GenomeNet

Database: PDB
Entry: 1RRJ
LinkDB: 1RRJ
Original site: 1RRJ 
HEADER    ISOMERASE/DNA                           08-DEC-03   1RRJ              
TITLE     STRUCTURAL MECHANISMS OF CAMPTOTHECIN RESISTANCE BY                   
TITLE    2 MUTATIONS IN HUMAN TOPOISOMERASE I                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-                                                        
COMPND   3 D(*AP*AP*AP*AP*AP*GP*AP*CP*TP*T*GP*GP*AP*AP*AP*AP*AP*TP*TP*          
COMPND   4 TP*TP*T)-3';                                                         
COMPND   5 CHAIN: B;                                                            
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: 5'-                                                        
COMPND   9 D(*AP*AP*AP*AP*AP*TP*TP*TP*TP*TP*CP*CP*AP*AP*GP*TP*CP*TP*TP          
COMPND  10 *TP*TP*T)-3';                                                        
COMPND  11 CHAIN: C;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: DNA TOPOISOMERASE I;                                       
COMPND  15 CHAIN: A;                                                            
COMPND  16 EC: 5.99.1.2;                                                        
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 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 GENE: TOP1;                                                          
SOURCE  10 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  11 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  13 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  14 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  15 EXPRESSION_SYSTEM_VECTOR: PFACTBAC1                                  
KEYWDS    HUMAN TOPOISOMERASE I, TOPOTECAN, CAMPTOTHECIN, X-RAY                 
KEYWDS   2 CRYSTALLOGRAPHY, ISOMERASE/DNA COMPLEX                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.CHRENCIK,B.L.STAKER,A.B.BURGIN,L.STEWART,M.R.REDINBO              
REVDAT   2   24-FEB-09 1RRJ    1       VERSN                                    
REVDAT   1   06-JUL-04 1RRJ    0                                                
JRNL        AUTH   J.E.CHRENCIK,B.L.STAKER,A.B.BURGIN,P.POURQUIER,              
JRNL        AUTH 2 Y.POMMIER,L.STEWART,M.R.REDINBO                              
JRNL        TITL   MECHANISMS OF CAMPTOTHECIN RESISTANCE BY HUMAN               
JRNL        TITL 2 TOPOISOMERASE I MUTATIONS                                    
JRNL        REF    J.MOL.BIOL.                   V. 339   773 2004              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   15165849                                                     
JRNL        DOI    10.1016/J.JMB.2004.03.077                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.69                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 56412                          
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) : 0.246                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4348                            
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            : 4701                                    
REMARK   3   NUCLEIC ACID ATOMS       : 892                                     
REMARK   3   HETEROGEN ATOMS          : 63                                      
REMARK   3   SOLVENT ATOMS            : 436                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.50000                                             
REMARK   3    B22 (A**2) : -0.57000                                             
REMARK   3    B33 (A**2) : 3.08000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.43000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.32                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.25                            
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) : 0.37                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.31                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.044                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.63                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1RRJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JAN-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB020987.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-FEB-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (TRUNCATE)                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56412                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.690                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1K4T                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, 200MM LITHIUM SULFATE,          
REMARK 280  100MM MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  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       57.67700            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, A                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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      DT B  10    O3'                                                 
REMARK 470      DG B  11    P    OP1  OP2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O5'  DG  B    11     O    HOH B  2319              1.79            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    PHE A 640   N     PHE A 640   CA      0.709                       
REMARK 500    LEU A 724   N     LEU A 724   CA      0.240                       
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    LEU A 335   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    PHE A 640   N   -  CA  -  C   ANGL. DEV. = -33.8 DEGREES          
REMARK 500    PHE A 640   C   -  N   -  CA  ANGL. DEV. = -20.0 DEGREES          
REMARK 500    LEU A 724   N   -  CA  -  CB  ANGL. DEV. =  19.5 DEGREES          
REMARK 500    LEU A 724   N   -  CA  -  C   ANGL. DEV. = -17.6 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    ASP A 344       88.41     34.92                                   
REMARK 500    ASP A 500       97.62    -64.67                                   
REMARK 500    PHE A 565       77.80   -102.52                                   
REMARK 500    PRO A 637      111.15    -35.91                                   
REMARK 500    LYS A 638       94.65    -22.68                                   
REMARK 500    THR A 639       -1.78     57.41                                   
REMARK 500    MET A 675       73.54     63.38                                   
REMARK 500    MET A 758       78.46   -103.20                                   
REMARK 500    ALA A 759      118.18    176.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR A  639     PHE A  640                 -113.95                    
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 TTG B 991                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTC B 990                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1K4T   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1RR8   RELATED DB: PDB                                   
REMARK 900 PHE361SER                                                            
DBREF  1RRJ A  201   765  UNP    P11387   TOP1_HUMAN     201    765             
DBREF  1RRJ B    1    22  PDB    1RRJ     1RRJ             1     22             
DBREF  1RRJ C  101   122  PDB    1RRJ     1RRJ           101    122             
SEQADV 1RRJ SER A  722  UNP  P11387    ASN   722 ENGINEERED                     
SEQADV 1RRJ PTR A  723  UNP  P11387    TYR   723 MODIFIED RESIDUE               
SEQRES   1 B   22   DA  DA  DA  DA  DA  DG  DA  DC  DT  DT  DG  DG  DA          
SEQRES   2 B   22   DA  DA  DA  DA  DT  DT  DT  DT  DT                          
SEQRES   1 C   22   DA  DA  DA  DA  DA  DT  DT  DT  DT  DT  DC  DC  DA          
SEQRES   2 C   22   DA  DG  DT  DC  DT  DT  DT  DT  DT                          
SEQRES   1 A  565  GLN LYS TRP LYS TRP TRP GLU GLU GLU ARG TYR PRO GLU          
SEQRES   2 A  565  GLY ILE LYS TRP LYS PHE LEU GLU HIS LYS GLY PRO VAL          
SEQRES   3 A  565  PHE ALA PRO PRO TYR GLU PRO LEU PRO GLU ASN VAL LYS          
SEQRES   4 A  565  PHE TYR TYR ASP GLY LYS VAL MET LYS LEU SER PRO LYS          
SEQRES   5 A  565  ALA GLU GLU VAL ALA THR PHE PHE ALA LYS MET LEU ASP          
SEQRES   6 A  565  HIS GLU TYR THR THR LYS GLU ILE PHE ARG LYS ASN PHE          
SEQRES   7 A  565  PHE LYS ASP TRP ARG LYS GLU MET THR ASN GLU GLU LYS          
SEQRES   8 A  565  ASN ILE ILE THR ASN LEU SER LYS CYS ASP PHE THR GLN          
SEQRES   9 A  565  MET SER GLN TYR PHE LYS ALA GLN THR GLU ALA ARG LYS          
SEQRES  10 A  565  GLN MET SER LYS GLU GLU LYS LEU LYS ILE LYS GLU GLU          
SEQRES  11 A  565  ASN GLU LYS LEU LEU LYS GLU TYR GLY PHE CYS ILE MET          
SEQRES  12 A  565  ASP ASN HIS LYS GLU ARG ILE ALA ASN PHE LYS ILE GLU          
SEQRES  13 A  565  PRO PRO GLY LEU PHE ARG GLY ARG GLY ASN HIS PRO LYS          
SEQRES  14 A  565  MET GLY MET LEU LYS ARG ARG ILE MET PRO GLU ASP ILE          
SEQRES  15 A  565  ILE ILE ASN CYS SER LYS ASP ALA LYS VAL PRO SER PRO          
SEQRES  16 A  565  PRO PRO GLY HIS LYS TRP LYS GLU VAL ARG HIS ASP ASN          
SEQRES  17 A  565  LYS VAL THR TRP LEU VAL SER TRP THR GLU ASN ILE GLN          
SEQRES  18 A  565  GLY SER ILE LYS TYR ILE MET LEU ASN PRO SER SER ARG          
SEQRES  19 A  565  ILE LYS GLY GLU LYS ASP TRP GLN LYS TYR GLU THR ALA          
SEQRES  20 A  565  ARG ARG LEU LYS LYS CYS VAL ASP LYS ILE ARG ASN GLN          
SEQRES  21 A  565  TYR ARG GLU ASP TRP LYS SER LYS GLU MET LYS VAL ARG          
SEQRES  22 A  565  GLN ARG ALA VAL ALA LEU TYR PHE ILE ASP LYS LEU ALA          
SEQRES  23 A  565  LEU ARG ALA GLY ASN GLU LYS GLU GLU GLY GLU THR ALA          
SEQRES  24 A  565  ASP THR VAL GLY CYS CYS SER LEU ARG VAL GLU HIS ILE          
SEQRES  25 A  565  ASN LEU HIS PRO GLU LEU ASP GLY GLN GLU TYR VAL VAL          
SEQRES  26 A  565  GLU PHE ASP PHE LEU GLY LYS ASP SER ILE ARG TYR TYR          
SEQRES  27 A  565  ASN LYS VAL PRO VAL GLU LYS ARG VAL PHE LYS ASN LEU          
SEQRES  28 A  565  GLN LEU PHE MET GLU ASN LYS GLN PRO GLU ASP ASP LEU          
SEQRES  29 A  565  PHE ASP ARG LEU ASN THR GLY ILE LEU ASN LYS HIS LEU          
SEQRES  30 A  565  GLN ASP LEU MET GLU GLY LEU THR ALA LYS VAL PHE ARG          
SEQRES  31 A  565  THR TYR ASN ALA SER ILE THR LEU GLN GLN GLN LEU LYS          
SEQRES  32 A  565  GLU LEU THR ALA PRO ASP GLU ASN ILE PRO ALA LYS ILE          
SEQRES  33 A  565  LEU SER TYR ASN ARG ALA ASN ARG ALA VAL ALA ILE LEU          
SEQRES  34 A  565  CYS ASN HIS GLN ARG ALA PRO PRO LYS THR PHE GLU LYS          
SEQRES  35 A  565  SER MET MET ASN LEU GLN THR LYS ILE ASP ALA LYS LYS          
SEQRES  36 A  565  GLU GLN LEU ALA ASP ALA ARG ARG ASP LEU LYS SER ALA          
SEQRES  37 A  565  LYS ALA ASP ALA LYS VAL MET LYS ASP ALA LYS THR LYS          
SEQRES  38 A  565  LYS VAL VAL GLU SER LYS LYS LYS ALA VAL GLN ARG LEU          
SEQRES  39 A  565  GLU GLU GLN LEU MET LYS LEU GLU VAL GLN ALA THR ASP          
SEQRES  40 A  565  ARG GLU GLU ASN LYS GLN ILE ALA LEU GLY THR SER LYS          
SEQRES  41 A  565  LEU SER PTR LEU ASP PRO ARG ILE THR VAL ALA TRP CYS          
SEQRES  42 A  565  LYS LYS TRP GLY VAL PRO ILE GLU LYS ILE TYR ASN LYS          
SEQRES  43 A  565  THR GLN ARG GLU LYS PHE ALA TRP ALA ILE ASP MET ALA          
SEQRES  44 A  565  ASP GLU ASP TYR GLU PHE                                      
MODRES 1RRJ PTR A  723  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  A 723      16                                                       
HET    TTG  B 991      32                                                       
HET    TTC  B 990      31                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     TTG 2-(1-DIMETHYLAMINOMETHYL-2-HYDROXY-8-HYDROXYMETHYL-9-            
HETNAM   2 TTG  OXO-9,11-DIHYDRO-INDOLIZINO[1,2-B]QUINOLIN-7-YL)-2-             
HETNAM   3 TTG  HYDROXY-BUTYRIC ACID                                            
HETNAM     TTC (S)-10-[(DIMETHYLAMINO)METHYL]-4-ETHYL-4,9-DIHYDROXY-            
HETNAM   2 TTC  1H-PYRANO[3',4':6,7]INOLIZINO[1,2-B]-QUINOLINE-3,               
HETNAM   3 TTC  14(4H,12H)-DIONE                                                
HETSYN     PTR PHOSPHONOTYROSINE                                                
HETSYN     TTG HYDROLYZED PRODUCT OF TOPOTECAN                                  
HETSYN     TTC TOPOTECAN, HYCAMTIN                                              
FORMUL   3  PTR    C9 H12 N O6 P                                                
FORMUL   4  TTG    C23 H25 N3 O6                                                
FORMUL   4  TTC    C23 H23 N3 O5                                                
FORMUL   5  HOH   *436(H2 O)                                                    
HELIX    1   1 LYS A  204  GLU A  208  5                                   5    
HELIX    2   2 SER A  250  LYS A  262  1                                  13    
HELIX    3   3 HIS A  266  THR A  270  5                                   5    
HELIX    4   4 LYS A  271  MET A  286  1                                  16    
HELIX    5   5 THR A  287  ASN A  292  1                                   6    
HELIX    6   6 PHE A  302  LYS A  317  1                                  16    
HELIX    7   7 SER A  320  GLY A  339  1                                  20    
HELIX    8   8 MET A  378  ASP A  381  5                                   4    
HELIX    9   9 SER A  433  LYS A  452  1                                  20    
HELIX   10  10 CYS A  453  ASP A  464  1                                  12    
HELIX   11  11 TRP A  465  SER A  467  5                                   3    
HELIX   12  12 GLU A  469  LEU A  485  1                                  17    
HELIX   13  13 ARG A  508  GLU A  510  5                                   3    
HELIX   14  14 LYS A  532  SER A  534  5                                   3    
HELIX   15  15 GLU A  544  MET A  555  1                                  12    
HELIX   16  16 ASN A  569  MET A  581  1                                  13    
HELIX   17  17 ALA A  586  THR A  606  1                                  21    
HELIX   18  18 ASN A  611  CYS A  630  1                                  20    
HELIX   19  19 THR A  639  GLU A  641  5                                   3    
HELIX   20  20 LYS A  642  ASP A  671  1                                  30    
HELIX   21  21 THR A  680  ASN A  711  1                                  32    
HELIX   22  22 LEU A  716  SER A  722  1                                   7    
HELIX   23  23 ASP A  725  GLY A  737  1                                  13    
HELIX   24  24 PRO A  739  ILE A  743  5                                   5    
HELIX   25  25 ASN A  745  PHE A  752  1                                   8    
HELIX   26  26 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  VAL A 246  0                                        
SHEET    2   B 3 TYR A 241  TYR A 242 -1  N  TYR A 242   O  LYS A 245           
SHEET    3   B 3 CYS A 300  ASP A 301 -1  O  ASP A 301   N  TYR A 241           
SHEET    1   C 2 GLY A 359  LEU A 360  0                                        
SHEET    2   C 2 LEU A 373  LYS A 374 -1  O  LYS A 374   N  GLY A 359           
SHEET    1   D 4 GLU A 403  ARG A 405  0                                        
SHEET    2   D 4 ILE A 383  ASN A 385  1  N  ILE A 384   O  ARG A 405           
SHEET    3   D 4 VAL A 414  THR A 417 -1  O  SER A 415   N  ILE A 383           
SHEET    4   D 4 ILE A 424  ILE A 427 -1  O  LYS A 425   N  TRP A 416           
SHEET    1   E 3 ILE A 512  LEU A 518  0                                        
SHEET    2   E 3 GLN A 521  LEU A 530 -1  O  GLU A 526   N  ASN A 513           
SHEET    3   E 3 ARG A 536  PRO A 542 -1  O  TYR A 537   N  PHE A 529           
LINK         C3'  DT B  10                 O3P PTR A 723     1555   1555  2.13  
LINK         C   SER A 722                 N   PTR A 723     1555   1555  1.34  
LINK         C   PTR A 723                 N   LEU A 724     1555   1555  1.42  
SITE     1 AC1 15 GLU A 356  ARG A 364  LYS A 532  ASP A 533                    
SITE     2 AC1 15 THR A 718   DT B  10   DG B  11  TTC B 990                    
SITE     3 AC1 15 HOH B2001  HOH B2180  HOH B2217  HOH B2293                    
SITE     4 AC1 15 HOH B2319   DC C 112   DA C 113                               
SITE     1 AC2 15 GLU A 356  ARG A 364  LYS A 532  ASP A 533                    
SITE     2 AC2 15 THR A 718  PTR A 723   DT B  10   DG B  11                    
SITE     3 AC2 15 TTG B 991  HOH B2001  HOH B2180  HOH B2217                    
SITE     4 AC2 15 HOH B2293   DC C 112   DA C 113                               
CRYST1   57.333  115.354   75.172  90.00  94.33  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      0.017442  0.000000  0.001320        0.00000                         
SCALE2      0.000000  0.008669  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013341        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system