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Database: PDB
Entry: 1LPQ
LinkDB: 1LPQ
Original site: 1LPQ 
HEADER    ISOMERASE/DNA                           08-MAY-02   1LPQ              
TITLE     HUMAN DNA TOPOISOMERASE I (70 KDA) IN NON-COVALENT COMPLEX            
TITLE    2 WITH A 22 BASE PAIR DNA DUPLEX CONTAINING AN 8-OXOG LESION           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-D(*AP*AP*AP*AP*AP*GP*AP*CP*TP*TP*(8OG)                  
COMPND   3 P*GP*AP*AP*AP*AP*AP*TP*TP*TP*TP*T)-3';                               
COMPND   4 CHAIN: B;                                                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: 5'-                                                        
COMPND   8 D(*AP*AP*AP*AP*AP*TP*TP*TP*TP*TP*CP*CP*AP*AP*GP*TP*CP*TP*TP          
COMPND   9 *TP*TP*T)-3';                                                        
COMPND  10 CHAIN: C;                                                            
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: DNA TOPOISOMERASE I;                                       
COMPND  14 CHAIN: A;                                                            
COMPND  15 EC: 5.99.1.2;                                                        
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MUTATION: 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 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606;                                                
SOURCE   9 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  10 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    PROTEIN-DNA COMPLEX, DNA DAMAGE, INDUCED CONFORMATIONAL               
KEYWDS   2 CHANGE, ISOMERASE/DNA COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.T.LESHER,Y.POMMIER,L.STEWART,M.R.REDINBO                            
REVDAT   3   24-FEB-09 1LPQ    1       VERSN                                    
REVDAT   2   25-SEP-02 1LPQ    1       JRNL                                     
REVDAT   1   16-AUG-02 1LPQ    0                                                
JRNL        AUTH   D.T.LESHER,Y.POMMIER,L.STEWART,M.R.REDINBO                   
JRNL        TITL   8-OXOGUANINE REARRANGES THE ACTIVE SITE OF HUMAN             
JRNL        TITL 2 TOPOISOMERASE I                                              
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  99 12102 2002              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   12209008                                                     
JRNL        DOI    10.1073/PNAS.192282699                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.14 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.14                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.87                          
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)   (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 16401                          
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) : 0.256                           
REMARK   3   FREE R VALUE                     : 0.298                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1132                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.14                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.34                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2380                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3600                       
REMARK   3   BIN FREE R VALUE                    : 0.3910                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 184                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.029                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4457                                    
REMARK   3   NUCLEIC ACID ATOMS       : 897                                     
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 27                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.68000                                             
REMARK   3    B22 (A**2) : 8.89000                                              
REMARK   3    B33 (A**2) : -4.21000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 13.32000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.43                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.41                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.54                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.55                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.02                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.260 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.260 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 10.600; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 12.710; 2.500                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1LPQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB016164.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
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) : 1.10                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRANDEIS                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17165                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.140                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.700                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : 0.33400                            
REMARK 200  R SYM                      (I) : 0.20000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.14                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.19                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.26500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS-HCL, MES, PEG 400, MAGNESIUM        
REMARK 280  CHLORIDE, DITHIOTHREITOL, PH 6.8, VAPOR DIFFUSION, HANGING          
REMARK 280  DROP, TEMPERATURE 295K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       61.25000            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, 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     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 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     GLU A 213    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 248    CG   CD   CE   NZ                                   
REMARK 470     LYS A 276    CG   CD   CE   NZ                                   
REMARK 470     GLU A 289    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 304    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 326    CG   CD   CE   NZ                                   
REMARK 470     GLU A 329    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 332    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 333    CG   CD   CE   NZ                                   
REMARK 470     ARG A 362    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 494    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 495    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 546    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 582    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 609    CG   OD1  OD2                                       
REMARK 470     GLU A 610    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 611    CG   OD1  ND2                                       
REMARK 470     GLN A 633    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 641    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 642    CG   CD   CE   NZ                                   
REMARK 470     SER A 643    OG                                                  
REMARK 470     MET A 645    CG   SD   CE                                        
REMARK 470     ASN A 646    CG   OD1  ND2                                       
REMARK 470     ASP A 660    CG   OD1  OD2                                       
REMARK 470     VAL A 674    CG1  CG2                                            
REMARK 470     GLU A 696    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 712    CG   CD   CE   NZ                                   
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     ASP A 760    CG   OD1  OD2                                       
REMARK 470     GLU A 764    CG   CD   OE1  OE2                                  
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    VAL A   414     O    TYR A   426              2.13            
REMARK 500   O    GLN A   460     OD1  ASP A   464              2.16            
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     DC C 112   C3' -  C2' -  C1' ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    VAL A 472   N   -  CA  -  C   ANGL. DEV. = -18.9 DEGREES          
REMARK 500    ASP A 664   N   -  CA  -  C   ANGL. DEV. = -21.0 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    PHE A 227      172.66    -52.22                                   
REMARK 500    PRO A 251      -71.60    -33.90                                   
REMARK 500    LYS A 262       -8.03    -58.77                                   
REMARK 500    ASN A 296      -24.26   -147.17                                   
REMARK 500    LEU A 297      -12.86     76.21                                   
REMARK 500    GLN A 318       77.36   -176.70                                   
REMARK 500    LYS A 324      -76.64    -58.54                                   
REMARK 500    LEU A 325      -14.76    -49.27                                   
REMARK 500    ASP A 344       85.47     41.14                                   
REMARK 500    ASN A 345       19.40     53.47                                   
REMARK 500    ASN A 366       45.90    -66.09                                   
REMARK 500    PRO A 379      -18.84    -45.50                                   
REMARK 500    ASN A 385      -81.19   -109.19                                   
REMARK 500    CYS A 386      172.13     40.82                                   
REMARK 500    PRO A 396      152.28    -44.07                                   
REMARK 500    PRO A 397      114.64    -38.15                                   
REMARK 500    GLU A 403      145.88   -171.13                                   
REMARK 500    SER A 415      138.58   -179.38                                   
REMARK 500    SER A 423     -165.79   -108.89                                   
REMARK 500    TYR A 426      -70.42   -119.80                                   
REMARK 500    ILE A 427      104.70     92.54                                   
REMARK 500    ARG A 434       11.52    -68.99                                   
REMARK 500    LYS A 452      -68.63    -96.30                                   
REMARK 500    CYS A 453       36.04    -81.16                                   
REMARK 500    GLN A 460      -82.86    -76.10                                   
REMARK 500    TYR A 461      -19.64    -48.56                                   
REMARK 500    GLU A 463       32.55    -85.54                                   
REMARK 500    LYS A 468      -32.51    -39.42                                   
REMARK 500    LYS A 471     -179.65    -57.53                                   
REMARK 500    VAL A 472     -149.65     57.31                                   
REMARK 500    ARG A 473       83.59      3.71                                   
REMARK 500    GLN A 474      -49.77    152.52                                   
REMARK 500    ALA A 486       59.47     36.71                                   
REMARK 500    ALA A 489      -75.25    -28.57                                   
REMARK 500    GLU A 494      107.13    -56.20                                   
REMARK 500    ASP A 519       43.04     24.61                                   
REMARK 500    TYR A 523       88.26     59.41                                   
REMARK 500    ASP A 533       -8.52     64.79                                   
REMARK 500    SER A 534       22.12     90.15                                   
REMARK 500    ASN A 539      107.12    176.28                                   
REMARK 500    PHE A 554       45.91    -76.98                                   
REMARK 500    ASN A 557       37.04     70.06                                   
REMARK 500    PHE A 565       54.58   -116.12                                   
REMARK 500    ARG A 567       31.56     77.99                                   
REMARK 500    ALA A 586      -56.81    -15.19                                   
REMARK 500    VAL A 588      -32.32    -38.77                                   
REMARK 500    GLN A 600      -82.88    -79.59                                   
REMARK 500    GLN A 601      -41.32    -23.97                                   
REMARK 500    LYS A 603       14.79    -64.42                                   
REMARK 500    LEU A 605       13.08   -148.26                                   
REMARK 500    PRO A 608        2.84    -65.18                                   
REMARK 500    ASP A 609      104.22    172.93                                   
REMARK 500    LYS A 615      -70.61    -74.72                                   
REMARK 500    ILE A 616      -11.17    -49.91                                   
REMARK 500    LEU A 617      -90.55    -66.76                                   
REMARK 500    TYR A 619      -72.98    -58.04                                   
REMARK 500    ASN A 620        4.09    -68.62                                   
REMARK 500    ASN A 623       -6.83    -49.79                                   
REMARK 500    LYS A 642       69.63   -103.73                                   
REMARK 500    THR A 649        1.26    -62.03                                   
REMARK 500    LYS A 650      -64.71   -121.72                                   
REMARK 500    ASP A 660      -74.19    -61.63                                   
REMARK 500    ARG A 662      -77.30    -71.67                                   
REMARK 500    ASP A 664     -174.93     78.43                                   
REMARK 500    LEU A 665      -27.60     61.48                                   
REMARK 500    ALA A 670      -36.59    -36.31                                   
REMARK 500    ASP A 671      -73.36    -86.37                                   
REMARK 500    ALA A 672       22.49    -68.74                                   
REMARK 500    LYS A 673     -107.48    -69.51                                   
REMARK 500    ASP A 677     -102.88   -130.37                                   
REMARK 500    ALA A 678      -25.85   -172.37                                   
REMARK 500    LYS A 681       13.34    -63.30                                   
REMARK 500    GLN A 697        2.80    -53.23                                   
REMARK 500    LEU A 701       -5.60   -150.33                                   
REMARK 500    GLN A 704      -17.99    -44.21                                   
REMARK 500    ASP A 707      -77.47    -75.35                                   
REMARK 500    ASN A 711       32.67   -156.11                                   
REMARK 500    LYS A 712      -91.72    -77.19                                   
REMARK 500    LYS A 720       35.82    -68.25                                   
REMARK 500    LEU A 721      -70.51   -152.21                                   
REMARK 500    ASN A 722     -157.28    -87.38                                   
REMARK 500    PHE A 723       -6.15     23.10                                   
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 C 112         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1A31   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1A35   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1A36   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1EJ9   RELATED DB: PDB                                   
DBREF  1LPQ A  202   765  UNP    P11387   TOP1_HUMAN     202    765             
DBREF  1LPQ B    1    22  PDB    1LPQ     1LPQ             1     22             
DBREF  1LPQ C  101   122  PDB    1LPQ     1LPQ           101    122             
SEQADV 1LPQ PHE A  723  UNP  P11387    TYR   723 ENGINEERED                     
SEQRES   1 B   22   DA  DA  DA  DA  DA  DG  DA  DC  DT  DT 8OG  DG  DA          
SEQRES   2 B   22   DA  DA  DA  DA  DT  DT  DT  DT  DT                          
SEQRES   1 C   22   DA  DA  DA  DA  DA  DT  DT  DT  DT  DT  DC  DC  DA          
SEQRES   2 C   22   DA  DG  DT  DC  DT  DT  DT  DT  DT                          
SEQRES   1 A  564  LYS TRP LYS TRP TRP GLU GLU GLU ARG TYR PRO GLU GLY          
SEQRES   2 A  564  ILE LYS TRP LYS PHE LEU GLU HIS LYS GLY PRO VAL PHE          
SEQRES   3 A  564  ALA PRO PRO TYR GLU PRO LEU PRO GLU ASN VAL LYS PHE          
SEQRES   4 A  564  TYR TYR ASP GLY LYS VAL MET LYS LEU SER PRO LYS ALA          
SEQRES   5 A  564  GLU GLU VAL ALA THR PHE PHE ALA LYS MET LEU ASP HIS          
SEQRES   6 A  564  GLU TYR THR THR LYS GLU ILE PHE ARG LYS ASN PHE PHE          
SEQRES   7 A  564  LYS ASP TRP ARG LYS GLU MET THR ASN GLU GLU LYS ASN          
SEQRES   8 A  564  ILE ILE THR ASN LEU SER LYS CYS ASP PHE THR GLN MET          
SEQRES   9 A  564  SER GLN TYR PHE LYS ALA GLN THR GLU ALA ARG LYS GLN          
SEQRES  10 A  564  MET SER LYS GLU GLU LYS LEU LYS ILE LYS GLU GLU ASN          
SEQRES  11 A  564  GLU LYS LEU LEU LYS GLU TYR GLY PHE CYS ILE MET ASP          
SEQRES  12 A  564  ASN HIS LYS GLU ARG ILE ALA ASN PHE LYS ILE GLU PRO          
SEQRES  13 A  564  PRO GLY LEU PHE ARG GLY ARG GLY ASN HIS PRO LYS MET          
SEQRES  14 A  564  GLY MET LEU LYS ARG ARG ILE MET PRO GLU ASP ILE ILE          
SEQRES  15 A  564  ILE ASN CYS SER LYS ASP ALA LYS VAL PRO SER PRO PRO          
SEQRES  16 A  564  PRO GLY HIS LYS TRP LYS GLU VAL ARG HIS ASP ASN LYS          
SEQRES  17 A  564  VAL THR TRP LEU VAL SER TRP THR GLU ASN ILE GLN GLY          
SEQRES  18 A  564  SER ILE LYS TYR ILE MET LEU ASN PRO SER SER ARG ILE          
SEQRES  19 A  564  LYS GLY GLU LYS ASP TRP GLN LYS TYR GLU THR ALA ARG          
SEQRES  20 A  564  ARG LEU LYS LYS CYS VAL ASP LYS ILE ARG ASN GLN TYR          
SEQRES  21 A  564  ARG GLU ASP TRP LYS SER LYS GLU MET LYS VAL ARG GLN          
SEQRES  22 A  564  ARG ALA VAL ALA LEU TYR PHE ILE ASP LYS LEU ALA LEU          
SEQRES  23 A  564  ARG ALA GLY ASN GLU LYS GLU GLU GLY GLU THR ALA ASP          
SEQRES  24 A  564  THR VAL GLY CYS CYS SER LEU ARG VAL GLU HIS ILE ASN          
SEQRES  25 A  564  LEU HIS PRO GLU LEU ASP GLY GLN GLU TYR VAL VAL GLU          
SEQRES  26 A  564  PHE ASP PHE LEU GLY LYS ASP SER ILE ARG TYR TYR ASN          
SEQRES  27 A  564  LYS VAL PRO VAL GLU LYS ARG VAL PHE LYS ASN LEU GLN          
SEQRES  28 A  564  LEU PHE MET GLU ASN LYS GLN PRO GLU ASP ASP LEU PHE          
SEQRES  29 A  564  ASP ARG LEU ASN THR GLY ILE LEU ASN LYS HIS LEU GLN          
SEQRES  30 A  564  ASP LEU MET GLU GLY LEU THR ALA LYS VAL PHE ARG THR          
SEQRES  31 A  564  TYR ASN ALA SER ILE THR LEU GLN GLN GLN LEU LYS GLU          
SEQRES  32 A  564  LEU THR ALA PRO ASP GLU ASN ILE PRO ALA LYS ILE LEU          
SEQRES  33 A  564  SER TYR ASN ARG ALA ASN ARG ALA VAL ALA ILE LEU CYS          
SEQRES  34 A  564  ASN HIS GLN ARG ALA PRO PRO LYS THR PHE GLU LYS SER          
SEQRES  35 A  564  MET MET ASN LEU GLN THR LYS ILE ASP ALA LYS LYS GLU          
SEQRES  36 A  564  GLN LEU ALA ASP ALA ARG ARG ASP LEU LYS SER ALA LYS          
SEQRES  37 A  564  ALA ASP ALA LYS VAL MET LYS ASP ALA LYS THR LYS LYS          
SEQRES  38 A  564  VAL VAL GLU SER LYS LYS LYS ALA VAL GLN ARG LEU GLU          
SEQRES  39 A  564  GLU GLN LEU MET LYS LEU GLU VAL GLN ALA THR ASP ARG          
SEQRES  40 A  564  GLU GLU ASN LYS GLN ILE ALA LEU GLY THR SER LYS LEU          
SEQRES  41 A  564  ASN PHE LEU ASP PRO ARG ILE THR VAL ALA TRP CYS LYS          
SEQRES  42 A  564  LYS TRP GLY VAL PRO ILE GLU LYS ILE TYR ASN LYS THR          
SEQRES  43 A  564  GLN ARG GLU LYS PHE ALA TRP ALA ILE ASP MET ALA ASP          
SEQRES  44 A  564  GLU ASP TYR GLU PHE                                          
MODRES 1LPQ 8OG B   11   DG                                                     
HET    8OG  B  11      23                                                       
HETNAM     8OG 8-OXO-2'-DEOXY-GUANOSINE-5'-MONOPHOSPHATE                        
HETSYN     8OG 8-OXO-7,8-DIHYDRO-2'-DEOXY-GUANOSINE-5'-MONOPHOSPHATE            
FORMUL   1  8OG    C10 H14 N5 O8 P                                              
FORMUL   4  HOH   *27(H2 O)                                                     
HELIX    1   1 LYS A  204  GLU A  208  5                                   5    
HELIX    2   2 SER A  250  LYS A  262  1                                  13    
HELIX    3   3 HIS A  266  THR A  270  5                                   5    
HELIX    4   4 LYS A  271  GLU A  285  1                                  15    
HELIX    5   5 THR A  287  ASN A  292  1                                   6    
HELIX    6   6 PHE A  302  LYS A  317  1                                  16    
HELIX    7   7 SER A  320  TYR A  338  1                                  19    
HELIX    8   8 LYS A  436  LYS A  451  1                                  16    
HELIX    9   9 VAL A  454  GLU A  463  1                                  10    
HELIX   10  10 GLN A  474  LEU A  485  1                                  12    
HELIX   11  11 ARG A  508  GLU A  510  5                                   3    
HELIX   12  12 LYS A  532  SER A  534  5                                   3    
HELIX   13  13 GLU A  544  PHE A  554  1                                  11    
HELIX   14  14 ASN A  569  MET A  581  1                                  13    
HELIX   15  15 THR A  585  THR A  606  1                                  22    
HELIX   16  16 ASN A  611  ASN A  623  1                                  13    
HELIX   17  17 ARG A  624  ILE A  628  5                                   5    
HELIX   18  18 LEU A  647  ARG A  663  1                                  17    
HELIX   19  19 LYS A  666  LYS A  673  1                                   8    
HELIX   20  20 LYS A  679  LYS A  682  5                                   4    
HELIX   21  21 VAL A  683  LYS A  688  1                                   6    
HELIX   22  22 LYS A  688  LYS A  700  1                                  13    
HELIX   23  23 LEU A  701  ARG A  708  1                                   8    
HELIX   24  24 ASP A  725  TRP A  736  1                                  12    
HELIX   25  25 PRO A  739  TYR A  744  1                                   6    
HELIX   26  26 ASN A  745  PHE A  752  1                                   8    
HELIX   27  27 PHE A  752  MET A  758  1                                   7    
SHEET    1   A 3 LEU A 220  GLU A 221  0                                        
SHEET    2   A 3 PHE A 340  MET A 343 -1  O  ILE A 342   N  GLU A 221           
SHEET    3   A 3 HIS A 346  ARG A 349 -1  O  GLU A 348   N  CYS A 341           
SHEET    1   B 3 LYS A 245  MET A 247  0                                        
SHEET    2   B 3 PHE A 240  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 2 GLY A 359  LEU A 360  0                                        
SHEET    2   C 2 LEU A 373  LYS A 374 -1  O  LYS A 374   N  GLY A 359           
SHEET    1   D 2 ILE A 383  ILE A 384  0                                        
SHEET    2   D 2 GLU A 403  VAL A 404  1  O  GLU A 403   N  ILE A 384           
SHEET    1   E 2 TRP A 416  THR A 417  0                                        
SHEET    2   E 2 ILE A 424  LYS A 425 -1  O  LYS A 425   N  TRP A 416           
SHEET    1   F 3 ILE A 512  GLU A 517  0                                        
SHEET    2   F 3 GLU A 522  LEU A 530 -1  O  VAL A 524   N  HIS A 515           
SHEET    3   F 3 ARG A 536  PRO A 542 -1  O  TYR A 537   N  PHE A 529           
LINK         O3'  DT B  10                 P   8OG B  11     1555   1555  1.59  
LINK         O3' 8OG B  11                 P    DG B  12     1555   1555  1.60  
CRYST1   57.200  122.500   72.000  90.00  97.40  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      0.017483  0.000000  0.002271        0.00000                         
SCALE2      0.000000  0.008163  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014006        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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