKYO)             V. 141   513 2007              
JRNL        REFN                   ISSN 0021-924X                               
JRNL        PMID   17301077                                                     
JRNL        DOI    10.1093/JB/MVM053                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 192029                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 3840                            
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           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 40352                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 420                                     
REMARK   3   SOLVENT ATOMS            : 949                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2E1Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-NOV-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB026116.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 192029                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1FO4                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% PEG 8000, 0.05M SODIUM CITRATE, PH    
REMARK 280  5.0, VAPOR DIFFUSION, TEMPERATURE 293K                              
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       70.47200            
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: THE BIOLOGICAL ASSEMBLY IS A HOMODIMER.                      
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 12280 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 84500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -141.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 12310 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 84620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -159.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     GLY A   168                                                      
REMARK 465     CYS A   169                                                      
REMARK 465     CYS A   170                                                      
REMARK 465     GLY A   171                                                      
REMARK 465     GLY A   172                                                      
REMARK 465     ASP A   173                                                      
REMARK 465     GLY A   174                                                      
REMARK 465     ASN A   175                                                      
REMARK 465     ASN A   176                                                      
REMARK 465     PRO A   177                                                      
REMARK 465     ASN A   178                                                      
REMARK 465     CYS A   179                                                      
REMARK 465     CYS A   180                                                      
REMARK 465     MET A   181                                                      
REMARK 465     ASN A   182                                                      
REMARK 465     GLN A   183                                                      
REMARK 465     LYS A   184                                                      
REMARK 465     LYS A   185                                                      
REMARK 465     ASP A   186                                                      
REMARK 465     HIS A   187                                                      
REMARK 465     SER A   188                                                      
REMARK 465     VAL A   189                                                      
REMARK 465     SER A   190                                                      
REMARK 465     LEU A   191                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     GLY B   168                                                      
REMARK 465     CYS B   169                                                      
REMARK 465     CYS B   170                                                      
REMARK 465     GLY B   171                                                      
REMARK 465     GLY B   172                                                      
REMARK 465     ASP B   173                                                      
REMARK 465     GLY B   174                                                      
REMARK 465     ASN B   175                                                      
REMARK 465     ASN B   176                                                      
REMARK 465     PRO B   177                                                      
REMARK 465     ASN B   178                                                      
REMARK 465     CYS B   179                                                      
REMARK 465     CYS B   180                                                      
REMARK 465     MET B   181                                                      
REMARK 465     ASN B   182                                                      
REMARK 465     GLN B   183                                                      
REMARK 465     LYS B   184                                                      
REMARK 465     LYS B   185                                                      
REMARK 465     ASP B   186                                                      
REMARK 465     HIS B   187                                                      
REMARK 465     SER B   188                                                      
REMARK 465     VAL B   189                                                      
REMARK 465     SER B   190                                                      
REMARK 465     LEU B   191                                                      
REMARK 465     MET C     1                                                      
REMARK 465     THR C     2                                                      
REMARK 465     GLY C   168                                                      
REMARK 465     CYS C   169                                                      
REMARK 465     CYS C   170                                                      
REMARK 465     GLY C   171                                                      
REMARK 465     GLY C   172                                                      
REMARK 465     ASP C   173                                                      
REMARK 465     GLY C   174                                                      
REMARK 465     ASN C   175                                                      
REMARK 465     ASN C   176                                                      
REMARK 465     PRO C   177                                                      
REMARK 465     ASN C   178                                                      
REMARK 465     CYS C   179                                                      
REMARK 465     CYS C   180                                                      
REMARK 465     MET C   181                                                      
REMARK 465     ASN C   182                                                      
REMARK 465     GLN C   183                                                      
REMARK 465     LYS C   184                                                      
REMARK 465     LYS C   185                                                      
REMARK 465     ASP C   186                                                      
REMARK 465     HIS C   187                                                      
REMARK 465     SER C   188                                                      
REMARK 465     VAL C   189                                                      
REMARK 465     SER C   190                                                      
REMARK 465     LEU C   191                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     GLY D   168                                                      
REMARK 465     CYS D   169                                                      
REMARK 465     CYS D   170                                                      
REMARK 465     GLY D   171                                                      
REMARK 465     GLY D   172                                                      
REMARK 465     ASP D   173                                                      
REMARK 465     GLY D   174                                                      
REMARK 465     ASN D   175                                                      
REMARK 465     ASN D   176                                                      
REMARK 465     PRO D   177                                                      
REMARK 465     ASN D   178                                                      
REMARK 465     CYS D   179                                                      
REMARK 465     CYS D   180                                                      
REMARK 465     MET D   181                                                      
REMARK 465     ASN D   182                                                      
REMARK 465     GLN D   183                                                      
REMARK 465     LYS D   184                                                      
REMARK 465     LYS D   185                                                      
REMARK 465     ASP D   186                                                      
REMARK 465     HIS D   187                                                      
REMARK 465     SER D   188                                                      
REMARK 465     VAL D   189                                                      
REMARK 465     SER D   190                                                      
REMARK 465     LEU D   191                                                      
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 D 410   C   -  N   -  CA  ANGL. DEV. =  11.5 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    ASP A   4      -79.99     80.37                                   
REMARK 500    CYS A  43      -21.74   -160.93                                   
REMARK 500    SER A  93      158.36    177.99                                   
REMARK 500    THR A  96      -91.79   -119.08                                   
REMARK 500    GLN A 112      -86.74    -98.23                                   
REMARK 500    TYR A 153      -44.15     70.16                                   
REMARK 500    ALA A 255      123.38    -37.67                                   
REMARK 500    VAL A 259      -79.77   -118.73                                   
REMARK 500    ASN A 272       68.22     37.66                                   
REMARK 500    ALA A 338     -129.72     46.54                                   
REMARK 500    ALA A 424     -144.29   -134.30                                   
REMARK 500    ASP A 429       80.75     26.18                                   
REMARK 500    PRO A 444      125.53    -39.01                                   
REMARK 500    THR A 446     -167.38   -113.42                                   
REMARK 500    ALA A 460     -165.93   -178.44                                   
REMARK 500    ARG A 462     -170.01   -171.50                                   
REMARK 500    GLU A 533       28.88    -68.74                                   
REMARK 500    HIS A 615      119.47   -171.41                                   
REMARK 500    SER A 624      -53.38    -24.14                                   
REMARK 500    ASP A 659      -26.80     67.27                                   
REMARK 500    CYS A 663      148.34    179.61                                   
REMARK 500    GLN A 740      141.47   -170.64                                   
REMARK 500    ALA A 758       28.96     44.44                                   
REMARK 500    PHE A 799       22.57     47.91                                   
REMARK 500    THR A 804      -41.86   -143.41                                   
REMARK 500    ASP A 873     -120.74     45.31                                   
REMARK 500    ASN A 888     -104.03     67.55                                   
REMARK 500    THR A 910     -153.48   -152.43                                   
REMARK 500    ARG A 913      111.26    -22.48                                   
REMARK 500    SER A1009      152.48    127.53                                   
REMARK 500    SER A1081       -2.27     71.78                                   
REMARK 500    CYS A1167       -8.94    -57.24                                   
REMARK 500    THR A1208      -16.71   -144.27                                   
REMARK 500    ASP A1247       76.79     37.08                                   
REMARK 500    CYS A1248       55.84   -155.02                                   
REMARK 500    VAL A1260       -7.53   -151.86                                   
REMARK 500    PRO A1263      -51.11    -27.39                                   
REMARK 500    THR A1287       77.79   -151.27                                   
REMARK 500    ASN A1289      176.38    170.43                                   
REMARK 500    ASN A1290       79.19    167.19                                   
REMARK 500    VAL A1319      103.25   -161.80                                   
REMARK 500    VAL A1322       79.69     84.87                                   
REMARK 500    PRO A1323     -177.44    -55.74                                   
REMARK 500    ASN A1325        0.45    -64.03                                   
REMARK 500    ASP B   4      -56.14     57.44                                   
REMARK 500    CYS B  43      -24.12   -156.20                                   
REMARK 500    THR B  96      -88.88   -129.01                                   
REMARK 500    GLN B 112      -95.64   -107.07                                   
REMARK 500    TYR B 153      -25.73     65.90                                   
REMARK 500    ASP B 166     -167.81   -108.02                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     172 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 A1105         0.09    SIDE CHAIN                              
REMARK 500    TYR C1105         0.06    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                             FES A2001  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 113   SG                                                     
REMARK 620 2 FES A2001   S1  123.3                                              
REMARK 620 3 FES A2001   S2  112.1 102.1                                        
REMARK 620 4 CYS A 150   SG  100.8 106.9 111.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES A2001  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 116   SG                                                     
REMARK 620 2 FES A2001   S1  125.3                                              
REMARK 620 3 FES A2001   S2  110.1 104.5                                        
REMARK 620 4 CYS A 148   SG  103.0 105.8 106.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES A2002  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  51   SG                                                     
REMARK 620 2 FES A2002   S1  116.2                                              
REMARK 620 3 FES A2002   S2  117.3 102.3                                        
REMARK 620 4 CYS A  73   SG   98.4 116.0 107.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES A2002  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  43   SG                                                     
REMARK 620 2 FES A2002   S1   96.0                                              
REMARK 620 3 FES A2002   S2  116.7 104.7                                        
REMARK 620 4 CYS A  48   SG  109.4 117.4 111.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B2001  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 113   SG                                                     
REMARK 620 2 FES B2001   S1  118.2                                              
REMARK 620 3 FES B2001   S2  120.6 101.7                                        
REMARK 620 4 CYS B 150   SG  100.3 101.2 113.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B2001  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 116   SG                                                     
REMARK 620 2 FES B2001   S1  116.8                                              
REMARK 620 3 FES B2001   S2  112.1 105.4                                        
REMARK 620 4 CYS B 148   SG  102.1 109.1 111.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B2002  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  51   SG                                                     
REMARK 620 2 FES B2002   S1  116.3                                              
REMARK 620 3 FES B2002   S2  116.2 102.2                                        
REMARK 620 4 CYS B  73   SG   94.9 118.4 109.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B2002  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  43   SG                                                     
REMARK 620 2 FES B2002   S1   96.1                                              
REMARK 620 3 FES B2002   S2  111.5 104.5                                        
REMARK 620 4 CYS B  48   SG  109.3 119.5 114.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES C2001  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 113   SG                                                     
REMARK 620 2 FES C2001   S1  114.7                                              
REMARK 620 3 FES C2001   S2  114.6 102.1                                        
REMARK 620 4 CYS C 150   SG  102.3 104.7 118.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES C2001  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 116   SG                                                     
REMARK 620 2 FES C2001   S1  124.2                                              
REMARK 620 3 FES C2001   S2  112.8 104.8                                        
REMARK 620 4 CYS C 148   SG  102.2 106.1 105.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES C2002  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  51   SG                                                     
REMARK 620 2 FES C2002   S1  116.7                                              
REMARK 620 3 FES C2002   S2  118.8 102.5                                        
REMARK 620 4 CYS C  73   SG   99.3 107.3 112.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES C2002  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  43   SG                                                     
REMARK 620 2 FES C2002   S1   97.7                                              
REMARK 620 3 FES C2002   S2  115.7 105.2                                        
REMARK 620 4 CYS C  48   SG  109.5 119.8 108.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES D2001  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 113   SG                                                     
REMARK 620 2 FES D2001   S1  115.7                                              
REMARK 620 3 FES D2001   S2  118.9 101.3                                        
REMARK 620 4 CYS D 150   SG  101.5  99.4 118.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES D2001  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 116   SG                                                     
REMARK 620 2 FES D2001   S1  124.4                                              
REMARK 620 3 FES D2001   S2  109.1 105.5                                        
REMARK 620 4 CYS D 148   SG  101.1 108.9 106.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES D2002  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D  51   SG                                                     
REMARK 620 2 FES D2002   S1  120.7                                              
REMARK 620 3 FES D2002   S2  116.8 101.9                                        
REMARK 620 4 CYS D  73   SG   95.0 115.9 106.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES D2002  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D  43   SG                                                     
REMARK 620 2 FES D2002   S1   99.1                                              
REMARK 620 3 FES D2002   S2  114.4 104.7                                        
REMARK 620 4 CYS D  48   SG  108.0 113.2 116.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A7001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 741   OE2                                                    
REMARK 620 2 HIS A 742   ND1  93.1                                              
REMARK 620 3 TYR A 744   OH  103.9  99.7                                        
REMARK 620 4 THR A 837   OG1  91.4 170.6  71.2                                  
REMARK 620 5 GLY A 838   O    82.4  95.8 162.8  93.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A7002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 773   OG1                                                    
REMARK 620 2 SER A 806   OG  104.3                                              
REMARK 620 3 SER A 810   OG  123.8 130.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B7003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 742   ND1                                                    
REMARK 620 2 TYR B 744   OH   99.5                                              
REMARK 620 3 THR B 837   OG1 173.5  74.7                                        
REMARK 620 4 GLY B 838   O    87.5 172.9  98.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B7004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B 773   OG1                                                    
REMARK 620 2 SER B 806   OG  101.4                                              
REMARK 620 3 SER B 810   OG  122.9 133.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C7005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 741   OE2                                                    
REMARK 620 2 HIS C 742   ND1  79.3                                              
REMARK 620 3 TYR C 744   OH   87.6  96.9                                        
REMARK 620 4 THR C 837   OG1 109.8 165.0  72.1                                  
REMARK 620 5 GLY C 838   O   105.2  88.3 166.9 100.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C7006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 773   OG1                                                    
REMARK 620 2 SER C 806   OG  107.9                                              
REMARK 620 3 SER C 810   OG  111.8 139.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D7007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 741   OE2                                                    
REMARK 620 2 HIS D 742   ND1  87.3                                              
REMARK 620 3 THR D 837   OG1  98.6 168.6                                        
REMARK 620 4 GLY D 838   O    87.8  92.9  97.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D7008  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR D 750   OG1                                                    
REMARK 620 2 SER D 806   O   123.1                                              
REMARK 620 3 HOH D7147   O   119.1 110.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             MOM A2005  MO1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MTE A2004   S1'                                                    
REMARK 620 2 MOM A2005   OM3  86.7                                              
REMARK 620 3 MOM A2005   OM1 150.3 102.5                                        
REMARK 620 4 MOM A2005   OM2 123.3 100.3  83.3                                  
REMARK 620 5 MTE A2004   S2'  79.2 152.6  80.2 107.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             MOM B3005  MO1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MTE B3004   S1'                                                    
REMARK 620 2 MOM B3005   OM3  95.2                                              
REMARK 620 3 MOM B3005   OM1 144.8 101.9                                        
REMARK 620 4 MOM B3005   OM2 123.7 100.0  83.6                                  
REMARK 620 5 MTE B3004   S2'  83.1 157.7  69.5  99.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             MOM C4005  MO1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MTE C4004   S1'                                                    
REMARK 620 2 MOM C4005   OM3  91.2                                              
REMARK 620 3 MOM C4005   OM1 153.5 102.9                                        
REMARK 620 4 MOM C4005   OM2 116.3 100.5  83.4                                  
REMARK 620 5 MTE C4004   S2'  80.0 155.2  78.0 104.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             MOM D5005  MO1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MTE D5004   S1'                                                    
REMARK 620 2 MOM D5005   OM3  87.4                                              
REMARK 620 3 MOM D5005   OM1 153.9 102.4                                        
REMARK 620 4 MOM D5005   OM2 118.5 100.2  84.0                                  
REMARK 620 5 MTE D5004   S2'  83.9 154.3  76.9 105.3                            
REMARK 620 N                    1     2     3     4                             
DBREF  2E1Q A    2  1333  UNP    P47989   XDH_HUMAN        1   1332             
DBREF  2E1Q B    2  1333  UNP    P47989   XDH_HUMAN        1   1332             
DBREF  2E1Q C    2  1333  UNP    P47989   XDH_HUMAN        1   1332             
DBREF  2E1Q D    2  1333  UNP    P47989   XDH_HUMAN        1   1332             
SEQADV 2E1Q MET A    1  UNP  P47989              INITIATING METHIONINE          
SEQADV 2E1Q VAL A  803  UNP  P47989    GLU   802 ENGINEERED                     
SEQADV 2E1Q MET B    1  UNP  P47989              INITIATING METHIONINE          
SEQADV 2E1Q VAL B  803  UNP  P47989    GLU   802 ENGINEERED                     
SEQADV 2E1Q MET C    1  UNP  P47989              INITIATING METHIONINE          
SEQADV 2E1Q VAL C  803  UNP  P47989    GLU   802 ENGINEERED                     
SEQADV 2E1Q MET D    1  UNP  P47989              INITIATING METHIONINE          
SEQADV 2E1Q VAL D  803  UNP  P47989    GLU   802 ENGINEERED                     
SEQRES   1 A 1333  MET THR ALA ASP LYS LEU VAL PHE PHE VAL ASN GLY ARG          
SEQRES   2 A 1333  LYS VAL VAL GLU LYS ASN ALA ASP PRO GLU THR THR LEU          
SEQRES   3 A 1333  LEU ALA TYR LEU ARG ARG LYS LEU GLY LEU SER GLY THR          
SEQRES   4 A 1333  LYS LEU GLY CYS GLY GLU GLY GLY CYS GLY ALA CYS THR          
SEQRES   5 A 1333  VAL MET LEU SER LYS TYR ASP ARG LEU GLN ASN LYS ILE          
SEQRES   6 A 1333  VAL HIS PHE SER ALA ASN ALA CYS LEU ALA PRO ILE CYS          
SEQRES   7 A 1333  SER LEU HIS HIS VAL ALA VAL THR THR VAL GLU GLY ILE          
SEQRES   8 A 1333  GLY SER THR LYS THR ARG LEU HIS PRO VAL GLN GLU ARG          
SEQRES   9 A 1333  ILE ALA LYS SER HIS GLY SER GLN CYS GLY PHE CYS THR          
SEQRES  10 A 1333  PRO GLY ILE VAL MET SER MET TYR THR LEU LEU ARG ASN          
SEQRES  11 A 1333  GLN PRO GLU PRO THR MET GLU GLU ILE GLU ASN ALA PHE          
SEQRES  12 A 1333  GLN GLY ASN LEU CYS ARG CYS THR GLY TYR ARG PRO ILE          
SEQRES  13 A 1333  LEU GLN GLY PHE ARG THR PHE ALA ARG ASP GLY GLY CYS          
SEQRES  14 A 1333  CYS GLY GLY ASP GLY ASN ASN PRO ASN CYS CYS MET ASN          
SEQRES  15 A 1333  GLN LYS LYS ASP HIS SER VAL SER LEU SER PRO SER LEU          
SEQRES  16 A 1333  PHE LYS PRO GLU GLU PHE THR PRO LEU ASP PRO THR GLN          
SEQRES  17 A 1333  GLU PRO ILE PHE PRO PRO GLU LEU LEU ARG LEU LYS ASP          
SEQRES  18 A 1333  THR PRO ARG LYS GLN LEU ARG PHE GLU GLY GLU ARG VAL          
SEQRES  19 A 1333  THR TRP ILE GLN ALA SER THR LEU LYS GLU LEU LEU ASP          
SEQRES  20 A 1333  LEU LYS ALA GLN HIS PRO ASP ALA LYS LEU VAL VAL GLY          
SEQRES  21 A 1333  ASN THR GLU ILE GLY ILE GLU MET LYS PHE LYS ASN MET          
SEQRES  22 A 1333  LEU PHE PRO MET ILE VAL CYS PRO ALA TRP ILE PRO GLU          
SEQRES  23 A 1333  LEU ASN SER VAL GLU HIS GLY PRO ASP GLY ILE SER PHE          
SEQRES  24 A 1333  GLY ALA ALA CYS PRO LEU SER ILE VAL GLU LYS THR LEU          
SEQRES  25 A 1333  VAL ASP ALA VAL ALA LYS LEU PRO ALA GLN LYS THR GLU          
SEQRES  26 A 1333  VAL PHE ARG GLY VAL LEU GLU GLN LEU ARG TRP PHE ALA          
SEQRES  27 A 1333  GLY LYS GLN VAL LYS SER VAL ALA SER VAL GLY GLY ASN          
SEQRES  28 A 1333  ILE ILE THR ALA SER PRO ILE SER ASP LEU ASN PRO VAL          
SEQRES  29 A 1333  PHE MET ALA SER GLY ALA LYS LEU THR LEU VAL SER ARG          
SEQRES  30 A 1333  GLY THR ARG ARG THR VAL GLN MET ASP HIS THR PHE PHE          
SEQRES  31 A 1333  PRO GLY TYR ARG LYS THR LEU LEU SER PRO GLU GLU ILE          
SEQRES  32 A 1333  LEU LEU SER ILE GLU ILE PRO TYR SER ARG GLU GLY GLU          
SEQRES  33 A 1333  TYR PHE SER ALA PHE LYS GLN ALA SER ARG ARG GLU ASP          
SEQRES  34 A 1333  ASP ILE ALA LYS VAL THR SER GLY MET ARG VAL LEU PHE          
SEQRES  35 A 1333  LYS PRO GLY THR THR GLU VAL GLN GLU LEU ALA LEU CYS          
SEQRES  36 A 1333  TYR GLY GLY MET ALA ASN ARG THR ILE SER ALA LEU LYS          
SEQRES  37 A 1333  THR THR GLN ARG GLN LEU SER LYS LEU TRP LYS GLU GLU          
SEQRES  38 A 1333  LEU LEU GLN ASP VAL CYS ALA GLY LEU ALA GLU GLU LEU          
SEQRES  39 A 1333  HIS LEU PRO PRO ASP ALA PRO GLY GLY MET VAL ASP PHE          
SEQRES  40 A 1333  ARG CYS THR LEU THR LEU SER PHE PHE PHE LYS PHE TYR          
SEQRES  41 A 1333  LEU THR VAL LEU GLN LYS LEU GLY GLN GLU ASN LEU GLU          
SEQRES  42 A 1333  ASP LYS CYS GLY LYS LEU ASP PRO THR PHE ALA SER ALA          
SEQRES  43 A 1333  THR LEU LEU PHE GLN LYS ASP PRO PRO ALA ASP VAL GLN          
SEQRES  44 A 1333  LEU PHE GLN GLU VAL PRO LYS GLY GLN SER GLU GLU ASP          
SEQRES  45 A 1333  MET VAL GLY ARG PRO LEU PRO HIS LEU ALA ALA ASP MET          
SEQRES  46 A 1333  GLN ALA SER GLY GLU ALA VAL TYR CYS ASP ASP ILE PRO          
SEQRES  47 A 1333  ARG TYR GLU ASN GLU LEU SER LEU ARG LEU VAL THR SER          
SEQRES  48 A 1333  THR ARG ALA HIS ALA LYS ILE LYS SER ILE ASP THR SER          
SEQRES  49 A 1333  GLU ALA LYS LYS VAL PRO GLY PHE VAL CYS PHE ILE SER          
SEQRES  50 A 1333  ALA ASP ASP VAL PRO GLY SER ASN ILE THR GLY ILE CYS          
SEQRES  51 A 1333  ASN ASP GLU THR VAL PHE ALA LYS ASP LYS VAL THR CYS          
SEQRES  52 A 1333  VAL GLY HIS ILE ILE GLY ALA VAL VAL ALA ASP THR PRO          
SEQRES  53 A 1333  GLU HIS THR GLN ARG ALA ALA GLN GLY VAL LYS ILE THR          
SEQRES  54 A 1333  TYR GLU GLU LEU PRO ALA ILE ILE THR ILE GLU ASP ALA          
SEQRES  55 A 1333  ILE LYS ASN ASN SER PHE TYR GLY PRO GLU LEU LYS ILE          
SEQRES  56 A 1333  GLU LYS GLY ASP LEU LYS LYS GLY PHE SER GLU ALA ASP          
SEQRES  57 A 1333  ASN VAL VAL SER GLY GLU ILE TYR ILE GLY GLY GLN GLU          
SEQRES  58 A 1333  HIS PHE TYR LEU GLU THR HIS CYS THR ILE ALA VAL PRO          
SEQRES  59 A 1333  LYS GLY GLU ALA GLY GLU MET GLU LEU PHE VAL SER THR          
SEQRES  60 A 1333  GLN ASN THR MET LYS THR GLN SER PHE VAL ALA LYS MET          
SEQRES  61 A 1333  LEU GLY VAL PRO ALA ASN ARG ILE VAL VAL ARG VAL LYS          
SEQRES  62 A 1333  ARG MET GLY GLY GLY PHE GLY GLY LYS VAL THR ARG SER          
SEQRES  63 A 1333  THR VAL VAL SER THR ALA VAL ALA LEU ALA ALA TYR LYS          
SEQRES  64 A 1333  THR GLY ARG PRO VAL ARG CYS MET LEU ASP ARG ASP GLU          
SEQRES  65 A 1333  ASP MET LEU ILE THR GLY GLY ARG HIS PRO PHE LEU ALA          
SEQRES  66 A 1333  ARG TYR LYS VAL GLY PHE MET LYS THR GLY THR VAL VAL          
SEQRES  67 A 1333  ALA LEU GLU VAL ASP HIS PHE SER ASN VAL GLY ASN THR          
SEQRES  68 A 1333  GLN ASP LEU SER GLN SER ILE MET GLU ARG ALA LEU PHE          
SEQRES  69 A 1333  HIS MET ASP ASN CYS TYR LYS ILE PRO ASN ILE ARG GLY          
SEQRES  70 A 1333  THR GLY ARG LEU CYS LYS THR ASN LEU PRO SER ASN THR          
SEQRES  71 A 1333  ALA PHE ARG GLY PHE GLY GLY PRO GLN GLY MET LEU ILE          
SEQRES  72 A 1333  ALA GLU CYS TRP MET SER GLU VAL ALA VAL THR CYS GLY          
SEQRES  73 A 1333  MET PRO ALA GLU GLU VAL ARG ARG LYS ASN LEU TYR LYS          
SEQRES  74 A 1333  GLU GLY ASP LEU THR HIS PHE ASN GLN LYS LEU GLU GLY          
SEQRES  75 A 1333  PHE THR LEU PRO ARG CYS TRP GLU GLU CYS LEU ALA SER          
SEQRES  76 A 1333  SER GLN TYR HIS ALA ARG LYS SER GLU VAL ASP LYS PHE          
SEQRES  77 A 1333  ASN LYS GLU ASN CYS TRP LYS LYS ARG GLY LEU CYS ILE          
SEQRES  78 A 1333  ILE PRO THR LYS PHE GLY ILE SER PHE THR VAL PRO PHE          
SEQRES  79 A 1333  LEU ASN GLN ALA GLY ALA LEU LEU HIS VAL TYR THR ASP          
SEQRES  80 A 1333  GLY SER VAL LEU LEU THR HIS GLY GLY THR GLU MET GLY          
SEQRES  81 A 1333  GLN GLY LEU HIS THR LYS MET VAL GLN VAL ALA SER ARG          
SEQRES  82 A 1333  ALA LEU LYS ILE PRO THR SER LYS ILE TYR ILE SER GLU          
SEQRES  83 A 1333  THR SER THR ASN THR VAL PRO ASN THR SER PRO THR ALA          
SEQRES  84 A 1333  ALA SER VAL SER ALA ASP LEU ASN GLY GLN ALA VAL TYR          
SEQRES  85 A 1333  ALA ALA CYS GLN THR ILE LEU LYS ARG LEU GLU PRO TYR          
SEQRES  86 A 1333  LYS LYS LYS ASN PRO SER GLY SER TRP GLU ASP TRP VAL          
SEQRES  87 A 1333  THR ALA ALA TYR MET ASP THR VAL SER LEU SER ALA THR          
SEQRES  88 A 1333  GLY PHE TYR ARG THR PRO ASN LEU GLY TYR SER PHE GLU          
SEQRES  89 A 1333  THR ASN SER GLY ASN PRO PHE HIS TYR PHE SER TYR GLY          
SEQRES  90 A 1333  VAL ALA CYS SER GLU VAL GLU ILE ASP CYS LEU THR GLY          
SEQRES  91 A 1333  ASP HIS LYS ASN LEU ARG THR ASP ILE VAL MET ASP VAL          
SEQRES  92 A 1333  GLY SER SER LEU ASN PRO ALA ILE ASP ILE GLY GLN VAL          
SEQRES  93 A 1333  GLU GLY ALA PHE VAL GLN GLY LEU GLY LEU PHE THR LEU          
SEQRES  94 A 1333  GLU GLU LEU HIS TYR SER PRO GLU GLY SER LEU HIS THR          
SEQRES  95 A 1333  ARG GLY PRO SER THR TYR LYS ILE PRO ALA PHE GLY SER          
SEQRES  96 A 1333  ILE PRO ILE GLU PHE ARG VAL SER LEU LEU ARG ASP CYS          
SEQRES  97 A 1333  PRO ASN LYS LYS ALA ILE TYR ALA SER LYS ALA VAL GLY          
SEQRES  98 A 1333  GLU PRO PRO LEU PHE LEU ALA ALA SER ILE PHE PHE ALA          
SEQRES  99 A 1333  ILE LYS ASP ALA ILE ARG ALA ALA ARG ALA GLN HIS THR          
SEQRES 100 A 1333  GLY ASN ASN VAL LYS GLU LEU PHE ARG LEU ASP SER PRO          
SEQRES 101 A 1333  ALA THR PRO GLU LYS ILE ARG ASN ALA CYS VAL ASP LYS          
SEQRES 102 A 1333  PHE THR THR LEU CYS VAL THR GLY VAL PRO GLU ASN CYS          
SEQRES 103 A 1333  LYS PRO TRP SER VAL ARG VAL                                  
SEQRES   1 B 1333  MET THR ALA ASP LYS LEU VAL PHE PHE VAL ASN GLY ARG          
SEQRES   2 B 1333  LYS VAL VAL GLU LYS ASN ALA ASP PRO GLU THR THR LEU          
SEQRES   3 B 1333  LEU ALA TYR LEU ARG ARG LYS LEU GLY LEU SER GLY THR          
SEQRES   4 B 1333  LYS LEU GLY CYS GLY GLU GLY GLY CYS GLY ALA CYS THR          
SEQRES   5 B 1333  VAL MET LEU SER LYS TYR ASP ARG LEU GLN ASN LYS ILE          
SEQRES   6 B 1333  VAL HIS PHE SER ALA ASN ALA CYS LEU ALA PRO ILE CYS          
SEQRES   7 B 1333  SER LEU HIS HIS VAL ALA VAL THR THR VAL GLU GLY ILE          
SEQRES   8 B 1333  GLY SER THR LYS THR ARG LEU HIS PRO VAL GLN GLU ARG          
SEQRES   9 B 1333  ILE ALA LYS SER HIS GLY SER GLN CYS GLY PHE CYS THR          
SEQRES  10 B 1333  PRO GLY ILE VAL MET SER MET TYR THR LEU LEU ARG ASN          
SEQRES  11 B 1333  GLN PRO GLU PRO THR MET GLU GLU ILE GLU ASN ALA PHE          
SEQRES  12 B 1333  GLN GLY ASN LEU CYS ARG CYS THR GLY TYR ARG PRO ILE          
SEQRES  13 B 1333  LEU GLN GLY PHE ARG THR PHE ALA ARG ASP GLY GLY CYS          
SEQRES  14 B 1333  CYS GLY GLY ASP GLY ASN ASN PRO ASN CYS CYS MET ASN          
SEQRES  15 B 1333  GLN LYS LYS ASP HIS SER VAL SER LEU SER PRO SER LEU          
SEQRES  16 B 1333  PHE LYS PRO GLU GLU PHE THR PRO LEU ASP PRO THR GLN          
SEQRES  17 B 1333  GLU PRO ILE PHE PRO PRO GLU LEU LEU ARG LEU LYS ASP          
SEQRES  18 B 1333  THR PRO ARG LYS GLN LEU ARG PHE GLU GLY GLU ARG VAL          
SEQRES  19 B 1333  THR TRP ILE GLN ALA SER THR LEU LYS GLU LEU LEU ASP          
SEQRES  20 B 1333  LEU LYS ALA GLN HIS PRO ASP ALA LYS LEU VAL VAL GLY          
SEQRES  21 B 1333  ASN THR GLU ILE GLY ILE GLU MET LYS PHE LYS ASN MET          
SEQRES  22 B 1333  LEU PHE PRO MET ILE VAL CYS PRO ALA TRP ILE PRO GLU          
SEQRES  23 B 1333  LEU ASN SER VAL GLU HIS GLY PRO ASP GLY ILE SER PHE          
SEQRES  24 B 1333  GLY ALA ALA CYS PRO LEU SER ILE VAL GLU LYS THR LEU          
SEQRES  25 B 1333  VAL ASP ALA VAL ALA LYS LEU PRO ALA GLN LYS THR GLU          
SEQRES  26 B 1333  VAL PHE ARG GLY VAL LEU GLU GLN LEU ARG TRP PHE ALA          
SEQRES  27 B 1333  GLY LYS GLN VAL LYS SER VAL ALA SER VAL GLY GLY ASN          
SEQRES  28 B 1333  ILE ILE THR ALA SER PRO ILE SER ASP LEU ASN PRO VAL          
SEQRES  29 B 1333  PHE MET ALA SER GLY ALA LYS LEU THR LEU VAL SER ARG          
SEQRES  30 B 1333  GLY THR ARG ARG THR VAL GLN MET ASP HIS THR PHE PHE          
SEQRES  31 B 1333  PRO GLY TYR ARG LYS THR LEU LEU SER PRO GLU GLU ILE          
SEQRES  32 B 1333  LEU LEU SER ILE GLU ILE PRO TYR SER ARG GLU GLY GLU          
SEQRES  33 B 1333  TYR PHE SER ALA PHE LYS GLN ALA SER ARG ARG GLU ASP          
SEQRES  34 B 1333  ASP ILE ALA LYS VAL THR SER GLY MET ARG VAL LEU PHE          
SEQRES  35 B 1333  LYS PRO GLY THR THR GLU VAL GLN GLU LEU ALA LEU CYS          
SEQRES  36 B 1333  TYR GLY GLY MET ALA ASN ARG THR ILE SER ALA LEU LYS          
SEQRES  37 B 1333  THR THR GLN ARG GLN LEU SER LYS LEU TRP LYS GLU GLU          
SEQRES  38 B 1333  LEU LEU GLN ASP VAL CYS ALA GLY LEU ALA GLU GLU LEU          
SEQRES  39 B 1333  HIS LEU PRO PRO ASP ALA PRO GLY GLY MET VAL ASP PHE          
SEQRES  40 B 1333  ARG CYS THR LEU THR LEU SER PHE PHE PHE LYS PHE TYR          
SEQRES  41 B 1333  LEU THR VAL LEU GLN LYS LEU GLY GLN GLU ASN LEU GLU          
SEQRES  42 B 1333  ASP LYS CYS GLY LYS LEU ASP PRO THR PHE ALA SER ALA          
SEQRES  43 B 1333  THR LEU LEU PHE GLN LYS ASP PRO PRO ALA ASP VAL GLN          
SEQRES  44 B 1333  LEU PHE GLN GLU VAL PRO LYS GLY GLN SER GLU GLU ASP          
SEQRES  45 B 1333  MET VAL GLY ARG PRO LEU PRO HIS LEU ALA ALA ASP MET          
SEQRES  46 B 1333  GLN ALA SER GLY GLU ALA VAL TYR CYS ASP ASP ILE PRO          
SEQRES  47 B 1333  ARG TYR GLU ASN GLU LEU SER LEU ARG LEU VAL THR SER          
SEQRES  48 B 1333  THR ARG ALA HIS ALA LYS ILE LYS SER ILE ASP THR SER          
SEQRES  49 B 1333  GLU ALA LYS LYS VAL PRO GLY PHE VAL CYS PHE ILE SER          
SEQRES  50 B 1333  ALA ASP ASP VAL PRO GLY SER ASN ILE THR GLY ILE CYS          
SEQRES  51 B 1333  ASN ASP GLU THR VAL PHE ALA LYS ASP LYS VAL THR CYS          
SEQRES  52 B 1333  VAL GLY HIS ILE ILE GLY ALA VAL VAL ALA ASP THR PRO          
SEQRES  53 B 1333  GLU HIS THR GLN ARG ALA ALA GLN GLY VAL LYS ILE THR          
SEQRES  54 B 1333  TYR GLU GLU LEU PRO ALA ILE ILE THR ILE GLU ASP ALA          
SEQRES  55 B 1333  ILE LYS ASN ASN SER PHE TYR GLY PRO GLU LEU LYS ILE          
SEQRES  56 B 1333  GLU LYS GLY ASP LEU LYS LYS GLY PHE SER GLU ALA ASP          
SEQRES  57 B 1333  ASN VAL VAL SER GLY GLU ILE TYR ILE GLY GLY GLN GLU          
SEQRES  58 B 1333  HIS PHE TYR LEU GLU THR HIS CYS THR ILE ALA VAL PRO          
SEQRES  59 B 1333  LYS GLY GLU ALA GLY GLU MET GLU LEU PHE VAL SER THR          
SEQRES  60 B 1333  GLN ASN THR MET LYS THR GLN SER PHE VAL ALA LYS MET          
SEQRES  61 B 1333  LEU GLY VAL PRO ALA ASN ARG ILE VAL VAL ARG VAL LYS          
SEQRES  62 B 1333  ARG MET GLY GLY GLY PHE GLY GLY LYS VAL THR ARG SER          
SEQRES  63 B 1333  THR VAL VAL SER THR ALA VAL ALA LEU ALA ALA TYR LYS          
SEQRES  64 B 1333  THR GLY ARG PRO VAL ARG CYS MET LEU ASP ARG ASP GLU          
SEQRES  65 B 1333  ASP MET LEU ILE THR GLY GLY ARG HIS PRO PHE LEU ALA          
SEQRES  66 B 1333  ARG TYR LYS VAL GLY PHE MET LYS THR GLY THR VAL VAL          
SEQRES  67 B 1333  ALA LEU GLU VAL ASP HIS PHE SER ASN VAL GLY ASN THR          
SEQRES  68 B 1333  GLN ASP LEU SER GLN SER ILE MET GLU ARG ALA LEU PHE          
SEQRES  69 B 1333  HIS MET ASP ASN CYS TYR LYS ILE PRO ASN ILE ARG GLY          
SEQRES  70 B 1333  THR GLY ARG LEU CYS LYS THR ASN LEU PRO SER ASN THR          
SEQRES  71 B 1333  ALA PHE ARG GLY PHE GLY GLY PRO GLN GLY MET LEU ILE          
SEQRES  72 B 1333  ALA GLU CYS TRP MET SER GLU VAL ALA VAL THR CYS GLY          
SEQRES  73 B 1333  MET PRO ALA GLU GLU VAL ARG ARG LYS ASN LEU TYR LYS          
SEQRES  74 B 1333  GLU GLY ASP LEU THR HIS PHE ASN GLN LYS LEU GLU GLY          
SEQRES  75 B 1333  PHE THR LEU PRO ARG CYS TRP GLU GLU CYS LEU ALA SER          
SEQRES  76 B 1333  SER GLN TYR HIS ALA ARG LYS SER GLU VAL ASP LYS PHE          
SEQRES  77 B 1333  ASN LYS GLU ASN CYS TRP LYS LYS ARG GLY LEU CYS ILE          
SEQRES  78 B 1333  ILE PRO THR LYS PHE GLY ILE SER PHE THR VAL PRO PHE          
SEQRES  79 B 1333  LEU ASN GLN ALA GLY ALA LEU LEU HIS VAL TYR THR ASP          
SEQRES  80 B 1333  GLY SER VAL LEU LEU THR HIS GLY GLY THR GLU MET GLY          
SEQRES  81 B 1333  GLN GLY LEU HIS THR LYS MET VAL GLN VAL ALA SER ARG          
SEQRES  82 B 1333  ALA LEU LYS ILE PRO THR SER LYS ILE TYR ILE SER GLU          
SEQRES  83 B 1333  THR SER THR ASN THR VAL PRO ASN THR SER PRO THR ALA          
SEQRES  84 B 1333  ALA SER VAL SER ALA ASP LEU ASN GLY GLN ALA VAL TYR          
SEQRES  85 B 1333  ALA ALA CYS GLN THR ILE LEU LYS ARG LEU GLU PRO TYR          
SEQRES  86 B 1333  LYS LYS LYS ASN PRO SER GLY SER TRP GLU ASP TRP VAL          
SEQRES  87 B 1333  THR ALA ALA TYR MET ASP THR VAL SER LEU SER ALA THR          
SEQRES  88 B 1333  GLY PHE TYR ARG THR PRO ASN LEU GLY TYR SER PHE GLU          
SEQRES  89 B 1333  THR ASN SER GLY ASN PRO PHE HIS TYR PHE SER TYR GLY          
SEQRES  90 B 1333  VAL ALA CYS SER GLU VAL GLU ILE ASP CYS LEU THR GLY          
SEQRES  91 B 1333  ASP HIS LYS ASN LEU ARG THR ASP ILE VAL MET ASP VAL          
SEQRES  92 B 1333  GLY SER SER LEU ASN PRO ALA ILE ASP ILE GLY GLN VAL          
SEQRES  93 B 1333  GLU GLY ALA PHE VAL GLN GLY LEU GLY LEU PHE THR LEU          
SEQRES  94 B 1333  GLU GLU LEU HIS TYR SER PRO GLU GLY SER LEU HIS THR          
SEQRES  95 B 1333  ARG GLY PRO SER THR TYR LYS ILE PRO ALA PHE GLY SER          
SEQRES  96 B 1333  ILE PRO ILE GLU PHE ARG VAL SER LEU LEU ARG ASP CYS          
SEQRES  97 B 1333  PRO ASN LYS LYS ALA ILE TYR ALA SER LYS ALA VAL GLY          
SEQRES  98 B 1333  GLU PRO PRO LEU PHE LEU ALA ALA SER ILE PHE PHE ALA          
SEQRES  99 B 1333  ILE LYS ASP ALA ILE ARG ALA ALA ARG ALA GLN HIS THR          
SEQRES 100 B 1333  GLY ASN ASN VAL LYS GLU LEU PHE ARG LEU ASP SER PRO          
SEQRES 101 B 1333  ALA THR PRO GLU LYS ILE ARG ASN ALA CYS VAL ASP LYS          
SEQRES 102 B 1333  PHE THR THR LEU CYS VAL THR GLY VAL PRO GLU ASN CYS          
SEQRES 103 B 1333  LYS PRO TRP SER VAL ARG VAL                                  
SEQRES   1 C 1333  MET THR ALA ASP LYS LEU VAL PHE PHE VAL ASN GLY ARG          
SEQRES   2 C 1333  LYS VAL VAL GLU LYS ASN ALA ASP PRO GLU THR THR LEU          
SEQRES   3 C 1333  LEU ALA TYR LEU ARG ARG LYS LEU GLY LEU SER GLY THR          
SEQRES   4 C 1333  LYS LEU GLY CYS GLY GLU GLY GLY CYS GLY ALA CYS THR          
SEQRES   5 C 1333  VAL MET LEU SER LYS TYR ASP ARG LEU GLN ASN LYS ILE          
SEQRES   6 C 1333  VAL HIS PHE SER ALA ASN ALA CYS LEU ALA PRO ILE CYS          
SEQRES   7 C 1333  SER LEU HIS HIS VAL ALA VAL THR THR VAL GLU GLY ILE          
SEQRES   8 C 1333  GLY SER THR LYS THR ARG LEU HIS PRO VAL GLN GLU ARG          
SEQRES   9 C 1333  ILE ALA LYS SER HIS GLY SER GLN CYS GLY PHE CYS THR          
SEQRES  10 C 1333  PRO GLY ILE VAL MET SER MET TYR THR LEU LEU ARG ASN          
SEQRES  11 C 1333  GLN PRO GLU PRO THR MET GLU GLU ILE GLU ASN ALA PHE          
SEQRES  12 C 1333  GLN GLY ASN LEU CYS ARG CYS THR GLY TYR ARG PRO ILE          
SEQRES  13 C 1333  LEU GLN GLY PHE ARG THR PHE ALA ARG ASP GLY GLY CYS          
SEQRES  14 C 1333  CYS GLY GLY ASP GLY ASN ASN PRO ASN CYS CYS MET ASN          
SEQRES  15 C 1333  GLN LYS LYS ASP HIS SER VAL SER LEU SER PRO SER LEU          
SEQRES  16 C 1333  PHE LYS PRO GLU GLU PHE THR PRO LEU ASP PRO THR GLN          
SEQRES  17 C 1333  GLU PRO ILE PHE PRO PRO GLU LEU LEU ARG LEU LYS ASP          
SEQRES  18 C 1333  THR PRO ARG LYS GLN LEU ARG PHE GLU GLY GLU ARG VAL          
SEQRES  19 C 1333  THR TRP ILE GLN ALA SER THR LEU LYS GLU LEU LEU ASP          
SEQRES  20 C 1333  LEU LYS ALA GLN HIS PRO ASP ALA LYS LEU VAL VAL GLY          
SEQRES  21 C 1333  ASN THR GLU ILE GLY ILE GLU MET LYS PHE LYS ASN MET          
SEQRES  22 C 1333  LEU PHE PRO MET ILE VAL CYS PRO ALA TRP ILE PRO GLU          
SEQRES  23 C 1333  LEU ASN SER VAL GLU HIS GLY PRO ASP GLY ILE SER PHE          
SEQRES  24 C 1333  GLY ALA ALA CYS PRO LEU SER ILE VAL GLU LYS THR LEU          
SEQRES  25 C 1333  VAL ASP ALA VAL ALA LYS LEU PRO ALA GLN LYS THR GLU          
SEQRES  26 C 1333  VAL PHE ARG GLY VAL LEU GLU GLN LEU ARG TRP PHE ALA          
SEQRES  27 C 1333  GLY LYS GLN VAL LYS SER VAL ALA SER VAL GLY GLY ASN          
SEQRES  28 C 1333  ILE ILE THR ALA SER PRO ILE SER ASP LEU ASN PRO VAL          
SEQRES  29 C 1333  PHE MET ALA SER GLY ALA LYS LEU THR LEU VAL SER ARG          
SEQRES  30 C 1333  GLY THR ARG ARG THR VAL GLN MET ASP HIS THR PHE PHE          
SEQRES  31 C 1333  PRO GLY TYR ARG LYS THR LEU LEU SER PRO GLU GLU ILE          
SEQRES  32 C 1333  LEU LEU SER ILE GLU ILE PRO TYR SER ARG GLU GLY GLU          
SEQRES  33 C 1333  TYR PHE SER ALA PHE LYS GLN ALA SER ARG ARG GLU ASP          
SEQRES  34 C 1333  ASP ILE ALA LYS VAL THR SER GLY MET ARG VAL LEU PHE          
SEQRES  35 C 1333  LYS PRO GLY THR THR GLU VAL GLN GLU LEU ALA LEU CYS          
SEQRES  36 C 1333  TYR GLY GLY MET ALA ASN ARG THR ILE SER ALA LEU LYS          
SEQRES  37 C 1333  THR THR GLN ARG GLN LEU SER LYS LEU TRP LYS GLU GLU          
SEQRES  38 C 1333  LEU LEU GLN ASP VAL CYS ALA GLY LEU ALA GLU GLU LEU          
SEQRES  39 C 1333  HIS LEU PRO PRO ASP ALA PRO GLY GLY MET VAL ASP PHE          
SEQRES  40 C 1333  ARG CYS THR LEU THR LEU SER PHE PHE PHE LYS PHE TYR          
SEQRES  41 C 1333  LEU THR VAL LEU GLN LYS LEU GLY GLN GLU ASN LEU GLU          
SEQRES  42 C 1333  ASP LYS CYS GLY LYS LEU ASP PRO THR PHE ALA SER ALA          
SEQRES  43 C 1333  THR LEU LEU PHE GLN LYS ASP PRO PRO ALA ASP VAL GLN          
SEQRES  44 C 1333  LEU PHE GLN GLU VAL PRO LYS GLY GLN SER GLU GLU ASP          
SEQRES  45 C 1333  MET VAL GLY ARG PRO LEU PRO HIS LEU ALA ALA ASP MET          
SEQRES  46 C 1333  GLN ALA SER GLY GLU ALA VAL TYR CYS ASP ASP ILE PRO          
SEQRES  47 C 1333  ARG TYR GLU ASN GLU LEU SER LEU ARG LEU VAL THR SER          
SEQRES  48 C 1333  THR ARG ALA HIS ALA LYS ILE LYS SER ILE ASP THR SER          
SEQRES  49 C 1333  GLU ALA LYS LYS VAL PRO GLY PHE VAL CYS PHE ILE SER          
SEQRES  50 C 1333  ALA ASP ASP VAL PRO GLY SER ASN ILE THR GLY ILE CYS          
SEQRES  51 C 1333  ASN ASP GLU THR VAL PHE ALA LYS ASP LYS VAL THR CYS          
SEQRES  52 C 1333  VAL GLY HIS ILE ILE GLY ALA VAL VAL ALA ASP THR PRO          
SEQRES  53 C 1333  GLU HIS THR GLN ARG ALA ALA GLN GLY VAL LYS ILE THR          
SEQRES  54 C 1333  TYR GLU GLU LEU PRO ALA ILE ILE THR ILE GLU ASP ALA          
SEQRES  55 C 1333  ILE LYS ASN ASN SER PHE TYR GLY PRO GLU LEU LYS ILE          
SEQRES  56 C 1333  GLU LYS GLY ASP LEU LYS LYS GLY PHE SER GLU ALA ASP          
SEQRES  57 C 1333  ASN VAL VAL SER GLY GLU ILE TYR ILE GLY GLY GLN GLU          
SEQRES  58 C 1333  HIS PHE TYR LEU GLU THR HIS CYS THR ILE ALA VAL PRO          
SEQRES  59 C 1333  LYS GLY GLU ALA GLY GLU MET GLU LEU PHE VAL SER THR          
SEQRES  60 C 1333  GLN ASN THR MET LYS THR GLN SER PHE VAL ALA LYS MET          
SEQRES  61 C 1333  LEU GLY VAL PRO ALA ASN ARG ILE VAL VAL ARG VAL LYS          
SEQRES  62 C 1333  ARG MET GLY GLY GLY PHE GLY GLY LYS VAL THR ARG SER          
SEQRES  63 C 1333  THR VAL VAL SER THR ALA VAL ALA LEU ALA ALA TYR LYS          
SEQRES  64 C 1333  THR GLY ARG PRO VAL ARG CYS MET LEU ASP ARG ASP GLU          
SEQRES  65 C 1333  ASP MET LEU ILE THR GLY GLY ARG HIS PRO PHE LEU ALA          
SEQRES  66 C 1333  ARG TYR LYS VAL GLY PHE MET LYS THR GLY THR VAL VAL          
SEQRES  67 C 1333  ALA LEU GLU VAL ASP HIS PHE SER ASN VAL GLY ASN THR          
SEQRES  68 C 1333  GLN ASP LEU SER GLN SER ILE MET GLU ARG ALA LEU PHE          
SEQRES  69 C 1333  HIS MET ASP ASN CYS TYR LYS ILE PRO ASN ILE ARG GLY          
SEQRES  70 C 1333  THR GLY ARG LEU CYS LYS THR ASN LEU PRO SER ASN THR          
SEQRES  71 C 1333  ALA PHE ARG GLY PHE GLY GLY PRO GLN GLY MET LEU ILE          
SEQRES  72 C 1333  ALA GLU CYS TRP MET SER GLU VAL ALA VAL THR CYS GLY          
SEQRES  73 C 1333  MET PRO ALA GLU GLU VAL ARG ARG LYS ASN LEU TYR LYS          
SEQRES  74 C 1333  GLU GLY ASP LEU THR HIS PHE ASN GLN LYS LEU GLU GLY          
SEQRES  75 C 1333  PHE THR LEU PRO ARG CYS TRP GLU GLU CYS LEU ALA SER          
SEQRES  76 C 1333  SER GLN TYR HIS ALA ARG LYS SER GLU VAL ASP LYS PHE          
SEQRES  77 C 1333  ASN LYS GLU ASN CYS TRP LYS LYS ARG GLY LEU CYS ILE          
SEQRES  78 C 1333  ILE PRO THR LYS PHE GLY ILE SER PHE THR VAL PRO PHE          
SEQRES  79 C 1333  LEU ASN GLN ALA GLY ALA LEU LEU HIS VAL TYR THR ASP          
SEQRES  80 C 1333  GLY SER VAL LEU LEU THR HIS GLY GLY THR GLU MET GLY          
SEQRES  81 C 1333  GLN GLY LEU HIS THR LYS MET VAL GLN VAL ALA SER ARG          
SEQRES  82 C 1333  ALA LEU LYS ILE PRO THR SER LYS ILE TYR ILE SER GLU          
SEQRES  83 C 1333  THR SER THR ASN THR VAL PRO ASN THR SER PRO THR ALA          
SEQRES  84 C 1333  ALA SER VAL SER ALA ASP LEU ASN GLY GLN ALA VAL TYR          
SEQRES  85 C 1333  ALA ALA CYS GLN THR ILE LEU LYS ARG LEU GLU PRO TYR          
SEQRES  86 C 1333  LYS LYS LYS ASN PRO SER GLY SER TRP GLU ASP TRP VAL          
SEQRES  87 C 1333  THR ALA ALA TYR MET ASP THR VAL SER LEU SER ALA THR          
SEQRES  88 C 1333  GLY PHE TYR ARG THR PRO ASN LEU GLY TYR SER PHE GLU          
SEQRES  89 C 1333  THR ASN SER GLY ASN PRO PHE HIS TYR PHE SER TYR GLY          
SEQRES  90 C 1333  VAL ALA CYS SER GLU VAL GLU ILE ASP CYS LEU THR GLY          
SEQRES  91 C 1333  ASP HIS LYS ASN LEU ARG THR ASP ILE VAL MET ASP VAL          
SEQRES  92 C 1333  GLY SER SER LEU ASN PRO ALA ILE ASP ILE GLY GLN VAL          
SEQRES  93 C 1333  GLU GLY ALA PHE VAL GLN GLY LEU GLY LEU PHE THR LEU          
SEQRES  94 C 1333  GLU GLU LEU HIS TYR SER PRO GLU GLY SER LEU HIS THR          
SEQRES  95 C 1333  ARG GLY PRO SER THR TYR LYS ILE PRO ALA PHE GLY SER          
SEQRES  96 C 1333  ILE PRO ILE GLU PHE ARG VAL SER LEU LEU ARG ASP CYS          
SEQRES  97 C 1333  PRO ASN LYS LYS ALA ILE TYR ALA SER LYS ALA VAL GLY          
SEQRES  98 C 1333  GLU PRO PRO LEU PHE LEU ALA ALA SER ILE PHE PHE ALA          
SEQRES  99 C 1333  ILE LYS ASP ALA ILE ARG ALA ALA ARG ALA GLN HIS THR          
SEQRES 100 C 1333  GLY ASN ASN VAL LYS GLU LEU PHE ARG LEU ASP SER PRO          
SEQRES 101 C 1333  ALA THR PRO GLU LYS ILE ARG ASN ALA CYS VAL ASP LYS          
SEQRES 102 C 1333  PHE THR THR LEU CYS VAL THR GLY VAL PRO GLU ASN CYS          
SEQRES 103 C 1333  LYS PRO TRP SER VAL ARG VAL                                  
SEQRES   1 D 1333  MET THR ALA ASP LYS LEU VAL PHE PHE VAL ASN GLY ARG          
SEQRES   2 D 1333  LYS VAL VAL GLU LYS ASN ALA ASP PRO GLU THR THR LEU          
SEQRES   3 D 1333  LEU ALA TYR LEU ARG ARG LYS LEU GLY LEU SER GLY THR          
SEQRES   4 D 1333  LYS LEU GLY CYS GLY GLU GLY GLY CYS GLY ALA CYS THR          
SEQRES   5 D 1333  VAL MET LEU SER LYS TYR ASP ARG LEU GLN ASN LYS ILE          
SEQRES   6 D 1333  VAL HIS PHE SER ALA ASN ALA CYS LEU ALA PRO ILE CYS          
SEQRES   7 D 1333  SER LEU HIS HIS VAL ALA VAL THR THR VAL GLU GLY ILE          
SEQRES   8 D 1333  GLY SER THR LYS THR ARG LEU HIS PRO VAL GLN GLU ARG          
SEQRES   9 D 1333  ILE ALA LYS SER HIS GLY SER GLN CYS GLY PHE CYS THR          
SEQRES  10 D 1333  PRO GLY ILE VAL MET SER MET TYR THR LEU LEU ARG ASN          
SEQRES  11 D 1333  GLN PRO GLU PRO THR MET GLU GLU ILE GLU ASN ALA PHE          
SEQRES  12 D 1333  GLN GLY ASN LEU CYS ARG CYS THR GLY TYR ARG PRO ILE          
SEQRES  13 D 1333  LEU GLN GLY PHE ARG THR PHE ALA ARG ASP GLY GLY CYS          
SEQRES  14 D 1333  CYS GLY GLY ASP GLY ASN ASN PRO ASN CYS CYS MET ASN          
SEQRES  15 D 1333  GLN LYS LYS ASP HIS SER VAL SER LEU SER PRO SER LEU          
SEQRES  16 D 1333  PHE LYS PRO GLU GLU PHE THR PRO LEU ASP PRO THR GLN          
SEQRES  17 D 1333  GLU PRO ILE PHE PRO PRO GLU LEU LEU ARG LEU LYS ASP          
SEQRES  18 D 1333  THR PRO ARG LYS GLN LEU ARG PHE GLU GLY GLU ARG VAL          
SEQRES  19 D 1333  THR TRP ILE GLN ALA SER THR LEU LYS GLU LEU LEU ASP          
SEQRES  20 D 1333  LEU LYS ALA GLN HIS PRO ASP ALA LYS LEU VAL VAL GLY          
SEQRES  21 D 1333  ASN THR GLU ILE GLY ILE GLU MET LYS PHE LYS ASN MET          
SEQRES  22 D 1333  LEU PHE PRO MET ILE VAL CYS PRO ALA TRP ILE PRO GLU          
SEQRES  23 D 1333  LEU ASN SER VAL GLU HIS GLY PRO ASP GLY ILE SER PHE          
SEQRES  24 D 1333  GLY ALA ALA CYS PRO LEU SER ILE VAL GLU LYS THR LEU          
SEQRES  25 D 1333  VAL ASP ALA VAL ALA LYS LEU PRO ALA GLN LYS THR GLU          
SEQRES  26 D 1333  VAL PHE ARG GLY VAL LEU GLU GLN LEU ARG TRP PHE ALA          
SEQRES  27 D 1333  GLY LYS GLN VAL LYS SER VAL ALA SER VAL GLY GLY ASN          
SEQRES  28 D 1333  ILE ILE THR ALA SER PRO ILE SER ASP LEU ASN PRO VAL          
SEQRES  29 D 1333  PHE MET ALA SER GLY ALA LYS LEU THR LEU VAL SER ARG          
SEQRES  30 D 1333  GLY THR ARG ARG THR VAL GLN MET ASP HIS THR PHE PHE          
SEQRES  31 D 1333  PRO GLY TYR ARG LYS THR LEU LEU SER PRO GLU GLU ILE          
SEQRES  32 D 1333  LEU LEU SER ILE GLU ILE PRO TYR SER ARG GLU GLY GLU          
SEQRES  33 D 1333  TYR PHE SER ALA PHE LYS GLN ALA SER ARG ARG GLU ASP          
SEQRES  34 D 1333  ASP ILE ALA LYS VAL THR SER GLY MET ARG VAL LEU PHE          
SEQRES  35 D 1333  LYS PRO GLY THR THR GLU VAL GLN GLU LEU ALA LEU CYS          
SEQRES  36 D 1333  TYR GLY GLY MET ALA ASN ARG THR ILE SER ALA LEU LYS          
SEQRES  37 D 1333  THR THR GLN ARG GLN LEU SER LYS LEU TRP LYS GLU GLU          
SEQRES  38 D 1333  LEU LEU GLN ASP VAL CYS ALA GLY LEU ALA GLU GLU LEU          
SEQRES  39 D 1333  HIS LEU PRO PRO ASP ALA PRO GLY GLY MET VAL ASP PHE          
SEQRES  40 D 1333  ARG CYS THR LEU THR LEU SER PHE PHE PHE LYS PHE TYR          
SEQRES  41 D 1333  LEU THR VAL LEU GLN LYS LEU GLY GLN GLU ASN LEU GLU          
SEQRES  42 D 1333  ASP LYS CYS GLY LYS LEU ASP PRO THR PHE ALA SER ALA          
SEQRES  43 D 1333  THR LEU LEU PHE GLN LYS ASP PRO PRO ALA ASP VAL GLN          
SEQRES  44 D 1333  LEU PHE GLN GLU VAL PRO LYS GLY GLN SER GLU GLU ASP          
SEQRES  45 D 1333  MET VAL GLY ARG PRO LEU PRO HIS LEU ALA ALA ASP MET          
SEQRES  46 D 1333  GLN ALA SER GLY GLU ALA VAL TYR CYS ASP ASP ILE PRO          
SEQRES  47 D 1333  ARG TYR GLU ASN GLU LEU SER LEU ARG LEU VAL THR SER          
SEQRES  48 D 1333  THR ARG ALA HIS ALA LYS ILE LYS SER ILE ASP THR SER          
SEQRES  49 D 1333  GLU ALA LYS LYS VAL PRO GLY PHE VAL CYS PHE ILE SER          
SEQRES  50 D 1333  ALA ASP ASP VAL PRO GLY SER ASN ILE THR GLY ILE CYS          
SEQRES  51 D 1333  ASN ASP GLU THR VAL PHE ALA LYS ASP LYS VAL THR CYS          
SEQRES  52 D 1333  VAL GLY HIS ILE ILE GLY ALA VAL VAL ALA ASP THR PRO          
SEQRES  53 D 1333  GLU HIS THR GLN ARG ALA ALA GLN GLY VAL LYS ILE THR          
SEQRES  54 D 1333  TYR GLU GLU LEU PRO ALA ILE ILE THR ILE GLU ASP ALA          
SEQRES  55 D 1333  ILE LYS ASN ASN SER PHE TYR GLY PRO GLU LEU LYS ILE          
SEQRES  56 D 1333  GLU LYS GLY ASP LEU LYS LYS GLY PHE SER GLU ALA ASP          
SEQRES  57 D 1333  ASN VAL VAL SER GLY GLU ILE TYR ILE GLY GLY GLN GLU          
SEQRES  58 D 1333  HIS PHE TYR LEU GLU THR HIS CYS THR ILE ALA VAL PRO          
SEQRES  59 D 1333  LYS GLY GLU ALA GLY GLU MET GLU LEU PHE VAL SER THR          
SEQRES  60 D 1333  GLN ASN THR MET LYS THR GLN SER PHE VAL ALA LYS MET          
SEQRES  61 D 1333  LEU GLY VAL PRO ALA ASN ARG ILE VAL VAL ARG VAL LYS          
SEQRES  62 D 1333  ARG MET GLY GLY GLY PHE GLY GLY LYS VAL THR ARG SER          
SEQRES  63 D 1333  THR VAL VAL SER THR ALA VAL ALA LEU ALA ALA TYR LYS          
SEQRES  64 D 1333  THR GLY ARG PRO VAL ARG CYS MET LEU ASP ARG ASP GLU          
SEQRES  65 D 1333  ASP MET LEU ILE THR GLY GLY ARG HIS PRO PHE LEU ALA          
SEQRES  66 D 1333  ARG TYR LYS VAL GLY PHE MET LYS THR GLY THR VAL VAL          
SEQRES  67 D 1333  ALA LEU GLU VAL ASP HIS PHE SER ASN VAL GLY ASN THR          
SEQRES  68 D 1333  GLN ASP LEU SER GLN SER ILE MET GLU ARG ALA LEU PHE          
SEQRES  69 D 1333  HIS MET ASP ASN CYS TYR LYS ILE PRO ASN ILE ARG GLY          
SEQRES  70 D 1333  THR GLY ARG LEU CYS LYS THR ASN LEU PRO SER ASN THR          
SEQRES  71 D 1333  ALA PHE ARG GLY PHE GLY GLY PRO GLN GLY MET LEU ILE          
SEQRES  72 D 1333  ALA GLU CYS TRP MET SER GLU VAL ALA VAL THR CYS GLY          
SEQRES  73 D 1333  MET PRO ALA GLU GLU VAL ARG ARG LYS ASN LEU TYR LYS          
SEQRES  74 D 1333  GLU GLY ASP LEU THR HIS PHE ASN GLN LYS LEU GLU GLY          
SEQRES  75 D 1333  PHE THR LEU PRO ARG CYS TRP GLU GLU CYS LEU ALA SER          
SEQRES  76 D 1333  SER GLN TYR HIS ALA ARG LYS SER GLU VAL ASP LYS PHE          
SEQRES  77 D 1333  ASN LYS GLU ASN CYS TRP LYS LYS ARG GLY LEU CYS ILE          
SEQRES  78 D 1333  ILE PRO THR LYS PHE GLY ILE SER PHE THR VAL PRO PHE          
SEQRES  79 D 1333  LEU ASN GLN ALA GLY ALA LEU LEU HIS VAL TYR THR ASP          
SEQRES  80 D 1333  GLY SER VAL LEU LEU THR HIS GLY GLY THR GLU MET GLY          
SEQRES  81 D 1333  GLN GLY LEU HIS THR LYS MET VAL GLN VAL ALA SER ARG          
SEQRES  82 D 1333  ALA LEU LYS ILE PRO THR SER LYS ILE TYR ILE SER GLU          
SEQRES  83 D 1333  THR SER THR ASN THR VAL PRO ASN THR SER PRO THR ALA          
SEQRES  84 D 1333  ALA SER VAL SER ALA ASP LEU ASN GLY GLN ALA VAL TYR          
SEQRES  85 D 1333  ALA ALA CYS GLN THR ILE LEU LYS ARG LEU GLU PRO TYR          
SEQRES  86 D 1333  LYS LYS LYS ASN PRO SER GLY SER TRP GLU ASP TRP VAL          
SEQRES  87 D 1333  THR ALA ALA TYR MET ASP THR VAL SER LEU SER ALA THR          
SEQRES  88 D 1333  GLY PHE TYR ARG THR PRO ASN LEU GLY TYR SER PHE GLU          
SEQRES  89 D 1333  THR ASN SER GLY ASN PRO PHE HIS TYR PHE SER TYR GLY          
SEQRES  90 D 1333  VAL ALA CYS SER GLU VAL GLU ILE ASP CYS LEU THR GLY          
SEQRES  91 D 1333  ASP HIS LYS ASN LEU ARG THR ASP ILE VAL MET ASP VAL          
SEQRES  92 D 1333  GLY SER SER LEU ASN PRO ALA ILE ASP ILE GLY GLN VAL          
SEQRES  93 D 1333  GLU GLY ALA PHE VAL GLN GLY LEU GLY LEU PHE THR LEU          
SEQRES  94 D 1333  GLU GLU LEU HIS TYR SER PRO GLU GLY SER LEU HIS THR          
SEQRES  95 D 1333  ARG GLY PRO SER THR TYR LYS ILE PRO ALA PHE GLY SER          
SEQRES  96 D 1333  ILE PRO ILE GLU PHE ARG VAL SER LEU LEU ARG ASP CYS          
SEQRES  97 D 1333  PRO ASN LYS LYS ALA ILE TYR ALA SER LYS ALA VAL GLY          
SEQRES  98 D 1333  GLU PRO PRO LEU PHE LEU ALA ALA SER ILE PHE PHE ALA          
SEQRES  99 D 1333  ILE LYS ASP ALA ILE ARG ALA ALA ARG ALA GLN HIS THR          
SEQRES 100 D 1333  GLY ASN ASN VAL LYS GLU LEU PHE ARG LEU ASP SER PRO          
SEQRES 101 D 1333  ALA THR PRO GLU LYS ILE ARG ASN ALA CYS VAL ASP LYS          
SEQRES 102 D 1333  PHE THR THR LEU CYS VAL THR GLY VAL PRO GLU ASN CYS          
SEQRES 103 D 1333  LYS PRO TRP SER VAL ARG VAL                                  
HET    BCT  A6001       4                                                       
HET    BCT  B6002       4                                                       
HET    BCT  C6003       4                                                       
HET    BCT  D6004       4                                                       
HET     CA  A7001       1                                                       
HET     CA  A7002       1                                                       
HET     CA  B7003       1                                                       
HET     CA  B7004       1                                                       
HET     CA  C7005       1                                                       
HET     CA  C7006       1                                                       
HET     CA  D7007       1                                                       
HET     CA  D7008       1                                                       
HET    FES  A2001       4                                                       
HET    FES  A2002       4                                                       
HET    FAD  A2003      53                                                       
HET    MTE  A2004      24                                                       
HET    MOM  A2005       4                                                       
HET    SAL  A2006      10                                                       
HET    FES  B2001       4                                                       
HET    FES  B2002       4                                                       
HET    FAD  B3003      53                                                       
HET    MTE  B3004      24                                                       
HET    MOM  B3005       4                                                       
HET    SAL  B3006      10                                                       
HET    FES  C2001       4                                                       
HET    FES  C2002       4                                                       
HET    FAD  C4003      53                                                       
HET    MTE  C4004      24                                                       
HET    MOM  C4005       4                                                       
HET    SAL  C4006      10                                                       
HET    FES  D2001       4                                                       
HET    FES  D2002       4                                                       
HET    FAD  D5003      53                                                       
HET    MTE  D5004      24                                                       
HET    MOM  D5005       4                                                       
HET    SAL  D5006      10                                                       
HETNAM     BCT BICARBONATE ION                                                  
HETNAM      CA CALCIUM ION                                                      
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     MTE PHOSPHONIC ACIDMONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,7,           
HETNAM   2 MTE  8A,9,10,10A-HEXAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-               
HETNAM   3 MTE  ANTHRACEN-7-YLMETHYL)ESTER                                      
HETNAM     MOM HYDROXY(DIOXO)MOLYBDENUM                                         
HETNAM     SAL 2-HYDROXYBENZOIC ACID                                            
HETSYN     SAL SALICYLIC ACID                                                   
FORMUL   5  BCT    4(C H O3 1-)                                                 
FORMUL   9   CA    8(CA 2+)                                                     
FORMUL  17  FES    8(FE2 S2)                                                    
FORMUL  19  FAD    4(C27 H33 N9 O15 P2)                                         
FORMUL  20  MTE    4(C10 H14 N5 O6 P S2)                                        
FORMUL  21  MOM    4(H MO O3)                                                   
FORMUL  22  SAL    4(C7 H6 O3)                                                  
FORMUL  41  HOH   *949(H2 O)                                                    
HELIX    1   1 THR A   25  LYS A   33  1                                   9    
HELIX    2   2 PRO A   76  LEU A   80  5                                   5    
HELIX    3   3 THR A   87  ILE A   91  5                                   5    
HELIX    4   4 HIS A   99  SER A  108  1                                  10    
HELIX    5   5 CYS A  116  GLN A  131  1                                  16    
HELIX    6   6 THR A  135  ALA A  142  1                                   8    
HELIX    7   7 TYR A  153  ARG A  161  1                                   9    
HELIX    8   8 THR A  162  ALA A  164  5                                   3    
HELIX    9   9 LYS A  197  PHE A  201  5                                   5    
HELIX   10  10 ASP A  205  GLU A  209  5                                   5    
HELIX   11  11 PRO A  213  LEU A  219  1                                   7    
HELIX   12  12 THR A  241  HIS A  252  1                                  12    
HELIX   13  13 GLU A  263  LYS A  271  1                                   9    
HELIX   14  14 ILE A  284  ASN A  288  5                                   5    
HELIX   15  15 PRO A  304  LEU A  319  1                                  16    
HELIX   16  16 PRO A  320  LYS A  323  5                                   4    
HELIX   17  17 THR A  324  TRP A  336  1                                  13    
HELIX   18  18 GLY A  339  ALA A  346  1                                   8    
HELIX   19  19 SER A  347  ALA A  355  1                                   9    
HELIX   20  20 LEU A  361  SER A  368  1                                   8    
HELIX   21  21 ASP A  386  PHE A  390  5                                   5    
HELIX   22  22 ALA A  466  ARG A  472  1                                   7    
HELIX   23  23 LYS A  479  LEU A  494  1                                  16    
HELIX   24  24 MET A  504  GLU A  530  1                                  27    
HELIX   25  25 PHE A  543  LEU A  548  5                                   6    
HELIX   26  26 ALA A  582  SER A  588  1                                   7    
HELIX   27  27 TYR A  593  ILE A  597  5                                   5    
HELIX   28  28 GLU A  625  VAL A  629  5                                   5    
HELIX   29  29 ASP A  639  VAL A  641  5                                   3    
HELIX   30  30 THR A  675  GLY A  685  1                                  11    
HELIX   31  31 THR A  698  ASN A  706  1                                   9    
HELIX   32  32 ASP A  719  ALA A  727  1                                   9    
HELIX   33  33 ASN A  769  GLY A  782  1                                  14    
HELIX   34  34 PRO A  784  ASN A  786  5                                   3    
HELIX   35  35 SER A  806  GLY A  821  1                                  16    
HELIX   36  36 ASP A  829  GLY A  838  1                                  10    
HELIX   37  37 LEU A  874  HIS A  885  1                                  12    
HELIX   38  38 GLY A  916  GLY A  936  1                                  21    
HELIX   39  39 PRO A  938  ASN A  946  1                                   9    
HELIX   40  40 THR A  964  GLN A  977  1                                  14    
HELIX   41  41 GLN A  977  ASN A  992  1                                  16    
HELIX   42  42 VAL A 1012  LEU A 1015  5                                   4    
HELIX   43  43 GLY A 1042  LYS A 1056  1                                  15    
HELIX   44  44 PRO A 1058  SER A 1060  5                                   3    
HELIX   45  45 VAL A 1082  ASN A 1109  1                                  28    
HELIX   46  46 SER A 1113  ASP A 1124  1                                  12    
HELIX   47  47 ASN A 1188  LEU A 1209  1                                  22    
HELIX   48  48 ALA A 1232  ILE A 1236  5                                   5    
HELIX   49  49 ALA A 1253  SER A 1257  5                                   5    
HELIX   50  50 GLU A 1262  LEU A 1267  5                                   6    
HELIX   51  51 ALA A 1268  THR A 1287  1                                  20    
HELIX   52  52 THR A 1302  CYS A 1310  1                                   9    
HELIX   53  53 PHE A 1314  CYS A 1318  5                                   5    
HELIX   54  54 THR B   25  LYS B   33  1                                   9    
HELIX   55  55 PRO B   76  LEU B   80  5                                   5    
HELIX   56  56 THR B   87  ILE B   91  5                                   5    
HELIX   57  57 HIS B   99  SER B  108  1                                  10    
HELIX   58  58 CYS B  116  GLN B  131  1                                  16    
HELIX   59  59 THR B  135  ALA B  142  1                                   8    
HELIX   60  60 TYR B  153  ARG B  161  1                                   9    
HELIX   61  61 THR B  162  ALA B  164  5                                   3    
HELIX   62  62 LYS B  197  PHE B  201  5                                   5    
HELIX   63  63 ASP B  205  GLU B  209  5                                   5    
HELIX   64  64 PRO B  213  LEU B  219  1                                   7    
HELIX   65  65 THR B  241  HIS B  252  1                                  12    
HELIX   66  66 GLU B  263  LYS B  271  1                                   9    
HELIX   67  67 ILE B  284  ASN B  288  5                                   5    
HELIX   68  68 PRO B  304  LEU B  319  1                                  16    
HELIX   69  69 PRO B  320  LYS B  323  5                                   4    
HELIX   70  70 THR B  324  TRP B  336  1                                  13    
HELIX   71  71 GLY B  339  SER B  344  1                                   6    
HELIX   72  72 SER B  347  ALA B  355  1                                   9    
HELIX   73  73 LEU B  361  SER B  368  1                                   8    
HELIX   74  74 ASP B  386  PHE B  390  5                                   5    
HELIX   75  75 ALA B  466  GLN B  471  1                                   6    
HELIX   76  76 ARG B  472  LEU B  474  5                                   3    
HELIX   77  77 LYS B  479  LEU B  494  1                                  16    
HELIX   78  78 MET B  504  GLU B  530  1                                  27    
HELIX   79  79 ASN B  531  CYS B  536  5                                   6    
HELIX   80  80 ASP B  540  LEU B  548  5                                   9    
HELIX   81  81 ALA B  582  SER B  588  1                                   7    
HELIX   82  82 TYR B  593  ILE B  597  5                                   5    
HELIX   83  83 GLU B  625  VAL B  629  5                                   5    
HELIX   84  84 ASP B  639  VAL B  641  5                                   3    
HELIX   85  85 THR B  675  GLY B  685  1                                  11    
HELIX   86  86 THR B  698  ASN B  705  1                                   8    
HELIX   87  87 ASP B  719  ALA B  727  1                                   9    
HELIX   88  88 ASN B  769  GLY B  782  1                                  14    
HELIX   89  89 PRO B  784  ASN B  786  5                                   3    
HELIX   90  90 SER B  806  GLY B  821  1                                  16    
HELIX   91  91 ASP B  829  THR B  837  1                                   9    
HELIX   92  92 LEU B  874  HIS B  885  1                                  12    
HELIX   93  93 GLY B  916  CYS B  935  1                                  20    
HELIX   94  94 PRO B  938  LEU B  947  1                                  10    
HELIX   95  95 THR B  964  SER B  976  1                                  13    
HELIX   96  96 GLN B  977  ASN B  992  1                                  16    
HELIX   97  97 VAL B 1012  LEU B 1015  5                                   4    
HELIX   98  98 GLY B 1042  LYS B 1056  1                                  15    
HELIX   99  99 PRO B 1058  SER B 1060  5                                   3    
HELIX  100 100 VAL B 1082  LYS B 1108  1                                  27    
HELIX  101 101 SER B 1113  ASP B 1124  1                                  12    
HELIX  102 102 ASN B 1188  LEU B 1209  1                                  22    
HELIX  103 103 ALA B 1232  ILE B 1236  5                                   5    
HELIX  104 104 ALA B 1253  SER B 1257  5                                   5    
HELIX  105 105 GLU B 1262  LEU B 1267  5                                   6    
HELIX  106 106 ALA B 1268  THR B 1287  1                                  20    
HELIX  107 107 THR B 1302  CYS B 1310  1                                   9    
HELIX  108 108 ASP B 1312  LEU B 1317  1                                   6    
HELIX  109 109 THR C   25  LYS C   33  1                                   9    
HELIX  110 110 PRO C   76  LEU C   80  5                                   5    
HELIX  111 111 THR C   87  GLY C   92  1                                   6    
HELIX  112 112 HIS C   99  SER C  108  1                                  10    
HELIX  113 113 CYS C  116  GLN C  131  1                                  16    
HELIX  114 114 THR C  135  ALA C  142  1                                   8    
HELIX  115 115 TYR C  153  ARG C  161  1                                   9    
HELIX  116 116 LYS C  197  PHE C  201  5                                   5    
HELIX  117 117 ASP C  205  GLU C  209  5                                   5    
HELIX  118 118 PRO C  213  LEU C  219  1                                   7    
HELIX  119 119 THR C  241  HIS C  252  1                                  12    
HELIX  120 120 GLU C  263  LYS C  271  1                                   9    
HELIX  121 121 ILE C  284  ASN C  288  5                                   5    
HELIX  122 122 PRO C  304  LYS C  318  1                                  15    
HELIX  123 123 PRO C  320  LYS C  323  5                                   4    
HELIX  124 124 THR C  324  TRP C  336  1                                  13    
HELIX  125 125 GLY C  339  SER C  344  1                                   6    
HELIX  126 126 SER C  347  ALA C  355  1                                   9    
HELIX  127 127 LEU C  361  GLY C  369  1                                   9    
HELIX  128 128 ASP C  386  PHE C  390  5                                   5    
HELIX  129 129 ALA C  466  GLN C  473  1                                   8    
HELIX  130 130 LYS C  479  LEU C  494  1                                  16    
HELIX  131 131 MET C  504  GLU C  530  1                                  27    
HELIX  132 132 ASP C  540  LEU C  548  5                                   9    
HELIX  133 133 ALA C  582  SER C  588  1                                   7    
HELIX  134 134 TYR C  593  ILE C  597  5                                   5    
HELIX  135 135 ASP C  639  VAL C  641  5                                   3    
HELIX  136 136 THR C  675  GLN C  684  1                                  10    
HELIX  137 137 THR C  698  ASN C  706  1                                   9    
HELIX  138 138 ASP C  719  ALA C  727  1                                   9    
HELIX  139 139 ASN C  769  GLY C  782  1                                  14    
HELIX  140 140 PRO C  784  ASN C  786  5                                   3    
HELIX  141 141 ARG C  805  GLY C  821  1                                  17    
HELIX  142 142 ASP C  829  THR C  837  1                                   9    
HELIX  143 143 LEU C  874  PHE C  884  1                                  11    
HELIX  144 144 GLY C  916  CYS C  935  1                                  20    
HELIX  145 145 PRO C  938  LEU C  947  1                                  10    
HELIX  146 146 THR C  964  GLN C  977  1                                  14    
HELIX  147 147 GLN C  977  ASN C  992  1                                  16    
HELIX  148 148 VAL C 1012  LEU C 1015  5                                   4    
HELIX  149 149 GLY C 1042  LYS C 1056  1                                  15    
HELIX  150 150 PRO C 1058  SER C 1060  5                                   3    
HELIX  151 151 VAL C 1082  ASN C 1109  1                                  28    
HELIX  152 152 SER C 1113  ASP C 1124  1                                  12    
HELIX  153 153 ASN C 1188  LEU C 1209  1                                  22    
HELIX  154 154 ALA C 1232  ILE C 1236  5                                   5    
HELIX  155 155 ALA C 1253  SER C 1257  5                                   5    
HELIX  156 156 GLU C 1262  LEU C 1267  5                                   6    
HELIX  157 157 ALA C 1268  THR C 1287  1                                  20    
HELIX  158 158 THR C 1302  CYS C 1310  1                                   9    
HELIX  159 159 PHE C 1314  CYS C 1318  5                                   5    
HELIX  160 160 THR D   25  LYS D   33  1                                   9    
HELIX  161 161 PRO D   76  LEU D   80  5                                   5    
HELIX  162 162 THR D   87  ILE D   91  5                                   5    
HELIX  163 163 HIS D   99  SER D  108  1                                  10    
HELIX  164 164 CYS D  116  GLN D  131  1                                  16    
HELIX  165 165 THR D  135  ALA D  142  1                                   8    
HELIX  166 166 TYR D  153  THR D  162  1                                  10    
HELIX  167 167 LYS D  197  PHE D  201  5                                   5    
HELIX  168 168 ASP D  205  GLU D  209  5                                   5    
HELIX  169 169 PRO D  213  LEU D  219  1                                   7    
HELIX  170 170 LYS D  220  THR D  222  5                                   3    
HELIX  171 171 THR D  241  HIS D  252  1                                  12    
HELIX  172 172 GLU D  263  LYS D  271  1                                   9    
HELIX  173 173 ILE D  284  ASN D  288  5                                   5    
HELIX  174 174 PRO D  304  LEU D  319  1                                  16    
HELIX  175 175 PRO D  320  LYS D  323  5                                   4    
HELIX  176 176 THR D  324  TRP D  336  1                                  13    
HELIX  177 177 GLY D  339  SER D  344  1                                   6    
HELIX  178 178 SER D  347  ALA D  355  1                                   9    
HELIX  179 179 LEU D  361  SER D  368  1                                   8    
HELIX  180 180 ASP D  386  PHE D  390  5                                   5    
HELIX  181 181 ALA D  466  GLN D  471  1                                   6    
HELIX  182 182 LYS D  479  LEU D  494  1                                  16    
HELIX  183 183 MET D  504  GLU D  530  1                                  27    
HELIX  184 184 ASN D  531  CYS D  536  5                                   6    
HELIX  185 185 ASP D  540  LEU D  548  5                                   9    
HELIX  186 186 ALA D  582  SER D  588  1                                   7    
HELIX  187 187 TYR D  593  ILE D  597  5                                   5    
HELIX  188 188 GLU D  625  VAL D  629  5                                   5    
HELIX  189 189 SER D  637  VAL D  641  5                                   5    
HELIX  190 190 THR D  675  GLY D  685  1                                  11    
HELIX  191 191 THR D  698  ASN D  705  1                                   8    
HELIX  192 192 ASP D  719  ALA D  727  1                                   9    
HELIX  193 193 ASN D  769  GLY D  782  1                                  14    
HELIX  194 194 PRO D  784  ASN D  786  5                                   3    
HELIX  195 195 SER D  806  GLY D  821  1                                  16    
HELIX  196 196 ASP D  829  THR D  837  1                                   9    
HELIX  197 197 LEU D  874  HIS D  885  1                                  12    
HELIX  198 198 GLY D  916  GLY D  936  1                                  21    
HELIX  199 199 PRO D  938  ASN D  946  1                                   9    
HELIX  200 200 THR D  964  SER D  976  1                                  13    
HELIX  201 201 GLN D  977  ASN D  992  1                                  16    
HELIX  202 202 VAL D 1012  LEU D 1015  5                                   4    
HELIX  203 203 GLY D 1042  LYS D 1056  1                                  15    
HELIX  204 204 PRO D 1058  SER D 1060  5                                   3    
HELIX  205 205 VAL D 1082  LYS D 1108  1                                  27    
HELIX  206 206 SER D 1113  ASP D 1124  1                                  12    
HELIX  207 207 ASN D 1188  LEU D 1209  1                                  22    
HELIX  208 208 ALA D 1232  ILE D 1236  5                                   5    
HELIX  209 209 ALA D 1253  SER D 1257  5                                   5    
HELIX  210 210 GLU D 1262  LEU D 1267  5                                   6    
HELIX  211 211 ALA D 1268  THR D 1287  1                                  20    
HELIX  212 212 THR D 1302  CYS D 1310  1                                   9    
HELIX  213 213 ASP D 1312  VAL D 1319  1                                   8    
SHEET    1   A 5 ARG A  13  GLU A  17  0                                        
SHEET    2   A 5 LEU A   6  VAL A  10 -1  N  LEU A   6   O  GLU A  17           
SHEET    3   A 5 ALA A  84  THR A  86  1  O  VAL A  85   N  PHE A   9           
SHEET    4   A 5 THR A  52  ASP A  59 -1  N  SER A  56   O  ALA A  84           
SHEET    5   A 5 LYS A  64  ASN A  71 -1  O  PHE A  68   N  LEU A  55           
SHEET    1   B 4 LEU A 227  GLU A 230  0                                        
SHEET    2   B 4 THR A 235  GLN A 238 -1  O  TRP A 236   N  PHE A 229           
SHEET    3   B 4 MET A 277  CYS A 280  1  O  CYS A 280   N  ILE A 237           
SHEET    4   B 4 LYS A 256  LEU A 257  1  N  LYS A 256   O  MET A 277           
SHEET    1   C 5 VAL A 290  HIS A 292  0                                        
SHEET    2   C 5 GLY A 296  GLY A 300 -1  O  SER A 298   N  GLU A 291           
SHEET    3   C 5 ILE A 403  PRO A 410 -1  O  ILE A 407   N  PHE A 299           
SHEET    4   C 5 LYS A 371  VAL A 375 -1  N  THR A 373   O  SER A 406           
SHEET    5   C 5 ARG A 380  GLN A 384 -1  O  VAL A 383   N  LEU A 372           
SHEET    1   D 4 GLU A 416  GLN A 423  0                                        
SHEET    2   D 4 VAL A 434  PHE A 442 -1  O  SER A 436   N  PHE A 421           
SHEET    3   D 4 VAL A 449  GLY A 457 -1  O  GLN A 450   N  LEU A 441           
SHEET    4   D 4 ILE A 464  SER A 465 -1  O  ILE A 464   N  TYR A 456           
SHEET    1   E 5 ALA A 556  LEU A 560  0                                        
SHEET    2   E 5 GLU A1239  LEU A1244  1  O  LEU A1244   N  LEU A 560           
SHEET    3   E 5 HIS A1172  ASP A1182  1  N  ILE A1179   O  ARG A1241           
SHEET    4   E 5 TYR A1153  ASP A1166 -1  N  GLU A1162   O  ARG A1176           
SHEET    5   E 5 LYS A 995  ILE A1008 -1  N  CYS A1000   O  SER A1161           
SHEET    1   F 8 PHE A 632  SER A 637  0                                        
SHEET    2   F 8 ILE A 667  ALA A 673 -1  O  VAL A 672   N  VAL A 633           
SHEET    3   F 8 LEU A 604  THR A 610 -1  N  SER A 605   O  ALA A 673           
SHEET    4   F 8 VAL A 824  MET A 827  1  O  ARG A 825   N  LEU A 604           
SHEET    5   F 8 CYS A 749  PRO A 754 -1  N  ALA A 752   O  VAL A 824           
SHEET    6   F 8 MET A 761  VAL A 765 -1  O  GLU A 762   N  VAL A 753           
SHEET    7   F 8 ILE A 788  VAL A 792  1  O  ARG A 791   N  LEU A 763           
SHEET    8   F 8 THR A1067  SER A1068 -1  O  THR A1067   N  VAL A 792           
SHEET    1   G 3 LYS A 660  VAL A 661  0                                        
SHEET    2   G 3 ALA A 616  ASP A 622 -1  N  ALA A 616   O  VAL A 661           
SHEET    3   G 3 LYS A 687  GLU A 692 -1  O  LYS A 687   N  ASP A 622           
SHEET    1   H 2 ILE A 646  THR A 647  0                                        
SHEET    2   H 2 GLU A 653  THR A 654 -1  O  GLU A 653   N  THR A 647           
SHEET    1   I 5 PHE A 708  LYS A 717  0                                        
SHEET    2   I 5 ASN A 894  LYS A 903 -1  O  GLY A 899   N  LEU A 713           
SHEET    3   I 5 VAL A 857  GLY A 869  1  N  HIS A 864   O  THR A 898           
SHEET    4   I 5 PHE A 843  PHE A 851 -1  N  GLY A 850   O  ALA A 859           
SHEET    5   I 5 ASN A 729  ILE A 737 -1  N  ILE A 737   O  PHE A 843           
SHEET    1   J 4 ILE A1062  TYR A1063  0                                        
SHEET    2   J 4 VAL A1030  HIS A1034  1  N  LEU A1032   O  TYR A1063           
SHEET    3   J 4 GLN A1017  VAL A1024 -1  N  LEU A1021   O  THR A1033           
SHEET    4   J 4 SER A1129  ARG A1135 -1  O  ALA A1130   N  LEU A1022           
SHEET    1   K 5 ARG B  13  GLU B  17  0                                        
SHEET    2   K 5 LEU B   6  VAL B  10 -1  N  PHE B   8   O  VAL B  15           
SHEET    3   K 5 ALA B  84  THR B  86  1  O  VAL B  85   N  PHE B   9           
SHEET    4   K 5 THR B  52  ASP B  59 -1  N  SER B  56   O  ALA B  84           
SHEET    5   K 5 LYS B  64  ASN B  71 -1  O  PHE B  68   N  LEU B  55           
SHEET    1   L 4 LEU B 227  GLU B 230  0                                        
SHEET    2   L 4 THR B 235  GLN B 238 -1  O  TRP B 236   N  PHE B 229           
SHEET    3   L 4 MET B 277  CYS B 280  1  O  ILE B 278   N  ILE B 237           
SHEET    4   L 4 LYS B 256  LEU B 257  1  N  LYS B 256   O  MET B 277           
SHEET    1   M 5 VAL B 290  HIS B 292  0                                        
SHEET    2   M 5 GLY B 296  GLY B 300 -1  O  SER B 298   N  GLU B 291           
SHEET    3   M 5 ILE B 403  PRO B 410 -1  O  ILE B 407   N  PHE B 299           
SHEET    4   M 5 LYS B 371  SER B 376 -1  N  THR B 373   O  LEU B 405           
SHEET    5   M 5 THR B 379  GLN B 384 -1  O  ARG B 381   N  LEU B 374           
SHEET    1   N 4 GLU B 416  GLN B 423  0                                        
SHEET    2   N 4 VAL B 434  PHE B 442 -1  O  SER B 436   N  PHE B 421           
SHEET    3   N 4 VAL B 449  GLY B 457 -1  O  CYS B 455   N  GLY B 437           
SHEET    4   N 4 ILE B 464  SER B 465 -1  O  ILE B 464   N  TYR B 456           
SHEET    1   O 5 ALA B 556  LEU B 560  0                                        
SHEET    2   O 5 GLU B1239  LEU B1244  1  O  LEU B1244   N  LEU B 560           
SHEET    3   O 5 HIS B1172  ASP B1182  1  N  THR B1177   O  GLU B1239           
SHEET    4   O 5 TYR B1153  ASP B1166 -1  N  CYS B1160   O  ASP B1178           
SHEET    5   O 5 LYS B 995  ILE B1008 -1  N  ILE B1002   O  ALA B1159           
SHEET    1   P 8 PHE B 632  SER B 637  0                                        
SHEET    2   P 8 ILE B 667  ALA B 673 -1  O  VAL B 672   N  CYS B 634           
SHEET    3   P 8 LEU B 604  THR B 610 -1  N  VAL B 609   O  GLY B 669           
SHEET    4   P 8 VAL B 824  MET B 827  1  O  ARG B 825   N  LEU B 604           
SHEET    5   P 8 CYS B 749  PRO B 754 -1  N  ALA B 752   O  VAL B 824           
SHEET    6   P 8 MET B 761  VAL B 765 -1  O  GLU B 762   N  VAL B 753           
SHEET    7   P 8 ILE B 788  VAL B 792  1  O  VAL B 789   N  LEU B 763           
SHEET    8   P 8 THR B1067  SER B1068 -1  O  THR B1067   N  VAL B 792           
SHEET    1   Q 3 LYS B 660  VAL B 661  0                                        
SHEET    2   Q 3 ALA B 616  ASP B 622 -1  N  ALA B 616   O  VAL B 661           
SHEET    3   Q 3 LYS B 687  GLU B 692 -1  O  LYS B 687   N  ASP B 622           
SHEET    1   R 2 ILE B 646  THR B 647  0                                        
SHEET    2   R 2 GLU B 653  THR B 654 -1  O  GLU B 653   N  THR B 647           
SHEET    1   S 5 LEU B 713  LYS B 717  0                                        
SHEET    2   S 5 ASN B 894  LYS B 903 -1  O  GLY B 899   N  LEU B 713           
SHEET    3   S 5 VAL B 857  GLY B 869  1  N  SER B 866   O  CYS B 902           
SHEET    4   S 5 PHE B 843  PHE B 851 -1  N  GLY B 850   O  ALA B 859           
SHEET    5   S 5 ASN B 729  ILE B 737 -1  N  VAL B 731   O  VAL B 849           
SHEET    1   T 4 ILE B1062  TYR B1063  0                                        
SHEET    2   T 4 VAL B1030  HIS B1034  1  N  VAL B1030   O  TYR B1063           
SHEET    3   T 4 GLN B1017  VAL B1024 -1  N  HIS B1023   O  LEU B1031           
SHEET    4   T 4 SER B1129  ARG B1135 -1  O  ALA B1130   N  LEU B1022           
SHEET    1   U 5 ARG C  13  GLU C  17  0                                        
SHEET    2   U 5 LEU C   6  VAL C  10 -1  N  PHE C   8   O  VAL C  15           
SHEET    3   U 5 ALA C  84  THR C  86  1  O  VAL C  85   N  PHE C   9           
SHEET    4   U 5 THR C  52  ASP C  59 -1  N  SER C  56   O  ALA C  84           
SHEET    5   U 5 LYS C  64  ASN C  71 -1  O  PHE C  68   N  LEU C  55           
SHEET    1   V 4 LEU C 227  GLU C 230  0                                        
SHEET    2   V 4 THR C 235  GLN C 238 -1  O  TRP C 236   N  PHE C 229           
SHEET    3   V 4 MET C 277  CYS C 280  1  O  ILE C 278   N  THR C 235           
SHEET    4   V 4 LYS C 256  LEU C 257  1  N  LYS C 256   O  MET C 277           
SHEET    1   W 5 VAL C 290  HIS C 292  0                                        
SHEET    2   W 5 GLY C 296  GLY C 300 -1  O  SER C 298   N  GLU C 291           
SHEET    3   W 5 ILE C 403  PRO C 410 -1  O  ILE C 407   N  PHE C 299           
SHEET    4   W 5 LYS C 371  VAL C 375 -1  N  THR C 373   O  LEU C 405           
SHEET    5   W 5 ARG C 380  GLN C 384 -1  O  VAL C 383   N  LEU C 372           
SHEET    1   X 4 GLU C 416  GLN C 423  0                                        
SHEET    2   X 4 VAL C 434  PHE C 442 -1  O  SER C 436   N  PHE C 421           
SHEET    3   X 4 VAL C 449  GLY C 457 -1  O  GLN C 450   N  LEU C 441           
SHEET    4   X 4 ILE C 464  SER C 465 -1  O  ILE C 464   N  TYR C 456           
SHEET    1   Y 5 ALA C 556  LEU C 560  0                                        
SHEET    2   Y 5 GLU C1239  LEU C1244  1  O  LEU C1244   N  LEU C 560           
SHEET    3   Y 5 HIS C1172  ASP C1182  1  N  ILE C1179   O  ARG C1241           
SHEET    4   Y 5 TYR C1153  ASP C1166 -1  N  TYR C1156   O  ASP C1182           
SHEET    5   Y 5 LYS C 995  ILE C1008 -1  N  ILE C1002   O  ALA C1159           
SHEET    1   Z 8 CYS C 634  SER C 637  0                                        
SHEET    2   Z 8 ILE C 667  ALA C 673 -1  O  VAL C 672   N  CYS C 634           
SHEET    3   Z 8 LEU C 604  THR C 610 -1  N  VAL C 609   O  GLY C 669           
SHEET    4   Z 8 VAL C 824  MET C 827  1  O  ARG C 825   N  LEU C 604           
SHEET    5   Z 8 CYS C 749  PRO C 754 -1  N  ALA C 752   O  VAL C 824           
SHEET    6   Z 8 MET C 761  VAL C 765 -1  O  GLU C 762   N  VAL C 753           
SHEET    7   Z 8 ILE C 788  VAL C 792  1  O  ARG C 791   N  LEU C 763           
SHEET    8   Z 8 THR C1067  SER C1068 -1  O  THR C1067   N  VAL C 792           
SHEET    1  AA 3 LYS C 660  VAL C 661  0                                        
SHEET    2  AA 3 ALA C 616  ASP C 622 -1  N  ALA C 616   O  VAL C 661           
SHEET    3  AA 3 LYS C 687  GLU C 692 -1  O  LYS C 687   N  ASP C 622           
SHEET    1  AB 2 ILE C 646  THR C 647  0                                        
SHEET    2  AB 2 GLU C 653  THR C 654 -1  O  GLU C 653   N  THR C 647           
SHEET    1  AC 5 LEU C 713  LYS C 717  0                                        
SHEET    2  AC 5 ASN C 894  CYS C 902 -1  O  GLY C 897   N  ILE C 715           
SHEET    3  AC 5 VAL C 857  ASN C 867  1  N  HIS C 864   O  THR C 898           
SHEET    4  AC 5 PHE C 843  PHE C 851 -1  N  GLY C 850   O  ALA C 859           
SHEET    5  AC 5 ASN C 729  ILE C 737 -1  N  ILE C 737   O  PHE C 843           
SHEET    1  AD 4 ILE C1062  TYR C1063  0                                        
SHEET    2  AD 4 VAL C1030  HIS C1034  1  N  LEU C1032   O  TYR C1063           
SHEET    3  AD 4 GLN C1017  VAL C1024 -1  N  HIS C1023   O  LEU C1031           
SHEET    4  AD 4 SER C1129  ARG C1135 -1  O  ALA C1130   N  LEU C1022           
SHEET    1  AE 5 ARG D  13  GLU D  17  0                                        
SHEET    2  AE 5 LEU D   6  VAL D  10 -1  N  LEU D   6   O  GLU D  17           
SHEET    3  AE 5 ALA D  84  THR D  86  1  O  VAL D  85   N  PHE D   9           
SHEET    4  AE 5 THR D  52  ASP D  59 -1  N  SER D  56   O  ALA D  84           
SHEET    5  AE 5 LYS D  64  ASN D  71 -1  O  PHE D  68   N  LEU D  55           
SHEET    1  AF 4 LEU D 227  GLU D 230  0                                        
SHEET    2  AF 4 THR D 235  GLN D 238 -1  O  TRP D 236   N  PHE D 229           
SHEET    3  AF 4 MET D 277  CYS D 280  1  O  ILE D 278   N  THR D 235           
SHEET    4  AF 4 LYS D 256  LEU D 257  1  N  LYS D 256   O  MET D 277           
SHEET    1  AG 5 VAL D 290  HIS D 292  0                                        
SHEET    2  AG 5 GLY D 296  GLY D 300 -1  O  SER D 298   N  GLU D 291           
SHEET    3  AG 5 ILE D 403  PRO D 410 -1  O  ILE D 407   N  PHE D 299           
SHEET    4  AG 5 LYS D 371  SER D 376 -1  N  THR D 373   O  LEU D 405           
SHEET    5  AG 5 THR D 379  GLN D 384 -1  O  ARG D 381   N  LEU D 374           
SHEET    1  AH 4 GLU D 416  GLN D 423  0                                        
SHEET    2  AH 4 VAL D 434  PHE D 442 -1  O  VAL D 440   N  TYR D 417           
SHEET    3  AH 4 VAL D 449  GLY D 457 -1  O  CYS D 455   N  GLY D 437           
SHEET    4  AH 4 ILE D 464  SER D 465 -1  O  ILE D 464   N  TYR D 456           
SHEET    1  AI 5 ALA D 556  LEU D 560  0                                        
SHEET    2  AI 5 GLU D1239  LEU D1244  1  O  VAL D1242   N  LEU D 560           
SHEET    3  AI 5 HIS D1172  ASP D1182  1  N  THR D1177   O  ARG D1241           
SHEET    4  AI 5 TYR D1153  ASP D1166 -1  N  GLU D1164   O  LYS D1173           
SHEET    5  AI 5 LYS D 995  ILE D1008 -1  N  ILE D1002   O  ALA D1159           
SHEET    1  AJ 8 PHE D 632  ILE D 636  0                                        
SHEET    2  AJ 8 ILE D 667  ALA D 673 -1  O  VAL D 672   N  VAL D 633           
SHEET    3  AJ 8 LEU D 604  THR D 610 -1  N  SER D 605   O  ALA D 673           
SHEET    4  AJ 8 VAL D 824  MET D 827  1  O  ARG D 825   N  LEU D 604           
SHEET    5  AJ 8 CYS D 749  PRO D 754 -1  N  ALA D 752   O  VAL D 824           
SHEET    6  AJ 8 MET D 761  VAL D 765 -1  O  PHE D 764   N  ILE D 751           
SHEET    7  AJ 8 ILE D 788  VAL D 792  1  O  ARG D 791   N  LEU D 763           
SHEET    8  AJ 8 THR D1067  SER D1068 -1  O  THR D1067   N  VAL D 792           
SHEET    1  AK 3 LYS D 660  VAL D 661  0                                        
SHEET    2  AK 3 ALA D 616  ASP D 622 -1  N  ALA D 616   O  VAL D 661           
SHEET    3  AK 3 LYS D 687  GLU D 692 -1  O  LYS D 687   N  ASP D 622           
SHEET    1  AL 2 ILE D 646  THR D 647  0                                        
SHEET    2  AL 2 GLU D 653  THR D 654 -1  O  GLU D 653   N  THR D 647           
SHEET    1  AM 5 LEU D 713  LYS D 717  0                                        
SHEET    2  AM 5 ASN D 894  LYS D 903 -1  O  GLY D 897   N  ILE D 715           
SHEET    3  AM 5 VAL D 857  GLY D 869  1  N  SER D 866   O  CYS D 902           
SHEET    4  AM 5 PHE D 843  PHE D 851 -1  N  GLY D 850   O  ALA D 859           
SHEET    5  AM 5 ASN D 729  ILE D 737 -1  N  ILE D 735   O  ALA D 845           
SHEET    1  AN 4 ILE D1062  ILE D1064  0                                        
SHEET    2  AN 4 VAL D1030  HIS D1034  1  N  LEU D1032   O  TYR D1063           
SHEET    3  AN 4 GLN D1017  VAL D1024 -1  N  LEU D1021   O  THR D1033           
SHEET    4  AN 4 SER D1129  ARG D1135 -1  O  GLY D1132   N  ALA D1020           
LINK        FE1  FES A2001                 SG  CYS A 113     1555   1555  2.37  
LINK        FE1  FES A2001                 SG  CYS A 150     1555   1555  2.39  
LINK        FE2  FES A2001                 SG  CYS A 116     1555   1555  2.38  
LINK        FE2  FES A2001                 SG  CYS A 148     1555   1555  2.41  
LINK        FE1  FES A2002                 SG  CYS A  51     1555   1555  2.40  
LINK        FE1  FES A2002                 SG  CYS A  73     1555   1555  2.38  
LINK        FE2  FES A2002                 SG  CYS A  43     1555   1555  2.39  
LINK        FE2  FES A2002                 SG  CYS A  48     1555   1555  2.38  
LINK        FE1  FES B2001                 SG  CYS B 113     1555   1555  2.39  
LINK        FE1  FES B2001                 SG  CYS B 150     1555   1555  2.42  
LINK        FE2  FES B2001                 SG  CYS B 116     1555   1555  2.38  
LINK        FE2  FES B2001                 SG  CYS B 148     1555   1555  2.41  
LINK        FE1  FES B2002                 SG  CYS B  51     1555   1555  2.40  
LINK        FE1  FES B2002                 SG  CYS B  73     1555   1555  2.40  
LINK        FE2  FES B2002                 SG  CYS B  43     1555   1555  2.40  
LINK        FE2  FES B2002                 SG  CYS B  48     1555   1555  2.37  
LINK        FE1  FES C2001                 SG  CYS C 113     1555   1555  2.37  
LINK        FE1  FES C2001                 SG  CYS C 150     1555   1555  2.41  
LINK        FE2  FES C2001                 SG  CYS C 116     1555   1555  2.39  
LINK        FE2  FES C2001                 SG  CYS C 148     1555   1555  2.40  
LINK        FE1  FES C2002                 SG  CYS C  51     1555   1555  2.39  
LINK        FE1  FES C2002                 SG  CYS C  73     1555   1555  2.36  
LINK        FE2  FES C2002                 SG  CYS C  43     1555   1555  2.38  
LINK        FE2  FES C2002                 SG  CYS C  48     1555   1555  2.38  
LINK        FE1  FES D2001                 SG  CYS D 113     1555   1555  2.40  
LINK        FE1  FES D2001                 SG  CYS D 150     1555   1555  2.40  
LINK        FE2  FES D2001                 SG  CYS D 116     1555   1555  2.38  
LINK        FE2  FES D2001                 SG  CYS D 148     1555   1555  2.41  
LINK        FE1  FES D2002                 SG  CYS D  51     1555   1555  2.39  
LINK        FE1  FES D2002                 SG  CYS D  73     1555   1555  2.39  
LINK        FE2  FES D2002                 SG  CYS D  43     1555   1555  2.41  
LINK        FE2  FES D2002                 SG  CYS D  48     1555   1555  2.36  
LINK         OE2 GLU A 741                CA    CA A7001     1555   1555  2.57  
LINK         ND1 HIS A 742                CA    CA A7001     1555   1555  2.67  
LINK         OH  TYR A 744                CA    CA A7001     1555   1555  2.90  
LINK         OG1 THR A 773                CA    CA A7002     1555   1555  2.71  
LINK         OG  SER A 806                CA    CA A7002     1555   1555  2.69  
LINK         OG  SER A 810                CA    CA A7002     1555   1555  2.96  
LINK         OG1 THR A 837                CA    CA A7001     1555   1555  2.77  
LINK         O   GLY A 838                CA    CA A7001     1555   1555  2.43  
LINK         ND1 HIS B 742                CA    CA B7003     1555   1555  2.99  
LINK         OH  TYR B 744                CA    CA B7003     1555   1555  2.94  
LINK         OG1 THR B 773                CA    CA B7004     1555   1555  2.86  
LINK         OG  SER B 806                CA    CA B7004     1555   1555  2.80  
LINK         OG  SER B 810                CA    CA B7004     1555   1555  2.76  
LINK         OG1 THR B 837                CA    CA B7003     1555   1555  2.59  
LINK         O   GLY B 838                CA    CA B7003     1555   1555  2.43  
LINK         OE2 GLU C 741                CA    CA C7005     1555   1555  2.60  
LINK         ND1 HIS C 742                CA    CA C7005     1555   1555  2.82  
LINK         OH  TYR C 744                CA    CA C7005     1555   1555  2.92  
LINK         OG1 THR C 773                CA    CA C7006     1555   1555  2.90  
LINK         OG  SER C 806                CA    CA C7006     1555   1555  2.54  
LINK         OG  SER C 810                CA    CA C7006     1555   1555  3.00  
LINK         OG1 THR C 837                CA    CA C7005     1555   1555  2.47  
LINK         O   GLY C 838                CA    CA C7005     1555   1555  2.41  
LINK         OE2 GLU D 741                CA    CA D7007     1555   1555  2.72  
LINK         ND1 HIS D 742                CA    CA D7007     1555   1555  2.93  
LINK         OG1 THR D 750                CA    CA D7008     1555   1555  2.65  
LINK         O   SER D 806                CA    CA D7008     1555   1555  2.66  
LINK         OG1 THR D 837                CA    CA D7007     1555   1555  2.68  
LINK         O   GLY D 838                CA    CA D7007     1555   1555  2.41  
LINK        CA    CA D7008                 O   HOH D7147     1555   1555  2.75  
LINK         S1' MTE A2004                MO1  MOM A2005     1555   1555  2.45  
LINK         S2' MTE A2004                MO1  MOM A2005     1555   1555  2.72  
LINK         S1' MTE B3004                MO1  MOM B3005     1555   1555  2.54  
LINK         S2' MTE B3004                MO1  MOM B3005     1555   1555  2.45  
LINK         S1' MTE C4004                MO1  MOM C4005     1555   1555  2.46  
LINK         S2' MTE C4004                MO1  MOM C4005     1555   1555  2.59  
LINK         S1' MTE D5004                MO1  MOM D5005     1555   1555  2.53  
LINK         S2' MTE D5004                MO1  MOM D5005     1555   1555  2.44  
CISPEP   1 SER A 1299    PRO A 1300          0         0.00                     
CISPEP   2 SER B 1299    PRO B 1300          0         0.11                     
CISPEP   3 SER C 1299    PRO C 1300          0        -0.13                     
CISPEP   4 SER D 1299    PRO D 1300          0         0.13                     
CRYST1  134.571  140.944  176.484  90.00  91.49  90.00 P 1 21 1      8          
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      0.007431  0.000000  0.000193        0.00000                         
SCALE2      0.000000  0.007095  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005668        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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