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Database: PDB
Entry: 1NH3
LinkDB: 1NH3
Original site: 1NH3 
HEADER    ISOMERASE/DNA                           18-DEC-02   1NH3              
TITLE     HUMAN TOPOISOMERASE I ARA-C COMPLEX                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-D(*AP*AP*AP*AP*AP*GP*AP*CP*UP*(UBB))-3';                
COMPND   3 CHAIN: B;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: 5'-D(*(GNG)P*GP*AP*AP*AP*AP*AP*UP*UP*UP*UP*T)-3';          
COMPND   7 CHAIN: C;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: 5'-D(*AP*AP*AP*AP*AP*TP*UP*UP*UP*UP*CP*(CAR)               
COMPND  11 P*AP*AP*GP*UP*CP*UP*UP*UP*UP*T)-3';                                  
COMPND  12 CHAIN: D;                                                            
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 4;                                                           
COMPND  15 MOLECULE: DNA TOPOISOMERASE I;                                       
COMPND  16 CHAIN: A;                                                            
COMPND  17 FRAGMENT: CORE SUBDOMAIN, C-TERMINAL DOMAIN;                         
COMPND  18 EC: 5.99.1.2;                                                        
COMPND  19 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 MOL_ID: 2;                                                           
SOURCE   4 SYNTHETIC: YES;                                                      
SOURCE   5 MOL_ID: 3;                                                           
SOURCE   6 SYNTHETIC: YES;                                                      
SOURCE   7 MOL_ID: 4;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 GENE: TOP1;                                                          
SOURCE  12 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  13 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  15 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    ARA-C, PROTEIN-DNA COMPLEX, DNA DAMAGE, ISOMERASE,                    
KEYWDS   2 ISOMERASE/DNA COMPLEX                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.CHRENCIK,A.B.BURGIN,Y.POMMIER,L.STEWART,M.R.REDINBO               
REVDAT   3   24-FEB-09 1NH3    1       VERSN                                    
REVDAT   2   08-APR-03 1NH3    1       JRNL                                     
REVDAT   1   04-MAR-03 1NH3    0                                                
JRNL        AUTH   J.E.CHRENCIK,A.B.BURGIN,Y.POMMIER,L.STEWART,                 
JRNL        AUTH 2 M.R.REDINBO                                                  
JRNL        TITL   STRUCTURAL IMPACT OF THE LEUKEMIA DRUG                       
JRNL        TITL 2 1-BETA-D-ARABINOFURANOSYLCYTOSINE (ARA-C) ON THE             
JRNL        TITL 3 COVALENT HUMAN TOPOISOMERASE I-DNA COMPLEX                   
JRNL        REF    J.BIOL.CHEM.                  V. 278 12461 2003              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   12533542                                                     
JRNL        DOI    10.1074/JBC.M212930200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.29                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 74.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 13878                          
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) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.311                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1351                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3483                                    
REMARK   3   NUCLEIC ACID ATOMS       : 878                                     
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 33                                      
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) : 27.26000                                             
REMARK   3    B22 (A**2) : 27.26000                                             
REMARK   3    B33 (A**2) : -54.52000                                            
REMARK   3    B12 (A**2) : 13.43700                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.48                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.71                            
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) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.026                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 3.88                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1NH3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-FEB-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB017864.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-FEB-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13878                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 69.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 54.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1A31                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS, MAGNESIUM CHLORIDE, PEG 400,       
REMARK 280  DTT, PH 7.7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 276K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      124.19333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       62.09667            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D, A                            
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     ALA A   627                                                      
REMARK 465     ILE A   628                                                      
REMARK 465     LEU A   629                                                      
REMARK 465     CYS A   630                                                      
REMARK 465     ASN A   631                                                      
REMARK 465     HIS A   632                                                      
REMARK 465     GLN A   633                                                      
REMARK 465     ARG A   634                                                      
REMARK 465     ALA A   635                                                      
REMARK 465     PRO A   636                                                      
REMARK 465     PRO A   637                                                      
REMARK 465     LYS A   638                                                      
REMARK 465     THR A   639                                                      
REMARK 465     PHE A   640                                                      
REMARK 465     GLU A   641                                                      
REMARK 465     LYS A   642                                                      
REMARK 465     SER A   643                                                      
REMARK 465     MET A   644                                                      
REMARK 465     MET A   645                                                      
REMARK 465     ASN A   646                                                      
REMARK 465     LEU A   647                                                      
REMARK 465     GLN A   648                                                      
REMARK 465     THR A   649                                                      
REMARK 465     LYS A   650                                                      
REMARK 465     ILE A   651                                                      
REMARK 465     ASP A   652                                                      
REMARK 465     ALA A   653                                                      
REMARK 465     LYS A   654                                                      
REMARK 465     LYS A   655                                                      
REMARK 465     GLU A   656                                                      
REMARK 465     GLN A   657                                                      
REMARK 465     LEU A   658                                                      
REMARK 465     ALA A   659                                                      
REMARK 465     ASP A   660                                                      
REMARK 465     ALA A   661                                                      
REMARK 465     ARG A   662                                                      
REMARK 465     ARG A   663                                                      
REMARK 465     ASP A   664                                                      
REMARK 465     LEU A   665                                                      
REMARK 465     LYS A   666                                                      
REMARK 465     SER A   667                                                      
REMARK 465     ALA A   668                                                      
REMARK 465     LYS A   669                                                      
REMARK 465     ALA A   670                                                      
REMARK 465     ASP A   671                                                      
REMARK 465     ALA A   672                                                      
REMARK 465     LYS A   673                                                      
REMARK 465     VAL A   674                                                      
REMARK 465     MET A   675                                                      
REMARK 465     LYS A   676                                                      
REMARK 465     ASP A   677                                                      
REMARK 465     ALA A   678                                                      
REMARK 465     LYS A   679                                                      
REMARK 465     THR A   680                                                      
REMARK 465     LYS A   681                                                      
REMARK 465     LYS A   682                                                      
REMARK 465     VAL A   683                                                      
REMARK 465     VAL A   684                                                      
REMARK 465     GLU A   685                                                      
REMARK 465     SER A   686                                                      
REMARK 465     LYS A   687                                                      
REMARK 465     LYS A   688                                                      
REMARK 465     LYS A   689                                                      
REMARK 465     ALA A   690                                                      
REMARK 465     VAL A   691                                                      
REMARK 465     GLN A   692                                                      
REMARK 465     ARG A   693                                                      
REMARK 465     LEU A   694                                                      
REMARK 465     GLU A   695                                                      
REMARK 465     GLU A   696                                                      
REMARK 465     GLN A   697                                                      
REMARK 465     LEU A   698                                                      
REMARK 465     MET A   699                                                      
REMARK 465     LYS A   700                                                      
REMARK 465     LEU A   701                                                      
REMARK 465     GLU A   702                                                      
REMARK 465     VAL A   703                                                      
REMARK 465     GLN A   704                                                      
REMARK 465     ALA A   705                                                      
REMARK 465     THR A   706                                                      
REMARK 465     ASP A   707                                                      
REMARK 465     ARG A   708                                                      
REMARK 465     GLU A   709                                                      
REMARK 465     GLU A   710                                                      
REMARK 465     ASN A   711                                                      
REMARK 465     LYS A   712                                                      
REMARK 465     GLN A   713                                                      
REMARK 465     ILE A   714                                                      
REMARK 465     ALA A   715                                                      
REMARK 465     LEU A   716                                                      
REMARK 465     GLY A   717                                                      
REMARK 465     THR A   718                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     UBB B  10    O3P                                                 
REMARK 470     ARG A 210    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     TYR A 211    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     TYR A 211    OH                                                  
REMARK 470     GLU A 213    CB   CG   CD   OE1  OE2                             
REMARK 470     ILE A 215    CB   CG1  CG2  CD1                                  
REMARK 470     LYS A 218    CB   CG   CD   CE   NZ                              
REMARK 470     GLU A 236    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS A 239    CB   CG   CD   CE   NZ                              
REMARK 470     ASP A 243    CB   CG   OD1  OD2                                  
REMARK 470     MET A 247    CB   CG   SD   CE                                   
REMARK 470     LYS A 248    CG   CD   CE   NZ                                   
REMARK 470     MET A 263    CG   SD   CE                                        
REMARK 470     GLU A 267    CB   CG   CD   OE1  OE2                             
REMARK 470     THR A 270    CB   OG1  CG2                                       
REMARK 470     LYS A 271    CB   CG   CD   CE   NZ                              
REMARK 470     GLU A 272    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS A 276    CG   CD   CE   NZ                                   
REMARK 470     LYS A 280    CB   CG   CD   CE   NZ                              
REMARK 470     ARG A 283    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     GLU A 285    CB   CG   CD   OE1  OE2                             
REMARK 470     ASN A 288    CB   CG   OD1  ND2                                  
REMARK 470     GLU A 289    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 291    CB   CG   CD   CE   NZ                              
REMARK 470     ASN A 292    CB   CG   OD1  ND2                                  
REMARK 470     ASN A 296    CB   CG   OD1  ND2                                  
REMARK 470     GLN A 304    CB   CG   CD   OE1  NE2                             
REMARK 470     GLN A 307    CB   CG   CD   OE1  NE2                             
REMARK 470     PHE A 309    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     GLN A 312    CB   CG   CD   OE1  NE2                             
REMARK 470     GLU A 314    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 316    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 317    CG   CD   CE   NZ                                   
REMARK 470     GLN A 318    CG   CD   OE1  NE2                                  
REMARK 470     MET A 319    CG   SD   CE                                        
REMARK 470     LYS A 321    CG   CD   CE   NZ                                   
REMARK 470     GLU A 322    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 323    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 324    CB   CG   CD   CE   NZ                              
REMARK 470     LYS A 326    CG   CD   CE   NZ                                   
REMARK 470     ILE A 327    CB   CG1  CG2  CD1                                  
REMARK 470     LYS A 328    CB   CG   CD   CE   NZ                              
REMARK 470     GLU A 329    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU A 330    CB   CG   CD   OE1  OE2                             
REMARK 470     ASN A 331    CB   CG   OD1  ND2                                  
REMARK 470     GLU A 332    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 333    CG   CD   CE   NZ                                   
REMARK 470     LEU A 335    CB   CG   CD1  CD2                                  
REMARK 470     GLU A 337    CB   CG   CD   OE1  OE2                             
REMARK 470     ILE A 342    CB   CG1  CG2  CD1                                  
REMARK 470     ASN A 345    CB   CG   OD1  ND2                                  
REMARK 470     HIS A 346    CB   CG   ND1  CD2  CE1  NE2                        
REMARK 470     GLU A 348    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 362    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ASN A 366    CB   CG   OD1  ND2                                  
REMARK 470     LYS A 388    CB   CG   CD   CE   NZ                              
REMARK 470     LYS A 452    CB   CG   CD   CE   NZ                              
REMARK 470     ASP A 455    CB   CG   OD1  OD2                                  
REMARK 470     GLN A 460    CB   CG   CD   OE1  NE2                             
REMARK 470     ARG A 462    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 463    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 466    CG   CD   CE   NZ                                   
REMARK 470     LYS A 468    CG   CD   CE   NZ                                   
REMARK 470     LYS A 471    CG   CD   CE   NZ                                   
REMARK 470     LYS A 484    CG   CD   CE   NZ                                   
REMARK 470     GLU A 492    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU A 494    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU A 495    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 497    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU A 517    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 522    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS A 532    O                                                   
REMARK 470     ASP A 533    CB   CG   OD1  OD2                                  
REMARK 470     ARG A 536    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ARG A 546    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 556    CB   CG   CD   OE1  OE2                             
REMARK 470     GLN A 559    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 561    CB   CG   CD   OE1  OE2                             
REMARK 470     ASP A 566    CG   OD1  OD2                                       
REMARK 470     ARG A 567    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ASP A 579    CB   CG   OD1  OD2                                  
REMARK 470     GLU A 582    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 600    CB   CG   CD   OE1  NE2                             
REMARK 470     LEU A 602    CB   CG   CD1  CD2                                  
REMARK 470     ASP A 609    CB   CG   OD1  OD2                                  
REMARK 470     GLU A 610    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 611    CG   OD1  ND2                                       
REMARK 470     ILE A 612    CB   CG1  CG2  CD1                                  
REMARK 470     LYS A 615    CB   CG   CD   CE   NZ                              
REMARK 470     LEU A 617    CB   CG   CD1  CD2                                  
REMARK 470     ARG A 621    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ASN A 623    CB   CG   OD1  ND2                                  
REMARK 470     ARG A 624    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LYS A 735    CG   CD   CE   NZ                                   
REMARK 470     GLU A 741    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 742    CG   CD   CE   NZ                                   
REMARK 470     LYS A 746    CB   CG   CD   CE   NZ                              
REMARK 470     THR A 747    CB   OG1  CG2                                       
REMARK 470     ARG A 749    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 750    CB   CG   CD   OE1  OE2                             
REMARK 470     PHE A 752    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     ASP A 760    CG   OD1  OD2                                       
REMARK 470     GLU A 761    CB   CG   CD   OE1  OE2                             
REMARK 470     ASP A 762    CG   OD1  OD2                                       
REMARK 470     GLU A 764    CG   CD   OE1  OE2                                  
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    MET A 555   CA  -  C   -  O   ANGL. DEV. = -14.2 DEGREES          
REMARK 500    GLU A 556   CA  -  C   -  O   ANGL. DEV. = -14.9 DEGREES          
REMARK 500    MET A 555   O   -  C   -  N   ANGL. DEV. = -23.8 DEGREES          
REMARK 500    GLU A 556   C   -  N   -  CA  ANGL. DEV. =  36.8 DEGREES          
REMARK 500    ASN A 557   N   -  CA  -  CB  ANGL. DEV. = -45.0 DEGREES          
REMARK 500    ASN A 557   N   -  CA  -  C   ANGL. DEV. = -16.9 DEGREES          
REMARK 500    GLU A 556   CA  -  C   -  N   ANGL. DEV. =  42.8 DEGREES          
REMARK 500    GLU A 556   O   -  C   -  N   ANGL. DEV. = -39.5 DEGREES          
REMARK 500    ASN A 557   C   -  N   -  CA  ANGL. DEV. =  16.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A 212      175.30    -58.83                                   
REMARK 500    PRO A 230      116.52    -27.32                                   
REMARK 500    TYR A 231      119.12    -27.57                                   
REMARK 500    LYS A 239     -164.98   -123.55                                   
REMARK 500    PHE A 240       96.23    179.79                                   
REMARK 500    ASP A 243       49.33     32.44                                   
REMARK 500    PRO A 251       -9.49    -50.50                                   
REMARK 500    MET A 263       64.33   -151.59                                   
REMARK 500    ASP A 265       45.92    -91.07                                   
REMARK 500    GLU A 267       -6.00    -58.37                                   
REMARK 500    GLU A 285       22.92    -79.42                                   
REMARK 500    SER A 320      171.79    -59.78                                   
REMARK 500    LYS A 321       34.18    -78.65                                   
REMARK 500    GLU A 322      -30.88   -156.71                                   
REMARK 500    MET A 343     -158.75   -154.83                                   
REMARK 500    ASP A 344      -74.37    -52.35                                   
REMARK 500    ASN A 345     -100.45    -78.52                                   
REMARK 500    PRO A 368       -9.29    -57.92                                   
REMARK 500    ARG A 375      160.57    -47.97                                   
REMARK 500    PRO A 397       98.06    -16.98                                   
REMARK 500    HIS A 406       50.45   -108.11                                   
REMARK 500    ILE A 420      -71.56    -73.70                                   
REMARK 500    PRO A 431       -3.92    -58.37                                   
REMARK 500    LYS A 451      -49.02    -26.78                                   
REMARK 500    LYS A 466       37.44    -98.15                                   
REMARK 500    MET A 470      -83.00    -43.10                                   
REMARK 500    LYS A 484      -72.29    -70.92                                   
REMARK 500    TYR A 523       76.00     56.26                                   
REMARK 500    MET A 555       17.46    -66.34                                   
REMARK 500    ARG A 567       70.36   -103.62                                   
REMARK 500    LEU A 568      135.27   -171.53                                   
REMARK 500    ASP A 609       37.07    -86.17                                   
REMARK 500    ASN A 611     -152.00   -106.87                                   
REMARK 500    ILE A 612      -99.35    -59.27                                   
REMARK 500    PRO A 613        0.47    -62.99                                   
REMARK 500    ILE A 743      -65.92    -94.12                                   
REMARK 500    ASN A 745     -168.52    -73.07                                   
REMARK 500    ASP A 760     -163.36   -104.55                                   
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 GLU A  556     ASN A  557                  -81.25                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500     DC B   8         0.07    SIDE_CHAIN                              
REMARK 500     DU C  18         0.07    SIDE_CHAIN                              
REMARK 500     DG D 115         0.06    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    MET A 555        -41.09                                           
REMARK 500    GLU A 556         55.55                                           
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 A  22        DISTANCE =  8.10 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1A31   RELATED DB: PDB                                   
REMARK 900 HUMAN RECONSTITUTED TOPOISOMERASE I IN COVALENT COMPLEX              
REMARK 900 WITH 22 BASE PAIR DNA OLIGONUCLEOTIDE                                
REMARK 900 RELATED ID: 1EJ9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TOPOISOMERASE I DNA COMPLEX               
REMARK 900 RELATED ID: 1LPQ   RELATED DB: PDB                                   
REMARK 900 HUMAN TOPOISOMERASE I IN NONCOVALENT COMPLEX WITH A 22 BASE          
REMARK 900 PAIR DNA DUPLEX CONTAINING AN 8-OXO-G LESION                         
REMARK 900 RELATED ID: 1K4T   RELATED DB: PDB                                   
REMARK 900 HUMAN DNA TOPOISOMERASE I (70 KDA) IN COMPLEX WITH THE               
REMARK 900 POISON TOPOTECAN AND COVALENT COMPLEX WITH A 22 BASE PAIR            
REMARK 900 DNA DUPLEX                                                           
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE DNA (DUPLEX OLIGO) WAS ADDED TO THE                              
REMARK 999 PROTEIN DURING CRYSTALLIZATION.  AT THIS                             
REMARK 999 TIME, THE PROTEIN INITIATES A TRANSESTERIFICATION                    
REMARK 999 REACTION IN WHICH ONE STRAND OF DNA IS BROKEN INTO                   
REMARK 999 CHAINS B AND C, AND THE PROTEIN CHAIN A IS COVALENTLY                
REMARK 999 LINKED TO THE DNA THROUGH RESIDUE 723.                               
DBREF  1NH3 A  203   765  UNP    P11387   TOP1_HUMAN     203    764             
DBREF  1NH3 B    1    10  PDB    1NH3     1NH3             1     10             
DBREF  1NH3 C   11    22  PDB    1NH3     1NH3            11     22             
DBREF  1NH3 D  101   122  PDB    1NH3     1NH3           101    122             
SEQADV 1NH3 MET A  699  UNP  P11387              INITIATING MET                 
SEQADV 1NH3 PTR A  723  UNP  P11387    TYR   722 MODIFIED RESIDUE               
SEQRES   1 B   10   DA  DA  DA  DA  DA  DG  DA  DC  DU UBB                      
SEQRES   1 C   12  GNG  DG  DA  DA  DA  DA  DA  DU  DU  DU  DU  DT              
SEQRES   1 D   22   DA  DA  DA  DA  DA  DT  DU  DU  DU  DU  DC CAR  DA          
SEQRES   2 D   22   DA  DG  DU  DC  DU  DU  DU  DU  DT                          
SEQRES   1 A  563  TRP LYS TRP TRP GLU GLU GLU ARG TYR PRO GLU GLY ILE          
SEQRES   2 A  563  LYS TRP LYS PHE LEU GLU HIS LYS GLY PRO VAL PHE ALA          
SEQRES   3 A  563  PRO PRO TYR GLU PRO LEU PRO GLU ASN VAL LYS PHE TYR          
SEQRES   4 A  563  TYR ASP GLY LYS VAL MET LYS LEU SER PRO LYS ALA GLU          
SEQRES   5 A  563  GLU VAL ALA THR PHE PHE ALA LYS MET LEU ASP HIS GLU          
SEQRES   6 A  563  TYR THR THR LYS GLU ILE PHE ARG LYS ASN PHE PHE LYS          
SEQRES   7 A  563  ASP TRP ARG LYS GLU MET THR ASN GLU GLU LYS ASN ILE          
SEQRES   8 A  563  ILE THR ASN LEU SER LYS CYS ASP PHE THR GLN MET SER          
SEQRES   9 A  563  GLN TYR PHE LYS ALA GLN THR GLU ALA ARG LYS GLN MET          
SEQRES  10 A  563  SER LYS GLU GLU LYS LEU LYS ILE LYS GLU GLU ASN GLU          
SEQRES  11 A  563  LYS LEU LEU LYS GLU TYR GLY PHE CYS ILE MET ASP ASN          
SEQRES  12 A  563  HIS LYS GLU ARG ILE ALA ASN PHE LYS ILE GLU PRO PRO          
SEQRES  13 A  563  GLY LEU PHE ARG GLY ARG GLY ASN HIS PRO LYS MET GLY          
SEQRES  14 A  563  MET LEU LYS ARG ARG ILE MET PRO GLU ASP ILE ILE ILE          
SEQRES  15 A  563  ASN CYS SER LYS ASP ALA LYS VAL PRO SER PRO PRO PRO          
SEQRES  16 A  563  GLY HIS LYS TRP LYS GLU VAL ARG HIS ASP ASN LYS VAL          
SEQRES  17 A  563  THR TRP LEU VAL SER TRP THR GLU ASN ILE GLN GLY SER          
SEQRES  18 A  563  ILE LYS TYR ILE MET LEU ASN PRO SER SER ARG ILE LYS          
SEQRES  19 A  563  GLY GLU LYS ASP TRP GLN LYS TYR GLU THR ALA ARG ARG          
SEQRES  20 A  563  LEU LYS LYS CYS VAL ASP LYS ILE ARG ASN GLN TYR ARG          
SEQRES  21 A  563  GLU ASP TRP LYS SER LYS GLU MET LYS VAL ARG GLN ARG          
SEQRES  22 A  563  ALA VAL ALA LEU TYR PHE ILE ASP LYS LEU ALA LEU ARG          
SEQRES  23 A  563  ALA GLY ASN GLU LYS GLU GLU GLY GLU THR ALA ASP THR          
SEQRES  24 A  563  VAL GLY CYS CYS SER LEU ARG VAL GLU HIS ILE ASN LEU          
SEQRES  25 A  563  HIS PRO GLU LEU ASP GLY GLN GLU TYR VAL VAL GLU PHE          
SEQRES  26 A  563  ASP PHE LEU GLY LYS ASP SER ILE ARG TYR TYR ASN LYS          
SEQRES  27 A  563  VAL PRO VAL GLU LYS ARG VAL PHE LYS ASN LEU GLN LEU          
SEQRES  28 A  563  PHE MET GLU ASN LYS GLN PRO GLU ASP ASP LEU PHE ASP          
SEQRES  29 A  563  ARG LEU ASN THR GLY ILE LEU ASN LYS HIS LEU GLN ASP          
SEQRES  30 A  563  LEU MET GLU GLY LEU THR ALA LYS VAL PHE ARG THR TYR          
SEQRES  31 A  563  ASN ALA SER ILE THR LEU GLN GLN GLN LEU LYS GLU LEU          
SEQRES  32 A  563  THR ALA PRO ASP GLU ASN ILE PRO ALA LYS ILE LEU SER          
SEQRES  33 A  563  TYR ASN ARG ALA ASN ARG ALA VAL ALA ILE LEU CYS ASN          
SEQRES  34 A  563  HIS GLN ARG ALA PRO PRO LYS THR PHE GLU LYS SER MET          
SEQRES  35 A  563  MET ASN LEU GLN THR LYS ILE ASP ALA LYS LYS GLU GLN          
SEQRES  36 A  563  LEU ALA ASP ALA ARG ARG ASP LEU LYS SER ALA LYS ALA          
SEQRES  37 A  563  ASP ALA LYS VAL MET LYS ASP ALA LYS THR LYS LYS VAL          
SEQRES  38 A  563  VAL GLU SER LYS LYS LYS ALA VAL GLN ARG LEU GLU GLU          
SEQRES  39 A  563  GLN LEU MET LYS LEU GLU VAL GLN ALA THR ASP ARG GLU          
SEQRES  40 A  563  GLU ASN LYS GLN ILE ALA LEU GLY THR SER LYS LEU ASN          
SEQRES  41 A  563  PTR LEU ASP PRO ARG ILE THR VAL ALA TRP CYS LYS LYS          
SEQRES  42 A  563  TRP GLY VAL PRO ILE GLU LYS ILE TYR ASN LYS THR GLN          
SEQRES  43 A  563  ARG GLU LYS PHE ALA TRP ALA ILE ASP MET ALA ASP GLU          
SEQRES  44 A  563  ASP TYR GLU PHE                                              
MODRES 1NH3 UBB B   10    U  2',3'-DIDEOXY-URIDINE-5'-MONOPHOSPHATE             
MODRES 1NH3 GNG C   11    G  2'-DEOXY-GUANOSINE                                 
MODRES 1NH3 CAR D  112   DC  CYTOSINE ARABINOSE-5'-PHOSPHATE                    
MODRES 1NH3 PTR A  723  TYR  O-PHOSPHOTYROSINE                                  
HET    UBB  B  10      18                                                       
HET    GNG  C  11      19                                                       
HET    CAR  D 112      20                                                       
HET    PTR  A 723      16                                                       
HETNAM     UBB 2',3'-DIDEOXY-URIDINE-5'-MONOPHOSPHATE                           
HETNAM     GNG 2'-DEOXY-GUANOSINE                                               
HETNAM     CAR CYTOSINE ARABINOSE-5'-PHOSPHATE                                  
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  UBB    C9 H13 N2 O7 P                                               
FORMUL   2  GNG    C10 H13 N5 O4                                                
FORMUL   3  CAR    C9 H14 N3 O8 P                                               
FORMUL   4  PTR    C9 H12 N O6 P                                                
FORMUL   5  HOH   *33(H2 O)                                                     
HELIX    1   1 LYS A  252  LYS A  262  1                                  11    
HELIX    2   2 LYS A  271  ASP A  281  1                                  11    
HELIX    3   3 GLU A  289  ILE A  294  1                                   6    
HELIX    4   4 ASN A  296  SER A  298  5                                   3    
HELIX    5   5 PHE A  302  ALA A  315  1                                  14    
HELIX    6   6 GLU A  322  ILE A  327  1                                   6    
HELIX    7   7 GLU A  332  TYR A  338  1                                   7    
HELIX    8   8 SER A  433  ARG A  449  1                                  17    
HELIX    9   9 CYS A  453  ASP A  464  1                                  12    
HELIX   10  10 TRP A  465  SER A  467  5                                   3    
HELIX   11  11 GLU A  469  LEU A  485  1                                  17    
HELIX   12  12 ARG A  508  GLU A  510  5                                   3    
HELIX   13  13 GLU A  544  GLU A  556  1                                  13    
HELIX   14  14 ASN A  569  MET A  581  1                                  13    
HELIX   15  15 LYS A  587  LEU A  605  1                                  19    
HELIX   16  16 LYS A  615  ASN A  623  1                                   9    
HELIX   17  17 ASP A  725  TRP A  736  1                                  12    
HELIX   18  18 PRO A  739  ILE A  743  5                                   5    
HELIX   19  19 THR A  747  PHE A  752  1                                   6    
HELIX   20  20 PHE A  752  ASP A  757  1                                   6    
SHEET    1   A 3 GLU A 221  HIS A 222  0                                        
SHEET    2   A 3 PHE A 340  ILE A 342 -1  O  ILE A 342   N  GLU A 221           
SHEET    3   A 3 GLU A 348  ARG A 349 -1  O  GLU A 348   N  CYS A 341           
SHEET    1   B 3 LYS A 245  VAL A 246  0                                        
SHEET    2   B 3 TYR A 241  TYR A 242 -1  N  TYR A 242   O  LYS A 245           
SHEET    3   B 3 CYS A 300  ASP A 301 -1  O  ASP A 301   N  TYR A 241           
SHEET    1   C 4 GLU A 403  ARG A 405  0                                        
SHEET    2   C 4 ILE A 383  ASN A 385  1  N  ILE A 384   O  ARG A 405           
SHEET    3   C 4 VAL A 414  THR A 417 -1  O  SER A 415   N  ILE A 383           
SHEET    4   C 4 ILE A 424  ILE A 427 -1  O  LYS A 425   N  TRP A 416           
SHEET    1   D 3 ILE A 512  LEU A 518  0                                        
SHEET    2   D 3 GLN A 521  LEU A 530 -1  O  GLN A 521   N  LEU A 518           
SHEET    3   D 3 ARG A 536  PRO A 542 -1  O  TYR A 537   N  PHE A 529           
LINK         O3P PTR A 723                 C3' UBB B  10     1555   1555  1.65  
LINK         O3' GNG C  11                 P    DG C  12     1555   1555  1.61  
LINK         O3'  DU B   9                 P   UBB B  10     1555   1555  1.61  
LINK         O3'  DC D 111                 P   CAR D 112     1555   1555  1.61  
LINK         O3' CAR D 112                 P    DA D 113     1555   1555  1.66  
LINK         C   ASN A 722                 N   PTR A 723     1555   1555  1.34  
LINK         C   PTR A 723                 N   LEU A 724     1555   1555  1.33  
CRYST1   72.970   72.970  186.290  90.00  90.00 120.00 P 32          3          
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      0.013704  0.007912  0.000000        0.00000                         
SCALE2      0.000000  0.015824  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005368        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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