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Database: PDB
Entry: 1EJ9
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HEADER    ISOMERASE/DNA                           01-MAR-00   1EJ9              
TITLE     CRYSTAL STRUCTURE OF HUMAN TOPOISOMERASE I DNA COMPLEX                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (5'-                                                   
COMPND   3 D(*C*AP*AP*AP*AP*AP*GP*AP*CP*TP*CP*AP*GP*AP*AP*AP*AP*AP*TP*          
COMPND   4 TP*TP*TP*T)-3');                                                     
COMPND   5 CHAIN: C;                                                            
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA (5'-                                                   
COMPND   9 D(*C*AP*AP*AP*AP*AP*TP*TP*TP*TP*TP*CP*TP*GP*AP*GP*TP*CP*TP*          
COMPND  10 TP*TP*TP*T)-3');                                                     
COMPND  11 CHAIN: D;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: DNA TOPOISOMERASE I;                                       
COMPND  15 CHAIN: A;                                                            
COMPND  16 FRAGMENT: C-TERMINAL DOMAIN, RESIDUES 203-765;                       
COMPND  17 EC: 5.99.1.2;                                                        
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 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_CELL: SF9 INSECT CELLS                             
KEYWDS    PROTEIN-DNA COMPLEX, TYPE I TOPOISOMERASE, HUMAN,                     
KEYWDS   2 ISOMERASE/DNA COMPLEX                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.R.REDINBO,J.J.CHAMPOUX,W.G.HOL                                      
REVDAT   2   24-FEB-09 1EJ9    1       VERSN                                    
REVDAT   1   03-AUG-00 1EJ9    0                                                
JRNL        AUTH   M.R.REDINBO,J.J.CHAMPOUX,W.G.HOL                             
JRNL        TITL   NOVEL INSIGHTS INTO CATALYTIC MECHANISM FROM A               
JRNL        TITL 2 CRYSTAL STRUCTURE OF HUMAN TOPOISOMERASE I IN                
JRNL        TITL 3 COMPLEX WITH DNA.                                            
JRNL        REF    BIOCHEMISTRY                  V.  39  6832 2000              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   10841763                                                     
JRNL        DOI    10.1021/BI992690T                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 29616                          
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) : 0.214                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2139                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3966                                    
REMARK   3   NUCLEIC ACID ATOMS       : 896                                     
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 353                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 56.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.015                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.74                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1EJ9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB010631.                                      
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               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : OTHER                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29834                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 1.0                                
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 0.9                                
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
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   (%): 61.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 27% PEG 400, 145 MM MGCL2, 20 MM         
REMARK 280  MES PH 6.8, 5 MM TRIS PH 8.0, 30 MM DTT, VAPOR DIFFUSION,           
REMARK 280  SITTING 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       62.46000            
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: 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      DC C     0                                                      
REMARK 465      DC D   100                                                      
REMARK 465     ILE A   634                                                      
REMARK 465     ALA A   635                                                      
REMARK 465     PRO A   636                                                      
REMARK 465     PRO A   637                                                      
REMARK 465     LYS A   638                                                      
REMARK 465     THR A   639                                                      
REMARK 465     PHE A   640                                                      
REMARK 465     GLU A   641                                                      
REMARK 465     LYS A   642                                                      
REMARK 465     SER A   643                                                      
REMARK 465     MET A   644                                                      
REMARK 465     MET A   645                                                      
REMARK 465     ASN A   646                                                      
REMARK 465     LEU A   647                                                      
REMARK 465     GLN A   648                                                      
REMARK 465     THR A   649                                                      
REMARK 465     LYS A   650                                                      
REMARK 465     ILE A   651                                                      
REMARK 465     ASP A   652                                                      
REMARK 465     ALA A   653                                                      
REMARK 465     LYS A   654                                                      
REMARK 465     LYS A   655                                                      
REMARK 465     GLU A   656                                                      
REMARK 465     GLN A   657                                                      
REMARK 465     LEU A   658                                                      
REMARK 465     ALA A   659                                                      
REMARK 465     ASP A   660                                                      
REMARK 465     ALA A   661                                                      
REMARK 465     ARG A   662                                                      
REMARK 465     ARG A   663                                                      
REMARK 465     ASP A   664                                                      
REMARK 465     LEU A   665                                                      
REMARK 465     LYS A   666                                                      
REMARK 465     SER A   667                                                      
REMARK 465     ALA A   668                                                      
REMARK 465     LYS A   669                                                      
REMARK 465     ALA A   670                                                      
REMARK 465     ASP A   671                                                      
REMARK 465     ALA A   672                                                      
REMARK 465     LYS A   673                                                      
REMARK 465     VAL A   674                                                      
REMARK 465     MET A   675                                                      
REMARK 465     LYS A   676                                                      
REMARK 465     ASP A   677                                                      
REMARK 465     ALA A   678                                                      
REMARK 465     LYS A   679                                                      
REMARK 465     THR A   680                                                      
REMARK 465     LYS A   681                                                      
REMARK 465     LYS A   682                                                      
REMARK 465     VAL A   683                                                      
REMARK 465     VAL A   684                                                      
REMARK 465     GLU A   685                                                      
REMARK 465     SER A   686                                                      
REMARK 465     LYS A   687                                                      
REMARK 465     LYS A   688                                                      
REMARK 465     LYS A   689                                                      
REMARK 465     ALA A   690                                                      
REMARK 465     VAL A   691                                                      
REMARK 465     GLN A   692                                                      
REMARK 465     ARG A   693                                                      
REMARK 465     LEU A   694                                                      
REMARK 465     GLU A   695                                                      
REMARK 465     GLU A   696                                                      
REMARK 465     GLN A   697                                                      
REMARK 465     LEU A   698                                                      
REMARK 465     MET A   699                                                      
REMARK 465     LYS A   700                                                      
REMARK 465     LEU A   701                                                      
REMARK 465     GLU A   702                                                      
REMARK 465     VAL A   703                                                      
REMARK 465     GLN A   704                                                      
REMARK 465     ALA A   705                                                      
REMARK 465     THR A   706                                                      
REMARK 465     ASP A   707                                                      
REMARK 465     ARG A   708                                                      
REMARK 465     GLU A   709                                                      
REMARK 465     GLU A   710                                                      
REMARK 465     ASN A   711                                                      
REMARK 465     LYS A   712                                                      
REMARK 465     GLN A   713                                                      
REMARK 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      DA C   1    P    OP1  OP2                                       
REMARK 470      DA D 101    P    OP1  OP2                                       
REMARK 470     GLU A 209    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 210    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 213    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 317    CG   CD   CE   NZ                                   
REMARK 470     LYS A 321    CG   CD   CE   NZ                                   
REMARK 470     GLU A 322    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 326    CG   CD   CE   NZ                                   
REMARK 470     LYS A 333    CG   CD   CE   NZ                                   
REMARK 470     GLU A 463    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 468    CG   CD   CE   NZ                                   
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     ASP A 760    CG   OD1  OD2                                       
REMARK 470     ASP A 762    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500     DA C   1   O5' -  C5' -  C4' ANGL. DEV. =  -6.3 DEGREES          
REMARK 500     DC C  10   C3' -  C2' -  C1' ANGL. DEV. =  -5.6 DEGREES          
REMARK 500     DA D 103   C3' -  C2' -  C1' ANGL. DEV. =  -5.2 DEGREES          
REMARK 500     DT D 112   C3' -  C2' -  C1' ANGL. DEV. =  -6.6 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 204       72.78    -67.70                                   
REMARK 500    PRO A 212     -179.39    -61.79                                   
REMARK 500    LEU A 264      -36.42    -33.26                                   
REMARK 500    THR A 269        0.25    -62.96                                   
REMARK 500    MET A 319      153.34    -38.25                                   
REMARK 500    ASP A 344     -117.65     57.49                                   
REMARK 500    CYS A 453       16.97   -141.56                                   
REMARK 500    SER A 467      156.01    -41.38                                   
REMARK 500    ALA A 486       38.27     75.69                                   
REMARK 500    LEU A 518      135.72   -172.75                                   
REMARK 500    ASP A 528       94.61   -161.87                                   
REMARK 500    PHE A 565       55.13    -96.15                                   
REMARK 500    ASP A 566      177.82    -57.43                                   
REMARK 500    ASP A 609       36.32    -80.34                                   
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   8         0.07    SIDE_CHAIN                              
REMARK 500     DA C  17         0.05    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1A36   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1A35   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1A31   RELATED DB: PDB                                   
DBREF  1EJ9 A  203   765  UNP    P11387   TOP1_HUMAN     203    765             
DBREF  1EJ9 C    0    22  PDB    1EJ9     1EJ9             0     22             
DBREF  1EJ9 D  100   122  PDB    1EJ9     1EJ9           100    122             
SEQADV 1EJ9 ILE A  634  UNP  P11387    ARG   634 ENGINEERED                     
SEQADV 1EJ9 PHE A  723  UNP  P11387    TYR   723 ENGINEERED                     
SEQRES   1 C   23   DC  DA  DA  DA  DA  DA  DG  DA  DC  DT  DC  DA  DG          
SEQRES   2 C   23   DA  DA  DA  DA  DA  DT  DT  DT  DT  DT                      
SEQRES   1 D   23   DC  DA  DA  DA  DA  DA  DT  DT  DT  DT  DT  DC  DT          
SEQRES   2 D   23   DG  DA  DG  DT  DC  DT  DT  DT  DT  DT                      
SEQRES   1 A  563  TRP LYS TRP TRP GLU GLU GLU ARG TYR PRO GLU GLY ILE          
SEQRES   2 A  563  LYS TRP LYS PHE LEU GLU HIS LYS GLY PRO VAL PHE ALA          
SEQRES   3 A  563  PRO PRO TYR GLU PRO LEU PRO GLU ASN VAL LYS PHE TYR          
SEQRES   4 A  563  TYR ASP GLY LYS VAL MET LYS LEU SER PRO LYS ALA GLU          
SEQRES   5 A  563  GLU VAL ALA THR PHE PHE ALA LYS MET LEU ASP HIS GLU          
SEQRES   6 A  563  TYR THR THR LYS GLU ILE PHE ARG LYS ASN PHE PHE LYS          
SEQRES   7 A  563  ASP TRP ARG LYS GLU MET THR ASN GLU GLU LYS ASN ILE          
SEQRES   8 A  563  ILE THR ASN LEU SER LYS CYS ASP PHE THR GLN MET SER          
SEQRES   9 A  563  GLN TYR PHE LYS ALA GLN THR GLU ALA ARG LYS GLN MET          
SEQRES  10 A  563  SER LYS GLU GLU LYS LEU LYS ILE LYS GLU GLU ASN GLU          
SEQRES  11 A  563  LYS LEU LEU LYS GLU TYR GLY PHE CYS ILE MET ASP ASN          
SEQRES  12 A  563  HIS LYS GLU ARG ILE ALA ASN PHE LYS ILE GLU PRO PRO          
SEQRES  13 A  563  GLY LEU PHE ARG GLY ARG GLY ASN HIS PRO LYS MET GLY          
SEQRES  14 A  563  MET LEU LYS ARG ARG ILE MET PRO GLU ASP ILE ILE ILE          
SEQRES  15 A  563  ASN CYS SER LYS ASP ALA LYS VAL PRO SER PRO PRO PRO          
SEQRES  16 A  563  GLY HIS LYS TRP LYS GLU VAL ARG HIS ASP ASN LYS VAL          
SEQRES  17 A  563  THR TRP LEU VAL SER TRP THR GLU ASN ILE GLN GLY SER          
SEQRES  18 A  563  ILE LYS TYR ILE MET LEU ASN PRO SER SER ARG ILE LYS          
SEQRES  19 A  563  GLY GLU LYS ASP TRP GLN LYS TYR GLU THR ALA ARG ARG          
SEQRES  20 A  563  LEU LYS LYS CYS VAL ASP LYS ILE ARG ASN GLN TYR ARG          
SEQRES  21 A  563  GLU ASP TRP LYS SER LYS GLU MET LYS VAL ARG GLN ARG          
SEQRES  22 A  563  ALA VAL ALA LEU TYR PHE ILE ASP LYS LEU ALA LEU ARG          
SEQRES  23 A  563  ALA GLY ASN GLU LYS GLU GLU GLY GLU THR ALA ASP THR          
SEQRES  24 A  563  VAL GLY CYS CYS SER LEU ARG VAL GLU HIS ILE ASN LEU          
SEQRES  25 A  563  HIS PRO GLU LEU ASP GLY GLN GLU TYR VAL VAL GLU PHE          
SEQRES  26 A  563  ASP PHE LEU GLY LYS ASP SER ILE ARG TYR TYR ASN LYS          
SEQRES  27 A  563  VAL PRO VAL GLU LYS ARG VAL PHE LYS ASN LEU GLN LEU          
SEQRES  28 A  563  PHE MET GLU ASN LYS GLN PRO GLU ASP ASP LEU PHE ASP          
SEQRES  29 A  563  ARG LEU ASN THR GLY ILE LEU ASN LYS HIS LEU GLN ASP          
SEQRES  30 A  563  LEU MET GLU GLY LEU THR ALA LYS VAL PHE ARG THR TYR          
SEQRES  31 A  563  ASN ALA SER ILE THR LEU GLN GLN GLN LEU LYS GLU LEU          
SEQRES  32 A  563  THR ALA PRO ASP GLU ASN ILE PRO ALA LYS ILE LEU SER          
SEQRES  33 A  563  TYR ASN ARG ALA ASN ARG ALA VAL ALA ILE LEU CYS ASN          
SEQRES  34 A  563  HIS GLN ILE ALA PRO PRO LYS THR PHE GLU LYS SER MET          
SEQRES  35 A  563  MET ASN LEU GLN THR LYS ILE ASP ALA LYS LYS GLU GLN          
SEQRES  36 A  563  LEU ALA ASP ALA ARG ARG ASP LEU LYS SER ALA LYS ALA          
SEQRES  37 A  563  ASP ALA LYS VAL MET LYS ASP ALA LYS THR LYS LYS VAL          
SEQRES  38 A  563  VAL GLU SER LYS LYS LYS ALA VAL GLN ARG LEU GLU GLU          
SEQRES  39 A  563  GLN LEU MET LYS LEU GLU VAL GLN ALA THR ASP ARG GLU          
SEQRES  40 A  563  GLU ASN LYS GLN ILE ALA LEU GLY THR SER LYS LEU ASN          
SEQRES  41 A  563  PHE LEU ASP PRO ARG ILE THR VAL ALA TRP CYS LYS LYS          
SEQRES  42 A  563  TRP GLY VAL PRO ILE GLU LYS ILE TYR ASN LYS THR GLN          
SEQRES  43 A  563  ARG GLU LYS PHE ALA TRP ALA ILE ASP MET ALA ASP GLU          
SEQRES  44 A  563  ASP TYR GLU PHE                                              
FORMUL   4  HOH   *353(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 GLU A  267  THR A  270  5                                   4    
HELIX    4   4 LYS A  271  GLU A  285  1                                  15    
HELIX    5   5 THR A  287  ILE A  294  1                                   8    
HELIX    6   6 PHE A  302  MET A  319  1                                  18    
HELIX    7   7 SER A  320  GLY A  339  1                                  20    
HELIX    8   8 MET A  378  ASP A  381  5                                   4    
HELIX    9   9 SER A  433  TRP A  465  1                                  33    
HELIX   10  10 GLU A  469  ALA A  486  1                                  18    
HELIX   11  11 LYS A  532  SER A  534  5                                   3    
HELIX   12  12 GLU A  544  MET A  555  1                                  12    
HELIX   13  13 ASN A  569  MET A  581  1                                  13    
HELIX   14  14 THR A  585  THR A  606  1                                  22    
HELIX   15  15 ASN A  611  ASN A  631  1                                  21    
HELIX   16  16 LEU A  716  PHE A  723  1                                   8    
HELIX   17  17 ASP A  725  TRP A  736  1                                  12    
HELIX   18  18 PRO A  739  ILE A  743  5                                   5    
HELIX   19  19 ASN A  745  ALA A  753  1                                   9    
HELIX   20  20 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  N  ILE A 342   O  GLU A 221           
SHEET    3   A 3 HIS A 346  ARG A 349 -1  N  HIS A 346   O  MET A 343           
SHEET    1   B 3 LYS A 245  VAL A 246  0                                        
SHEET    2   B 3 TYR A 241  TYR A 242 -1  N  TYR A 242   O  LYS A 245           
SHEET    3   B 3 CYS A 300  ASP A 301 -1  N  ASP A 301   O  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  N  LYS A 374   O  GLY A 359           
SHEET    1   D 4 GLU A 403  ARG A 405  0                                        
SHEET    2   D 4 ILE A 383  ASN A 385  1  O  ILE A 384   N  ARG A 405           
SHEET    3   D 4 VAL A 414  GLU A 418 -1  O  SER A 415   N  ILE A 383           
SHEET    4   D 4 SER A 423  ILE A 427 -1  O  SER A 423   N  GLU A 418           
SHEET    1   E 3 ILE A 512  LEU A 518  0                                        
SHEET    2   E 3 GLN A 521  LEU A 530 -1  O  GLN A 521   N  LEU A 518           
SHEET    3   E 3 ARG A 536  PRO A 542 -1  N  TYR A 537   O  PHE A 529           
CRYST1   56.980  124.920   72.290  90.00  93.84  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      0.017550  0.000000  0.001178        0.00000                         
SCALE2      0.000000  0.008005  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013864        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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