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Database: PDB
Entry: 1T8I
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Original site: 1T8I 
HEADER    ISOMERASE/DNA                           12-MAY-04   1T8I              
TITLE     HUMAN DNA TOPOISOMERASE I (70 KDA) IN COMPLEX WITH THE POISON         
TITLE    2 CAMPTOTHECIN AND COVALENT COMPLEX WITH A 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(*(TGP)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'-D(*AP*AP*AP*AP*AP*TP*TP*TP*TP*TP*CP*CP*AP*AP*GP*TP*CP*TP
COMPND  11 *TP*TP*TP*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 EC: 5.99.1.2;                                                        
COMPND  18 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 ISOMERASE-DNA COMPLEX                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.L.STAKER,M.D.FEESE,M.CUSHMAN,Y.POMMIER,D.ZEMBOWER,L.STEWART,        
AUTHOR   2 A.B.BURGIN                                                           
REVDAT   3   11-OCT-17 1T8I    1       REMARK                                   
REVDAT   2   24-FEB-09 1T8I    1       VERSN                                    
REVDAT   1   31-MAY-05 1T8I    0                                                
JRNL        AUTH   B.L.STAKER,M.D.FEESE,M.CUSHMAN,Y.POMMIER,D.ZEMBOWER,         
JRNL        AUTH 2 L.STEWART,A.B.BURGIN                                         
JRNL        TITL   STRUCTURES OF THREE CLASSES OF ANTICANCER AGENTS BOUND TO    
JRNL        TITL 2 THE HUMAN TOPOISOMERASE I-DNA COVALENT COMPLEX               
JRNL        REF    J.MED.CHEM.                   V.  48  2336 2005              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   15801827                                                     
JRNL        DOI    10.1021/JM049146P                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 16492                          
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) : 0.244                           
REMARK   3   R VALUE            (WORKING SET) : 0.241                           
REMARK   3   FREE R VALUE                     : 0.292                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 900                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1427                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 83                           
REMARK   3   BIN FREE R VALUE                    : 0.4490                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4687                                    
REMARK   3   NUCLEIC ACID ATOMS       : 892                                     
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 72.19                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.10000                                             
REMARK   3    B22 (A**2) : -3.25000                                             
REMARK   3    B33 (A**2) : 5.77000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 3.41000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.536         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.456         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.369        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.913                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.862                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5818 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8007 ; 1.859 ; 2.161       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   564 ; 3.449 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   996 ;22.299 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   800 ; 0.101 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4044 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3758 ; 0.329 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   445 ; 0.246 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    45 ; 0.234 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2830 ; 0.744 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4574 ; 1.410 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2988 ; 1.830 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3433 ; 3.426 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1T8I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAY-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000022444.                                   
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                             : 6.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 32-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16492                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08000                            
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) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 47.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.42700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
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: 1K4T                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, AMMONIUM SULFATE, MES, PH      
REMARK 280  6.4, 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       57.21150            
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 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     GLN A 201    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 202    CG   CD   CE   NZ                                   
REMARK 470     THR A 639    OG1  CG2                                            
REMARK 470     PHE A 640    CG   CD1  CD2  CE1  CE2  CZ                         
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    LEU A 335   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    PRO A 368   C   -  N   -  CA  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    LEU A 487   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES          
REMARK 500    LEU A 617   CA  -  CB  -  CG  ANGL. DEV. =  17.3 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    LYS A 202      107.51     66.44                                   
REMARK 500    GLU A 213      130.44    -38.46                                   
REMARK 500    ASP A 243       18.84     56.51                                   
REMARK 500    LYS A 321       26.06    -73.78                                   
REMARK 500    ASP A 344       96.96     28.26                                   
REMARK 500    ASN A 345        0.07     59.45                                   
REMARK 500    ARG A 362      -50.85   -122.76                                   
REMARK 500    PRO A 397      125.05    -34.61                                   
REMARK 500    CYS A 453       38.69   -146.40                                   
REMARK 500    ASP A 483      -84.50    -73.23                                   
REMARK 500    ALA A 486       41.04     38.78                                   
REMARK 500    ASP A 519       12.32     48.89                                   
REMARK 500    ASN A 557       29.18     46.93                                   
REMARK 500    ARG A 567       13.58     83.14                                   
REMARK 500    TYR A 592      -70.70    -61.85                                   
REMARK 500    LEU A 605      -43.82   -132.46                                   
REMARK 500    GLU A 610      137.86    -38.50                                   
REMARK 500    LYS A 638       73.30    -17.51                                   
REMARK 500    THR A 639       -3.49     58.80                                   
REMARK 500    GLU A 641       33.59    -84.02                                   
REMARK 500    MET A 675       68.59     72.73                                   
REMARK 500    ASP A 725      108.30    -57.34                                   
REMARK 500    PRO A 739      109.66    -56.59                                   
REMARK 500    ILE A 740      -39.81    -25.81                                   
REMARK 500    MET A 758       42.07    -98.23                                   
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   9         0.07    SIDE CHAIN                              
REMARK 500     DC D 112         0.11    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 ATOM O3* OF THYMINE 10, CHAIN B IS MISSING                           
REMARK 600 DUE TO THE COVALENT BOND FORMED BETWEEN                              
REMARK 600 THYMINE 10 AND PHOSPHOTYROSINE (PTR) 723                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EHD D 990                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1K4T   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN, SAME DNA                                               
DBREF  1T8I A  174   765  UNP    P11387   TOP1_HUMAN     174    765             
DBREF  1T8I B    1    10  PDB    1T8I     1T8I             1     10             
DBREF  1T8I C   11    22  PDB    1T8I     1T8I            11     22             
DBREF  1T8I D  101   122  PDB    1T8I     1T8I           101    122             
SEQADV 1T8I 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  TGP  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  DC  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 1T8I TGP C   11   DG                                                     
MODRES 1T8I PTR A  723  TYR  O-PHOSPHOTYROSINE                                  
HET    TGP  C  11      19                                                       
HET    PTR  A 723      16                                                       
HET    EHD  D 990      26                                                       
HETNAM     TGP 5'-THIO-2'-DEOXY-GUANOSINE PHOSPHONIC ACID                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     EHD 4-ETHYL-4-HYDROXY-1,12-DIHYDRO-4H-2-OXA-6,12A-DIAZA-             
HETNAM   2 EHD  DIBENZO[B,H]FLUORENE-3,13-DIONE                                 
HETSYN     PTR PHOSPHONOTYROSINE                                                
HETSYN     EHD CAMPTOTHECIN                                                     
FORMUL   2  TGP    C10 H14 N5 O6 P S                                            
FORMUL   4  PTR    C9 H12 N O6 P                                                
FORMUL   5  EHD    C20 H16 N2 O4                                                
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 ASN A  296  SER A  298  5                                   3    
HELIX    7   7 PHE A  302  LYS A  317  1                                  16    
HELIX    8   8 GLU A  322  ASN A  331  1                                  10    
HELIX    9   9 ASN A  331  GLY A  339  1                                   9    
HELIX   10  10 MET A  378  ASP A  381  5                                   4    
HELIX   11  11 SER A  433  LYS A  452  1                                  20    
HELIX   12  12 CYS A  453  ASP A  464  1                                  12    
HELIX   13  13 TRP A  465  SER A  467  5                                   3    
HELIX   14  14 GLU A  469  LYS A  484  1                                  16    
HELIX   15  15 GLY A  503  LEU A  507  5                                   5    
HELIX   16  16 ARG A  508  GLU A  510  5                                   3    
HELIX   17  17 LYS A  532  SER A  534  5                                   3    
HELIX   18  18 GLU A  544  GLU A  556  1                                  13    
HELIX   19  19 ASN A  569  MET A  581  1                                  13    
HELIX   20  20 LYS A  587  GLU A  604  1                                  18    
HELIX   21  21 ASN A  611  CYS A  630  1                                  20    
HELIX   22  22 MET A  644  LYS A  673  1                                  30    
HELIX   23  23 THR A  680  LYS A  687  1                                   8    
HELIX   24  24 LYS A  688  ASN A  711  1                                  24    
HELIX   25  25 LEU A  716  PTR A  723  1                                   8    
HELIX   26  26 ASP A  725  TRP A  736  1                                  12    
HELIX   27  27 PRO A  739  ILE A  743  5                                   5    
HELIX   28  28 ASN A  745  PHE A  752  1                                   8    
HELIX   29  29 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  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 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  TYR A 523   N  PRO A 516           
SHEET    3   D 3 ARG A 536  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         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  
LINK         O3' TGP C  11                 P    DG C  12     1555   1555  1.62  
SITE     1 AC1  9 ARG A 364  ASP A 533  THR A 718  ASN A 722                    
SITE     2 AC1  9  DT B  10  TGP C  11   DG C  12   DC D 112                    
SITE     3 AC1  9  DA D 113                                                     
CRYST1   57.363  114.423   74.118  90.00  93.49  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      0.017433  0.000000  0.001063        0.00000                         
SCALE2      0.000000  0.008740  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013517        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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