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Database: PDB
Entry: 1TL8
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HEADER    ISOMERASE/DNA                           09-JUN-04   1TL8              
TITLE     HUMAN DNA TOPOISOMERASE I (70 KDA) IN COMPLEX WITH THE                
TITLE    2 INDENOISOQUINOLINE AI-III-52 AND COVALENT COMPLEX WITH A             
TITLE    3 22 BASE PAIR DNA DUPLEX                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-D(*AP*AP*AP*AP*AP*GP*AP*CP*TP*T)-3';                    
COMPND   3 CHAIN: B;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: 5'-D(*(TPC)P*GP*AP*AP*AP*AP*AP*TP*TP*TP*TP*T)-3';          
COMPND   7 CHAIN: C;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: 5'-                                                        
COMPND  11 D(*AP*AP*AP*AP*AP*TP*TP*TP*TP*TP*CP*GP*AP*AP*GP*TP*CP*TP*TP          
COMPND  12 *TP*TP*T)-3';                                                        
COMPND  13 CHAIN: D;                                                            
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: DNA TOPOISOMERASE I;                                       
COMPND  17 CHAIN: A;                                                            
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_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    COMPLEX (ISOMERASE/DNA), DNA, TOPOISOMERASE I, DRUG, POISON,          
KEYWDS   2 IDENOISOQUINOLINE                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.IOANOVICIU,S.ANTONY,Y.POMMIER,B.L.STAKER,L.STEWART,                 
AUTHOR   2 M.CUSHMAN                                                            
REVDAT   3   24-FEB-09 1TL8    1       VERSN                                    
REVDAT   2   26-JUL-05 1TL8    1       JRNL                                     
REVDAT   1   21-JUN-05 1TL8    0                                                
JRNL        AUTH   A.IOANOVICIU,S.ANTONY,Y.POMMIER,B.L.STAKER,                  
JRNL        AUTH 2 L.STEWART,M.CUSHMAN                                          
JRNL        TITL   SYNTHESIS AND MECHANISM OF ACTION STUDIES OF A               
JRNL        TITL 2 SERIES OF NORINDENOISOQUINOLINE TOPOISOMERASE I              
JRNL        TITL 3 POISONS REVEAL AN INHIBITOR WITH A FLIPPED                   
JRNL        TITL 4 ORIENTATION IN THE TERNARY DNA-ENZYME-INHIBITOR              
JRNL        TITL 5 COMPLEX AS DETERMINED BY X-RAY CRYSTALLOGRAPHIC              
JRNL        TITL 6 ANALYSIS                                                     
JRNL        REF    J.MED.CHEM.                   V.  48  4803 2005              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   16033260                                                     
JRNL        DOI    10.1021/JM050076B                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX 2002                                             
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN,ACCELRYS                   
REMARK   3               : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,            
REMARK   3               : YIP,DZAKULA)                                         
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 947731.540                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 16687                          
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 + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.305                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 808                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.011                           
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : NULL                 
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) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.29                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2549                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3320                       
REMARK   3   BIN FREE R VALUE                    : 0.3950                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 106                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.038                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4703                                    
REMARK   3   NUCLEIC ACID ATOMS       : 892                                     
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 60.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 60.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -19.82000                                            
REMARK   3    B22 (A**2) : -9.32000                                             
REMARK   3    B33 (A**2) : 29.14000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 13.09000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.37                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.47                            
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) : 0.52                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.64                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.017                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.90                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 3.94                            
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) : 2.670 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 4.550 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.700 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.730 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.27                                                 
REMARK   3   BSOL        : 15.33                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN.PARAM                                  
REMARK   3  PARAMETER FILE  2  : DNA-RNA.PARAM                                  
REMARK   3  PARAMETER FILE  3  : WATER_REP.PAR                                  
REMARK   3  PARAMETER FILE  4  : ION.PAR                                        
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER_REP.TOP                                  
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1TL8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUL-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB022744.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-DEC-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.40                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.3                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
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   : 16738                              
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     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.7000                            
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     (%) : 93.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.52200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, MES, AMMONIUM SULFATE, PH      
REMARK 280  6.40, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K               
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       57.07050            
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: 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     LYS A   174                                                      
REMARK 465     LYS A   175                                                      
REMARK 465     PRO A   176                                                      
REMARK 465     LYS A   177                                                      
REMARK 465     ASN A   178                                                      
REMARK 465     LYS A   179                                                      
REMARK 465     ASP A   180                                                      
REMARK 465     LYS A   181                                                      
REMARK 465     ASP A   182                                                      
REMARK 465     LYS A   183                                                      
REMARK 465     LYS A   184                                                      
REMARK 465     VAL A   185                                                      
REMARK 465     PRO A   186                                                      
REMARK 465     GLU A   187                                                      
REMARK 465     PRO A   188                                                      
REMARK 465     ASP A   189                                                      
REMARK 465     ASN A   190                                                      
REMARK 465     LYS A   191                                                      
REMARK 465     LYS A   192                                                      
REMARK 465     LYS A   193                                                      
REMARK 465     LYS A   194                                                      
REMARK 465     PRO A   195                                                      
REMARK 465     LYS A   196                                                      
REMARK 465     LYS A   197                                                      
REMARK 465     GLU A   198                                                      
REMARK 465     GLU A   199                                                      
REMARK 465     GLU A   200                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500     DA D 114   C5     DA D 114   C6     -0.069                       
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     DG D 112   C3' -  C2' -  C1' ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    LEU A 617   CA  -  CB  -  CG  ANGL. DEV. =  16.4 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    LYS A 202       62.24     83.18                                   
REMARK 500    PRO A 212       88.31    -56.59                                   
REMARK 500    GLU A 213      121.77      4.74                                   
REMARK 500    LYS A 223       12.96    -64.58                                   
REMARK 500    PRO A 233      170.25    -47.98                                   
REMARK 500    GLU A 236      -51.85     -8.10                                   
REMARK 500    VAL A 238       79.93   -109.91                                   
REMARK 500    THR A 269        4.40    -66.62                                   
REMARK 500    THR A 287     -169.48    -76.95                                   
REMARK 500    ALA A 315       42.82    -95.01                                   
REMARK 500    ARG A 316      -43.23   -131.36                                   
REMARK 500    LYS A 321      -10.96    -49.97                                   
REMARK 500    ASP A 344       76.47     51.54                                   
REMARK 500    ASN A 345       -3.38     76.06                                   
REMARK 500    ALA A 351      -77.36    -52.22                                   
REMARK 500    ARG A 362      -46.28   -133.81                                   
REMARK 500    ASN A 366       49.53    -79.63                                   
REMARK 500    GLU A 403      149.88   -170.68                                   
REMARK 500    ASP A 407       93.53    -51.74                                   
REMARK 500    ARG A 458        1.72    -69.91                                   
REMARK 500    SER A 467      133.60     -1.46                                   
REMARK 500    TYR A 523       69.00     66.11                                   
REMARK 500    SER A 534       15.75     59.51                                   
REMARK 500    GLU A 556      121.65    -38.65                                   
REMARK 500    PRO A 637      122.49    -36.21                                   
REMARK 500    LYS A 638       91.00    -37.23                                   
REMARK 500    GLU A 641       31.96    -96.44                                   
REMARK 500    MET A 675      101.81     86.13                                   
REMARK 500    THR A 680      -58.67   -158.04                                   
REMARK 500    ASN A 711       40.41   -103.76                                   
REMARK 500    ASN A 745     -170.35    -69.46                                   
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     DT B  10         0.06    SIDE_CHAIN                              
REMARK 500     DA D 102         0.06    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AI3 D 901                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
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                                                           
DBREF  1TL8 A  174   765  UNP    P11387   TOP1_HUMAN     174    765             
DBREF  1TL8 B    1    10  PDB    1TL8     1TL8             1     10             
DBREF  1TL8 C   11    22  PDB    1TL8     1TL8            11     22             
DBREF  1TL8 D  101   122  PDB    1TL8     1TL8           101    122             
SEQADV 1TL8 PTR A  723  UNP  P11387    TYR   723 MODIFIED RESIDUE               
SEQRES   1 B   10   DA  DA  DA  DA  DA  DG  DA  DC  DT  DT                      
SEQRES   1 C   12  TPC  DG  DA  DA  DA  DA  DA  DT  DT  DT  DT  DT              
SEQRES   1 D   22   DA  DA  DA  DA  DA  DT  DT  DT  DT  DT  DC  DG  DA          
SEQRES   2 D   22   DA  DG  DT  DC  DT  DT  DT  DT  DT                          
SEQRES   1 A  592  LYS LYS PRO LYS ASN LYS ASP LYS ASP LYS LYS VAL PRO          
SEQRES   2 A  592  GLU PRO ASP ASN LYS LYS LYS LYS PRO LYS LYS GLU GLU          
SEQRES   3 A  592  GLU GLN LYS TRP LYS TRP TRP GLU GLU GLU ARG TYR PRO          
SEQRES   4 A  592  GLU GLY ILE LYS TRP LYS PHE LEU GLU HIS LYS GLY PRO          
SEQRES   5 A  592  VAL PHE ALA PRO PRO TYR GLU PRO LEU PRO GLU ASN VAL          
SEQRES   6 A  592  LYS PHE TYR TYR ASP GLY LYS VAL MET LYS LEU SER PRO          
SEQRES   7 A  592  LYS ALA GLU GLU VAL ALA THR PHE PHE ALA LYS MET LEU          
SEQRES   8 A  592  ASP HIS GLU TYR THR THR LYS GLU ILE PHE ARG LYS ASN          
SEQRES   9 A  592  PHE PHE LYS ASP TRP ARG LYS GLU MET THR ASN GLU GLU          
SEQRES  10 A  592  LYS ASN ILE ILE THR ASN LEU SER LYS CYS ASP PHE THR          
SEQRES  11 A  592  GLN MET SER GLN TYR PHE LYS ALA GLN THR GLU ALA ARG          
SEQRES  12 A  592  LYS GLN MET SER LYS GLU GLU LYS LEU LYS ILE LYS GLU          
SEQRES  13 A  592  GLU ASN GLU LYS LEU LEU LYS GLU TYR GLY PHE CYS ILE          
SEQRES  14 A  592  MET ASP ASN HIS LYS GLU ARG ILE ALA ASN PHE LYS ILE          
SEQRES  15 A  592  GLU PRO PRO GLY LEU PHE ARG GLY ARG GLY ASN HIS PRO          
SEQRES  16 A  592  LYS MET GLY MET LEU LYS ARG ARG ILE MET PRO GLU ASP          
SEQRES  17 A  592  ILE ILE ILE ASN CYS SER LYS ASP ALA LYS VAL PRO SER          
SEQRES  18 A  592  PRO PRO PRO GLY HIS LYS TRP LYS GLU VAL ARG HIS ASP          
SEQRES  19 A  592  ASN LYS VAL THR TRP LEU VAL SER TRP THR GLU ASN ILE          
SEQRES  20 A  592  GLN GLY SER ILE LYS TYR ILE MET LEU ASN PRO SER SER          
SEQRES  21 A  592  ARG ILE LYS GLY GLU LYS ASP TRP GLN LYS TYR GLU THR          
SEQRES  22 A  592  ALA ARG ARG LEU LYS LYS CYS VAL ASP LYS ILE ARG ASN          
SEQRES  23 A  592  GLN TYR ARG GLU ASP TRP LYS SER LYS GLU MET LYS VAL          
SEQRES  24 A  592  ARG GLN ARG ALA VAL ALA LEU TYR PHE ILE ASP LYS LEU          
SEQRES  25 A  592  ALA LEU ARG ALA GLY ASN GLU LYS GLU GLU GLY GLU THR          
SEQRES  26 A  592  ALA ASP THR VAL GLY CYS CYS SER LEU ARG VAL GLU HIS          
SEQRES  27 A  592  ILE ASN LEU HIS PRO GLU LEU ASP GLY GLN GLU TYR VAL          
SEQRES  28 A  592  VAL GLU PHE ASP PHE LEU GLY LYS ASP SER ILE ARG TYR          
SEQRES  29 A  592  TYR ASN LYS VAL PRO VAL GLU LYS ARG VAL PHE LYS ASN          
SEQRES  30 A  592  LEU GLN LEU PHE MET GLU ASN LYS GLN PRO GLU ASP ASP          
SEQRES  31 A  592  LEU PHE ASP ARG LEU ASN THR GLY ILE LEU ASN LYS HIS          
SEQRES  32 A  592  LEU GLN ASP LEU MET GLU GLY LEU THR ALA LYS VAL PHE          
SEQRES  33 A  592  ARG THR TYR ASN ALA SER ILE THR LEU GLN GLN GLN LEU          
SEQRES  34 A  592  LYS GLU LEU THR ALA PRO ASP GLU ASN ILE PRO ALA LYS          
SEQRES  35 A  592  ILE LEU SER TYR ASN ARG ALA ASN ARG ALA VAL ALA ILE          
SEQRES  36 A  592  LEU CYS ASN HIS GLN ARG ALA PRO PRO LYS THR PHE GLU          
SEQRES  37 A  592  LYS SER MET MET ASN LEU GLN THR LYS ILE ASP ALA LYS          
SEQRES  38 A  592  LYS GLU GLN LEU ALA ASP ALA ARG ARG ASP LEU LYS SER          
SEQRES  39 A  592  ALA LYS ALA ASP ALA LYS VAL MET LYS ASP ALA LYS THR          
SEQRES  40 A  592  LYS LYS VAL VAL GLU SER LYS LYS LYS ALA VAL GLN ARG          
SEQRES  41 A  592  LEU GLU GLU GLN LEU MET LYS LEU GLU VAL GLN ALA THR          
SEQRES  42 A  592  ASP ARG GLU GLU ASN LYS GLN ILE ALA LEU GLY THR SER          
SEQRES  43 A  592  LYS LEU ASN PTR LEU ASP PRO ARG ILE THR VAL ALA TRP          
SEQRES  44 A  592  CYS LYS LYS TRP GLY VAL PRO ILE GLU LYS ILE TYR ASN          
SEQRES  45 A  592  LYS THR GLN ARG GLU LYS PHE ALA TRP ALA ILE ASP MET          
SEQRES  46 A  592  ALA ASP GLU ASP TYR GLU PHE                                  
MODRES 1TL8 TPC C   11   DC                                                     
MODRES 1TL8 PTR A  723  TYR  O-PHOSPHOTYROSINE                                  
HET    TPC  C  11      16                                                       
HET    PTR  A 723      16                                                       
HET    AI3  D 901      24                                                       
HETNAM     TPC 5'-THIO-2'-DEOXY-CYTOSINE PHOSPHONIC ACID                        
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     AI3 2,3-DIMETHOXY-12H-[1,3]DIOXOLO[5,6]INDENO[1,2-                   
HETNAM   2 AI3  C]ISOQUINOLIN-6-IUM                                             
HETSYN     PTR PHOSPHONOTYROSINE                                                
HETSYN     AI3 AI-III-52                                                        
FORMUL   2  TPC    C9 H14 N3 O6 P S                                             
FORMUL   4  PTR    C9 H12 N O6 P                                                
FORMUL   5  AI3    C19 H16 N O4 1+                                              
HELIX    1   1 SER A  250  LEU A  264  1                                  15    
HELIX    2   2 ASP A  265  THR A  270  5                                   6    
HELIX    3   3 LYS A  271  GLU A  285  1                                  15    
HELIX    4   4 THR A  287  ILE A  294  1                                   8    
HELIX    5   5 PHE A  302  ALA A  315  1                                  14    
HELIX    6   6 SER A  320  TYR A  338  1                                  19    
HELIX    7   7 MET A  378  GLU A  380  5                                   3    
HELIX    8   8 SER A  433  CYS A  453  1                                  21    
HELIX    9   9 CYS A  453  ASP A  464  1                                  12    
HELIX   10  10 GLU A  469  ALA A  486  1                                  18    
HELIX   11  11 ARG A  508  GLU A  510  5                                   3    
HELIX   12  12 GLY A  531  ILE A  535  5                                   5    
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  GLU A  604  1                                  18    
HELIX   16  16 ASN A  611  CYS A  630  1                                  20    
HELIX   17  17 LYS A  650  ASP A  664  1                                  15    
HELIX   18  18 ASP A  664  LYS A  669  1                                   6    
HELIX   19  19 LYS A  688  GLU A  710  1                                  23    
HELIX   20  20 LEU A  716  ASN A  722  1                                   7    
HELIX   21  21 ASP A  725  TRP A  736  1                                  12    
HELIX   22  22 PRO A  739  ILE A  743  5                                   5    
HELIX   23  23 ASN A  745  PHE A  752  1                                   8    
HELIX   24  24 PHE A  752  ALA A  759  1                                   8    
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 LYS A 347  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  PHE A 240   O  MET A 247           
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 382  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  ILE A 427   N  VAL A 414           
SHEET    1   D 3 ILE A 512  LEU A 518  0                                        
SHEET    2   D 3 GLN A 521  PHE A 527 -1  O  GLU A 526   N  ASN A 513           
SHEET    3   D 3 ASN A 539  PRO A 542 -1  O  ASN A 539   N  PHE A 527           
LINK         C3'  DT B  10                 O3P PTR A 723     1555   1555  1.43  
LINK         O3' TPC C  11                 P    DG C  12     1555   1555  1.62  
LINK         C   ASN A 722                 N   PTR A 723     1555   1555  1.32  
LINK         C   PTR A 723                 N   LEU A 724     1555   1555  1.34  
SITE     1 AC1  7 ARG A 364  THR A 718  ASN A 722   DT B  10                    
SITE     2 AC1  7 TPC C  11   DG D 112   DA D 113                               
CRYST1   56.949  114.141   73.499  90.00  94.18  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      0.017560  0.000000  0.001282        0.00000                         
SCALE2      0.000000  0.008761  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013642        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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