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Database: PDB
Entry: 1RR8
LinkDB: 1RR8
Original site: 1RR8 
HEADER    ISOMERASE/DNA                           08-DEC-03   1RR8              
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: A;                                                            
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: B;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: DNA TOPOISOMERASE I;                                       
COMPND  15 CHAIN: C;                                                            
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    PROTEIN-DNA COMPLEX, TOPOTECAN, CAMPTOTHECIN, NUCLEIC ACID,           
KEYWDS   2 HUMAN TOPOISOMERASE I, 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 1RR8    1       VERSN                                    
REVDAT   1   06-JUL-04 1RR8    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.    2.60 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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.70                          
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)   (%) : 10.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 27855                          
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) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.294                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2744                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.72                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2420                       
REMARK   3   BIN FREE R VALUE                    : 0.2940                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 2744                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.006                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4124                                    
REMARK   3   NUCLEIC ACID ATOMS       : 895                                     
REMARK   3   HETEROGEN ATOMS          : 63                                      
REMARK   3   SOLVENT ATOMS            : 304                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.53000                                              
REMARK   3    B22 (A**2) : -7.52000                                             
REMARK   3    B33 (A**2) : 5.99000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 5.78000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.38                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.42                            
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) : 0.48                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.53                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.054                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.55                            
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 1RR8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB020981.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-FEB-02                          
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                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (TRUNCATE)                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27855                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.020                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08500                            
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) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.8                               
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: PDB ENTRY 1K4T                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, 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       57.79250            
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: A, B, C                               
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     PRO C   637                                                      
REMARK 465     LYS C   638                                                      
REMARK 465     THR C   639                                                      
REMARK 465     PHE C   640                                                      
REMARK 465     GLU C   641                                                      
REMARK 465     LYS C   642                                                      
REMARK 465     SER C   643                                                      
REMARK 465     MET C   644                                                      
REMARK 465     MET C   645                                                      
REMARK 465     ASN C   646                                                      
REMARK 465     LEU C   647                                                      
REMARK 465     GLN C   648                                                      
REMARK 465     THR C   649                                                      
REMARK 465     LYS C   650                                                      
REMARK 465     ILE C   651                                                      
REMARK 465     ASP C   652                                                      
REMARK 465     ALA C   653                                                      
REMARK 465     LYS C   654                                                      
REMARK 465     LYS C   655                                                      
REMARK 465     GLU C   656                                                      
REMARK 465     GLN C   657                                                      
REMARK 465     LEU C   658                                                      
REMARK 465     ALA C   659                                                      
REMARK 465     ASP C   660                                                      
REMARK 465     ALA C   661                                                      
REMARK 465     ARG C   662                                                      
REMARK 465     ARG C   663                                                      
REMARK 465     ASP C   664                                                      
REMARK 465     LEU C   665                                                      
REMARK 465     LYS C   666                                                      
REMARK 465     SER C   667                                                      
REMARK 465     ALA C   668                                                      
REMARK 465     LYS C   669                                                      
REMARK 465     ALA C   670                                                      
REMARK 465     ASP C   671                                                      
REMARK 465     ALA C   672                                                      
REMARK 465     LYS C   673                                                      
REMARK 465     VAL C   674                                                      
REMARK 465     MET C   675                                                      
REMARK 465     LYS C   676                                                      
REMARK 465     ASP C   677                                                      
REMARK 465     ALA C   678                                                      
REMARK 465     LYS C   679                                                      
REMARK 465     THR C   680                                                      
REMARK 465     LYS C   681                                                      
REMARK 465     LYS C   682                                                      
REMARK 465     VAL C   683                                                      
REMARK 465     VAL C   684                                                      
REMARK 465     GLU C   685                                                      
REMARK 465     SER C   686                                                      
REMARK 465     LYS C   687                                                      
REMARK 465     LYS C   688                                                      
REMARK 465     LYS C   689                                                      
REMARK 465     ALA C   690                                                      
REMARK 465     VAL C   691                                                      
REMARK 465     GLN C   692                                                      
REMARK 465     ARG C   693                                                      
REMARK 465     LEU C   694                                                      
REMARK 465     GLU C   695                                                      
REMARK 465     GLU C   696                                                      
REMARK 465     GLN C   697                                                      
REMARK 465     LEU C   698                                                      
REMARK 465     MET C   699                                                      
REMARK 465     LYS C   700                                                      
REMARK 465     LEU C   701                                                      
REMARK 465     GLU C   702                                                      
REMARK 465     VAL C   703                                                      
REMARK 465     GLN C   704                                                      
REMARK 465     ALA C   705                                                      
REMARK 465     THR C   706                                                      
REMARK 465     ASP C   707                                                      
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 A  10    O3'                                                 
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   OP1  DG  A    11     O    HOH A   886              1.67            
REMARK 500   P    DG  A    11     O    HOH A   886              2.19            
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     DG A  11   P      DG A  11   O5'     1.590                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500     DG A  11   O5' -  P   -  OP2 ANGL. DEV. = -13.1 DEGREES          
REMARK 500     DG A  11   P   -  O5' -  C5' ANGL. DEV. = -86.9 DEGREES          
REMARK 500    LEU C 335   CA  -  CB  -  CG  ANGL. DEV. =  13.9 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    THR C 303      -38.73    -39.83                                   
REMARK 500    ASP C 344       89.33     47.48                                   
REMARK 500    ASN C 345       -2.31     59.44                                   
REMARK 500    ALA C 351      -83.43    -66.51                                   
REMARK 500    ASN C 352       78.58   -117.93                                   
REMARK 500    CYS C 453      -15.38   -145.46                                   
REMARK 500    ASN C 711       30.91    -83.71                                   
REMARK 500    ALA C 759      136.69    170.65                                   
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 PTR C  723     LEU C  724                 -131.63                    
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     DA A   1         0.05    SIDE_CHAIN                              
REMARK 500     DT A   9         0.06    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 856        DISTANCE = 10.18 ANGSTROMS                       
REMARK 525    HOH C 783        DISTANCE =  5.17 ANGSTROMS                       
REMARK 525    HOH A 916        DISTANCE = 16.84 ANGSTROMS                       
REMARK 525    HOH C 934        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH C1024        DISTANCE =  7.04 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTG A 1991                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTC A 100                 
DBREF  1RR8 C  203   765  UNP    P11387   TOP1_HUMAN     203    765             
DBREF  1RR8 A    1    22  PDB    1RR8     1RR8             1     22             
DBREF  1RR8 B  101   122  PDB    1RR8     1RR8           101    122             
SEQADV 1RR8 ALA C  201  UNP  P11387              CLONING ARTIFACT               
SEQADV 1RR8 ALA C  202  UNP  P11387              CLONING ARTIFACT               
SEQADV 1RR8 SER C  361  UNP  P11387    PHE   361 ENGINEERED                     
SEQADV 1RR8 GLN C  634  UNP  P11387    ARG   634 ENGINEERED                     
SEQADV 1RR8 PTR C  723  UNP  P11387    TYR   723 MODIFIED RESIDUE               
SEQRES   1 A   22   DA  DA  DA  DA  DA  DG  DA  DC  DT  DT  DG  DG  DA          
SEQRES   2 A   22   DA  DA  DA  DA  DT  DT  DT  DT  DT                          
SEQRES   1 B   22   DA  DA  DA  DA  DA  DT  DT  DT  DT  DT  DC  DC  DA          
SEQRES   2 B   22   DA  DG  DT  DC  DT  DT  DT  DT  DT                          
SEQRES   1 C  565  ALA ALA TRP LYS TRP TRP GLU GLU GLU ARG TYR PRO GLU          
SEQRES   2 C  565  GLY ILE LYS TRP LYS PHE LEU GLU HIS LYS GLY PRO VAL          
SEQRES   3 C  565  PHE ALA PRO PRO TYR GLU PRO LEU PRO GLU ASN VAL LYS          
SEQRES   4 C  565  PHE TYR TYR ASP GLY LYS VAL MET LYS LEU SER PRO LYS          
SEQRES   5 C  565  ALA GLU GLU VAL ALA THR PHE PHE ALA LYS MET LEU ASP          
SEQRES   6 C  565  HIS GLU TYR THR THR LYS GLU ILE PHE ARG LYS ASN PHE          
SEQRES   7 C  565  PHE LYS ASP TRP ARG LYS GLU MET THR ASN GLU GLU LYS          
SEQRES   8 C  565  ASN ILE ILE THR ASN LEU SER LYS CYS ASP PHE THR GLN          
SEQRES   9 C  565  MET SER GLN TYR PHE LYS ALA GLN THR GLU ALA ARG LYS          
SEQRES  10 C  565  GLN MET SER LYS GLU GLU LYS LEU LYS ILE LYS GLU GLU          
SEQRES  11 C  565  ASN GLU LYS LEU LEU LYS GLU TYR GLY PHE CYS ILE MET          
SEQRES  12 C  565  ASP ASN HIS LYS GLU ARG ILE ALA ASN PHE LYS ILE GLU          
SEQRES  13 C  565  PRO PRO GLY LEU SER ARG GLY ARG GLY ASN HIS PRO LYS          
SEQRES  14 C  565  MET GLY MET LEU LYS ARG ARG ILE MET PRO GLU ASP ILE          
SEQRES  15 C  565  ILE ILE ASN CYS SER LYS ASP ALA LYS VAL PRO SER PRO          
SEQRES  16 C  565  PRO PRO GLY HIS LYS TRP LYS GLU VAL ARG HIS ASP ASN          
SEQRES  17 C  565  LYS VAL THR TRP LEU VAL SER TRP THR GLU ASN ILE GLN          
SEQRES  18 C  565  GLY SER ILE LYS TYR ILE MET LEU ASN PRO SER SER ARG          
SEQRES  19 C  565  ILE LYS GLY GLU LYS ASP TRP GLN LYS TYR GLU THR ALA          
SEQRES  20 C  565  ARG ARG LEU LYS LYS CYS VAL ASP LYS ILE ARG ASN GLN          
SEQRES  21 C  565  TYR ARG GLU ASP TRP LYS SER LYS GLU MET LYS VAL ARG          
SEQRES  22 C  565  GLN ARG ALA VAL ALA LEU TYR PHE ILE ASP LYS LEU ALA          
SEQRES  23 C  565  LEU ARG ALA GLY ASN GLU LYS GLU GLU GLY GLU THR ALA          
SEQRES  24 C  565  ASP THR VAL GLY CYS CYS SER LEU ARG VAL GLU HIS ILE          
SEQRES  25 C  565  ASN LEU HIS PRO GLU LEU ASP GLY GLN GLU TYR VAL VAL          
SEQRES  26 C  565  GLU PHE ASP PHE LEU GLY LYS ASP SER ILE ARG TYR TYR          
SEQRES  27 C  565  ASN LYS VAL PRO VAL GLU LYS ARG VAL PHE LYS ASN LEU          
SEQRES  28 C  565  GLN LEU PHE MET GLU ASN LYS GLN PRO GLU ASP ASP LEU          
SEQRES  29 C  565  PHE ASP ARG LEU ASN THR GLY ILE LEU ASN LYS HIS LEU          
SEQRES  30 C  565  GLN ASP LEU MET GLU GLY LEU THR ALA LYS VAL PHE ARG          
SEQRES  31 C  565  THR TYR ASN ALA SER ILE THR LEU GLN GLN GLN LEU LYS          
SEQRES  32 C  565  GLU LEU THR ALA PRO ASP GLU ASN ILE PRO ALA LYS ILE          
SEQRES  33 C  565  LEU SER TYR ASN ARG ALA ASN ARG ALA VAL ALA ILE LEU          
SEQRES  34 C  565  CYS ASN HIS GLN GLN ALA PRO PRO LYS THR PHE GLU LYS          
SEQRES  35 C  565  SER MET MET ASN LEU GLN THR LYS ILE ASP ALA LYS LYS          
SEQRES  36 C  565  GLU GLN LEU ALA ASP ALA ARG ARG ASP LEU LYS SER ALA          
SEQRES  37 C  565  LYS ALA ASP ALA LYS VAL MET LYS ASP ALA LYS THR LYS          
SEQRES  38 C  565  LYS VAL VAL GLU SER LYS LYS LYS ALA VAL GLN ARG LEU          
SEQRES  39 C  565  GLU GLU GLN LEU MET LYS LEU GLU VAL GLN ALA THR ASP          
SEQRES  40 C  565  ARG GLU GLU ASN LYS GLN ILE ALA LEU GLY THR SER LYS          
SEQRES  41 C  565  LEU ASN PTR LEU ASP PRO ARG ILE THR VAL ALA TRP CYS          
SEQRES  42 C  565  LYS LYS TRP GLY VAL PRO ILE GLU LYS ILE TYR ASN LYS          
SEQRES  43 C  565  THR GLN ARG GLU LYS PHE ALA TRP ALA ILE ASP MET ALA          
SEQRES  44 C  565  ASP GLU ASP TYR GLU PHE                                      
MODRES 1RR8 PTR C  723  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  C 723      16                                                       
HET    TTG  A1991      32                                                       
HET    TTC  A 100      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   *304(H2 O)                                                    
HELIX    1   1 SER C  250  LEU C  264  1                                  15    
HELIX    2   2 HIS C  266  THR C  270  5                                   5    
HELIX    3   3 LYS C  271  GLU C  285  1                                  15    
HELIX    4   4 THR C  287  ASN C  292  1                                   6    
HELIX    5   5 PHE C  302  LYS C  317  1                                  16    
HELIX    6   6 SER C  320  TYR C  338  1                                  19    
HELIX    7   7 MET C  378  ASP C  381  5                                   4    
HELIX    8   8 SER C  433  LYS C  452  1                                  20    
HELIX    9   9 CYS C  453  ASP C  464  1                                  12    
HELIX   10  10 GLU C  469  LEU C  485  1                                  17    
HELIX   11  11 ARG C  508  GLU C  510  5                                   3    
HELIX   12  12 LYS C  532  SER C  534  5                                   3    
HELIX   13  13 GLU C  544  GLU C  556  1                                  13    
HELIX   14  14 ASN C  569  MET C  581  1                                  13    
HELIX   15  15 LYS C  587  THR C  606  1                                  20    
HELIX   16  16 ASN C  611  CYS C  630  1                                  20    
HELIX   17  17 LEU C  716  PTR C  723  1                                   8    
HELIX   18  18 ASP C  725  GLY C  737  1                                  13    
HELIX   19  19 PRO C  739  ILE C  743  5                                   5    
HELIX   20  20 ASN C  745  PHE C  752  1                                   8    
HELIX   21  21 PHE C  752  MET C  758  1                                   7    
SHEET    1   A 3 LEU C 220  GLU C 221  0                                        
SHEET    2   A 3 PHE C 340  MET C 343 -1  O  ILE C 342   N  GLU C 221           
SHEET    3   A 3 HIS C 346  ARG C 349 -1  O  GLU C 348   N  CYS C 341           
SHEET    1   B 3 LYS C 245  VAL C 246  0                                        
SHEET    2   B 3 TYR C 241  TYR C 242 -1  N  TYR C 242   O  LYS C 245           
SHEET    3   B 3 CYS C 300  ASP C 301 -1  O  ASP C 301   N  TYR C 241           
SHEET    1   C 2 GLY C 359  LEU C 360  0                                        
SHEET    2   C 2 LEU C 373  LYS C 374 -1  O  LYS C 374   N  GLY C 359           
SHEET    1   D 4 GLU C 403  ARG C 405  0                                        
SHEET    2   D 4 ILE C 383  ASN C 385  1  N  ILE C 384   O  ARG C 405           
SHEET    3   D 4 VAL C 414  THR C 417 -1  O  SER C 415   N  ILE C 383           
SHEET    4   D 4 ILE C 424  ILE C 427 -1  O  LYS C 425   N  TRP C 416           
SHEET    1   E 3 ILE C 512  LEU C 518  0                                        
SHEET    2   E 3 GLN C 521  LEU C 530 -1  O  VAL C 524   N  HIS C 515           
SHEET    3   E 3 ARG C 536  PRO C 542 -1  O  TYR C 537   N  PHE C 529           
LINK         C   ASN C 722                 N   PTR C 723     1555   1555  1.33  
LINK         C   PTR C 723                 N   LEU C 724     1555   1555  1.34  
LINK         C21 TTC A 100                 C25 TTG A1991     1555   1555  1.86  
LINK         O26 TTC A 100                 C2  TTG A1991     1555   1555  1.42  
LINK         C30 TTC A 100                 N28 TTG A1991     1555   1555  1.61  
LINK         C29 TTC A 100                 N28 TTG A1991     1555   1555  1.39  
LINK         C31 TTC A 100                 C25 TTG A1991     1555   1555  1.49  
LINK         C25 TTC A 100                 C31 TTG A1991     1555   1555  1.67  
LINK         O24 TTC A 100                 C21 TTG A1991     1555   1555  1.65  
LINK         C16 TTC A 100                 C21 TTG A1991     1555   1555  1.51  
LINK         C25 TTC A 100                 C21 TTG A1991     1555   1555  1.32  
LINK         C20 TTC A 100                 C21 TTG A1991     1555   1555  1.76  
LINK         C21 TTC A 100                 O24 TTG A1991     1555   1555  1.26  
LINK         C21 TTC A 100                 C16 TTG A1991     1555   1555  1.71  
LINK         C15 TTC A 100                 C16 TTG A1991     1555   1555  1.24  
LINK         C17 TTC A 100                 C16 TTG A1991     1555   1555  1.48  
LINK         C21 TTC A 100                 C20 TTG A1991     1555   1555  1.47  
LINK         O23 TTC A 100                 C20 TTG A1991     1555   1555  1.23  
LINK         O22 TTC A 100                 C20 TTG A1991     1555   1555  1.53  
LINK         C16 TTC A 100                 C15 TTG A1991     1555   1555  1.61  
LINK         C14 TTC A 100                 C15 TTG A1991     1555   1555  1.41  
LINK         C19 TTC A 100                 C15 TTG A1991     1555   1555  1.58  
LINK         C16 TTC A 100                 C17 TTG A1991     1555   1555  1.43  
LINK         C13 TTC A 100                 C17 TTG A1991     1555   1555  1.31  
LINK         O22 TTC A 100                 O23 TTG A1991     1555   1555  1.84  
LINK         C20 TTC A 100                 O22 TTG A1991     1555   1555  1.41  
LINK         O23 TTC A 100                 O22 TTG A1991     1555   1555  1.63  
LINK         O22 TTC A 100                 O22 TTG A1991     1555   1555  1.76  
LINK         C15 TTC A 100                 C14 TTG A1991     1555   1555  1.80  
LINK         N12 TTC A 100                 C14 TTG A1991     1555   1555  1.36  
LINK         O18 TTC A 100                 C14 TTG A1991     1555   1555  1.16  
LINK         C15 TTC A 100                 C19 TTG A1991     1555   1555  1.66  
LINK         C17 TTC A 100                 C13 TTG A1991     1555   1555  1.55  
LINK         N12 TTC A 100                 C13 TTG A1991     1555   1555  1.26  
LINK         C9  TTC A 100                 C13 TTG A1991     1555   1555  1.40  
LINK         C14 TTC A 100                 O18 TTG A1991     1555   1555  1.46  
LINK         C14 TTC A 100                 N12 TTG A1991     1555   1555  1.47  
LINK         C13 TTC A 100                 N12 TTG A1991     1555   1555  1.48  
LINK         C11 TTC A 100                 N12 TTG A1991     1555   1555  1.37  
LINK         C13 TTC A 100                 C9  TTG A1991     1555   1555  1.43  
LINK         C8  TTC A 100                 C9  TTG A1991     1555   1555  1.41  
LINK         N10 TTC A 100                 C9  TTG A1991     1555   1555  1.40  
LINK         N12 TTC A 100                 C11 TTG A1991     1555   1555  1.69  
LINK         C8  TTC A 100                 C11 TTG A1991     1555   1555  1.50  
LINK         C7  TTC A 100                 C8  TTG A1991     1555   1555  1.31  
LINK         C9  TTC A 100                 C8  TTG A1991     1555   1555  1.56  
LINK         C11 TTC A 100                 C8  TTG A1991     1555   1555  1.56  
LINK         C5  TTC A 100                 N10 TTG A1991     1555   1555  1.44  
LINK         C9  TTC A 100                 N10 TTG A1991     1555   1555  1.30  
LINK         C6  TTC A 100                 C7  TTG A1991     1555   1555  1.45  
LINK         C8  TTC A 100                 C7  TTG A1991     1555   1555  1.43  
LINK         C6  TTC A 100                 C5  TTG A1991     1555   1555  1.44  
LINK         C4  TTC A 100                 C5  TTG A1991     1555   1555  1.42  
LINK         N10 TTC A 100                 C5  TTG A1991     1555   1555  1.39  
LINK         C7  TTC A 100                 C6  TTG A1991     1555   1555  1.47  
LINK         C5  TTC A 100                 C6  TTG A1991     1555   1555  1.44  
LINK         C1  TTC A 100                 C6  TTG A1991     1555   1555  1.45  
LINK         C5  TTC A 100                 C4  TTG A1991     1555   1555  1.33  
LINK         C3  TTC A 100                 C4  TTG A1991     1555   1555  1.48  
LINK         C6  TTC A 100                 C1  TTG A1991     1555   1555  1.45  
LINK         C2  TTC A 100                 C1  TTG A1991     1555   1555  1.41  
LINK         C27 TTC A 100                 C1  TTG A1991     1555   1555  1.58  
LINK         C4  TTC A 100                 C3  TTG A1991     1555   1555  1.35  
LINK         C2  TTC A 100                 C3  TTG A1991     1555   1555  1.44  
LINK         C1  TTC A 100                 C2  TTG A1991     1555   1555  1.44  
LINK         C3  TTC A 100                 C2  TTG A1991     1555   1555  1.36  
LINK         C1  TTC A 100                 C27 TTG A1991     1555   1555  1.52  
LINK         N28 TTC A 100                 C27 TTG A1991     1555   1555  1.60  
LINK         C27 TTC A 100                 N28 TTG A1991     1555   1555  1.36  
LINK         N28 TTC A 100                 C29 TTG A1991     1555   1555  1.67  
LINK         N28 TTC A 100                 C30 TTG A1991     1555   1555  1.47  
LINK         C2  TTC A 100                 O26 TTG A1991     1555   1555  1.35  
LINK         C19 TTC A 100                 O19 TTG A1991     1555   1555  1.47  
LINK         O   PTR C 723                 N   LEU C 724     1555   1555  1.80  
SITE     1 AC1 13  DT A  10   DG A  11   DG A  12  TTC A 100                    
SITE     2 AC1 13 HOH A 886   DC B 112   DA B 113  GLU C 356                    
SITE     3 AC1 13 ARG C 364  LYS C 532  ASP C 533  THR C 718                    
SITE     4 AC1 13 ASN C 722                                                     
SITE     1 AC2 14  DT A  10   DG A  11   DG A  12  HOH A 886                    
SITE     2 AC2 14 TTG A1991   DC B 112   DA B 113  HOH B 878                    
SITE     3 AC2 14 GLU C 356  ARG C 364  LYS C 532  ASP C 533                    
SITE     4 AC2 14 THR C 718  PTR C 723                                          
CRYST1   57.590  115.585   75.010  90.00  96.29  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      0.017364  0.000000  0.001914        0.00000                         
SCALE2      0.000000  0.008652  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013412        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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