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Database: PDB
Entry: 1GTE
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Original site: 1GTE 
HEADER    OXIDOREDUCTASE                          15-JAN-02   1GTE              
TITLE     DIHYDROPYRIMIDINE DEHYDROGENASE (DPD) FROM PIG, BINARY COMPLEX WITH 5-
TITLE    2 IODOURACIL                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROPYRIMIDINE DEHYDROGENASE;                           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: DPD, DHPDHASE, DIHYDROURACIL DEHYDROGENASE, DIHYDROTHYMINE  
COMPND   5 DEHYDROGENASE;                                                       
COMPND   6 EC: 1.3.1.2;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 ORGAN: LIVER;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI DH5[ALPHA];                      
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 668369;                                     
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PSE420                                    
KEYWDS    ELECTRON TRANSFER, FLAVIN, IRON-SULFUR CLUSTERS, PYRIMIDINE           
KEYWDS   2 CATABOLISM, 5-FLUOROURACIL DEGRADATION, OXIDOREDUCTASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.DOBRITZSCH,S.RICAGNO,G.SCHNEIDER,K.D.SCHNACKERZ,Y.LINDQVIST         
REVDAT   5   23-JAN-19 1GTE    1       JRNL   REMARK ATOM                       
REVDAT   4   07-FEB-18 1GTE    1       SOURCE                                   
REVDAT   3   24-FEB-09 1GTE    1       VERSN                                    
REVDAT   2   12-SEP-02 1GTE    1       COMPND SITE                              
REVDAT   1   11-APR-02 1GTE    0                                                
JRNL        AUTH   D.DOBRITZSCH,S.RICAGNO,G.SCHNEIDER,K.D.SCHNACKERZ,           
JRNL        AUTH 2 Y.LINDQVIST                                                  
JRNL        TITL   CRYSTAL STRUCTURE OF THE PRODUCTIVE TERNARY COMPLEX OF       
JRNL        TITL 2 DIHYDROPYRIMIDINE DEHYDROGENASE WITH NADPH AND 5-IODOURACIL. 
JRNL        TITL 3 IMPLICATIONS FOR MECHANISM OF INHIBITION AND ELECTRON        
JRNL        TITL 4 TRANSFER.                                                    
JRNL        REF    J. BIOL. CHEM.                V. 277 13155 2002              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   11796730                                                     
JRNL        DOI    10.1074/JBC.M111877200                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   D.DOBRITZSCH,K.PERSSON,G.SCHNEIDER,Y.LINDQVIST               
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY STUDY OF PIG LIVER     
REMARK   1  TITL 2 DIHYDROPYRIMIDINE DEHYDROGENASE                              
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  57   153 2001              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  PMID   11134942                                                     
REMARK   1  DOI    10.1107/S0907444900015250                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 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) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 3440087.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 481625                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.197                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9508                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.002                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.73                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 56343                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2250                       
REMARK   3   BIN FREE R VALUE                    : 0.2330                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 1.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1114                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.007                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 30790                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 500                                     
REMARK   3   SOLVENT ATOMS            : 4848                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.46000                                             
REMARK   3    B22 (A**2) : 4.08000                                              
REMARK   3    B33 (A**2) : 0.38000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -2.03000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.17                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.12                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.18                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.13                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 3.120                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : OVERALL                                   
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 : FLAT MODEL                                           
REMARK   3   KSOL        : 0.39                                                 
REMARK   3   BSOL        : 51.87                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : PG2.PAR                                        
REMARK   3  PARAMETER FILE  3  : CIS_PEPTIDE.PARAM                              
REMARK   3  PARAMETER FILE  4  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : PG2.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : SUBS.TOP                                       
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE 5 C-TERMINAL RESIDUES AND A FEW       
REMARK   3  LOOP-RESIDUES WERE NOT SEEN IN THE DENSITY DUE TO DISORDER          
REMARK   4                                                                      
REMARK   4 1GTE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JAN-02.                  
REMARK 100 THE DEPOSITION ID IS D_1290009265.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-FEB-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.70                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8424                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 489160                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.04700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: DIHYDROPYRIMIDINE DEHYDROGENASE, NON-LIGANDED FORM   
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE PH 4.7, 16-20 %    
REMARK 280  POLYETHYLENE GLYCOL 6000, 1 MM DTT, 1 MM 5-IODOURACIL, PH 4.70      
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       79.18500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
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: PQS                                                   
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 INVOLVED IN THE CATABOLISM OF URACIL AND                             
REMARK 400 THYMIDINE LEADING TO THE FORMATION OF BETA-ALANINE.                  
REMARK 400 CATALYSES THE REDUCTION OF URACIL AND THYMINE.                       
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     MET A   675                                                      
REMARK 465     GLY A   676                                                      
REMARK 465     GLU A   677                                                      
REMARK 465     ARG A   678                                                      
REMARK 465     GLY A   679                                                      
REMARK 465     ALA A   902                                                      
REMARK 465     ALA A   903                                                      
REMARK 465     PHE A   904                                                      
REMARK 465     PRO A   905                                                      
REMARK 465     PRO A   906                                                      
REMARK 465     LEU A   907                                                      
REMARK 465     PRO A  1018                                                      
REMARK 465     LEU A  1019                                                      
REMARK 465     ALA A  1020                                                      
REMARK 465     VAL A  1021                                                      
REMARK 465     ASN A  1022                                                      
REMARK 465     PRO A  1023                                                      
REMARK 465     VAL A  1024                                                      
REMARK 465     CYS A  1025                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B   674                                                      
REMARK 465     MET B   675                                                      
REMARK 465     GLY B   676                                                      
REMARK 465     GLU B   677                                                      
REMARK 465     ARG B   678                                                      
REMARK 465     GLY B   679                                                      
REMARK 465     ALA B   902                                                      
REMARK 465     ALA B   903                                                      
REMARK 465     PHE B   904                                                      
REMARK 465     PRO B   905                                                      
REMARK 465     PRO B   906                                                      
REMARK 465     LEU B   907                                                      
REMARK 465     LEU B  1019                                                      
REMARK 465     ALA B  1020                                                      
REMARK 465     VAL B  1021                                                      
REMARK 465     ASN B  1022                                                      
REMARK 465     PRO B  1023                                                      
REMARK 465     VAL B  1024                                                      
REMARK 465     CYS B  1025                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLY C   676                                                      
REMARK 465     GLU C   677                                                      
REMARK 465     ARG C   678                                                      
REMARK 465     GLY C   679                                                      
REMARK 465     MET C   680                                                      
REMARK 465     GLY C   681                                                      
REMARK 465     PRO C  1018                                                      
REMARK 465     LEU C  1019                                                      
REMARK 465     ALA C  1020                                                      
REMARK 465     VAL C  1021                                                      
REMARK 465     ASN C  1022                                                      
REMARK 465     PRO C  1023                                                      
REMARK 465     VAL C  1024                                                      
REMARK 465     CYS C  1025                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D   903                                                      
REMARK 465     PHE D   904                                                      
REMARK 465     PRO D   905                                                      
REMARK 465     PRO D   906                                                      
REMARK 465     ALA D  1020                                                      
REMARK 465     VAL D  1021                                                      
REMARK 465     ASN D  1022                                                      
REMARK 465     PRO D  1023                                                      
REMARK 465     VAL D  1024                                                      
REMARK 465     CYS D  1025                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP B   634     O    HOH B  2852              1.81            
REMARK 500   OE1  GLN B   156    FE3   SF4 B  1026              1.94            
REMARK 500   OE1  GLN A   156    FE3   SF4 A  1026              1.94            
REMARK 500   OE1  GLN C   156    FE3   SF4 C  1026              1.95            
REMARK 500   OD1  ASP C   634     O    HOH C  2816              1.97            
REMARK 500   O    HOH A  2119     O    HOH A  3032              2.02            
REMARK 500   O    HOH B  2841     O    HOH B  2842              2.03            
REMARK 500   OD1  ASP D   634     O    HOH D  2891              2.04            
REMARK 500   NE2  GLN B   623     O    HOH B  2841              2.11            
REMARK 500   OD1  ASP B   414     O    HOH B  2652              2.12            
REMARK 500   OD2  ASP A   634     O    HOH A  2819              2.14            
REMARK 500   O    HOH C  3096     O    HOH D  2844              2.15            
REMARK 500   O    CYS B   831     O    HOH B  3001              2.15            
REMARK 500   SG   CYS A    87    FE2   SF4 A  1027              2.18            
REMARK 500   SG   CYS C   136    FE2   SF4 C  1026              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  2001     O    HOH A  2818     1655     1.98            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASN C 167   CA    ASN C 167   CB     -0.163                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A   3   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    ARG B 410   CB  -  CA  -  C   ANGL. DEV. =  12.1 DEGREES          
REMARK 500    ASN C 167   CB  -  CA  -  C   ANGL. DEV. =  15.5 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    GLU A  53      156.41    -38.43                                   
REMARK 500    LEU A 135     -123.38   -130.54                                   
REMARK 500    ALA A 195       54.55    -98.45                                   
REMARK 500    GLU A 230      -39.02   -131.29                                   
REMARK 500    ASN A 264      -12.67     78.29                                   
REMARK 500    GLU A 265     -121.99   -116.91                                   
REMARK 500    LYS A 365     -159.36   -112.61                                   
REMARK 500    GLU A 415       56.07    -68.44                                   
REMARK 500    THR A 416      -25.82   -164.61                                   
REMARK 500    ASP A 444      109.10    -42.50                                   
REMARK 500    ALA A 551     -160.22   -171.38                                   
REMARK 500    ARG A 589       -8.54   -142.53                                   
REMARK 500    LEU A 612     -165.77   -102.06                                   
REMARK 500    LEU A 669       34.10    -98.05                                   
REMARK 500    HIS A 673      137.31   -178.85                                   
REMARK 500    CYS A 816      -70.84   -134.27                                   
REMARK 500    GLN A 822     -106.81   -146.46                                   
REMARK 500    THR A 990        5.17     87.79                                   
REMARK 500    LEU B 135     -123.56   -131.50                                   
REMARK 500    ALA B 195       54.11    -98.19                                   
REMARK 500    GLU B 230      -38.44   -132.07                                   
REMARK 500    GLU B 265     -116.38   -124.72                                   
REMARK 500    LYS B 365     -159.08   -113.86                                   
REMARK 500    ASP B 414     -161.39   -113.96                                   
REMARK 500    THR B 416       43.62    -96.17                                   
REMARK 500    LYS B 418      117.94      4.86                                   
REMARK 500    ALA B 551     -163.39   -174.46                                   
REMARK 500    ARG B 589       -8.39   -141.80                                   
REMARK 500    LEU B 612     -165.34   -102.97                                   
REMARK 500    LEU B 669       33.67    -98.80                                   
REMARK 500    CYS B 816      -71.24   -133.89                                   
REMARK 500    GLN B 822     -107.90   -146.42                                   
REMARK 500    ARG B 867       57.85    -92.64                                   
REMARK 500    SER B 966       11.19   -140.01                                   
REMARK 500    THR B 990        8.22     83.63                                   
REMARK 500    LEU C 135     -124.65   -130.48                                   
REMARK 500    ALA C 195       53.69    -99.02                                   
REMARK 500    GLU C 230      -38.29   -131.74                                   
REMARK 500    GLU C 265     -123.21   -133.07                                   
REMARK 500    CYS C 324      -99.30    -20.80                                   
REMARK 500    HIS C 325       60.75    156.37                                   
REMARK 500    LYS C 365     -158.54   -113.61                                   
REMARK 500    GLU C 415      -66.70    -27.47                                   
REMARK 500    ASP C 444      109.02    -44.59                                   
REMARK 500    ALA C 551     -163.09   -175.74                                   
REMARK 500    ARG C 589       -8.42   -141.10                                   
REMARK 500    LEU C 612     -165.67   -102.45                                   
REMARK 500    LEU C 669       33.56    -97.61                                   
REMARK 500    ASP C 797       19.90   -140.40                                   
REMARK 500    CYS C 816      -70.76   -134.13                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      76 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2004        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH A2008        DISTANCE =  6.33 ANGSTROMS                       
REMARK 525    HOH A2071        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH A2082        DISTANCE =  7.16 ANGSTROMS                       
REMARK 525    HOH A2106        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH A2162        DISTANCE =  6.93 ANGSTROMS                       
REMARK 525    HOH A2196        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH A2371        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH B2073        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH B2087        DISTANCE =  6.57 ANGSTROMS                       
REMARK 525    HOH B2101        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH B2189        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH B2264        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH B2266        DISTANCE =  6.37 ANGSTROMS                       
REMARK 525    HOH B2267        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH B2404        DISTANCE =  6.18 ANGSTROMS                       
REMARK 525    HOH B2485        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH C2067        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH C2074        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH C2156        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH C2366        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH D2005        DISTANCE =  6.73 ANGSTROMS                       
REMARK 525    HOH D2006        DISTANCE =  6.47 ANGSTROMS                       
REMARK 525    HOH D2010        DISTANCE =  6.84 ANGSTROMS                       
REMARK 525    HOH D2187        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH D2422        DISTANCE =  6.22 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C1027  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 140   SG                                                     
REMARK 620 2 SF4 C1027   S2  111.7                                              
REMARK 620 3 SF4 C1027   S3  113.0 106.7                                        
REMARK 620 4 SF4 C1027   S4  105.9 102.5 116.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C1027  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  87   SG                                                     
REMARK 620 2 SF4 C1027   S1  119.7                                              
REMARK 620 3 SF4 C1027   S3  107.1 102.4                                        
REMARK 620 4 SF4 C1027   S4  116.1 102.7 107.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C1027  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  79   SG                                                     
REMARK 620 2 SF4 C1027   S1   94.1                                              
REMARK 620 3 SF4 C1027   S2  115.9 108.6                                        
REMARK 620 4 SF4 C1027   S4  120.0 111.0 106.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C1027  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  82   SG                                                     
REMARK 620 2 SF4 C1027   S1  107.1                                              
REMARK 620 3 SF4 C1027   S2  106.8 103.6                                        
REMARK 620 4 SF4 C1027   S3  115.9 116.3 106.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C1028  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 996   SG                                                     
REMARK 620 2 SF4 C1028   S2  110.0                                              
REMARK 620 3 SF4 C1028   S3  106.0 107.5                                        
REMARK 620 4 SF4 C1028   S4  114.7 102.3 116.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C1028  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 959   SG                                                     
REMARK 620 2 SF4 C1028   S1  110.5                                              
REMARK 620 3 SF4 C1028   S3  115.3 103.0                                        
REMARK 620 4 SF4 C1028   S4  117.8 103.0 105.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C1028  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 953   SG                                                     
REMARK 620 2 SF4 C1028   S1   93.7                                              
REMARK 620 3 SF4 C1028   S2  118.8 108.0                                        
REMARK 620 4 SF4 C1028   S4  117.1 112.2 106.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C1028  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 956   SG                                                     
REMARK 620 2 SF4 C1028   S1  118.1                                              
REMARK 620 3 SF4 C1028   S2  118.6 102.1                                        
REMARK 620 4 SF4 C1028   S3   94.7 116.9 106.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C1029  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 963   SG                                                     
REMARK 620 2 SF4 C1029   S2  110.8                                              
REMARK 620 3 SF4 C1029   S3  105.8 108.4                                        
REMARK 620 4 SF4 C1029   S4  114.0 101.9 115.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C1029  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 992   SG                                                     
REMARK 620 2 SF4 C1029   S1  107.5                                              
REMARK 620 3 SF4 C1029   S3  119.6 103.2                                        
REMARK 620 4 SF4 C1029   S4  115.0 103.6 106.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C1029  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 986   SG                                                     
REMARK 620 2 SF4 C1029   S1  101.6                                              
REMARK 620 3 SF4 C1029   S2  119.6 108.0                                        
REMARK 620 4 SF4 C1029   S4  108.7 112.9 106.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C1029  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 989   SG                                                     
REMARK 620 2 SF4 C1029   S1  119.4                                              
REMARK 620 3 SF4 C1029   S2  117.2 101.9                                        
REMARK 620 4 SF4 C1029   S3   95.0 116.1 107.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D1026  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D  91   SG                                                     
REMARK 620 2 SF4 D1026   S2  116.7                                              
REMARK 620 3 SF4 D1026   S3  111.3 107.9                                        
REMARK 620 4 SF4 D1026   S4  101.8 102.3 116.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D1026  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 136   SG                                                     
REMARK 620 2 SF4 D1026   S1  119.3                                              
REMARK 620 3 SF4 D1026   S3  113.9 103.6                                        
REMARK 620 4 SF4 D1026   S4  110.4 102.4 105.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D1026  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN D 156   OE1                                                    
REMARK 620 2 SF4 D1026   S1  107.2                                              
REMARK 620 3 SF4 D1026   S2  111.0 108.0                                        
REMARK 620 4 SF4 D1026   S4  112.0 112.5 106.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D1026  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 130   SG                                                     
REMARK 620 2 SF4 D1026   S1  103.7                                              
REMARK 620 3 SF4 D1026   S2  114.5 102.4                                        
REMARK 620 4 SF4 D1026   S3  112.5 117.1 106.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D1027  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D  87   SG                                                     
REMARK 620 2 SF4 D1027   S1  118.4                                              
REMARK 620 3 SF4 D1027   S3  108.1 102.6                                        
REMARK 620 4 SF4 D1027   S4  115.9 102.6 108.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D1027  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D  79   SG                                                     
REMARK 620 2 SF4 D1027   S1   94.8                                              
REMARK 620 3 SF4 D1027   S2  114.1 108.6                                        
REMARK 620 4 SF4 D1027   S4  121.2 111.1 106.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D1027  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D  82   SG                                                     
REMARK 620 2 SF4 D1027   S1  107.1                                              
REMARK 620 3 SF4 D1027   S2  106.7 103.7                                        
REMARK 620 4 SF4 D1027   S3  116.4 115.7 106.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D1027  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 140   SG                                                     
REMARK 620 2 SF4 D1027   S2  110.9                                              
REMARK 620 3 SF4 D1027   S3  113.2 106.7                                        
REMARK 620 4 SF4 D1027   S4  107.2 102.3 116.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D1028  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 959   SG                                                     
REMARK 620 2 SF4 D1028   S1  110.9                                              
REMARK 620 3 SF4 D1028   S3  114.8 102.7                                        
REMARK 620 4 SF4 D1028   S4  118.0 102.9 105.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D1028  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 953   SG                                                     
REMARK 620 2 SF4 D1028   S1   94.9                                              
REMARK 620 3 SF4 D1028   S2  118.0 108.0                                        
REMARK 620 4 SF4 D1028   S4  116.7 112.8 106.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D1028  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 956   SG                                                     
REMARK 620 2 SF4 D1028   S1  118.1                                              
REMARK 620 3 SF4 D1028   S2  118.0 102.4                                        
REMARK 620 4 SF4 D1028   S3   94.9 117.0 106.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D1028  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 996   SG                                                     
REMARK 620 2 SF4 D1028   S2  109.5                                              
REMARK 620 3 SF4 D1028   S3  106.0 107.6                                        
REMARK 620 4 SF4 D1028   S4  115.0 102.1 116.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D1029  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 992   SG                                                     
REMARK 620 2 SF4 D1029   S1  107.6                                              
REMARK 620 3 SF4 D1029   S3  119.5 102.7                                        
REMARK 620 4 SF4 D1029   S4  115.1 103.8 106.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D1029  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 986   SG                                                     
REMARK 620 2 SF4 D1029   S1  101.5                                              
REMARK 620 3 SF4 D1029   S2  119.5 107.9                                        
REMARK 620 4 SF4 D1029   S4  109.2 113.2 105.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D1029  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 989   SG                                                     
REMARK 620 2 SF4 D1029   S1  118.9                                              
REMARK 620 3 SF4 D1029   S2  118.5 101.8                                        
REMARK 620 4 SF4 D1029   S3   93.4 116.6 107.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D1029  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 963   SG                                                     
REMARK 620 2 SF4 D1029   S2  110.1                                              
REMARK 620 3 SF4 D1029   S3  105.9 108.2                                        
REMARK 620 4 SF4 D1029   S4  114.2 101.8 116.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AF", "BF", "CF" AND "DF" IN EACH CHAIN      
REMARK 700 ON SHEET RECORDS BELOW IS ACTUALLY AN  8-STRANDED BARREL, THIS       
REMARK 700 IS REPRESENTED BY A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST    
REMARK 700 STRANDS ARE IDENTICAL.                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A1026                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A1027                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A1028                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A1029                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN A1030                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A1031                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IUR A1034                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B1026                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B1027                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B1028                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B1029                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN B1030                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B1031                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IUR B1034                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C1026                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C1027                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C1028                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C1029                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN C1030                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C1031                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IUR C1034                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 D1026                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 D1027                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 D1028                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 D1029                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN D1030                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD D1031                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IUR D1034                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1H7W   RELATED DB: PDB                                   
REMARK 900 DIHYDROPYRIMIDINE DEHYDROGENASE (DPD) FROM PIG                       
REMARK 900 RELATED ID: 1H7X   RELATED DB: PDB                                   
REMARK 900 DIHYDROPYRIMIDINE DEHYDROGENASE (DPD) FROM PIG, TERNARY COMPLEX OF   
REMARK 900 A MUTANT ENZYME (C671A), NADPH AND 5-FLUOROURACIL                    
REMARK 900 RELATED ID: 1GT8   RELATED DB: PDB                                   
REMARK 900 DIHYDROPYRIMIDINE DEHYDROGENASE (DPD) FROM PIG, BINARY COMPLEX WITH  
REMARK 900 NADPH AND URACIL-4-ACETIC ACID                                       
REMARK 900 RELATED ID: 1GTH   RELATED DB: PDB                                   
REMARK 900 DIHYDROPYRIMIDINE DEHYDROGENASE (DPD) FROM PIG, BINARY COMPLEX WITH  
REMARK 900 NADPH AND 5-IODOURACIL                                               
DBREF  1GTE A    1  1025  UNP    Q28943   DPYD_PIG         1   1025             
DBREF  1GTE B    1  1025  UNP    Q28943   DPYD_PIG         1   1025             
DBREF  1GTE C    1  1025  UNP    Q28943   DPYD_PIG         1   1025             
DBREF  1GTE D    1  1025  UNP    Q28943   DPYD_PIG         1   1025             
SEQADV 1GTE ASP A   60  UNP  Q28943    GLY    60 CONFLICT                       
SEQADV 1GTE ASP B   60  UNP  Q28943    GLY    60 CONFLICT                       
SEQADV 1GTE ASP C   60  UNP  Q28943    GLY    60 CONFLICT                       
SEQADV 1GTE ASP D   60  UNP  Q28943    GLY    60 CONFLICT                       
SEQRES   1 A 1025  MET ALA PRO VAL LEU SER LYS ASP VAL ALA ASP ILE GLU          
SEQRES   2 A 1025  SER ILE LEU ALA LEU ASN PRO ARG THR GLN SER HIS ALA          
SEQRES   3 A 1025  ALA LEU HIS SER THR LEU ALA LYS LYS LEU ASP LYS LYS          
SEQRES   4 A 1025  HIS TRP LYS ARG ASN PRO ASP LYS ASN CYS PHE HIS CYS          
SEQRES   5 A 1025  GLU LYS LEU GLU ASN ASN PHE ASP ASP ILE LYS HIS THR          
SEQRES   6 A 1025  THR LEU GLY GLU ARG GLY ALA LEU ARG GLU ALA MET ARG          
SEQRES   7 A 1025  CYS LEU LYS CYS ALA ASP ALA PRO CYS GLN LYS SER CYS          
SEQRES   8 A 1025  PRO THR HIS LEU ASP ILE LYS SER PHE ILE THR SER ILE          
SEQRES   9 A 1025  SER ASN LYS ASN TYR TYR GLY ALA ALA LYS MET ILE PHE          
SEQRES  10 A 1025  SER ASP ASN PRO LEU GLY LEU THR CYS GLY MET VAL CYS          
SEQRES  11 A 1025  PRO THR SER ASP LEU CYS VAL GLY GLY CYS ASN LEU TYR          
SEQRES  12 A 1025  ALA THR GLU GLU GLY SER ILE ASN ILE GLY GLY LEU GLN          
SEQRES  13 A 1025  GLN PHE ALA SER GLU VAL PHE LYS ALA MET ASN ILE PRO          
SEQRES  14 A 1025  GLN ILE ARG ASN PRO CYS LEU PRO SER GLN GLU LYS MET          
SEQRES  15 A 1025  PRO GLU ALA TYR SER ALA LYS ILE ALA LEU LEU GLY ALA          
SEQRES  16 A 1025  GLY PRO ALA SER ILE SER CYS ALA SER PHE LEU ALA ARG          
SEQRES  17 A 1025  LEU GLY TYR SER ASP ILE THR ILE PHE GLU LYS GLN GLU          
SEQRES  18 A 1025  TYR VAL GLY GLY LEU SER THR SER GLU ILE PRO GLN PHE          
SEQRES  19 A 1025  ARG LEU PRO TYR ASP VAL VAL ASN PHE GLU ILE GLU LEU          
SEQRES  20 A 1025  MET LYS ASP LEU GLY VAL LYS ILE ILE CYS GLY LYS SER          
SEQRES  21 A 1025  LEU SER GLU ASN GLU ILE THR LEU ASN THR LEU LYS GLU          
SEQRES  22 A 1025  GLU GLY TYR LYS ALA ALA PHE ILE GLY ILE GLY LEU PRO          
SEQRES  23 A 1025  GLU PRO LYS THR ASP ASP ILE PHE GLN GLY LEU THR GLN          
SEQRES  24 A 1025  ASP GLN GLY PHE TYR THR SER LYS ASP PHE LEU PRO LEU          
SEQRES  25 A 1025  VAL ALA LYS SER SER LYS ALA GLY MET CYS ALA CYS HIS          
SEQRES  26 A 1025  SER PRO LEU PRO SER ILE ARG GLY ALA VAL ILE VAL LEU          
SEQRES  27 A 1025  GLY ALA GLY ASP THR ALA PHE ASP CYS ALA THR SER ALA          
SEQRES  28 A 1025  LEU ARG CYS GLY ALA ARG ARG VAL PHE LEU VAL PHE ARG          
SEQRES  29 A 1025  LYS GLY PHE VAL ASN ILE ARG ALA VAL PRO GLU GLU VAL          
SEQRES  30 A 1025  GLU LEU ALA LYS GLU GLU LYS CYS GLU PHE LEU PRO PHE          
SEQRES  31 A 1025  LEU SER PRO ARG LYS VAL ILE VAL LYS GLY GLY ARG ILE          
SEQRES  32 A 1025  VAL ALA VAL GLN PHE VAL ARG THR GLU GLN ASP GLU THR          
SEQRES  33 A 1025  GLY LYS TRP ASN GLU ASP GLU ASP GLN ILE VAL HIS LEU          
SEQRES  34 A 1025  LYS ALA ASP VAL VAL ILE SER ALA PHE GLY SER VAL LEU          
SEQRES  35 A 1025  ARG ASP PRO LYS VAL LYS GLU ALA LEU SER PRO ILE LYS          
SEQRES  36 A 1025  PHE ASN ARG TRP ASP LEU PRO GLU VAL ASP PRO GLU THR          
SEQRES  37 A 1025  MET GLN THR SER GLU PRO TRP VAL PHE ALA GLY GLY ASP          
SEQRES  38 A 1025  ILE VAL GLY MET ALA ASN THR THR VAL GLU SER VAL ASN          
SEQRES  39 A 1025  ASP GLY LYS GLN ALA SER TRP TYR ILE HIS LYS TYR ILE          
SEQRES  40 A 1025  GLN ALA GLN TYR GLY ALA SER VAL SER ALA LYS PRO GLU          
SEQRES  41 A 1025  LEU PRO LEU PHE TYR THR PRO VAL ASP LEU VAL ASP ILE          
SEQRES  42 A 1025  SER VAL GLU MET ALA GLY LEU LYS PHE ILE ASN PRO PHE          
SEQRES  43 A 1025  GLY LEU ALA SER ALA ALA PRO THR THR SER SER SER MET          
SEQRES  44 A 1025  ILE ARG ARG ALA PHE GLU ALA GLY TRP GLY PHE ALA LEU          
SEQRES  45 A 1025  THR LYS THR PHE SER LEU ASP LYS ASP ILE VAL THR ASN          
SEQRES  46 A 1025  VAL SER PRO ARG ILE VAL ARG GLY THR THR SER GLY PRO          
SEQRES  47 A 1025  MET TYR GLY PRO GLY GLN SER SER PHE LEU ASN ILE GLU          
SEQRES  48 A 1025  LEU ILE SER GLU LYS THR ALA ALA TYR TRP CYS GLN SER          
SEQRES  49 A 1025  VAL THR GLU LEU LYS ALA ASP PHE PRO ASP ASN ILE VAL          
SEQRES  50 A 1025  ILE ALA SER ILE MET CYS SER TYR ASN LYS ASN ASP TRP          
SEQRES  51 A 1025  MET GLU LEU SER ARG LYS ALA GLU ALA SER GLY ALA ASP          
SEQRES  52 A 1025  ALA LEU GLU LEU ASN LEU SER CYS PRO HIS GLY MET GLY          
SEQRES  53 A 1025  GLU ARG GLY MET GLY LEU ALA CYS GLY GLN ASP PRO GLU          
SEQRES  54 A 1025  LEU VAL ARG ASN ILE CYS ARG TRP VAL ARG GLN ALA VAL          
SEQRES  55 A 1025  GLN ILE PRO PHE PHE ALA LYS LEU THR PRO ASN VAL THR          
SEQRES  56 A 1025  ASP ILE VAL SER ILE ALA ARG ALA ALA LYS GLU GLY GLY          
SEQRES  57 A 1025  ALA ASP GLY VAL THR ALA THR ASN THR VAL SER GLY LEU          
SEQRES  58 A 1025  MET GLY LEU LYS ALA ASP GLY THR PRO TRP PRO ALA VAL          
SEQRES  59 A 1025  GLY ALA GLY LYS ARG THR THR TYR GLY GLY VAL SER GLY          
SEQRES  60 A 1025  THR ALA ILE ARG PRO ILE ALA LEU ARG ALA VAL THR THR          
SEQRES  61 A 1025  ILE ALA ARG ALA LEU PRO GLY PHE PRO ILE LEU ALA THR          
SEQRES  62 A 1025  GLY GLY ILE ASP SER ALA GLU SER GLY LEU GLN PHE LEU          
SEQRES  63 A 1025  HIS SER GLY ALA SER VAL LEU GLN VAL CYS SER ALA VAL          
SEQRES  64 A 1025  GLN ASN GLN ASP PHE THR VAL ILE GLN ASP TYR CYS THR          
SEQRES  65 A 1025  GLY LEU LYS ALA LEU LEU TYR LEU LYS SER ILE GLU GLU          
SEQRES  66 A 1025  LEU GLN GLY TRP ASP GLY GLN SER PRO GLY THR GLU SER          
SEQRES  67 A 1025  HIS GLN LYS GLY LYS PRO VAL PRO ARG ILE ALA GLU LEU          
SEQRES  68 A 1025  MET GLY LYS LYS LEU PRO ASN PHE GLY PRO TYR LEU GLU          
SEQRES  69 A 1025  GLN ARG LYS LYS ILE ILE ALA GLU GLU LYS MET ARG LEU          
SEQRES  70 A 1025  LYS GLU GLN ASN ALA ALA PHE PRO PRO LEU GLU ARG LYS          
SEQRES  71 A 1025  PRO PHE ILE PRO LYS LYS PRO ILE PRO ALA ILE LYS ASP          
SEQRES  72 A 1025  VAL ILE GLY LYS ALA LEU GLN TYR LEU GLY THR PHE GLY          
SEQRES  73 A 1025  GLU LEU SER ASN ILE GLU GLN VAL VAL ALA VAL ILE ASP          
SEQRES  74 A 1025  GLU GLU MET CYS ILE ASN CYS GLY LYS CYS TYR MET THR          
SEQRES  75 A 1025  CYS ASN ASP SER GLY TYR GLN ALA ILE GLN PHE ASP PRO          
SEQRES  76 A 1025  GLU THR HIS LEU PRO THR VAL THR ASP THR CYS THR GLY          
SEQRES  77 A 1025  CYS THR LEU CYS LEU SER VAL CYS PRO ILE ILE ASP CYS          
SEQRES  78 A 1025  ILE ARG MET VAL SER ARG THR THR PRO TYR GLU PRO LYS          
SEQRES  79 A 1025  ARG GLY LEU PRO LEU ALA VAL ASN PRO VAL CYS                  
SEQRES   1 B 1025  MET ALA PRO VAL LEU SER LYS ASP VAL ALA ASP ILE GLU          
SEQRES   2 B 1025  SER ILE LEU ALA LEU ASN PRO ARG THR GLN SER HIS ALA          
SEQRES   3 B 1025  ALA LEU HIS SER THR LEU ALA LYS LYS LEU ASP LYS LYS          
SEQRES   4 B 1025  HIS TRP LYS ARG ASN PRO ASP LYS ASN CYS PHE HIS CYS          
SEQRES   5 B 1025  GLU LYS LEU GLU ASN ASN PHE ASP ASP ILE LYS HIS THR          
SEQRES   6 B 1025  THR LEU GLY GLU ARG GLY ALA LEU ARG GLU ALA MET ARG          
SEQRES   7 B 1025  CYS LEU LYS CYS ALA ASP ALA PRO CYS GLN LYS SER CYS          
SEQRES   8 B 1025  PRO THR HIS LEU ASP ILE LYS SER PHE ILE THR SER ILE          
SEQRES   9 B 1025  SER ASN LYS ASN TYR TYR GLY ALA ALA LYS MET ILE PHE          
SEQRES  10 B 1025  SER ASP ASN PRO LEU GLY LEU THR CYS GLY MET VAL CYS          
SEQRES  11 B 1025  PRO THR SER ASP LEU CYS VAL GLY GLY CYS ASN LEU TYR          
SEQRES  12 B 1025  ALA THR GLU GLU GLY SER ILE ASN ILE GLY GLY LEU GLN          
SEQRES  13 B 1025  GLN PHE ALA SER GLU VAL PHE LYS ALA MET ASN ILE PRO          
SEQRES  14 B 1025  GLN ILE ARG ASN PRO CYS LEU PRO SER GLN GLU LYS MET          
SEQRES  15 B 1025  PRO GLU ALA TYR SER ALA LYS ILE ALA LEU LEU GLY ALA          
SEQRES  16 B 1025  GLY PRO ALA SER ILE SER CYS ALA SER PHE LEU ALA ARG          
SEQRES  17 B 1025  LEU GLY TYR SER ASP ILE THR ILE PHE GLU LYS GLN GLU          
SEQRES  18 B 1025  TYR VAL GLY GLY LEU SER THR SER GLU ILE PRO GLN PHE          
SEQRES  19 B 1025  ARG LEU PRO TYR ASP VAL VAL ASN PHE GLU ILE GLU LEU          
SEQRES  20 B 1025  MET LYS ASP LEU GLY VAL LYS ILE ILE CYS GLY LYS SER          
SEQRES  21 B 1025  LEU SER GLU ASN GLU ILE THR LEU ASN THR LEU LYS GLU          
SEQRES  22 B 1025  GLU GLY TYR LYS ALA ALA PHE ILE GLY ILE GLY LEU PRO          
SEQRES  23 B 1025  GLU PRO LYS THR ASP ASP ILE PHE GLN GLY LEU THR GLN          
SEQRES  24 B 1025  ASP GLN GLY PHE TYR THR SER LYS ASP PHE LEU PRO LEU          
SEQRES  25 B 1025  VAL ALA LYS SER SER LYS ALA GLY MET CYS ALA CYS HIS          
SEQRES  26 B 1025  SER PRO LEU PRO SER ILE ARG GLY ALA VAL ILE VAL LEU          
SEQRES  27 B 1025  GLY ALA GLY ASP THR ALA PHE ASP CYS ALA THR SER ALA          
SEQRES  28 B 1025  LEU ARG CYS GLY ALA ARG ARG VAL PHE LEU VAL PHE ARG          
SEQRES  29 B 1025  LYS GLY PHE VAL ASN ILE ARG ALA VAL PRO GLU GLU VAL          
SEQRES  30 B 1025  GLU LEU ALA LYS GLU GLU LYS CYS GLU PHE LEU PRO PHE          
SEQRES  31 B 1025  LEU SER PRO ARG LYS VAL ILE VAL LYS GLY GLY ARG ILE          
SEQRES  32 B 1025  VAL ALA VAL GLN PHE VAL ARG THR GLU GLN ASP GLU THR          
SEQRES  33 B 1025  GLY LYS TRP ASN GLU ASP GLU ASP GLN ILE VAL HIS LEU          
SEQRES  34 B 1025  LYS ALA ASP VAL VAL ILE SER ALA PHE GLY SER VAL LEU          
SEQRES  35 B 1025  ARG ASP PRO LYS VAL LYS GLU ALA LEU SER PRO ILE LYS          
SEQRES  36 B 1025  PHE ASN ARG TRP ASP LEU PRO GLU VAL ASP PRO GLU THR          
SEQRES  37 B 1025  MET GLN THR SER GLU PRO TRP VAL PHE ALA GLY GLY ASP          
SEQRES  38 B 1025  ILE VAL GLY MET ALA ASN THR THR VAL GLU SER VAL ASN          
SEQRES  39 B 1025  ASP GLY LYS GLN ALA SER TRP TYR ILE HIS LYS TYR ILE          
SEQRES  40 B 1025  GLN ALA GLN TYR GLY ALA SER VAL SER ALA LYS PRO GLU          
SEQRES  41 B 1025  LEU PRO LEU PHE TYR THR PRO VAL ASP LEU VAL ASP ILE          
SEQRES  42 B 1025  SER VAL GLU MET ALA GLY LEU LYS PHE ILE ASN PRO PHE          
SEQRES  43 B 1025  GLY LEU ALA SER ALA ALA PRO THR THR SER SER SER MET          
SEQRES  44 B 1025  ILE ARG ARG ALA PHE GLU ALA GLY TRP GLY PHE ALA LEU          
SEQRES  45 B 1025  THR LYS THR PHE SER LEU ASP LYS ASP ILE VAL THR ASN          
SEQRES  46 B 1025  VAL SER PRO ARG ILE VAL ARG GLY THR THR SER GLY PRO          
SEQRES  47 B 1025  MET TYR GLY PRO GLY GLN SER SER PHE LEU ASN ILE GLU          
SEQRES  48 B 1025  LEU ILE SER GLU LYS THR ALA ALA TYR TRP CYS GLN SER          
SEQRES  49 B 1025  VAL THR GLU LEU LYS ALA ASP PHE PRO ASP ASN ILE VAL          
SEQRES  50 B 1025  ILE ALA SER ILE MET CYS SER TYR ASN LYS ASN ASP TRP          
SEQRES  51 B 1025  MET GLU LEU SER ARG LYS ALA GLU ALA SER GLY ALA ASP          
SEQRES  52 B 1025  ALA LEU GLU LEU ASN LEU SER CYS PRO HIS GLY MET GLY          
SEQRES  53 B 1025  GLU ARG GLY MET GLY LEU ALA CYS GLY GLN ASP PRO GLU          
SEQRES  54 B 1025  LEU VAL ARG ASN ILE CYS ARG TRP VAL ARG GLN ALA VAL          
SEQRES  55 B 1025  GLN ILE PRO PHE PHE ALA LYS LEU THR PRO ASN VAL THR          
SEQRES  56 B 1025  ASP ILE VAL SER ILE ALA ARG ALA ALA LYS GLU GLY GLY          
SEQRES  57 B 1025  ALA ASP GLY VAL THR ALA THR ASN THR VAL SER GLY LEU          
SEQRES  58 B 1025  MET GLY LEU LYS ALA ASP GLY THR PRO TRP PRO ALA VAL          
SEQRES  59 B 1025  GLY ALA GLY LYS ARG THR THR TYR GLY GLY VAL SER GLY          
SEQRES  60 B 1025  THR ALA ILE ARG PRO ILE ALA LEU ARG ALA VAL THR THR          
SEQRES  61 B 1025  ILE ALA ARG ALA LEU PRO GLY PHE PRO ILE LEU ALA THR          
SEQRES  62 B 1025  GLY GLY ILE ASP SER ALA GLU SER GLY LEU GLN PHE LEU          
SEQRES  63 B 1025  HIS SER GLY ALA SER VAL LEU GLN VAL CYS SER ALA VAL          
SEQRES  64 B 1025  GLN ASN GLN ASP PHE THR VAL ILE GLN ASP TYR CYS THR          
SEQRES  65 B 1025  GLY LEU LYS ALA LEU LEU TYR LEU LYS SER ILE GLU GLU          
SEQRES  66 B 1025  LEU GLN GLY TRP ASP GLY GLN SER PRO GLY THR GLU SER          
SEQRES  67 B 1025  HIS GLN LYS GLY LYS PRO VAL PRO ARG ILE ALA GLU LEU          
SEQRES  68 B 1025  MET GLY LYS LYS LEU PRO ASN PHE GLY PRO TYR LEU GLU          
SEQRES  69 B 1025  GLN ARG LYS LYS ILE ILE ALA GLU GLU LYS MET ARG LEU          
SEQRES  70 B 1025  LYS GLU GLN ASN ALA ALA PHE PRO PRO LEU GLU ARG LYS          
SEQRES  71 B 1025  PRO PHE ILE PRO LYS LYS PRO ILE PRO ALA ILE LYS ASP          
SEQRES  72 B 1025  VAL ILE GLY LYS ALA LEU GLN TYR LEU GLY THR PHE GLY          
SEQRES  73 B 1025  GLU LEU SER ASN ILE GLU GLN VAL VAL ALA VAL ILE ASP          
SEQRES  74 B 1025  GLU GLU MET CYS ILE ASN CYS GLY LYS CYS TYR MET THR          
SEQRES  75 B 1025  CYS ASN ASP SER GLY TYR GLN ALA ILE GLN PHE ASP PRO          
SEQRES  76 B 1025  GLU THR HIS LEU PRO THR VAL THR ASP THR CYS THR GLY          
SEQRES  77 B 1025  CYS THR LEU CYS LEU SER VAL CYS PRO ILE ILE ASP CYS          
SEQRES  78 B 1025  ILE ARG MET VAL SER ARG THR THR PRO TYR GLU PRO LYS          
SEQRES  79 B 1025  ARG GLY LEU PRO LEU ALA VAL ASN PRO VAL CYS                  
SEQRES   1 C 1025  MET ALA PRO VAL LEU SER LYS ASP VAL ALA ASP ILE GLU          
SEQRES   2 C 1025  SER ILE LEU ALA LEU ASN PRO ARG THR GLN SER HIS ALA          
SEQRES   3 C 1025  ALA LEU HIS SER THR LEU ALA LYS LYS LEU ASP LYS LYS          
SEQRES   4 C 1025  HIS TRP LYS ARG ASN PRO ASP LYS ASN CYS PHE HIS CYS          
SEQRES   5 C 1025  GLU LYS LEU GLU ASN ASN PHE ASP ASP ILE LYS HIS THR          
SEQRES   6 C 1025  THR LEU GLY GLU ARG GLY ALA LEU ARG GLU ALA MET ARG          
SEQRES   7 C 1025  CYS LEU LYS CYS ALA ASP ALA PRO CYS GLN LYS SER CYS          
SEQRES   8 C 1025  PRO THR HIS LEU ASP ILE LYS SER PHE ILE THR SER ILE          
SEQRES   9 C 1025  SER ASN LYS ASN TYR TYR GLY ALA ALA LYS MET ILE PHE          
SEQRES  10 C 1025  SER ASP ASN PRO LEU GLY LEU THR CYS GLY MET VAL CYS          
SEQRES  11 C 1025  PRO THR SER ASP LEU CYS VAL GLY GLY CYS ASN LEU TYR          
SEQRES  12 C 1025  ALA THR GLU GLU GLY SER ILE ASN ILE GLY GLY LEU GLN          
SEQRES  13 C 1025  GLN PHE ALA SER GLU VAL PHE LYS ALA MET ASN ILE PRO          
SEQRES  14 C 1025  GLN ILE ARG ASN PRO CYS LEU PRO SER GLN GLU LYS MET          
SEQRES  15 C 1025  PRO GLU ALA TYR SER ALA LYS ILE ALA LEU LEU GLY ALA          
SEQRES  16 C 1025  GLY PRO ALA SER ILE SER CYS ALA SER PHE LEU ALA ARG          
SEQRES  17 C 1025  LEU GLY TYR SER ASP ILE THR ILE PHE GLU LYS GLN GLU          
SEQRES  18 C 1025  TYR VAL GLY GLY LEU SER THR SER GLU ILE PRO GLN PHE          
SEQRES  19 C 1025  ARG LEU PRO TYR ASP VAL VAL ASN PHE GLU ILE GLU LEU          
SEQRES  20 C 1025  MET LYS ASP LEU GLY VAL LYS ILE ILE CYS GLY LYS SER          
SEQRES  21 C 1025  LEU SER GLU ASN GLU ILE THR LEU ASN THR LEU LYS GLU          
SEQRES  22 C 1025  GLU GLY TYR LYS ALA ALA PHE ILE GLY ILE GLY LEU PRO          
SEQRES  23 C 1025  GLU PRO LYS THR ASP ASP ILE PHE GLN GLY LEU THR GLN          
SEQRES  24 C 1025  ASP GLN GLY PHE TYR THR SER LYS ASP PHE LEU PRO LEU          
SEQRES  25 C 1025  VAL ALA LYS SER SER LYS ALA GLY MET CYS ALA CYS HIS          
SEQRES  26 C 1025  SER PRO LEU PRO SER ILE ARG GLY ALA VAL ILE VAL LEU          
SEQRES  27 C 1025  GLY ALA GLY ASP THR ALA PHE ASP CYS ALA THR SER ALA          
SEQRES  28 C 1025  LEU ARG CYS GLY ALA ARG ARG VAL PHE LEU VAL PHE ARG          
SEQRES  29 C 1025  LYS GLY PHE VAL ASN ILE ARG ALA VAL PRO GLU GLU VAL          
SEQRES  30 C 1025  GLU LEU ALA LYS GLU GLU LYS CYS GLU PHE LEU PRO PHE          
SEQRES  31 C 1025  LEU SER PRO ARG LYS VAL ILE VAL LYS GLY GLY ARG ILE          
SEQRES  32 C 1025  VAL ALA VAL GLN PHE VAL ARG THR GLU GLN ASP GLU THR          
SEQRES  33 C 1025  GLY LYS TRP ASN GLU ASP GLU ASP GLN ILE VAL HIS LEU          
SEQRES  34 C 1025  LYS ALA ASP VAL VAL ILE SER ALA PHE GLY SER VAL LEU          
SEQRES  35 C 1025  ARG ASP PRO LYS VAL LYS GLU ALA LEU SER PRO ILE LYS          
SEQRES  36 C 1025  PHE ASN ARG TRP ASP LEU PRO GLU VAL ASP PRO GLU THR          
SEQRES  37 C 1025  MET GLN THR SER GLU PRO TRP VAL PHE ALA GLY GLY ASP          
SEQRES  38 C 1025  ILE VAL GLY MET ALA ASN THR THR VAL GLU SER VAL ASN          
SEQRES  39 C 1025  ASP GLY LYS GLN ALA SER TRP TYR ILE HIS LYS TYR ILE          
SEQRES  40 C 1025  GLN ALA GLN TYR GLY ALA SER VAL SER ALA LYS PRO GLU          
SEQRES  41 C 1025  LEU PRO LEU PHE TYR THR PRO VAL ASP LEU VAL ASP ILE          
SEQRES  42 C 1025  SER VAL GLU MET ALA GLY LEU LYS PHE ILE ASN PRO PHE          
SEQRES  43 C 1025  GLY LEU ALA SER ALA ALA PRO THR THR SER SER SER MET          
SEQRES  44 C 1025  ILE ARG ARG ALA PHE GLU ALA GLY TRP GLY PHE ALA LEU          
SEQRES  45 C 1025  THR LYS THR PHE SER LEU ASP LYS ASP ILE VAL THR ASN          
SEQRES  46 C 1025  VAL SER PRO ARG ILE VAL ARG GLY THR THR SER GLY PRO          
SEQRES  47 C 1025  MET TYR GLY PRO GLY GLN SER SER PHE LEU ASN ILE GLU          
SEQRES  48 C 1025  LEU ILE SER GLU LYS THR ALA ALA TYR TRP CYS GLN SER          
SEQRES  49 C 1025  VAL THR GLU LEU LYS ALA ASP PHE PRO ASP ASN ILE VAL          
SEQRES  50 C 1025  ILE ALA SER ILE MET CYS SER TYR ASN LYS ASN ASP TRP          
SEQRES  51 C 1025  MET GLU LEU SER ARG LYS ALA GLU ALA SER GLY ALA ASP          
SEQRES  52 C 1025  ALA LEU GLU LEU ASN LEU SER CYS PRO HIS GLY MET GLY          
SEQRES  53 C 1025  GLU ARG GLY MET GLY LEU ALA CYS GLY GLN ASP PRO GLU          
SEQRES  54 C 1025  LEU VAL ARG ASN ILE CYS ARG TRP VAL ARG GLN ALA VAL          
SEQRES  55 C 1025  GLN ILE PRO PHE PHE ALA LYS LEU THR PRO ASN VAL THR          
SEQRES  56 C 1025  ASP ILE VAL SER ILE ALA ARG ALA ALA LYS GLU GLY GLY          
SEQRES  57 C 1025  ALA ASP GLY VAL THR ALA THR ASN THR VAL SER GLY LEU          
SEQRES  58 C 1025  MET GLY LEU LYS ALA ASP GLY THR PRO TRP PRO ALA VAL          
SEQRES  59 C 1025  GLY ALA GLY LYS ARG THR THR TYR GLY GLY VAL SER GLY          
SEQRES  60 C 1025  THR ALA ILE ARG PRO ILE ALA LEU ARG ALA VAL THR THR          
SEQRES  61 C 1025  ILE ALA ARG ALA LEU PRO GLY PHE PRO ILE LEU ALA THR          
SEQRES  62 C 1025  GLY GLY ILE ASP SER ALA GLU SER GLY LEU GLN PHE LEU          
SEQRES  63 C 1025  HIS SER GLY ALA SER VAL LEU GLN VAL CYS SER ALA VAL          
SEQRES  64 C 1025  GLN ASN GLN ASP PHE THR VAL ILE GLN ASP TYR CYS THR          
SEQRES  65 C 1025  GLY LEU LYS ALA LEU LEU TYR LEU LYS SER ILE GLU GLU          
SEQRES  66 C 1025  LEU GLN GLY TRP ASP GLY GLN SER PRO GLY THR GLU SER          
SEQRES  67 C 1025  HIS GLN LYS GLY LYS PRO VAL PRO ARG ILE ALA GLU LEU          
SEQRES  68 C 1025  MET GLY LYS LYS LEU PRO ASN PHE GLY PRO TYR LEU GLU          
SEQRES  69 C 1025  GLN ARG LYS LYS ILE ILE ALA GLU GLU LYS MET ARG LEU          
SEQRES  70 C 1025  LYS GLU GLN ASN ALA ALA PHE PRO PRO LEU GLU ARG LYS          
SEQRES  71 C 1025  PRO PHE ILE PRO LYS LYS PRO ILE PRO ALA ILE LYS ASP          
SEQRES  72 C 1025  VAL ILE GLY LYS ALA LEU GLN TYR LEU GLY THR PHE GLY          
SEQRES  73 C 1025  GLU LEU SER ASN ILE GLU GLN VAL VAL ALA VAL ILE ASP          
SEQRES  74 C 1025  GLU GLU MET CYS ILE ASN CYS GLY LYS CYS TYR MET THR          
SEQRES  75 C 1025  CYS ASN ASP SER GLY TYR GLN ALA ILE GLN PHE ASP PRO          
SEQRES  76 C 1025  GLU THR HIS LEU PRO THR VAL THR ASP THR CYS THR GLY          
SEQRES  77 C 1025  CYS THR LEU CYS LEU SER VAL CYS PRO ILE ILE ASP CYS          
SEQRES  78 C 1025  ILE ARG MET VAL SER ARG THR THR PRO TYR GLU PRO LYS          
SEQRES  79 C 1025  ARG GLY LEU PRO LEU ALA VAL ASN PRO VAL CYS                  
SEQRES   1 D 1025  MET ALA PRO VAL LEU SER LYS ASP VAL ALA ASP ILE GLU          
SEQRES   2 D 1025  SER ILE LEU ALA LEU ASN PRO ARG THR GLN SER HIS ALA          
SEQRES   3 D 1025  ALA LEU HIS SER THR LEU ALA LYS LYS LEU ASP LYS LYS          
SEQRES   4 D 1025  HIS TRP LYS ARG ASN PRO ASP LYS ASN CYS PHE HIS CYS          
SEQRES   5 D 1025  GLU LYS LEU GLU ASN ASN PHE ASP ASP ILE LYS HIS THR          
SEQRES   6 D 1025  THR LEU GLY GLU ARG GLY ALA LEU ARG GLU ALA MET ARG          
SEQRES   7 D 1025  CYS LEU LYS CYS ALA ASP ALA PRO CYS GLN LYS SER CYS          
SEQRES   8 D 1025  PRO THR HIS LEU ASP ILE LYS SER PHE ILE THR SER ILE          
SEQRES   9 D 1025  SER ASN LYS ASN TYR TYR GLY ALA ALA LYS MET ILE PHE          
SEQRES  10 D 1025  SER ASP ASN PRO LEU GLY LEU THR CYS GLY MET VAL CYS          
SEQRES  11 D 1025  PRO THR SER ASP LEU CYS VAL GLY GLY CYS ASN LEU TYR          
SEQRES  12 D 1025  ALA THR GLU GLU GLY SER ILE ASN ILE GLY GLY LEU GLN          
SEQRES  13 D 1025  GLN PHE ALA SER GLU VAL PHE LYS ALA MET ASN ILE PRO          
SEQRES  14 D 1025  GLN ILE ARG ASN PRO CYS LEU PRO SER GLN GLU LYS MET          
SEQRES  15 D 1025  PRO GLU ALA TYR SER ALA LYS ILE ALA LEU LEU GLY ALA          
SEQRES  16 D 1025  GLY PRO ALA SER ILE SER CYS ALA SER PHE LEU ALA ARG          
SEQRES  17 D 1025  LEU GLY TYR SER ASP ILE THR ILE PHE GLU LYS GLN GLU          
SEQRES  18 D 1025  TYR VAL GLY GLY LEU SER THR SER GLU ILE PRO GLN PHE          
SEQRES  19 D 1025  ARG LEU PRO TYR ASP VAL VAL ASN PHE GLU ILE GLU LEU          
SEQRES  20 D 1025  MET LYS ASP LEU GLY VAL LYS ILE ILE CYS GLY LYS SER          
SEQRES  21 D 1025  LEU SER GLU ASN GLU ILE THR LEU ASN THR LEU LYS GLU          
SEQRES  22 D 1025  GLU GLY TYR LYS ALA ALA PHE ILE GLY ILE GLY LEU PRO          
SEQRES  23 D 1025  GLU PRO LYS THR ASP ASP ILE PHE GLN GLY LEU THR GLN          
SEQRES  24 D 1025  ASP GLN GLY PHE TYR THR SER LYS ASP PHE LEU PRO LEU          
SEQRES  25 D 1025  VAL ALA LYS SER SER LYS ALA GLY MET CYS ALA CYS HIS          
SEQRES  26 D 1025  SER PRO LEU PRO SER ILE ARG GLY ALA VAL ILE VAL LEU          
SEQRES  27 D 1025  GLY ALA GLY ASP THR ALA PHE ASP CYS ALA THR SER ALA          
SEQRES  28 D 1025  LEU ARG CYS GLY ALA ARG ARG VAL PHE LEU VAL PHE ARG          
SEQRES  29 D 1025  LYS GLY PHE VAL ASN ILE ARG ALA VAL PRO GLU GLU VAL          
SEQRES  30 D 1025  GLU LEU ALA LYS GLU GLU LYS CYS GLU PHE LEU PRO PHE          
SEQRES  31 D 1025  LEU SER PRO ARG LYS VAL ILE VAL LYS GLY GLY ARG ILE          
SEQRES  32 D 1025  VAL ALA VAL GLN PHE VAL ARG THR GLU GLN ASP GLU THR          
SEQRES  33 D 1025  GLY LYS TRP ASN GLU ASP GLU ASP GLN ILE VAL HIS LEU          
SEQRES  34 D 1025  LYS ALA ASP VAL VAL ILE SER ALA PHE GLY SER VAL LEU          
SEQRES  35 D 1025  ARG ASP PRO LYS VAL LYS GLU ALA LEU SER PRO ILE LYS          
SEQRES  36 D 1025  PHE ASN ARG TRP ASP LEU PRO GLU VAL ASP PRO GLU THR          
SEQRES  37 D 1025  MET GLN THR SER GLU PRO TRP VAL PHE ALA GLY GLY ASP          
SEQRES  38 D 1025  ILE VAL GLY MET ALA ASN THR THR VAL GLU SER VAL ASN          
SEQRES  39 D 1025  ASP GLY LYS GLN ALA SER TRP TYR ILE HIS LYS TYR ILE          
SEQRES  40 D 1025  GLN ALA GLN TYR GLY ALA SER VAL SER ALA LYS PRO GLU          
SEQRES  41 D 1025  LEU PRO LEU PHE TYR THR PRO VAL ASP LEU VAL ASP ILE          
SEQRES  42 D 1025  SER VAL GLU MET ALA GLY LEU LYS PHE ILE ASN PRO PHE          
SEQRES  43 D 1025  GLY LEU ALA SER ALA ALA PRO THR THR SER SER SER MET          
SEQRES  44 D 1025  ILE ARG ARG ALA PHE GLU ALA GLY TRP GLY PHE ALA LEU          
SEQRES  45 D 1025  THR LYS THR PHE SER LEU ASP LYS ASP ILE VAL THR ASN          
SEQRES  46 D 1025  VAL SER PRO ARG ILE VAL ARG GLY THR THR SER GLY PRO          
SEQRES  47 D 1025  MET TYR GLY PRO GLY GLN SER SER PHE LEU ASN ILE GLU          
SEQRES  48 D 1025  LEU ILE SER GLU LYS THR ALA ALA TYR TRP CYS GLN SER          
SEQRES  49 D 1025  VAL THR GLU LEU LYS ALA ASP PHE PRO ASP ASN ILE VAL          
SEQRES  50 D 1025  ILE ALA SER ILE MET CYS SER TYR ASN LYS ASN ASP TRP          
SEQRES  51 D 1025  MET GLU LEU SER ARG LYS ALA GLU ALA SER GLY ALA ASP          
SEQRES  52 D 1025  ALA LEU GLU LEU ASN LEU SER CYS PRO HIS GLY MET GLY          
SEQRES  53 D 1025  GLU ARG GLY MET GLY LEU ALA CYS GLY GLN ASP PRO GLU          
SEQRES  54 D 1025  LEU VAL ARG ASN ILE CYS ARG TRP VAL ARG GLN ALA VAL          
SEQRES  55 D 1025  GLN ILE PRO PHE PHE ALA LYS LEU THR PRO ASN VAL THR          
SEQRES  56 D 1025  ASP ILE VAL SER ILE ALA ARG ALA ALA LYS GLU GLY GLY          
SEQRES  57 D 1025  ALA ASP GLY VAL THR ALA THR ASN THR VAL SER GLY LEU          
SEQRES  58 D 1025  MET GLY LEU LYS ALA ASP GLY THR PRO TRP PRO ALA VAL          
SEQRES  59 D 1025  GLY ALA GLY LYS ARG THR THR TYR GLY GLY VAL SER GLY          
SEQRES  60 D 1025  THR ALA ILE ARG PRO ILE ALA LEU ARG ALA VAL THR THR          
SEQRES  61 D 1025  ILE ALA ARG ALA LEU PRO GLY PHE PRO ILE LEU ALA THR          
SEQRES  62 D 1025  GLY GLY ILE ASP SER ALA GLU SER GLY LEU GLN PHE LEU          
SEQRES  63 D 1025  HIS SER GLY ALA SER VAL LEU GLN VAL CYS SER ALA VAL          
SEQRES  64 D 1025  GLN ASN GLN ASP PHE THR VAL ILE GLN ASP TYR CYS THR          
SEQRES  65 D 1025  GLY LEU LYS ALA LEU LEU TYR LEU LYS SER ILE GLU GLU          
SEQRES  66 D 1025  LEU GLN GLY TRP ASP GLY GLN SER PRO GLY THR GLU SER          
SEQRES  67 D 1025  HIS GLN LYS GLY LYS PRO VAL PRO ARG ILE ALA GLU LEU          
SEQRES  68 D 1025  MET GLY LYS LYS LEU PRO ASN PHE GLY PRO TYR LEU GLU          
SEQRES  69 D 1025  GLN ARG LYS LYS ILE ILE ALA GLU GLU LYS MET ARG LEU          
SEQRES  70 D 1025  LYS GLU GLN ASN ALA ALA PHE PRO PRO LEU GLU ARG LYS          
SEQRES  71 D 1025  PRO PHE ILE PRO LYS LYS PRO ILE PRO ALA ILE LYS ASP          
SEQRES  72 D 1025  VAL ILE GLY LYS ALA LEU GLN TYR LEU GLY THR PHE GLY          
SEQRES  73 D 1025  GLU LEU SER ASN ILE GLU GLN VAL VAL ALA VAL ILE ASP          
SEQRES  74 D 1025  GLU GLU MET CYS ILE ASN CYS GLY LYS CYS TYR MET THR          
SEQRES  75 D 1025  CYS ASN ASP SER GLY TYR GLN ALA ILE GLN PHE ASP PRO          
SEQRES  76 D 1025  GLU THR HIS LEU PRO THR VAL THR ASP THR CYS THR GLY          
SEQRES  77 D 1025  CYS THR LEU CYS LEU SER VAL CYS PRO ILE ILE ASP CYS          
SEQRES  78 D 1025  ILE ARG MET VAL SER ARG THR THR PRO TYR GLU PRO LYS          
SEQRES  79 D 1025  ARG GLY LEU PRO LEU ALA VAL ASN PRO VAL CYS                  
HET    SF4  A1026       8                                                       
HET    SF4  A1027       8                                                       
HET    SF4  A1028       8                                                       
HET    SF4  A1029       8                                                       
HET    FMN  A1030      31                                                       
HET    FAD  A1031      53                                                       
HET    IUR  A1034       9                                                       
HET    SF4  B1026       8                                                       
HET    SF4  B1027       8                                                       
HET    SF4  B1028       8                                                       
HET    SF4  B1029       8                                                       
HET    FMN  B1030      31                                                       
HET    FAD  B1031      53                                                       
HET    IUR  B1034       9                                                       
HET    SF4  C1026       8                                                       
HET    SF4  C1027       8                                                       
HET    SF4  C1028       8                                                       
HET    SF4  C1029       8                                                       
HET    FMN  C1030      31                                                       
HET    FAD  C1031      53                                                       
HET    IUR  C1034       9                                                       
HET    SF4  D1026       8                                                       
HET    SF4  D1027       8                                                       
HET    SF4  D1028       8                                                       
HET    SF4  D1029       8                                                       
HET    FMN  D1030      31                                                       
HET    FAD  D1031      53                                                       
HET    IUR  D1034       9                                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     FMN FLAVIN MONONUCLEOTIDE                                            
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     IUR 5-IODOURACIL                                                     
HETSYN     FMN RIBOFLAVIN MONOPHOSPHATE                                         
FORMUL   5  SF4    16(FE4 S4)                                                   
FORMUL   9  FMN    4(C17 H21 N4 O9 P)                                           
FORMUL  10  FAD    4(C27 H33 N9 O15 P2)                                         
FORMUL  11  IUR    4(C4 H3 I N2 O2)                                             
FORMUL  33  HOH   *4848(H2 O)                                                   
HELIX    1   1 VAL A    9  LEU A   16  1                                   8    
HELIX    2   2 SER A   30  LYS A   42  1                                  13    
HELIX    3   3 GLY A   68  CYS A   79  1                                  12    
HELIX    4   4 ALA A   85  SER A   90  1                                   6    
HELIX    5   5 ASP A   96  ASN A  106  1                                  11    
HELIX    6   6 ASN A  108  ASN A  120  1                                  13    
HELIX    7   7 LEU A  122  CYS A  130  1                                   9    
HELIX    8   8 PRO A  131  LEU A  135  5                                   5    
HELIX    9   9 LEU A  135  CYS A  140  5                                   6    
HELIX   10  10 CYS A  140  THR A  145  5                                   6    
HELIX   11  11 ASN A  151  ASN A  167  1                                  17    
HELIX   12  12 SER A  178  MET A  182  5                                   5    
HELIX   13  13 PRO A  183  ALA A  188  5                                   6    
HELIX   14  14 GLY A  196  LEU A  209  1                                  14    
HELIX   15  15 GLY A  225  GLU A  230  1                                   6    
HELIX   16  16 PRO A  237  ASP A  250  1                                  14    
HELIX   17  17 THR A  267  GLU A  274  1                                   8    
HELIX   18  18 ASP A  291  GLN A  295  5                                   5    
HELIX   19  19 SER A  306  LYS A  318  1                                  13    
HELIX   20  20 GLY A  341  CYS A  354  1                                  14    
HELIX   21  21 GLY A  366  ILE A  370  5                                   5    
HELIX   22  22 VAL A  373  GLU A  383  1                                  11    
HELIX   23  23 ASP A  444  LEU A  451  1                                   8    
HELIX   24  24 GLY A  480  GLY A  484  5                                   5    
HELIX   25  25 THR A  488  TYR A  511  1                                  24    
HELIX   26  26 THR A  526  VAL A  531  5                                   6    
HELIX   27  27 ALA A  551  THR A  555  5                                   5    
HELIX   28  28 SER A  556  GLY A  567  1                                  12    
HELIX   29  29 LEU A  578  ILE A  582  5                                   5    
HELIX   30  30 THR A  617  PHE A  632  1                                  16    
HELIX   31  31 ASN A  646  SER A  660  1                                  15    
HELIX   32  32 CYS A  684  GLN A  686  5                                   3    
HELIX   33  33 ASP A  687  VAL A  702  1                                  16    
HELIX   34  34 ASP A  716  GLY A  728  1                                  13    
HELIX   35  35 GLY A  767  ALA A  769  5                                   3    
HELIX   36  36 ILE A  770  LEU A  785  1                                  16    
HELIX   37  37 SER A  798  SER A  808  1                                  11    
HELIX   38  38 CYS A  816  ASN A  821  1                                   6    
HELIX   39  39 THR A  825  LYS A  841  1                                  17    
HELIX   40  40 SER A  842  GLN A  847  5                                   6    
HELIX   41  41 PHE A  879  GLN A  900  1                                  22    
HELIX   42  42 ALA A  920  ILE A  925  1                                   6    
HELIX   43  43 ALA A  928  TYR A  931  5                                   4    
HELIX   44  44 THR A  934  LEU A  938  5                                   5    
HELIX   45  45 GLY A  957  GLY A  967  1                                  11    
HELIX   46  46 THR A  990  CYS A  996  1                                   7    
HELIX   47  47 VAL B    9  LEU B   16  1                                   8    
HELIX   48  48 SER B   30  LYS B   42  1                                  13    
HELIX   49  49 GLY B   68  CYS B   79  1                                  12    
HELIX   50  50 ALA B   85  SER B   90  1                                   6    
HELIX   51  51 ASP B   96  ASN B  106  1                                  11    
HELIX   52  52 ASN B  108  ASN B  120  1                                  13    
HELIX   53  53 LEU B  122  CYS B  130  1                                   9    
HELIX   54  54 PRO B  131  LEU B  135  5                                   5    
HELIX   55  55 LEU B  135  CYS B  140  5                                   6    
HELIX   56  56 CYS B  140  THR B  145  5                                   6    
HELIX   57  57 ASN B  151  ASN B  167  1                                  17    
HELIX   58  58 SER B  178  MET B  182  5                                   5    
HELIX   59  59 PRO B  183  ALA B  188  5                                   6    
HELIX   60  60 GLY B  196  GLY B  210  1                                  15    
HELIX   61  61 GLY B  225  GLU B  230  1                                   6    
HELIX   62  62 PRO B  237  ASP B  250  1                                  14    
HELIX   63  63 THR B  267  GLU B  274  1                                   8    
HELIX   64  64 ASP B  291  GLN B  295  5                                   5    
HELIX   65  65 SER B  306  LYS B  318  1                                  13    
HELIX   66  66 GLY B  341  CYS B  354  1                                  14    
HELIX   67  67 GLY B  366  ILE B  370  5                                   5    
HELIX   68  68 VAL B  373  GLU B  383  1                                  11    
HELIX   69  69 ASP B  444  LEU B  451  1                                   8    
HELIX   70  70 GLY B  480  GLY B  484  5                                   5    
HELIX   71  71 THR B  488  TYR B  511  1                                  24    
HELIX   72  72 THR B  526  VAL B  531  5                                   6    
HELIX   73  73 ALA B  551  THR B  555  5                                   5    
HELIX   74  74 SER B  556  GLY B  567  1                                  12    
HELIX   75  75 LEU B  578  ILE B  582  5                                   5    
HELIX   76  76 THR B  617  PHE B  632  1                                  16    
HELIX   77  77 ASN B  646  SER B  660  1                                  15    
HELIX   78  78 CYS B  684  GLN B  686  5                                   3    
HELIX   79  79 ASP B  687  VAL B  702  1                                  16    
HELIX   80  80 ASP B  716  GLY B  727  1                                  12    
HELIX   81  81 GLY B  767  ALA B  769  5                                   3    
HELIX   82  82 ILE B  770  LEU B  785  1                                  16    
HELIX   83  83 SER B  798  SER B  808  1                                  11    
HELIX   84  84 CYS B  816  ASN B  821  1                                   6    
HELIX   85  85 THR B  825  LYS B  841  1                                  17    
HELIX   86  86 SER B  842  GLN B  847  5                                   6    
HELIX   87  87 PHE B  879  GLN B  900  1                                  22    
HELIX   88  88 ALA B  920  ILE B  925  1                                   6    
HELIX   89  89 ALA B  928  TYR B  931  5                                   4    
HELIX   90  90 THR B  934  LEU B  938  5                                   5    
HELIX   91  91 GLY B  957  GLY B  967  1                                  11    
HELIX   92  92 THR B  990  CYS B  996  1                                   7    
HELIX   93  93 VAL C    9  LEU C   16  1                                   8    
HELIX   94  94 SER C   30  LYS C   42  1                                  13    
HELIX   95  95 GLY C   68  CYS C   79  1                                  12    
HELIX   96  96 ALA C   85  SER C   90  1                                   6    
HELIX   97  97 ASP C   96  ASN C  106  1                                  11    
HELIX   98  98 ASN C  108  ASN C  120  1                                  13    
HELIX   99  99 LEU C  122  CYS C  130  1                                   9    
HELIX  100 100 PRO C  131  LEU C  135  5                                   5    
HELIX  101 101 LEU C  135  CYS C  140  5                                   6    
HELIX  102 102 CYS C  140  THR C  145  5                                   6    
HELIX  103 103 ASN C  151  ASN C  167  1                                  17    
HELIX  104 104 SER C  178  MET C  182  5                                   5    
HELIX  105 105 PRO C  183  ALA C  188  5                                   6    
HELIX  106 106 GLY C  196  GLY C  210  1                                  15    
HELIX  107 107 GLY C  225  GLU C  230  1                                   6    
HELIX  108 108 PRO C  237  ASP C  250  1                                  14    
HELIX  109 109 THR C  267  GLU C  274  1                                   8    
HELIX  110 110 ASP C  291  GLN C  295  5                                   5    
HELIX  111 111 SER C  306  LYS C  318  1                                  13    
HELIX  112 112 GLY C  341  CYS C  354  1                                  14    
HELIX  113 113 GLY C  366  ILE C  370  5                                   5    
HELIX  114 114 VAL C  373  GLU C  383  1                                  11    
HELIX  115 115 ASP C  444  LEU C  451  1                                   8    
HELIX  116 116 GLY C  480  GLY C  484  5                                   5    
HELIX  117 117 THR C  488  TYR C  511  1                                  24    
HELIX  118 118 THR C  526  VAL C  531  5                                   6    
HELIX  119 119 ALA C  551  THR C  555  5                                   5    
HELIX  120 120 SER C  556  GLY C  567  1                                  12    
HELIX  121 121 LEU C  578  ILE C  582  5                                   5    
HELIX  122 122 THR C  617  PHE C  632  1                                  16    
HELIX  123 123 ASN C  646  SER C  660  1                                  15    
HELIX  124 124 CYS C  684  GLN C  686  5                                   3    
HELIX  125 125 ASP C  687  VAL C  702  1                                  16    
HELIX  126 126 ASP C  716  GLY C  727  1                                  12    
HELIX  127 127 GLY C  767  ALA C  769  5                                   3    
HELIX  128 128 ILE C  770  LEU C  785  1                                  16    
HELIX  129 129 SER C  798  SER C  808  1                                  11    
HELIX  130 130 CYS C  816  ASN C  821  1                                   6    
HELIX  131 131 THR C  825  LYS C  841  1                                  17    
HELIX  132 132 SER C  842  GLN C  847  5                                   6    
HELIX  133 133 PHE C  879  LYS C  898  1                                  20    
HELIX  134 134 ALA C  920  ILE C  925  1                                   6    
HELIX  135 135 ALA C  928  TYR C  931  5                                   4    
HELIX  136 136 THR C  934  LEU C  938  5                                   5    
HELIX  137 137 GLY C  957  GLY C  967  1                                  11    
HELIX  138 138 THR C  990  CYS C  996  1                                   7    
HELIX  139 139 VAL D    9  LEU D   16  1                                   8    
HELIX  140 140 SER D   30  LYS D   42  1                                  13    
HELIX  141 141 GLY D   68  CYS D   79  1                                  12    
HELIX  142 142 ALA D   85  SER D   90  1                                   6    
HELIX  143 143 ASP D   96  ASN D  106  1                                  11    
HELIX  144 144 ASN D  108  ASN D  120  1                                  13    
HELIX  145 145 LEU D  122  CYS D  130  1                                   9    
HELIX  146 146 PRO D  131  LEU D  135  5                                   5    
HELIX  147 147 LEU D  135  CYS D  140  5                                   6    
HELIX  148 148 CYS D  140  THR D  145  5                                   6    
HELIX  149 149 ASN D  151  ASN D  167  1                                  17    
HELIX  150 150 SER D  178  MET D  182  5                                   5    
HELIX  151 151 PRO D  183  ALA D  188  5                                   6    
HELIX  152 152 GLY D  196  GLY D  210  1                                  15    
HELIX  153 153 GLY D  225  GLU D  230  1                                   6    
HELIX  154 154 PRO D  237  ASP D  250  1                                  14    
HELIX  155 155 THR D  267  GLU D  274  1                                   8    
HELIX  156 156 ASP D  291  GLN D  295  5                                   5    
HELIX  157 157 SER D  306  LYS D  318  1                                  13    
HELIX  158 158 GLY D  341  CYS D  354  1                                  14    
HELIX  159 159 GLY D  366  ILE D  370  5                                   5    
HELIX  160 160 VAL D  373  GLU D  383  1                                  11    
HELIX  161 161 ASP D  444  LEU D  451  1                                   8    
HELIX  162 162 GLY D  480  GLY D  484  5                                   5    
HELIX  163 163 THR D  488  TYR D  511  1                                  24    
HELIX  164 164 THR D  526  VAL D  531  5                                   6    
HELIX  165 165 ALA D  551  THR D  555  5                                   5    
HELIX  166 166 SER D  556  GLY D  567  1                                  12    
HELIX  167 167 LEU D  578  ILE D  582  5                                   5    
HELIX  168 168 THR D  617  PHE D  632  1                                  16    
HELIX  169 169 ASN D  646  SER D  660  1                                  15    
HELIX  170 170 CYS D  684  GLN D  686  5                                   3    
HELIX  171 171 ASP D  687  VAL D  702  1                                  16    
HELIX  172 172 ASP D  716  GLY D  728  1                                  13    
HELIX  173 173 GLY D  767  ALA D  769  5                                   3    
HELIX  174 174 ILE D  770  LEU D  785  1                                  16    
HELIX  175 175 SER D  798  SER D  808  1                                  11    
HELIX  176 176 CYS D  816  ASN D  821  1                                   6    
HELIX  177 177 THR D  825  LYS D  841  1                                  17    
HELIX  178 178 SER D  842  GLN D  847  5                                   6    
HELIX  179 179 PHE D  879  GLU D  899  1                                  21    
HELIX  180 180 ALA D  920  ILE D  925  1                                   6    
HELIX  181 181 ALA D  928  TYR D  931  5                                   4    
HELIX  182 182 THR D  934  LEU D  938  5                                   5    
HELIX  183 183 GLY D  957  GLY D  967  1                                  11    
HELIX  184 184 THR D  990  CYS D  996  1                                   7    
SHEET    1  AA 5 LYS A 254  CYS A 257  0                                        
SHEET    2  AA 5 ILE A 214  GLU A 218  1  O  ILE A 214   N  LYS A 254           
SHEET    3  AA 5 ILE A 190  LEU A 193  1  O  ILE A 190   N  THR A 215           
SHEET    4  AA 5 ALA A 278  ILE A 281  1  O  ALA A 278   N  ALA A 191           
SHEET    5  AA 5 VAL A 476  ALA A 478  1  O  PHE A 477   N  ILE A 281           
SHEET    1  AB 2 GLU A 287  PRO A 288  0                                        
SHEET    2  AB 2 SER A 440  VAL A 441 -1  O  VAL A 441   N  GLU A 287           
SHEET    1  AC 5 PHE A 303  THR A 305  0                                        
SHEET    2  AC 5 VAL A 433  SER A 436  1  O  VAL A 434   N  TYR A 304           
SHEET    3  AC 5 ALA A 334  LEU A 338  1  O  ILE A 336   N  ILE A 435           
SHEET    4  AC 5 ARG A 358  VAL A 362  1  O  ARG A 358   N  VAL A 335           
SHEET    5  AC 5 GLU A 386  LEU A 388  1  O  GLU A 386   N  LEU A 361           
SHEET    1  AD 3 LEU A 391  LYS A 399  0                                        
SHEET    2  AD 3 ARG A 402  GLN A 413 -1  O  ARG A 402   N  LYS A 399           
SHEET    3  AD 3 TRP A 419  LYS A 430 -1  O  ASN A 420   N  GLU A 412           
SHEET    1  AE 2 VAL A 535  MET A 537  0                                        
SHEET    2  AE 2 LEU A 540  PHE A 542 -1  O  LEU A 540   N  MET A 537           
SHEET    1  AF 9 PHE A 546  LEU A 548  0                                        
SHEET    2  AF 9 VAL A 812  VAL A 815  1  O  LEU A 813   N  GLY A 547           
SHEET    3  AF 9 ILE A 790  THR A 793  1  O  ALA A 792   N  GLN A 814           
SHEET    4  AF 9 GLY A 731  ALA A 734  1  O  VAL A 732   N  LEU A 791           
SHEET    5  AF 9 PHE A 706  LEU A 710  1  O  ALA A 708   N  THR A 733           
SHEET    6  AF 9 ALA A 664  ASN A 668  1  O  LEU A 665   N  PHE A 707           
SHEET    7  AF 9 ILE A 636  ILE A 641  1  O  ALA A 639   N  GLU A 666           
SHEET    8  AF 9 PHE A 570  LEU A 572  1  O  ALA A 571   N  ILE A 638           
SHEET    9  AF 9 PHE A 546  LEU A 548  1  O  LEU A 548   N  LEU A 572           
SHEET    1  AG 4 ILE A 590  ARG A 592  0                                        
SHEET    2  AG 4 PHE A 607  ASN A 609 -1  O  LEU A 608   N  VAL A 591           
SHEET    3  AG 4 GLY A 763  SER A 766 -1  O  GLY A 764   N  ASN A 609           
SHEET    4  AG 4 VAL A 738  GLY A 740 -1  O  VAL A 738   N  VAL A 765           
SHEET    1  AH 2 HIS A 859  GLN A 860  0                                        
SHEET    2  AH 2 LYS A 863  PRO A 864 -1  O  LYS A 863   N  GLN A 860           
SHEET    1  AI 2 VAL A 944  ILE A 948  0                                        
SHEET    2  AI 2 ILE A1002  SER A1006 -1  O  ARG A1003   N  VAL A 947           
SHEET    1  AJ 2 ILE A 971  PHE A 973  0                                        
SHEET    2  AJ 2 PRO A 980  VAL A 982 -1  O  THR A 981   N  GLN A 972           
SHEET    1  BA 5 LYS B 254  CYS B 257  0                                        
SHEET    2  BA 5 ILE B 214  GLU B 218  1  O  ILE B 214   N  LYS B 254           
SHEET    3  BA 5 ILE B 190  LEU B 193  1  O  ILE B 190   N  THR B 215           
SHEET    4  BA 5 ALA B 278  ILE B 281  1  O  ALA B 278   N  ALA B 191           
SHEET    5  BA 5 VAL B 476  ALA B 478  1  O  PHE B 477   N  ILE B 281           
SHEET    1  BB 2 GLU B 287  PRO B 288  0                                        
SHEET    2  BB 2 SER B 440  VAL B 441 -1  O  VAL B 441   N  GLU B 287           
SHEET    1  BC 5 PHE B 303  THR B 305  0                                        
SHEET    2  BC 5 VAL B 433  SER B 436  1  O  VAL B 434   N  TYR B 304           
SHEET    3  BC 5 ALA B 334  LEU B 338  1  O  ILE B 336   N  ILE B 435           
SHEET    4  BC 5 ARG B 358  VAL B 362  1  O  ARG B 358   N  VAL B 335           
SHEET    5  BC 5 GLU B 386  LEU B 388  1  O  GLU B 386   N  LEU B 361           
SHEET    1  BD 3 LEU B 391  LYS B 399  0                                        
SHEET    2  BD 3 ARG B 402  ASP B 414 -1  O  ARG B 402   N  LYS B 399           
SHEET    3  BD 3 GLY B 417  LYS B 430 -1  O  GLY B 417   N  ASP B 414           
SHEET    1  BE 2 VAL B 535  MET B 537  0                                        
SHEET    2  BE 2 LEU B 540  PHE B 542 -1  O  LEU B 540   N  MET B 537           
SHEET    1  BF 9 PHE B 546  LEU B 548  0                                        
SHEET    2  BF 9 VAL B 812  VAL B 815  1  O  LEU B 813   N  GLY B 547           
SHEET    3  BF 9 ILE B 790  THR B 793  1  O  ALA B 792   N  GLN B 814           
SHEET    4  BF 9 GLY B 731  ALA B 734  1  O  VAL B 732   N  LEU B 791           
SHEET    5  BF 9 PHE B 706  LEU B 710  1  O  ALA B 708   N  THR B 733           
SHEET    6  BF 9 ALA B 664  ASN B 668  1  O  LEU B 665   N  PHE B 707           
SHEET    7  BF 9 ILE B 636  ILE B 641  1  O  ALA B 639   N  GLU B 666           
SHEET    8  BF 9 PHE B 570  LEU B 572  1  O  ALA B 571   N  ILE B 638           
SHEET    9  BF 9 PHE B 546  LEU B 548  1  O  LEU B 548   N  LEU B 572           
SHEET    1  BG 4 ILE B 590  ARG B 592  0                                        
SHEET    2  BG 4 PHE B 607  ASN B 609 -1  O  LEU B 608   N  VAL B 591           
SHEET    3  BG 4 GLY B 763  SER B 766 -1  O  GLY B 764   N  ASN B 609           
SHEET    4  BG 4 VAL B 738  GLY B 740 -1  O  VAL B 738   N  VAL B 765           
SHEET    1  BH 2 HIS B 859  GLN B 860  0                                        
SHEET    2  BH 2 LYS B 863  PRO B 864 -1  O  LYS B 863   N  GLN B 860           
SHEET    1  BI 2 VAL B 944  ILE B 948  0                                        
SHEET    2  BI 2 ILE B1002  SER B1006 -1  O  ARG B1003   N  VAL B 947           
SHEET    1  BJ 2 ILE B 971  PHE B 973  0                                        
SHEET    2  BJ 2 PRO B 980  VAL B 982 -1  O  THR B 981   N  GLN B 972           
SHEET    1  CA 5 LYS C 254  CYS C 257  0                                        
SHEET    2  CA 5 ILE C 214  GLU C 218  1  O  ILE C 214   N  LYS C 254           
SHEET    3  CA 5 ILE C 190  LEU C 193  1  O  ILE C 190   N  THR C 215           
SHEET    4  CA 5 ALA C 278  ILE C 281  1  O  ALA C 278   N  ALA C 191           
SHEET    5  CA 5 VAL C 476  ALA C 478  1  O  PHE C 477   N  ILE C 281           
SHEET    1  CB 2 GLU C 287  PRO C 288  0                                        
SHEET    2  CB 2 SER C 440  VAL C 441 -1  O  VAL C 441   N  GLU C 287           
SHEET    1  CC 5 PHE C 303  THR C 305  0                                        
SHEET    2  CC 5 VAL C 433  SER C 436  1  O  VAL C 434   N  TYR C 304           
SHEET    3  CC 5 ALA C 334  LEU C 338  1  O  ILE C 336   N  ILE C 435           
SHEET    4  CC 5 ARG C 358  VAL C 362  1  O  ARG C 358   N  VAL C 335           
SHEET    5  CC 5 GLU C 386  LEU C 388  1  O  GLU C 386   N  LEU C 361           
SHEET    1  CD 3 LEU C 391  LYS C 399  0                                        
SHEET    2  CD 3 ARG C 402  GLN C 413 -1  O  ARG C 402   N  LYS C 399           
SHEET    3  CD 3 TRP C 419  LYS C 430 -1  O  ASN C 420   N  GLU C 412           
SHEET    1  CE 2 VAL C 535  MET C 537  0                                        
SHEET    2  CE 2 LEU C 540  PHE C 542 -1  O  LEU C 540   N  MET C 537           
SHEET    1  CF 9 PHE C 546  LEU C 548  0                                        
SHEET    2  CF 9 VAL C 812  VAL C 815  1  O  LEU C 813   N  GLY C 547           
SHEET    3  CF 9 ILE C 790  THR C 793  1  O  ALA C 792   N  GLN C 814           
SHEET    4  CF 9 GLY C 731  ALA C 734  1  O  VAL C 732   N  LEU C 791           
SHEET    5  CF 9 PHE C 706  LEU C 710  1  O  ALA C 708   N  THR C 733           
SHEET    6  CF 9 ALA C 664  ASN C 668  1  O  LEU C 665   N  PHE C 707           
SHEET    7  CF 9 ILE C 636  ILE C 641  1  O  ALA C 639   N  GLU C 666           
SHEET    8  CF 9 PHE C 570  LEU C 572  1  O  ALA C 571   N  ILE C 638           
SHEET    9  CF 9 PHE C 546  LEU C 548  1  O  LEU C 548   N  LEU C 572           
SHEET    1  CG 4 ILE C 590  ARG C 592  0                                        
SHEET    2  CG 4 PHE C 607  ASN C 609 -1  O  LEU C 608   N  VAL C 591           
SHEET    3  CG 4 GLY C 763  SER C 766 -1  O  GLY C 764   N  ASN C 609           
SHEET    4  CG 4 VAL C 738  GLY C 740 -1  O  VAL C 738   N  VAL C 765           
SHEET    1  CH 2 HIS C 859  GLN C 860  0                                        
SHEET    2  CH 2 LYS C 863  PRO C 864 -1  O  LYS C 863   N  GLN C 860           
SHEET    1  CI 2 VAL C 944  ILE C 948  0                                        
SHEET    2  CI 2 ILE C1002  SER C1006 -1  O  ARG C1003   N  VAL C 947           
SHEET    1  CJ 2 ILE C 971  PHE C 973  0                                        
SHEET    2  CJ 2 PRO C 980  VAL C 982 -1  O  THR C 981   N  GLN C 972           
SHEET    1  DA 5 LYS D 254  CYS D 257  0                                        
SHEET    2  DA 5 ILE D 214  GLU D 218  1  O  ILE D 214   N  LYS D 254           
SHEET    3  DA 5 ILE D 190  LEU D 193  1  O  ILE D 190   N  THR D 215           
SHEET    4  DA 5 ALA D 278  ILE D 281  1  O  ALA D 278   N  ALA D 191           
SHEET    5  DA 5 VAL D 476  ALA D 478  1  O  PHE D 477   N  ILE D 281           
SHEET    1  DB 2 GLU D 287  PRO D 288  0                                        
SHEET    2  DB 2 SER D 440  VAL D 441 -1  O  VAL D 441   N  GLU D 287           
SHEET    1  DC 5 PHE D 303  THR D 305  0                                        
SHEET    2  DC 5 VAL D 433  SER D 436  1  O  VAL D 434   N  TYR D 304           
SHEET    3  DC 5 ALA D 334  LEU D 338  1  O  ILE D 336   N  ILE D 435           
SHEET    4  DC 5 ARG D 358  VAL D 362  1  O  ARG D 358   N  VAL D 335           
SHEET    5  DC 5 GLU D 386  LEU D 388  1  O  GLU D 386   N  LEU D 361           
SHEET    1  DD 3 LEU D 391  LYS D 399  0                                        
SHEET    2  DD 3 ARG D 402  ASP D 414 -1  O  ARG D 402   N  LYS D 399           
SHEET    3  DD 3 LYS D 418  LYS D 430 -1  O  LYS D 418   N  ASP D 414           
SHEET    1  DE 2 VAL D 535  MET D 537  0                                        
SHEET    2  DE 2 LEU D 540  PHE D 542 -1  O  LEU D 540   N  MET D 537           
SHEET    1  DF 9 PHE D 546  LEU D 548  0                                        
SHEET    2  DF 9 VAL D 812  VAL D 815  1  O  LEU D 813   N  GLY D 547           
SHEET    3  DF 9 ILE D 790  THR D 793  1  O  ALA D 792   N  GLN D 814           
SHEET    4  DF 9 GLY D 731  ALA D 734  1  O  VAL D 732   N  LEU D 791           
SHEET    5  DF 9 PHE D 706  LEU D 710  1  O  ALA D 708   N  THR D 733           
SHEET    6  DF 9 ALA D 664  ASN D 668  1  O  LEU D 665   N  PHE D 707           
SHEET    7  DF 9 ILE D 636  ILE D 641  1  O  ALA D 639   N  GLU D 666           
SHEET    8  DF 9 PHE D 570  LEU D 572  1  O  ALA D 571   N  ILE D 638           
SHEET    9  DF 9 PHE D 546  LEU D 548  1  O  LEU D 548   N  LEU D 572           
SHEET    1  DG 4 ILE D 590  ARG D 592  0                                        
SHEET    2  DG 4 PHE D 607  ASN D 609 -1  O  LEU D 608   N  VAL D 591           
SHEET    3  DG 4 GLY D 763  SER D 766 -1  O  GLY D 764   N  ASN D 609           
SHEET    4  DG 4 VAL D 738  GLY D 740 -1  O  VAL D 738   N  VAL D 765           
SHEET    1  DH 2 HIS D 859  GLN D 860  0                                        
SHEET    2  DH 2 LYS D 863  PRO D 864 -1  O  LYS D 863   N  GLN D 860           
SHEET    1  DI 2 VAL D 944  ILE D 948  0                                        
SHEET    2  DI 2 ILE D1002  SER D1006 -1  O  ARG D1003   N  VAL D 947           
SHEET    1  DJ 2 ILE D 971  PHE D 973  0                                        
SHEET    2  DJ 2 PRO D 980  VAL D 982 -1  O  THR D 981   N  GLN D 972           
LINK        FE1  SF4 C1027                 SG  CYS C 140     1555   1555  2.28  
LINK        FE2  SF4 C1027                 SG  CYS C  87     1555   1555  2.20  
LINK        FE3  SF4 C1027                 SG  CYS C  79     1555   1555  2.20  
LINK        FE4  SF4 C1027                 SG  CYS C  82     1555   1555  2.29  
LINK        FE1  SF4 C1028                 SG  CYS C 996     1555   1555  2.29  
LINK        FE2  SF4 C1028                 SG  CYS C 959     1555   1555  2.25  
LINK        FE3  SF4 C1028                 SG  CYS C 953     1555   1555  2.31  
LINK        FE4  SF4 C1028                 SG  CYS C 956     1555   1555  2.34  
LINK        FE1  SF4 C1029                 SG  CYS C 963     1555   1555  2.26  
LINK        FE2  SF4 C1029                 SG  CYS C 992     1555   1555  2.24  
LINK        FE3  SF4 C1029                 SG  CYS C 986     1555   1555  2.22  
LINK        FE4  SF4 C1029                 SG  CYS C 989     1555   1555  2.34  
LINK        FE1  SF4 D1026                 SG  CYS D  91     1555   1555  2.26  
LINK        FE2  SF4 D1026                 SG  CYS D 136     1555   1555  2.13  
LINK        FE3  SF4 D1026                 OE1 GLN D 156     1555   1555  1.91  
LINK        FE4  SF4 D1026                 SG  CYS D 130     1555   1555  2.29  
LINK        FE2  SF4 D1027                 SG  CYS D  87     1555   1555  2.18  
LINK        FE3  SF4 D1027                 SG  CYS D  79     1555   1555  2.23  
LINK        FE4  SF4 D1027                 SG  CYS D  82     1555   1555  2.30  
LINK        FE1  SF4 D1027                 SG  CYS D 140     1555   1555  2.29  
LINK        FE2  SF4 D1028                 SG  CYS D 959     1555   1555  2.23  
LINK        FE3  SF4 D1028                 SG  CYS D 953     1555   1555  2.20  
LINK        FE4  SF4 D1028                 SG  CYS D 956     1555   1555  2.35  
LINK        FE1  SF4 D1028                 SG  CYS D 996     1555   1555  2.29  
LINK        FE2  SF4 D1029                 SG  CYS D 992     1555   1555  2.20  
LINK        FE3  SF4 D1029                 SG  CYS D 986     1555   1555  2.21  
LINK        FE4  SF4 D1029                 SG  CYS D 989     1555   1555  2.34  
LINK        FE1  SF4 D1029                 SG  CYS D 963     1555   1555  2.28  
CISPEP   1 SER A  452    PRO A  453          0         0.59                     
CISPEP   2 SER A  587    PRO A  588          0        -0.48                     
CISPEP   3 ALA A  734    THR A  735          0        -0.20                     
CISPEP   4 TRP A  751    PRO A  752          0         1.36                     
CISPEP   5 SER B  452    PRO B  453          0         0.82                     
CISPEP   6 SER B  587    PRO B  588          0        -0.92                     
CISPEP   7 ALA B  734    THR B  735          0        -0.64                     
CISPEP   8 TRP B  751    PRO B  752          0         1.07                     
CISPEP   9 SER C  452    PRO C  453          0         0.66                     
CISPEP  10 SER C  587    PRO C  588          0        -0.69                     
CISPEP  11 ALA C  734    THR C  735          0        -0.23                     
CISPEP  12 TRP C  751    PRO C  752          0         1.35                     
CISPEP  13 SER D  452    PRO D  453          0         0.62                     
CISPEP  14 SER D  587    PRO D  588          0        -0.51                     
CISPEP  15 ALA D  734    THR D  735          0        -0.74                     
CISPEP  16 TRP D  751    PRO D  752          0         1.34                     
SITE     1 AC1  8 CYS A  91  PRO A  92  ILE A  97  ASN A 120                    
SITE     2 AC1  8 CYS A 130  THR A 132  CYS A 136  GLN A 156                    
SITE     1 AC2 11 CYS A  79  LEU A  80  LYS A  81  CYS A  82                    
SITE     2 AC2 11 PRO A  86  CYS A  87  CYS A 140  ASN A 141                    
SITE     3 AC2 11 LEU A 142  ILE A 150  ILE A 152                               
SITE     1 AC3 12 ILE A 948  CYS A 953  ILE A 954  ASN A 955                    
SITE     2 AC3 12 CYS A 956  GLY A 957  LYS A 958  CYS A 959                    
SITE     3 AC3 12 CYS A 996  PRO A 997  CYS A1001  ILE A1002                    
SITE     1 AC4 11 CYS A 963  TYR A 968  ILE A 971  VAL A 982                    
SITE     2 AC4 11 CYS A 986  THR A 987  GLY A 988  CYS A 989                    
SITE     3 AC4 11 THR A 990  CYS A 992  MET A1004                               
SITE     1 AC5 24 ALA A 549  SER A 550  ALA A 551  LYS A 574                    
SITE     2 AC5 24 THR A 575  ILE A 590  ASN A 609  GLU A 611                    
SITE     3 AC5 24 ASN A 668  LYS A 709  THR A 735  ASN A 736                    
SITE     4 AC5 24 SER A 766  GLY A 767  THR A 793  GLY A 794                    
SITE     5 AC5 24 GLY A 795  CYS A 816  SER A 817  GLN A 820                    
SITE     6 AC5 24 IUR A1034  HOH A2823  HOH A3162  HOH A3163                    
SITE     1 AC6 37 VAL A 129  PRO A 131  GLY A 194  GLY A 196                    
SITE     2 AC6 37 PRO A 197  ALA A 198  GLU A 218  LYS A 219                    
SITE     3 AC6 37 GLN A 220  GLY A 225  LEU A 226  GLU A 230                    
SITE     4 AC6 37 ARG A 235  SER A 260  LEU A 261  GLY A 282                    
SITE     5 AC6 37 ILE A 283  GLY A 284  PRO A 286  LEU A 310                    
SITE     6 AC6 37 THR A 343  ASP A 346  GLY A 480  ASP A 481                    
SITE     7 AC6 37 ASN A 487  THR A 488  THR A 489  SER A 492                    
SITE     8 AC6 37 HOH A2376  HOH A2670  HOH A3164  HOH A3165                    
SITE     9 AC6 37 HOH A3166  HOH A3167  HOH A3168  HOH A3169                    
SITE    10 AC6 37 HOH A3170                                                     
SITE     1 AC7  8 ASN A 609  GLU A 611  ASN A 668  SER A 670                    
SITE     2 AC7  8 ASN A 736  THR A 737  FMN A1030  HOH A2798                    
SITE     1 AC8  9 CYS B  91  PRO B  92  LEU B  95  ILE B  97                    
SITE     2 AC8  9 ASN B 120  CYS B 130  THR B 132  CYS B 136                    
SITE     3 AC8  9 GLN B 156                                                     
SITE     1 AC9 11 CYS B  79  LEU B  80  LYS B  81  CYS B  82                    
SITE     2 AC9 11 PRO B  86  CYS B  87  CYS B 140  ASN B 141                    
SITE     3 AC9 11 LEU B 142  ILE B 150  ILE B 152                               
SITE     1 BC1 12 ILE B 948  CYS B 953  ILE B 954  CYS B 956                    
SITE     2 BC1 12 GLY B 957  LYS B 958  CYS B 959  CYS B 996                    
SITE     3 BC1 12 PRO B 997  ILE B 998  CYS B1001  ILE B1002                    
SITE     1 BC2 10 CYS B 963  TYR B 968  ILE B 971  VAL B 982                    
SITE     2 BC2 10 CYS B 986  THR B 987  GLY B 988  CYS B 989                    
SITE     3 BC2 10 THR B 990  CYS B 992                                          
SITE     1 BC3 26 ALA B 549  SER B 550  ALA B 551  LYS B 574                    
SITE     2 BC3 26 THR B 575  ILE B 590  ASN B 609  GLU B 611                    
SITE     3 BC3 26 ASN B 668  LYS B 709  THR B 735  ASN B 736                    
SITE     4 BC3 26 THR B 737  SER B 766  GLY B 767  THR B 793                    
SITE     5 BC3 26 GLY B 794  GLY B 795  CYS B 816  SER B 817                    
SITE     6 BC3 26 GLN B 820  IUR B1034  HOH B2857  HOH B2973                    
SITE     7 BC3 26 HOH B3211  HOH B3212                                          
SITE     1 BC4 38 VAL B 129  PRO B 131  GLY B 194  GLY B 196                    
SITE     2 BC4 38 PRO B 197  ALA B 198  GLU B 218  LYS B 219                    
SITE     3 BC4 38 GLN B 220  GLY B 225  LEU B 226  GLU B 230                    
SITE     4 BC4 38 ARG B 235  SER B 260  LEU B 261  GLY B 282                    
SITE     5 BC4 38 ILE B 283  GLY B 284  PRO B 286  LEU B 310                    
SITE     6 BC4 38 THR B 343  ASP B 346  GLY B 480  ASP B 481                    
SITE     7 BC4 38 ASN B 487  THR B 488  THR B 489  SER B 492                    
SITE     8 BC4 38 HOH B2400  HOH B2406  HOH B3213  HOH B3214                    
SITE     9 BC4 38 HOH B3215  HOH B3216  HOH B3217  HOH B3218                    
SITE    10 BC4 38 HOH B3219  HOH B3220                                          
SITE     1 BC5  9 ASN B 609  GLU B 611  ASN B 668  SER B 670                    
SITE     2 BC5  9 ASN B 736  THR B 737  FMN B1030  HOH B2825                    
SITE     3 BC5  9 HOH B3212                                                     
SITE     1 BC6 10 CYS C  91  PRO C  92  LEU C  95  ILE C  97                    
SITE     2 BC6 10 ASN C 120  CYS C 130  THR C 132  LEU C 135                    
SITE     3 BC6 10 CYS C 136  GLN C 156                                          
SITE     1 BC7 11 CYS C  79  LEU C  80  LYS C  81  CYS C  82                    
SITE     2 BC7 11 PRO C  86  CYS C  87  CYS C 140  ASN C 141                    
SITE     3 BC7 11 LEU C 142  ILE C 150  ILE C 152                               
SITE     1 BC8 12 ILE C 948  CYS C 953  ILE C 954  ASN C 955                    
SITE     2 BC8 12 CYS C 956  GLY C 957  LYS C 958  CYS C 959                    
SITE     3 BC8 12 CYS C 996  PRO C 997  CYS C1001  ILE C1002                    
SITE     1 BC9 10 CYS C 963  TYR C 968  ILE C 971  VAL C 982                    
SITE     2 BC9 10 CYS C 986  THR C 987  GLY C 988  CYS C 989                    
SITE     3 BC9 10 THR C 990  CYS C 992                                          
SITE     1 CC1 24 ALA C 549  SER C 550  ALA C 551  LYS C 574                    
SITE     2 CC1 24 THR C 575  ILE C 590  ASN C 609  GLU C 611                    
SITE     3 CC1 24 ASN C 668  LYS C 709  THR C 735  ASN C 736                    
SITE     4 CC1 24 SER C 766  GLY C 767  THR C 793  GLY C 794                    
SITE     5 CC1 24 GLY C 795  CYS C 816  SER C 817  GLN C 820                    
SITE     6 CC1 24 IUR C1034  HOH C2821  HOH C2948  HOH C3181                    
SITE     1 CC2 36 VAL C 129  PRO C 131  GLY C 194  GLY C 196                    
SITE     2 CC2 36 PRO C 197  ALA C 198  GLU C 218  LYS C 219                    
SITE     3 CC2 36 GLN C 220  GLY C 225  LEU C 226  GLU C 230                    
SITE     4 CC2 36 ARG C 235  SER C 260  LEU C 261  GLY C 282                    
SITE     5 CC2 36 ILE C 283  GLY C 284  LEU C 310  THR C 343                    
SITE     6 CC2 36 ASP C 346  GLY C 480  ASP C 481  ASN C 487                    
SITE     7 CC2 36 THR C 488  THR C 489  SER C 492  HOH C2370                    
SITE     8 CC2 36 HOH C3182  HOH C3183  HOH C3184  HOH C3185                    
SITE     9 CC2 36 HOH C3186  HOH C3187  HOH C3188  HOH C3189                    
SITE     1 CC3  7 ASN C 609  GLU C 611  ASN C 668  SER C 670                    
SITE     2 CC3  7 ASN C 736  THR C 737  FMN C1030                               
SITE     1 CC4  8 CYS D  91  PRO D  92  ILE D  97  ASN D 120                    
SITE     2 CC4  8 CYS D 130  THR D 132  CYS D 136  GLN D 156                    
SITE     1 CC5 11 CYS D  79  LEU D  80  LYS D  81  CYS D  82                    
SITE     2 CC5 11 PRO D  86  CYS D  87  CYS D 140  ASN D 141                    
SITE     3 CC5 11 LEU D 142  ILE D 150  ILE D 152                               
SITE     1 CC6 11 ILE D 948  CYS D 953  ILE D 954  CYS D 956                    
SITE     2 CC6 11 GLY D 957  LYS D 958  CYS D 959  CYS D 996                    
SITE     3 CC6 11 PRO D 997  CYS D1001  ILE D1002                               
SITE     1 CC7  9 CYS D 963  TYR D 968  ILE D 971  CYS D 986                    
SITE     2 CC7  9 THR D 987  GLY D 988  CYS D 989  THR D 990                    
SITE     3 CC7  9 CYS D 992                                                     
SITE     1 CC8 24 ALA D 549  SER D 550  ALA D 551  LYS D 574                    
SITE     2 CC8 24 THR D 575  ILE D 590  ASN D 609  GLU D 611                    
SITE     3 CC8 24 ASN D 668  LYS D 709  THR D 735  ASN D 736                    
SITE     4 CC8 24 SER D 766  GLY D 767  THR D 793  GLY D 794                    
SITE     5 CC8 24 GLY D 795  CYS D 816  SER D 817  GLN D 820                    
SITE     6 CC8 24 IUR D1034  HOH D2895  HOH D3053  HOH D3261                    
SITE     1 CC9 36 VAL D 129  PRO D 131  GLY D 194  GLY D 196                    
SITE     2 CC9 36 PRO D 197  ALA D 198  GLU D 218  LYS D 219                    
SITE     3 CC9 36 GLN D 220  GLY D 225  LEU D 226  GLU D 230                    
SITE     4 CC9 36 ARG D 235  SER D 260  LEU D 261  GLY D 282                    
SITE     5 CC9 36 ILE D 283  GLY D 284  LEU D 310  THR D 343                    
SITE     6 CC9 36 ASP D 346  GLY D 480  ASP D 481  ASN D 487                    
SITE     7 CC9 36 THR D 488  THR D 489  SER D 492  HOH D2426                    
SITE     8 CC9 36 HOH D2736  HOH D3262  HOH D3263  HOH D3264                    
SITE     9 CC9 36 HOH D3265  HOH D3266  HOH D3267  HOH D3268                    
SITE     1 DC1  7 ASN D 609  GLU D 611  ASN D 668  SER D 670                    
SITE     2 DC1  7 ASN D 736  THR D 737  FMN D1030                               
CRYST1   81.710  158.370  162.330  90.00  95.84  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      0.012238  0.000000  0.001252        0.00000                         
SCALE2      0.000000  0.006314  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006192        0.00000                         
MTRIX1   1 -1.000000  0.001900 -0.003200      155.96680    1                    
MTRIX2   1 -0.003300 -0.837900  0.545800       63.09360    1                    
MTRIX3   1 -0.001600  0.545800  0.837900      -18.55900    1                    
MTRIX1   2 -1.000000 -0.004000  0.004100      130.23109    1                    
MTRIX2   2 -0.005700  0.795100 -0.606400       86.97160    1                    
MTRIX3   2 -0.000900 -0.606400 -0.795200       95.51080    1                    
MTRIX1   3  1.000000  0.008500 -0.000300      -26.35700    1                    
MTRIX2   3  0.008500 -0.997600  0.069100      147.42090    1                    
MTRIX3   3  0.000200 -0.069100 -0.997600       72.76020    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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