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Database: PDB
Entry: 4CEI
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Original site: 4CEI 
HEADER    HYDROLASE/DNA                           11-NOV-13   4CEI              
TITLE     CRYSTAL STRUCTURE OF ADPNP-BOUND ADDAB WITH A FORKED DNA SUBSTRATE    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ATP-DEPENDENT HELICASE/NUCLEASE SUBUNIT A;                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ATP-DEPENDENT HELICAS E-NUCLEASE SUBUNIT A;                 
COMPND   5 EC: 3.1.-.-, 3.6.4.12;                                               
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: ATP-DEPENDENT HELICASE/DEOXYRIBONUCLEASE SUBUNIT B;        
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: ATP-DEPENDENT HELICAS E-NUCLEASE SUBUNIT B;                 
COMPND  12 EC: 3.1.-.-, 3.6.4.12;                                               
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MUTATION: YES;                                                       
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: DNA;                                                       
COMPND  17 CHAIN: X;                                                            
COMPND  18 OTHER_DETAILS: ANNEALED HAIRPIN DUPLEX WITH UNPAIRED SINGLE-         
COMPND  19  STRANDED 3' AND 5' TAILS                                            
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168;     
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 ATCC: 23857;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;                               
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 37762;                                      
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: B834 (DE3);                                
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PCOLADUET-1;                              
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168;     
SOURCE  12 ORGANISM_TAXID: 224308;                                              
SOURCE  13 ATCC: 23857;                                                         
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;                               
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 37762;                                      
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: B834 (DE3);                                
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PCOLADUET-1;                              
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 SYNTHETIC: YES;                                                      
SOURCE  21 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  22 ORGANISM_TAXID: 32630                                                
KEYWDS    HYDROLASE-DNA COMPLEX, HELICASE-NUCLEASE, BACTERIAL PROTEINS,         
KEYWDS   2 BINDING SITES, DNA BREAKS, DOUBLE-STRANDED, DNA HELICASES, DNA       
KEYWDS   3 REPAIR, SINGLE-STRANDED, DNA- BINDING PROTEINS, DEOXYRIBONUCLEASES,  
KEYWDS   4 EXODEOXYRIBONUCLEASE V, EXODEOXYRIBONUCLEASES, HOMOLOGOUS            
KEYWDS   5 RECOMBINATION                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.W.KRAJEWSKI,M.WILKINSON,X.FU,N.B.CRONIN,D.WIGLEY                    
REVDAT   3   23-APR-14 4CEI    1       JRNL                                     
REVDAT   2   09-APR-14 4CEI    1       JRNL                                     
REVDAT   1   12-MAR-14 4CEI    0                                                
JRNL        AUTH   W.W.KRAJEWSKI,X.FU,M.WILKINSON,N.B.CRONIN,M.S.DILLINGHAM,    
JRNL        AUTH 2 D.B.WIGLEY                                                   
JRNL        TITL   STRUCTURAL BASIS FOR TRANSLOCATION BY ADDAB                  
JRNL        TITL 2 HELICASE-NUCLEASE AND ITS ARREST AT CHI SITES.               
JRNL        REF    NATURE                        V. 508   416 2014              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   24670664                                                     
JRNL        DOI    10.1038/NATURE13037                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.800                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.949                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.35                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.74                          
REMARK   3   NUMBER OF REFLECTIONS             : 68623                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1976                          
REMARK   3   R VALUE            (WORKING SET) : 0.1953                          
REMARK   3   FREE R VALUE                     : 0.2398                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3455                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.9508 -  8.1345    0.99     2656   139  0.1613 0.1754        
REMARK   3     2  8.1345 -  6.4780    1.00     2637   137  0.1740 0.1895        
REMARK   3     3  6.4780 -  5.6655    1.00     2608   149  0.1872 0.1991        
REMARK   3     4  5.6655 -  5.1503    1.00     2612   149  0.1662 0.1961        
REMARK   3     5  5.1503 -  4.7827    1.00     2603   138  0.1560 0.1963        
REMARK   3     6  4.7827 -  4.5018    1.00     2645   135  0.1588 0.1814        
REMARK   3     7  4.5018 -  4.2770    1.00     2623   123  0.1561 0.1953        
REMARK   3     8  4.2770 -  4.0913    1.00     2632   135  0.1738 0.2293        
REMARK   3     9  4.0913 -  3.9341    1.00     2599   136  0.1743 0.2268        
REMARK   3    10  3.9341 -  3.7986    1.00     2581   152  0.1867 0.2253        
REMARK   3    11  3.7986 -  3.6801    1.00     2622   137  0.1860 0.2495        
REMARK   3    12  3.6801 -  3.5751    1.00     2602   144  0.2029 0.2511        
REMARK   3    13  3.5751 -  3.4811    1.00     2617   124  0.2023 0.2379        
REMARK   3    14  3.4811 -  3.3963    1.00     2593   159  0.2122 0.2790        
REMARK   3    15  3.3963 -  3.3192    1.00     2558   134  0.2311 0.3011        
REMARK   3    16  3.3192 -  3.2486    1.00     2643   146  0.2359 0.3041        
REMARK   3    17  3.2486 -  3.1837    1.00     2597   128  0.2447 0.3032        
REMARK   3    18  3.1837 -  3.1237    1.00     2582   148  0.2513 0.3276        
REMARK   3    19  3.1237 -  3.0680    1.00     2587   125  0.2593 0.3134        
REMARK   3    20  3.0680 -  3.0160    1.00     2595   132  0.2610 0.3006        
REMARK   3    21  3.0160 -  2.9674    1.00     2584   160  0.2758 0.3886        
REMARK   3    22  2.9674 -  2.9218    1.00     2594   127  0.2851 0.3646        
REMARK   3    23  2.9218 -  2.8789    1.00     2591   142  0.2654 0.3319        
REMARK   3    24  2.8789 -  2.8383    0.99     2618   126  0.2751 0.3451        
REMARK   3    25  2.8383 -  2.8000    0.99     2589   130  0.2786 0.3388        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.37             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.61            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004          20171                                  
REMARK   3   ANGLE     :  0.749          27365                                  
REMARK   3   CHIRALITY :  0.031           2983                                  
REMARK   3   PLANARITY :  0.003           3399                                  
REMARK   3   DIHEDRAL  : 17.273           7726                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4CEI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-DEC-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-58911.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97950                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 68664                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.80                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.93                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.4                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.90                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.5                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.36                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.80                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX PHASER-MR                                      
REMARK 200 STARTING MODEL: PDB ENTRY 3U44                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.7                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.5, 17.5 % PEG            
REMARK 280  1500, 0.25M NACL, 0.1M SODIUM FORMATE, 0.1M MGCL2, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, 285K                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       75.66750            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 24920 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 100710 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -105.6 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, X                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     ILE A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     ASP A   535                                                      
REMARK 465     THR A   536                                                      
REMARK 465     ASP A   537                                                      
REMARK 465     ALA A   538                                                      
REMARK 465     SER A   539                                                      
REMARK 465     GLU A   540                                                      
REMARK 465     GLU A   541                                                      
REMARK 465     ALA A   542                                                      
REMARK 465     GLU A   543                                                      
REMARK 465     GLY A   931                                                      
REMARK 465     ASP A   932                                                      
REMARK 465     LEU A   933                                                      
REMARK 465     ALA A   934                                                      
REMARK 465     GLY A   935                                                      
REMARK 465     VAL A   936                                                      
REMARK 465     PRO A   937                                                      
REMARK 465     ALA A   938                                                      
REMARK 465     ASP A   961                                                      
REMARK 465     ASP A   962                                                      
REMARK 465     ASP A   963                                                      
REMARK 465     LEU A   964                                                      
REMARK 465     GLU A   965                                                      
REMARK 465     GLU A   966                                                      
REMARK 465     ARG A   967                                                      
REMARK 465     MET A   968                                                      
REMARK 465     GLU A   969                                                      
REMARK 465     LYS A  1020                                                      
REMARK 465     ARG A  1021                                                      
REMARK 465     LYS A  1022                                                      
REMARK 465     ARG A  1023                                                      
REMARK 465     GLU A  1024                                                      
REMARK 465     TYR A  1025                                                      
REMARK 465     GLU A  1026                                                      
REMARK 465     ASP A  1027                                                      
REMARK 465     GLU A  1028                                                      
REMARK 465     TYR A  1029                                                      
REMARK 465     SER A  1030                                                      
REMARK 465     GLY A  1031                                                      
REMARK 465     ARG A  1032                                                      
REMARK 465     ALA A  1033                                                      
REMARK 465     PRO A  1034                                                      
REMARK 465     VAL A  1035                                                      
REMARK 465     LYS A  1036                                                      
REMARK 465     PRO A  1037                                                      
REMARK 465     ALA A  1038                                                      
REMARK 465     ASP A  1039                                                      
REMARK 465     GLY A  1040                                                      
REMARK 465     SER A  1041                                                      
REMARK 465     ILE A  1042                                                      
REMARK 465     GLY A  1180                                                      
REMARK 465     LYS A  1181                                                      
REMARK 465     PHE A  1182                                                      
REMARK 465     GLN A  1183                                                      
REMARK 465     HIS A  1184                                                      
REMARK 465     GLY A  1185                                                      
REMARK 465     PHE A  1186                                                      
REMARK 465     GLU A  1187                                                      
REMARK 465     GLY A  1188                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B   144                                                      
REMARK 465     GLU B   145                                                      
REMARK 465     SER B   146                                                      
REMARK 465     GLY B   147                                                      
REMARK 465     THR B   148                                                      
REMARK 465     ALA B   149                                                      
REMARK 465     ALA B  1160                                                      
REMARK 465     ASP B  1161                                                      
REMARK 465     GLY B  1162                                                      
REMARK 465     ASN B  1163                                                      
REMARK 465     GLU B  1164                                                      
REMARK 465     HIS B  1165                                                      
REMARK 465     SER B  1166                                                      
REMARK 465      DT X     1                                                      
REMARK 465      DT X     2                                                      
REMARK 465      DT X     3                                                      
REMARK 465      DT X     4                                                      
REMARK 465      DT X     5                                                      
REMARK 465      DT X     6                                                      
REMARK 465      DT X     7                                                      
REMARK 465      DG X    22                                                      
REMARK 465      DC X    23                                                      
REMARK 465      DT X    24                                                      
REMARK 465      DA X    25                                                      
REMARK 465      DT X    26                                                      
REMARK 465      DT X    27                                                      
REMARK 465      DC X    28                                                      
REMARK 465      DC X    29                                                      
REMARK 465      DC X    30                                                      
REMARK 465      DT X    31                                                      
REMARK 465      DA X    32                                                      
REMARK 465      DG X    33                                                      
REMARK 465      DC X    34                                                      
REMARK 465      DT X    58                                                      
REMARK 465      DT X    59                                                      
REMARK 465      DT X    60                                                      
REMARK 465      DA X    61                                                      
REMARK 465      DG X    62                                                      
REMARK 465      DC X    63                                                      
REMARK 465      DG X    64                                                      
REMARK 465      DG X    65                                                      
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   O    ASP A   531     OG   SER A   956              2.19            
REMARK 500   OH   TYR B   180     OE1  GLU B   553              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   OG1  THR A   901     NH1  ARG B   756     2545     2.18            
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     DA X  11   O4' -  C1' -  N9  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DT X  37   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DG X  48   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DA X  49   C3' -  C2' -  C1' ANGL. DEV. =  -6.1 DEGREES          
REMARK 500     DA X  49   O4' -  C1' -  N9  ANGL. DEV. =   3.0 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    THR A  49       55.28    -96.38                                   
REMARK 500    SER A 107     -163.94   -164.47                                   
REMARK 500    ARG A 253       -8.45    -56.43                                   
REMARK 500    THR A 430       45.34   -142.17                                   
REMARK 500    ASP A 438      119.48   -162.24                                   
REMARK 500    ASN A 532       59.49   -113.36                                   
REMARK 500    LYS A 575       -4.04     78.90                                   
REMARK 500    TYR A 637       43.40    -81.34                                   
REMARK 500    ASN A 665      103.12   -167.81                                   
REMARK 500    ALA A 754        5.75   -164.97                                   
REMARK 500    PRO A 946       32.99    -65.66                                   
REMARK 500    LEU A1055       71.86     56.71                                   
REMARK 500    ALA A1102       50.67    -95.61                                   
REMARK 500    ASP A1144       10.54     81.68                                   
REMARK 500    ILE A1178      -60.87   -133.16                                   
REMARK 500    LYS B  53       66.75   -100.58                                   
REMARK 500    ILE B  61      -53.63   -137.96                                   
REMARK 500    PRO B  85      154.30    -47.72                                   
REMARK 500    VAL B 109      -35.00   -135.23                                   
REMARK 500    GLN B 179      -49.90   -137.82                                   
REMARK 500    GLU B 184       36.38    -99.08                                   
REMARK 500    SER B 279      -71.12   -101.09                                   
REMARK 500    GLU B 307     -158.49    -94.14                                   
REMARK 500    GLU B 310      -47.97   -150.24                                   
REMARK 500    ASN B 397       67.64     60.72                                   
REMARK 500    LEU B 639     -163.12   -112.46                                   
REMARK 500    GLU B 705        5.05    -69.21                                   
REMARK 500    ASP B 755       52.67   -108.46                                   
REMARK 500    ASN B 770       66.70    -68.84                                   
REMARK 500    CYS B 801      116.79   -166.86                                   
REMARK 500    GLN B 872       67.65     39.66                                   
REMARK 500    SER B 964       32.11    -95.18                                   
REMARK 500    GLU B1138        3.60     86.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS A  574     LYS A  575                  144.14                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (ANP):                   
REMARK 600  NON-HYDROLYSABLE ATP ANALOGUE                                       
REMARK 600 MAGNESIUM ION (MG): COORDINATED BY PROTEIN, ANP AND WATER            
REMARK 600  MOLECULES                                                           
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 B2160  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 B2160   S4                                                     
REMARK 620 2 SF4 B2160  FE2   45.2                                              
REMARK 620 3 SF4 B2160  FE3   44.8  60.2                                        
REMARK 620 4 SF4 B2160  FE4   89.5  59.7  59.6                                  
REMARK 620 5 SF4 B2160   S2   89.8  90.2  44.9  45.1                            
REMARK 620 6 SF4 B2160   S3   90.4  45.2  90.4  45.2  90.3                      
REMARK 620 7 CYS B 801   SG  133.2 148.3 147.5 137.4 120.7 121.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B2160  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1121   SG                                                     
REMARK 620 2 SF4 B2160   S4  127.1                                              
REMARK 620 3 SF4 B2160  FE1  142.5  45.3                                        
REMARK 620 4 SF4 B2160  FE3  148.6  44.8  60.2                                  
REMARK 620 5 SF4 B2160  FE4  142.7  90.0  60.2  59.8                            
REMARK 620 6 SF4 B2160   S1  126.6  89.8  90.7  45.0  45.5                      
REMARK 620 7 SF4 B2160   S3  121.0  90.6  45.3  90.4  45.5  91.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B2160  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 B2160   S4                                                     
REMARK 620 2 SF4 B2160  FE1   45.0                                              
REMARK 620 3 SF4 B2160  FE2   44.8  59.6                                        
REMARK 620 4 SF4 B2160  FE4   89.8  60.0  59.6                                  
REMARK 620 5 SF4 B2160   S1   89.7  90.1  44.8  45.4                            
REMARK 620 6 SF4 B2160   S2   89.9  45.0  89.7  45.3  90.7                      
REMARK 620 7 CYS B1130   SG  118.2 145.9 135.9 151.1 122.2 134.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B2160  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1124   SG                                                     
REMARK 620 2 SF4 B2160  FE1  147.9                                              
REMARK 620 3 SF4 B2160  FE2  145.7  60.1                                        
REMARK 620 4 SF4 B2160  FE3  139.4  60.4  60.6                                  
REMARK 620 5 SF4 B2160   S1  121.3  90.6  45.4  45.5                            
REMARK 620 6 SF4 B2160   S2  123.3  45.2  90.6  45.4  90.8                      
REMARK 620 7 SF4 B2160   S3  129.5  45.2  45.4  91.0  90.8  90.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A2234  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP A2233   O2G                                                    
REMARK 620 2 THR A  37   OG1 169.0                                              
REMARK 620 3 ANP A2233   O1B  82.7  87.9                                        
REMARK 620 4 HOH A2001   O    96.0  86.9  74.9                                  
REMARK 620 5 HOH A2002   O    89.1  88.4 107.7 174.5                            
REMARK 620 6 HOH A2003   O   101.2  89.1 168.6  94.0  83.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B2162  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP B2161   O2G                                                    
REMARK 620 2 ANP B2161   O1B  74.6                                              
REMARK 620 3 HOH B2001   O    88.9  93.6                                        
REMARK 620 4 HOH B2002   O    94.5  88.1 176.5                                  
REMARK 620 5 HOH B2003   O   111.0 174.1  88.6  89.4                            
REMARK 620 6 THR B  15   OG1 158.5  86.0  83.1  94.0  88.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A2233                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A2234                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B2160                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B2161                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B2162                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CEH   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ADDAB WITH A FORKED DNA SUBSTRATE              
REMARK 900 RELATED ID: 4CEJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ADDAB-DNA-ADPNP COMPLEX AT 3                   
REMARK 900  ANGSTROM RESOLUTION                                                 
DBREF  4CEI A    1  1232  UNP    P23478   ADDA_BACSU       1   1232             
DBREF  4CEI B    1  1166  UNP    P23477   ADDB_BACSU       1   1166             
DBREF  4CEI X    1    65  PDB    4CEI     4CEI             1     65             
SEQADV 4CEI GLY A  780  UNP  P23478    ALA   780 VARIANT                        
SEQADV 4CEI ALA A 1172  UNP  P23478    ASP  1172 ENGINEERED MUTATION            
SEQADV 4CEI ASP B  843  UNP  P23477    GLU   843 VARIANT                        
SEQADV 4CEI GLU B  844  UNP  P23477    GLN   844 VARIANT                        
SEQADV 4CEI ALA B  961  UNP  P23477    ASP   961 ENGINEERED MUTATION            
SEQRES   1 A 1232  MET ASN ILE PRO LYS PRO ALA ASP SER THR TRP THR ASP          
SEQRES   2 A 1232  ASP GLN TRP ASN ALA ILE VAL SER THR GLY GLN ASP ILE          
SEQRES   3 A 1232  LEU VAL ALA ALA ALA ALA GLY SER GLY LYS THR ALA VAL          
SEQRES   4 A 1232  LEU VAL GLU ARG MET ILE ARG LYS ILE THR ALA GLU GLU          
SEQRES   5 A 1232  ASN PRO ILE ASP VAL ASP ARG LEU LEU VAL VAL THR PHE          
SEQRES   6 A 1232  THR ASN ALA SER ALA ALA GLU MET LYS HIS ARG ILE ALA          
SEQRES   7 A 1232  GLU ALA LEU GLU LYS GLU LEU VAL GLN ARG PRO GLY SER          
SEQRES   8 A 1232  LEU HIS ILE ARG ARG GLN LEU SER LEU LEU ASN ARG ALA          
SEQRES   9 A 1232  SER ILE SER THR LEU HIS SER PHE CYS LEU GLN VAL LEU          
SEQRES  10 A 1232  LYS LYS TYR TYR TYR LEU ILE ASP LEU ASP PRO GLY PHE          
SEQRES  11 A 1232  ARG ILE ALA ASP GLN THR GLU GLY GLU LEU ILE GLY ASP          
SEQRES  12 A 1232  GLU VAL LEU ASP GLU LEU PHE GLU ASP GLU TYR ALA LYS          
SEQRES  13 A 1232  GLY GLU LYS ALA PHE PHE GLU LEU VAL ASP ARG TYR THR          
SEQRES  14 A 1232  THR ASP ARG HIS ASP LEU ASP LEU GLN PHE LEU VAL LYS          
SEQRES  15 A 1232  GLN VAL TYR GLU TYR SER ARG SER HIS PRO ASN PRO GLU          
SEQRES  16 A 1232  ALA TRP LEU GLU SER PHE VAL HIS LEU TYR ASP VAL SER          
SEQRES  17 A 1232  GLU LYS SER ALA ILE GLU GLU LEU PRO PHE TYR GLN TYR          
SEQRES  18 A 1232  VAL LYS GLU ASP ILE ALA MET VAL LEU ASN GLY ALA LYS          
SEQRES  19 A 1232  GLU LYS LEU LEU ARG ALA LEU GLU LEU THR LYS ALA PRO          
SEQRES  20 A 1232  GLY GLY PRO ALA PRO ARG ALA ASP ASN PHE LEU ASP ASP          
SEQRES  21 A 1232  LEU ALA GLN ILE ASP GLU LEU ILE GLN HIS GLN ASP ASP          
SEQRES  22 A 1232  PHE SER GLU LEU TYR LYS ARG VAL PRO ALA VAL SER PHE          
SEQRES  23 A 1232  LYS ARG ALA LYS ALA VAL LYS GLY ASP GLU PHE ASP PRO          
SEQRES  24 A 1232  ALA LEU LEU ASP GLU ALA THR ASP LEU ARG ASN GLY ALA          
SEQRES  25 A 1232  LYS LYS LEU LEU GLU LYS LEU LYS THR ASP TYR PHE THR          
SEQRES  26 A 1232  ARG SER PRO GLU GLN HIS LEU LYS SER LEU ALA GLU MET          
SEQRES  27 A 1232  LYS PRO VAL ILE GLU THR LEU VAL GLN LEU VAL ILE SER          
SEQRES  28 A 1232  TYR GLY LYS ARG PHE GLU ALA ALA LYS GLN GLU LYS SER          
SEQRES  29 A 1232  ILE ILE ASP PHE SER ASP LEU GLU HIS TYR CYS LEU ALA          
SEQRES  30 A 1232  ILE LEU THR ALA GLU ASN ASP LYS GLY GLU ARG GLU PRO          
SEQRES  31 A 1232  SER GLU ALA ALA ARG PHE TYR GLN GLU GLN PHE HIS GLU          
SEQRES  32 A 1232  VAL LEU VAL ASP GLU TYR GLN ASP THR ASN LEU VAL GLN          
SEQRES  33 A 1232  GLU SER ILE LEU GLN LEU VAL THR SER GLY PRO GLU GLU          
SEQRES  34 A 1232  THR GLY ASN LEU PHE MET VAL GLY ASP VAL LYS GLN SER          
SEQRES  35 A 1232  ILE TYR ARG PHE ARG LEU ALA GLU PRO LEU LEU PHE LEU          
SEQRES  36 A 1232  SER LYS TYR LYS ARG PHE THR GLU SER GLY GLU GLY THR          
SEQRES  37 A 1232  GLY ARG LYS ILE ASP LEU ASN LYS ASN PHE ARG SER ARG          
SEQRES  38 A 1232  ALA ASP ILE LEU ASP SER THR ASN PHE LEU PHE LYS GLN          
SEQRES  39 A 1232  LEU MET GLY GLY LYS ILE GLY GLU VAL ASP TYR ASP GLU          
SEQRES  40 A 1232  GLN ALA GLU LEU LYS LEU GLY ALA ALA TYR PRO ASP ASN          
SEQRES  41 A 1232  ASP GLU THR GLU THR GLU LEU LEU LEU ILE ASP ASN ALA          
SEQRES  42 A 1232  GLU ASP THR ASP ALA SER GLU GLU ALA GLU GLU LEU GLU          
SEQRES  43 A 1232  THR VAL GLN PHE GLU ALA LYS ALA ILE ALA LYS GLU ILE          
SEQRES  44 A 1232  ARG LYS LEU ILE SER SER PRO PHE LYS VAL TYR ASP GLY          
SEQRES  45 A 1232  LYS LYS LYS THR HIS ARG ASN ILE GLN TYR ARG ASP ILE          
SEQRES  46 A 1232  VAL ILE LEU LEU ARG SER MET PRO TRP ALA PRO GLN ILE          
SEQRES  47 A 1232  MET GLU GLU LEU ARG ALA GLN GLY ILE PRO VAL TYR ALA          
SEQRES  48 A 1232  ASN LEU THR SER GLY TYR PHE GLU ALA VAL GLU VAL ALA          
SEQRES  49 A 1232  VAL ALA LEU SER VAL LEU LYS VAL ILE ASP ASN PRO TYR          
SEQRES  50 A 1232  GLN ASP ILE PRO LEU ALA SER VAL LEU ARG SER PRO ILE          
SEQRES  51 A 1232  VAL GLY ALA ASP GLU ASN GLU LEU SER LEU ILE ARG LEU          
SEQRES  52 A 1232  GLU ASN LYS LYS ALA PRO TYR TYR GLU ALA MET LYS ASP          
SEQRES  53 A 1232  TYR LEU ALA ALA GLY ASP ARG SER ASP GLU LEU TYR GLN          
SEQRES  54 A 1232  LYS LEU ASN THR PHE TYR GLY HIS LEU GLN LYS TRP ARG          
SEQRES  55 A 1232  ALA PHE SER LYS ASN HIS SER VAL SER GLU LEU ILE TRP          
SEQRES  56 A 1232  GLU VAL TYR ARG ASP THR LYS TYR MET ASP TYR VAL GLY          
SEQRES  57 A 1232  GLY MET PRO GLY GLY LYS GLN ARG GLN ALA ASN LEU ARG          
SEQRES  58 A 1232  VAL LEU TYR ASP ARG ALA ARG GLN TYR GLU SER THR ALA          
SEQRES  59 A 1232  PHE ARG GLY LEU PHE ARG PHE LEU ARG PHE ILE GLU ARG          
SEQRES  60 A 1232  MET GLN GLU ARG GLY ASP ASP LEU GLY THR ALA ARG GLY          
SEQRES  61 A 1232  LEU SER GLU GLN GLU ASP VAL VAL ARG LEU MET THR ILE          
SEQRES  62 A 1232  HIS SER SER LYS GLY LEU GLU PHE PRO VAL VAL PHE VAL          
SEQRES  63 A 1232  ALA GLY LEU GLY ARG ASN PHE ASN MET MET ASP LEU ASN          
SEQRES  64 A 1232  LYS SER TYR LEU LEU ASP LYS GLU LEU GLY PHE GLY THR          
SEQRES  65 A 1232  LYS TYR ILE HIS PRO GLN LEU ARG ILE SER TYR PRO THR          
SEQRES  66 A 1232  LEU PRO LEU ILE ALA MET LYS LYS LYS MET ARG ARG GLU          
SEQRES  67 A 1232  LEU LEU SER GLU GLU LEU ARG VAL LEU TYR VAL ALA LEU          
SEQRES  68 A 1232  THR ARG ALA LYS GLU LYS LEU PHE LEU ILE GLY SER CYS          
SEQRES  69 A 1232  LYS ASP HIS GLN LYS GLN LEU ALA LYS TRP GLN ALA SER          
SEQRES  70 A 1232  ALA SER GLN THR ASP TRP LEU LEU PRO GLU PHE ASP ARG          
SEQRES  71 A 1232  TYR GLN ALA ARG THR TYR LEU ASP PHE ILE GLY PRO ALA          
SEQRES  72 A 1232  LEU ALA ARG HIS ARG ASP LEU GLY ASP LEU ALA GLY VAL          
SEQRES  73 A 1232  PRO ALA HIS ALA ASP ILE SER GLY HIS PRO ALA ARG PHE          
SEQRES  74 A 1232  ALA VAL GLN MET ILE HIS SER TYR ASP LEU LEU ASP ASP          
SEQRES  75 A 1232  ASP LEU GLU GLU ARG MET GLU GLU LYS SER GLU ARG LEU          
SEQRES  76 A 1232  GLU ALA ILE ARG ARG GLY GLU PRO VAL PRO GLY SER PHE          
SEQRES  77 A 1232  ALA PHE ASP GLU LYS ALA ARG GLU GLN LEU SER TRP THR          
SEQRES  78 A 1232  TYR PRO HIS GLN GLU VAL THR GLN ILE ARG THR LYS GLN          
SEQRES  79 A 1232  SER VAL SER GLU ILE LYS ARG LYS ARG GLU TYR GLU ASP          
SEQRES  80 A 1232  GLU TYR SER GLY ARG ALA PRO VAL LYS PRO ALA ASP GLY          
SEQRES  81 A 1232  SER ILE LEU TYR ARG ARG PRO ALA PHE MET MET LYS LYS          
SEQRES  82 A 1232  GLY LEU THR ALA ALA GLU LYS GLY THR ALA MET HIS THR          
SEQRES  83 A 1232  VAL MET GLN HIS ILE PRO LEU SER HIS VAL PRO SER ILE          
SEQRES  84 A 1232  GLU GLU ALA GLU GLN THR VAL HIS ARG LEU TYR GLU LYS          
SEQRES  85 A 1232  GLU LEU LEU THR GLU GLU GLN LYS ASP ALA ILE ASP ILE          
SEQRES  86 A 1232  GLU GLU ILE VAL GLN PHE PHE HIS THR GLU ILE GLY GLY          
SEQRES  87 A 1232  GLN LEU ILE GLY ALA LYS TRP LYS ASP ARG GLU ILE PRO          
SEQRES  88 A 1232  PHE SER LEU ALA LEU PRO ALA LYS GLU ILE TYR PRO ASP          
SEQRES  89 A 1232  ALA HIS GLU ALA ASP GLU PRO LEU LEU VAL GLN GLY ILE          
SEQRES  90 A 1232  ILE ASP CYS LEU TYR GLU THR GLU ASP GLY LEU TYR LEU          
SEQRES  91 A 1232  LEU ALA TYR LYS SER ASP ARG ILE GLU GLY LYS PHE GLN          
SEQRES  92 A 1232  HIS GLY PHE GLU GLY ALA ALA PRO ILE LEU LYS LYS ARG          
SEQRES  93 A 1232  TYR GLU THR GLN ILE GLN LEU TYR THR LYS ALA VAL GLU          
SEQRES  94 A 1232  GLN ILE ALA LYS THR LYS VAL LYS GLY CYS ALA LEU TYR          
SEQRES  95 A 1232  PHE PHE ASP GLY GLY HIS ILE LEU THR LEU                      
SEQRES   1 B 1166  MET GLY ALA GLU PHE LEU VAL GLY ARG SER GLY SER GLY          
SEQRES   2 B 1166  LYS THR LYS LEU ILE ILE ASN SER ILE GLN ASP GLU LEU          
SEQRES   3 B 1166  ARG ARG ALA PRO PHE GLY LYS PRO ILE ILE PHE LEU VAL          
SEQRES   4 B 1166  PRO ASP GLN MET THR PHE LEU MET GLU TYR GLU LEU ALA          
SEQRES   5 B 1166  LYS THR PRO ASP MET GLY GLY MET ILE ARG ALA GLN VAL          
SEQRES   6 B 1166  PHE SER PHE SER ARG LEU ALA TRP ARG VAL LEU GLN HIS          
SEQRES   7 B 1166  THR GLY GLY MET SER ARG PRO PHE LEU THR SER THR GLY          
SEQRES   8 B 1166  VAL GLN MET LEU LEU ARG LYS LEU ILE GLU GLU HIS LYS          
SEQRES   9 B 1166  GLN GLU PHE LYS VAL TYR GLN LYS ALA SER ASP LYS SER          
SEQRES  10 B 1166  GLY PHE THR ALA GLN VAL GLU ARG MET LEU THR GLU PHE          
SEQRES  11 B 1166  LYS ARG TYR CYS LEU GLU PRO GLU ASP ILE ARG ARG MET          
SEQRES  12 B 1166  ALA GLU SER GLY THR ALA SER GLU TYR ARG GLY GLU ARG          
SEQRES  13 B 1166  VAL LEU SER GLU LYS LEU HIS ASP LEU SER ILE LEU TYR          
SEQRES  14 B 1166  GLN GLN MET GLU LYS SER LEU ALA ASP GLN TYR LEU HIS          
SEQRES  15 B 1166  SER GLU ASP TYR LEU THR LEU LEU ALA GLU HIS ILE PRO          
SEQRES  16 B 1166  LEU ALA GLU ASP ILE LYS GLY ALA HIS ILE TYR VAL ASP          
SEQRES  17 B 1166  GLY PHE TYR GLN PHE THR PRO GLN GLU PHE ARG VAL LEU          
SEQRES  18 B 1166  GLU GLN LEU MET VAL HIS ALA GLU HIS ILE THR PHE SER          
SEQRES  19 B 1166  LEU THR ALA ASP LYS PRO SER TYR GLU ARG GLU PRO HIS          
SEQRES  20 B 1166  GLU LEU GLU LEU PHE ARG MET THR GLY LYS THR TYR TYR          
SEQRES  21 B 1166  ARG LEU HIS GLN LYS ALA LYS GLU LEU ASN LEU ASP ILE          
SEQRES  22 B 1166  THR TYR LYS GLU LEU SER GLY THR GLU ARG HIS THR LYS          
SEQRES  23 B 1166  THR PRO GLU LEU ALA HIS LEU GLU ALA GLN TYR GLU ALA          
SEQRES  24 B 1166  ARG PRO ALA ILE PRO TYR ALA GLU LYS GLN GLU ALA LEU          
SEQRES  25 B 1166  THR VAL MET GLN ALA ALA ASN ARG ARG ALA GLU LEU GLU          
SEQRES  26 B 1166  GLY ILE ALA ARG GLU ILE HIS ALA LEU VAL ARG GLU LYS          
SEQRES  27 B 1166  GLY TYR ARG TYR LYS ASP VAL ALA ILE LEU ALA ARG GLN          
SEQRES  28 B 1166  PRO GLU ASP TYR LYS ASP MET VAL LYS GLU VAL PHE ALA          
SEQRES  29 B 1166  ASP TYR GLU ILE PRO TYR PHE ILE ASP GLY LYS ALA SER          
SEQRES  30 B 1166  MET LEU ASN HIS PRO LEU ILE GLU PHE ILE ARG SER SER          
SEQRES  31 B 1166  LEU ASP VAL LEU LYS GLY ASN TRP ARG TYR GLU ALA VAL          
SEQRES  32 B 1166  PHE ARG CYS VAL LYS THR GLU LEU LEU PHE PRO LEU ASN          
SEQRES  33 B 1166  GLU PRO LYS ALA LYS VAL ARG GLU GLN VAL ASP GLN LEU          
SEQRES  34 B 1166  GLU ASN TYR CYS ILE ALA TYR GLY ILE LYS GLY ASP ARG          
SEQRES  35 B 1166  TRP THR LYS GLY ASP ARG PHE GLN TYR ARG ARG PHE VAL          
SEQRES  36 B 1166  SER LEU ASP ASP ASP PHE ALA GLN THR ASP GLN GLU ILE          
SEQRES  37 B 1166  GLU MET GLU ASN MET LEU ASN ASP THR ARG ASP TRP ILE          
SEQRES  38 B 1166  VAL PRO PRO LEU PHE GLN LEU GLN LYS ARG MET LYS LYS          
SEQRES  39 B 1166  ALA LYS THR VAL GLN GLU LYS ALA GLU ALA LEU TYR ARG          
SEQRES  40 B 1166  TYR LEU GLU GLU THR ASP VAL PRO LEU LYS LEU ASP GLN          
SEQRES  41 B 1166  GLU ARG GLN ARG ALA GLU ASP ASP GLY ARG ILE ILE GLU          
SEQRES  42 B 1166  ALA GLN GLN HIS GLN GLN ALA TRP ASP ALA VAL ILE GLN          
SEQRES  43 B 1166  LEU LEU GLU GLU PHE VAL GLU MET MET GLY ASP ASP GLU          
SEQRES  44 B 1166  ILE SER LEU ASP LEU PHE GLN GLN MET ILE GLU ALA GLY          
SEQRES  45 B 1166  ALA GLU SER LEU THR PHE SER LEU ILE PRO PRO ALA LEU          
SEQRES  46 B 1166  ASP GLN VAL PHE VAL GLY ASN MET ASP LEU SER ARG MET          
SEQRES  47 B 1166  TYR GLY THR SER CYS THR PHE VAL LEU GLY ALA ASN ASP          
SEQRES  48 B 1166  GLY VAL LEU PRO ALA ARG PRO ASP GLU ASN GLY VAL LEU          
SEQRES  49 B 1166  SER ASP ASP ASP ARG GLU TRP LEU LYS THR ILE GLY VAL          
SEQRES  50 B 1166  GLU LEU SER SER GLY GLY ARG GLU ARG LEU LEU ASP GLU          
SEQRES  51 B 1166  HIS PHE LEU ILE TYR MET ALA PHE SER SER PRO SER ASP          
SEQRES  52 B 1166  ARG LEU TYR VAL SER TYR PRO ILE ALA ASP ALA GLU GLY          
SEQRES  53 B 1166  LYS THR LEU LEU PRO SER MET ILE VAL LYS ARG LEU GLU          
SEQRES  54 B 1166  GLU LEU PHE PRO HIS HIS LYS GLU ARG LEU LEU THR ASN          
SEQRES  55 B 1166  GLU PRO GLU GLN VAL SER ASP GLU GLU GLN LEU MET TYR          
SEQRES  56 B 1166  VAL VAL ASN LYS SER VAL ALA GLN SER PHE THR ALA SER          
SEQRES  57 B 1166  GLN LEU ARG LEU TRP THR ARG GLU TYR ASP ILE SER ASP          
SEQRES  58 B 1166  VAL TRP TRP SER THR TYR ASN VAL LEU MET SER GLU GLN          
SEQRES  59 B 1166  ASP ARG LEU GLN SER LYS LYS LEU PHE SER SER LEU PHE          
SEQRES  60 B 1166  PHE ARG ASN GLU VAL LYS GLN LEU GLU ARG SER VAL SER          
SEQRES  61 B 1166  ARG GLN LEU TYR GLY GLU ARG ILE GLN GLY SER VAL SER          
SEQRES  62 B 1166  ARG MET GLU THR PHE ASN ALA CYS PRO PHE SER HIS PHE          
SEQRES  63 B 1166  ALA SER HIS GLY LEU HIS LEU LYS GLU ARG GLN PHE PHE          
SEQRES  64 B 1166  LYS LEU GLU ALA PRO ASP ILE GLY GLN LEU PHE HIS SER          
SEQRES  65 B 1166  SER LEU LYS LEU ILE SER ASP ARG LEU ARG ASP GLU LYS          
SEQRES  66 B 1166  LEU ASP TRP ARG ASP LEU THR LYS GLU GLN CYS GLU LEU          
SEQRES  67 B 1166  PHE SER TYR ASP ALA VAL GLU ARG LEU ALA PRO LYS LEU          
SEQRES  68 B 1166  GLN LYS GLU ILE LEU LEU SER SER ASN ARG HIS TYR TYR          
SEQRES  69 B 1166  VAL LYS GLU LYS LEU GLN LYS ILE VAL THR ARG VAL SER          
SEQRES  70 B 1166  GLY ILE LEU SER GLU HIS ALA LYS ALA SER GLY PHE VAL          
SEQRES  71 B 1166  PRO ILE GLY LEU GLU LEU GLY PHE GLY GLY LYS GLY PRO          
SEQRES  72 B 1166  LEU PRO PRO LEU THR PHE GLN LEU LYS ASN GLY CYS THR          
SEQRES  73 B 1166  MET GLU LEU VAL GLY ARG ILE ASP ARG VAL ASP LYS ALA          
SEQRES  74 B 1166  GLU SER SER LYS GLY LEU LEU LEU ARG ILE VAL ALA TYR          
SEQRES  75 B 1166  LYS SER SER ASP LYS GLY LEU ASP LEU ALA GLU VAL TYR          
SEQRES  76 B 1166  TYR GLY LEU ALA LEU GLN MET LEU THR TYR LEU ASP LEU          
SEQRES  77 B 1166  SER ILE THR HIS SER ALA ASP TRP LEU GLY MET ARG ALA          
SEQRES  78 B 1166  THR PRO ALA GLY VAL LEU TYR PHE HIS ILE HIS ASP PRO          
SEQRES  79 B 1166  MET ILE GLN SER ASN LEU PRO LEU GLY LEU ASP GLU ILE          
SEQRES  80 B 1166  GLU GLN GLU ILE PHE LYS LYS PHE LYS MET LYS GLY LEU          
SEQRES  81 B 1166  LEU LEU GLY ASP GLN GLU VAL VAL ARG LEU MET ASP THR          
SEQRES  82 B 1166  THR LEU GLN GLU GLY ARG SER ASN ILE ILE ASN ALA GLY          
SEQRES  83 B 1166  LEU LYS LYS ASP GLY SER LEU ARG SER ASP SER ALA ALA          
SEQRES  84 B 1166  VAL GLY GLU LYS GLU PHE ASP LEU LEU THR LYS HIS VAL          
SEQRES  85 B 1166  ARG ARG THR PHE GLN GLU ALA GLY GLU GLN ILE THR ASP          
SEQRES  86 B 1166  GLY ARG VAL SER ILE GLU PRO TYR LYS MET LYS ASN LYS          
SEQRES  87 B 1166  THR PRO CYS THR TYR CYS ALA PHE LYS SER VAL CYS GLN          
SEQRES  88 B 1166  PHE ASP GLU SER LEU GLU GLU ASN GLU TYR ARG PRO LEU          
SEQRES  89 B 1166  LYS ALA GLU LYS ASP LYS THR ILE LEU GLU TRP ILE LYS          
SEQRES  90 B 1166  LYS GLU ALA ASP GLY ASN GLU HIS SER                          
SEQRES   1 X   65   DT  DT  DT  DT  DT  DT  DT  DC  DT  DA  DA  DT  DG          
SEQRES   2 X   65   DC  DG  DA  DG  DC  DA  DC  DT  DG  DC  DT  DA  DT          
SEQRES   3 X   65   DT  DC  DC  DC  DT  DA  DG  DC  DA  DG  DT  DG  DC          
SEQRES   4 X   65   DT  DC  DG  DC  DA  DT  DT  DA  DG  DA  DT  DT  DT          
SEQRES   5 X   65   DT  DG  DT  DT  DT  DT  DT  DT  DA  DG  DC  DG  DG          
HET    ANP  A2233      31                                                       
HET     MG  A2234       1                                                       
HET    SF4  B2160       8                                                       
HET    ANP  B2161      31                                                       
HET     MG  B2162       1                                                       
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   4  ANP    2(C10 H17 N6 O12 P3)                                         
FORMUL   5  SF4    FE4 S4                                                       
FORMUL   6   MG    2(MG 2+)                                                     
FORMUL   8  HOH   *8(H2 O)                                                      
HELIX    1   1 THR A   12  SER A   21  1                                  10    
HELIX    2   2 GLY A   35  THR A   49  1                                  15    
HELIX    3   3 ASP A   56  ASP A   58  5                                   3    
HELIX    4   4 THR A   66  ARG A   88  1                                  23    
HELIX    5   5 SER A   91  LEU A  101  1                                  11    
HELIX    6   6 LEU A  109  TYR A  121  1                                  13    
HELIX    7   7 TYR A  122  ILE A  124  5                                   3    
HELIX    8   8 ASP A  134  GLY A  157  1                                  24    
HELIX    9   9 GLU A  158  THR A  169  1                                  12    
HELIX   10  10 ASP A  174  ARG A  189  1                                  16    
HELIX   11  11 ASN A  193  SER A  200  1                                   8    
HELIX   12  12 PHE A  201  TYR A  205  5                                   5    
HELIX   13  13 ALA A  212  PRO A  217  5                                   6    
HELIX   14  14 PHE A  218  ALA A  246  1                                  29    
HELIX   15  15 ARG A  253  GLN A  269  1                                  17    
HELIX   16  16 ASP A  273  VAL A  281  1                                   9    
HELIX   17  17 PRO A  282  VAL A  284  5                                   3    
HELIX   18  18 ASP A  298  PHE A  324  1                                  27    
HELIX   19  19 SER A  327  MET A  338  1                                  12    
HELIX   20  20 MET A  338  LYS A  363  1                                  26    
HELIX   21  21 PHE A  368  LEU A  379  1                                  12    
HELIX   22  22 SER A  391  PHE A  401  1                                  11    
HELIX   23  23 GLU A  408  THR A  412  5                                   5    
HELIX   24  24 ASN A  413  THR A  424  1                                  12    
HELIX   25  25 PRO A  427  GLY A  431  5                                   5    
HELIX   26  26 ASP A  438  SER A  442  5                                   5    
HELIX   27  27 TYR A  444  LEU A  448  5                                   5    
HELIX   28  28 GLU A  450  PHE A  461  1                                  12    
HELIX   29  29 ARG A  481  LYS A  493  1                                  13    
HELIX   30  30 GLU A  546  SER A  565  1                                  20    
HELIX   31  31 GLY A  572  LYS A  575  5                                   4    
HELIX   32  32 GLN A  581  ARG A  583  5                                   3    
HELIX   33  33 SER A  591  PRO A  593  5                                   3    
HELIX   34  34 TRP A  594  ALA A  604  1                                  11    
HELIX   35  35 TYR A  617  GLU A  619  5                                   3    
HELIX   36  36 ALA A  620  ASN A  635  1                                  16    
HELIX   37  37 GLN A  638  SER A  648  1                                  11    
HELIX   38  38 ASP A  654  GLU A  664  1                                  11    
HELIX   39  39 PRO A  669  GLY A  681  1                                  13    
HELIX   40  40 ASP A  685  LYS A  706  1                                  22    
HELIX   41  41 SER A  709  LYS A  722  1                                  14    
HELIX   42  42 LYS A  722  GLY A  728  1                                   7    
HELIX   43  43 GLY A  732  SER A  752  1                                  21    
HELIX   44  44 GLY A  757  ARG A  771  1                                  15    
HELIX   45  45 MET A  815  LYS A  820  5                                   6    
HELIX   46  46 THR A  845  THR A  872  1                                  28    
HELIX   47  47 ASP A  886  ALA A  896  1                                  11    
HELIX   48  48 PRO A  906  GLN A  912  1                                   7    
HELIX   49  49 TYR A  916  ARG A  926  1                                  11    
HELIX   50  50 HIS A  939  GLY A  944  1                                   6    
HELIX   51  51 HIS A  955  LEU A  960  1                                   6    
HELIX   52  52 SER A  972  GLY A  981  1                                  10    
HELIX   53  53 PHE A  990  SER A  999  1                                  10    
HELIX   54  54 HIS A 1004  THR A 1008  5                                   5    
HELIX   55  55 PRO A 1047  MET A 1051  5                                   5    
HELIX   56  56 THR A 1056  GLN A 1069  1                                  14    
HELIX   57  57 SER A 1078  LYS A 1092  1                                  15    
HELIX   58  58 THR A 1096  ALA A 1102  1                                   7    
HELIX   59  59 ASP A 1104  GLN A 1110  1                                   7    
HELIX   60  60 PHE A 1111  HIS A 1113  5                                   3    
HELIX   61  61 THR A 1114  GLY A 1122  1                                   9    
HELIX   62  62 ALA A 1138  TYR A 1142  1                                   5    
HELIX   63  63 ALA A 1189  TYR A 1197  1                                   9    
HELIX   64  64 TYR A 1197  ALA A 1212  1                                  16    
HELIX   65  65 ASP A 1225  GLY A 1227  5                                   3    
HELIX   66  66 GLY B   13  ALA B   29  1                                  17    
HELIX   67  67 PRO B   40  GLN B   42  5                                   3    
HELIX   68  68 MET B   43  ALA B   52  1                                  10    
HELIX   69  69 SER B   67  GLY B   80  1                                  14    
HELIX   70  70 THR B   88  LYS B  104  1                                  17    
HELIX   71  71 GLN B  105  PHE B  107  5                                   3    
HELIX   72  72 LYS B  112  ASP B  115  5                                   4    
HELIX   73  73 LYS B  116  TYR B  133  1                                  18    
HELIX   74  74 GLU B  136  MET B  143  1                                   8    
HELIX   75  75 GLY B  154  ALA B  177  1                                  24    
HELIX   76  76 HIS B  182  GLU B  184  5                                   3    
HELIX   77  77 ASP B  185  GLU B  192  1                                   8    
HELIX   78  78 ALA B  197  GLY B  202  1                                   6    
HELIX   79  79 THR B  214  ALA B  228  1                                  15    
HELIX   80  80 PHE B  252  LEU B  269  1                                  18    
HELIX   81  81 THR B  287  GLN B  296  1                                  10    
HELIX   82  82 ASN B  319  GLU B  337  1                                  19    
HELIX   83  83 ARG B  341  LYS B  343  5                                   3    
HELIX   84  84 GLN B  351  ASP B  354  5                                   4    
HELIX   85  85 TYR B  355  TYR B  366  1                                  12    
HELIX   86  86 HIS B  381  GLY B  396  1                                  16    
HELIX   87  87 ARG B  399  LYS B  408  1                                  10    
HELIX   88  88 PRO B  418  GLY B  437  1                                  20    
HELIX   89  89 GLY B  440  LYS B  445  1                                   6    
HELIX   90  90 THR B  464  ALA B  495  1                                  32    
HELIX   91  91 THR B  497  THR B  512  1                                  16    
HELIX   92  92 ASP B  513  ASP B  528  1                                  16    
HELIX   93  93 ARG B  530  GLY B  556  1                                  27    
HELIX   94  94 SER B  561  LEU B  576  1                                  16    
HELIX   95  95 SER B  625  ILE B  635  1                                  11    
HELIX   96  96 GLY B  642  SER B  659  1                                  18    
HELIX   97  97 SER B  682  PHE B  692  1                                  11    
HELIX   98  98 GLU B  703  VAL B  707  5                                   5    
HELIX   99  99 SER B  708  LEU B  713  1                                   6    
HELIX  100 100 MET B  714  VAL B  716  5                                   3    
HELIX  101 101 ASN B  718  THR B  734  1                                  17    
HELIX  102 102 SER B  740  GLU B  753  1                                  14    
HELIX  103 103 ASP B  755  SER B  764  1                                  10    
HELIX  104 104 SER B  765  PHE B  768  5                                   4    
HELIX  105 105 GLU B  776  GLY B  785  1                                  10    
HELIX  106 106 SER B  791  CYS B  801  1                                  11    
HELIX  107 107 CYS B  801  GLY B  810  1                                  10    
HELIX  108 108 GLU B  822  GLU B  844  1                                  23    
HELIX  109 109 ASP B  847  LEU B  851  5                                   5    
HELIX  110 110 THR B  852  ALA B  868  1                                  17    
HELIX  111 111 LEU B  871  SER B  878  5                                   8    
HELIX  112 112 SER B  879  LYS B  905  1                                  27    
HELIX  113 113 ASP B  970  TYR B  976  1                                   7    
HELIX  114 114 LEU B  980  HIS B  992  1                                  13    
HELIX  115 115 HIS B  992  LEU B  997  1                                   6    
HELIX  116 116 GLY B 1023  LYS B 1034  1                                  12    
HELIX  117 117 ASP B 1044  ASP B 1052  1                                   9    
HELIX  118 118 GLY B 1081  ASP B 1105  1                                  25    
HELIX  119 119 PRO B 1120  CYS B 1124  5                                   5    
HELIX  120 120 PHE B 1126  GLN B 1131  1                                   6    
HELIX  121 121 LYS B 1148  GLU B 1159  1                                  12    
SHEET    1  AA 6 SER A 105  THR A 108  0                                        
SHEET    2  AA 6 LEU A  60  THR A  64  1  O  VAL A  62   N  SER A 107           
SHEET    3  AA 6 GLU A 403  VAL A 406  1  O  GLU A 403   N  LEU A  61           
SHEET    4  AA 6 LEU A 433  GLY A 437  1  O  PHE A 434   N  VAL A 406           
SHEET    5  AA 6 ILE A  26  ALA A  30  1  O  ILE A  26   N  MET A 435           
SHEET    6  AA 6 ARG A 470  LEU A 474  1  O  ARG A 470   N  LEU A  27           
SHEET    1  AB 2 ARG A 131  ILE A 132  0                                        
SHEET    2  AB 2 ILE A 365  ILE A 366  1  N  ILE A 366   O  ARG A 131           
SHEET    1  AC 2 THR A 380  ASP A 384  0                                        
SHEET    2  AC 2 GLU A 387  PRO A 390 -1  O  GLU A 387   N  ASP A 384           
SHEET    1  AD 2 LYS A 476  ASN A 477  0                                        
SHEET    2  AD 2 LYS A 512  LEU A 513  1  O  LYS A 512   N  ASN A 477           
SHEET    1  AE 7 VAL A 609  TYR A 610  0                                        
SHEET    2  AE 7 VAL A 788  THR A 792  1  O  VAL A 788   N  TYR A 610           
SHEET    3  AE 7 ILE A 585  LEU A 589  1  O  ILE A 585   N  ARG A 789           
SHEET    4  AE 7 PHE A 801  ALA A 807  1  O  VAL A 803   N  VAL A 586           
SHEET    5  AE 7 ALA A 874  SER A 883  1  N  LYS A 875   O  PHE A 801           
SHEET    6  AE 7 THR A 525  ILE A 530  1  O  GLU A 526   N  LEU A 880           
SHEET    7  AE 7 PHE A 949  GLN A 952  1  O  ALA A 950   N  LEU A 527           
SHEET    1  AF 2 LYS A 568  ASP A 571  0                                        
SHEET    2  AF 2 THR A 576  ASN A 579 -1  O  THR A 576   N  ASP A 571           
SHEET    1  AG 4 TYR A 822  ASP A 825  0                                        
SHEET    2  AG 4 GLY A 829  HIS A 836 -1  O  GLY A 829   N  ASP A 825           
SHEET    3  AG 4 ILE A 841  PRO A 844 -1  O  ILE A 841   N  HIS A 836           
SHEET    4  AG 4 ILE B1016  GLN B1017  1  O  ILE B1016   N  SER A 842           
SHEET    1  AH 2 LYS A1013  SER A1015  0                                        
SHEET    2  AH 2 PRO A1151  GLU A1163  1  O  LEU A1153   N  GLN A1014           
SHEET    1  AI 6 HIS A1228  LEU A1232  0                                        
SHEET    2  AI 6 CYS A1219  PHE A1223 -1  O  CYS A1219   N  LEU A1232           
SHEET    3  AI 6 LEU A1168  LYS A1174  1  O  LEU A1170   N  ALA A1220           
SHEET    4  AI 6 PRO A1151  GLU A1163 -1  O  CYS A1160   N  LEU A1171           
SHEET    5  AI 6 TRP A1125  PRO A1137 -1  O  TRP A1125   N  GLU A1163           
SHEET    6  AI 6 GLY B  59  MET B  60 -1  O  MET B  60   N  SER A1133           
SHEET    1  AJ 5 HIS A1228  LEU A1232  0                                        
SHEET    2  AJ 5 CYS A1219  PHE A1223 -1  O  CYS A1219   N  LEU A1232           
SHEET    3  AJ 5 LEU A1168  LYS A1174  1  O  LEU A1170   N  ALA A1220           
SHEET    4  AJ 5 PRO A1151  GLU A1163 -1  O  CYS A1160   N  LEU A1171           
SHEET    5  AJ 5 LYS A1013  SER A1015  1  O  GLN A1014   N  GLN A1155           
SHEET    1  BA 6 ALA B  63  PHE B  66  0                                        
SHEET    2  BA 6 ILE B  35  LEU B  38  1  O  ILE B  35   N  GLN B  64           
SHEET    3  BA 6 HIS B 204  ASP B 208  1  O  HIS B 204   N  ILE B  36           
SHEET    4  BA 6 HIS B 230  THR B 236  1  O  HIS B 230   N  ILE B 205           
SHEET    5  BA 6 ALA B   3  GLY B   8  1  O  GLU B   4   N  PHE B 233           
SHEET    6  BA 6 ILE B 273  LEU B 278  1  O  THR B 274   N  PHE B   5           
SHEET    1  BB 7 TYR B 370  ILE B 372  0                                        
SHEET    2  BB 7 VAL B 588  ASN B 592  1  O  VAL B 588   N  PHE B 371           
SHEET    3  BB 7 VAL B 345  ALA B 349  1  O  VAL B 345   N  PHE B 589           
SHEET    4  BB 7 CYS B 603  LEU B 607  1  O  CYS B 603   N  ALA B 346           
SHEET    5  BB 7 ARG B 664  PRO B 670  1  O  ARG B 664   N  THR B 604           
SHEET    6  BB 7 LEU B 312  ALA B 317  1  O  THR B 313   N  VAL B 667           
SHEET    7  BB 7 ARG B 698  LEU B 700  1  O  ARG B 698   N  GLN B 316           
SHEET    1  BC 3 ARG B 787  GLY B 790  0                                        
SHEET    2  BC 3 THR B 936  LEU B 939  1  O  THR B 936   N  ILE B 788           
SHEET    3  BC 3 LEU B 927  GLN B 930 -1  O  LEU B 927   N  LEU B 939           
SHEET    1  BD 6 VAL B 910  PHE B 918  0                                        
SHEET    2  BD 6 GLY B 941  GLU B 950 -1  O  GLY B 941   N  PHE B 918           
SHEET    3  BD 6 LEU B 955  LYS B 963 -1  O  LEU B 956   N  ALA B 949           
SHEET    4  BD 6 ALA B1001  HIS B1010  1  O  THR B1002   N  LEU B 957           
SHEET    5  BD 6 LYS B1038  LEU B1042 -1  O  LYS B1038   N  TYR B1008           
SHEET    6  BD 6 ALA B1079  VAL B1080  1  N  VAL B1080   O  LEU B1041           
SHEET    1  BE 2 GLY B1058  ARG B1059  0                                        
SHEET    2  BE 2 GLY B1066  LEU B1067 -1  O  LEU B1067   N  GLY B1058           
SHEET    1  BF 2 TYR B1113  LYS B1114  0                                        
SHEET    2  BF 2 ARG B1142  PRO B1143  1  O  ARG B1142   N  LYS B1114           
LINK         O2G ANP A2233                MG    MG A2234     1555   1555  2.08  
LINK         O1B ANP A2233                MG    MG A2234     1555   1555  2.06  
LINK        MG    MG A2234                 OG1 THR A  37     1555   1555  2.09  
LINK        MG    MG A2234                 O   HOH A2001     1555   1555  2.03  
LINK        MG    MG A2234                 O   HOH A2002     1555   1555  2.02  
LINK        MG    MG A2234                 O   HOH A2003     1555   1555  2.04  
LINK         SG  CYS B 801                FE1  SF4 B2160     1555   1555  2.30  
LINK         SG  CYS B1121                FE2  SF4 B2160     1555   1555  2.31  
LINK         SG  CYS B1124                FE4  SF4 B2160     1555   1555  2.28  
LINK         SG  CYS B1130                FE3  SF4 B2160     1555   1555  2.27  
LINK         O1B ANP B2161                MG    MG B2162     1555   1555  2.08  
LINK         O2G ANP B2161                MG    MG B2162     1555   1555  2.07  
LINK        MG    MG B2162                 O   HOH B2002     1555   1555  1.99  
LINK        MG    MG B2162                 O   HOH B2003     1555   1555  2.06  
LINK        MG    MG B2162                 OG1 THR B  15     1555   1555  2.09  
LINK        MG    MG B2162                 O   HOH B2001     1555   1555  1.99  
CISPEP   1 ARG B  300    PRO B  301          0        -2.31                     
CISPEP   2 LEU B  614    PRO B  615          0         5.96                     
SITE     1 AC1 22 THR A  10  GLN A  15  ALA A  32  GLY A  33                    
SITE     2 AC1 22 SER A  34  GLY A  35  LYS A  36  THR A  37                    
SITE     3 AC1 22 ALA A  38  ARG A  76  GLU A 408  GLN A 441                    
SITE     4 AC1 22 PHE A 478  ARG A 479  LYS A 573  GLY A 798                    
SITE     5 AC1 22 GLU A 800  ARG A 873  HOH A2001  HOH A2002                    
SITE     6 AC1 22 HOH A2004   MG A2234                                          
SITE     1 AC2  5 THR A  37  HOH A2001  HOH A2002  HOH A2003                    
SITE     2 AC2  5 ANP A2233                                                     
SITE     1 AC3  5 CYS B 801  PRO B1112  CYS B1121  CYS B1124                    
SITE     2 AC3  5 CYS B1130                                                     
SITE     1 AC4 15 SER B  10  GLY B  11  GLY B  13  LYS B  14                    
SITE     2 AC4 15 THR B  15  LYS B  16  THR B 236  GLU B 282                    
SITE     3 AC4 15 ARG B 283  GLY B 600  MET B 656  HOH B2001                    
SITE     4 AC4 15 HOH B2002  HOH B2004   MG B2162                               
SITE     1 AC5  6 THR B  15  ASP B 208  HOH B2001  HOH B2002                    
SITE     2 AC5  6 HOH B2003  ANP B2161                                          
CRYST1   75.944  151.335  124.560  90.00  95.95  90.00 P 1 21 1      2          
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      0.013168  0.000000  0.001372        0.00000                         
SCALE2      0.000000  0.006608  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008072        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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