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Database: PDB
Entry: 1A36
LinkDB: 1A36
Original site: 1A36 
HEADER    ISOMERASE/DNA                           29-JAN-98   1A36              
TITLE     TOPOISOMERASE I/DNA COMPLEX                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (5'-                                                   
COMPND   3 D(*AP*AP*AP*AP*AP*GP*AP*CP*TP*TP*AP*GP*AP*AP*AP*AP*A                 
COMPND   4 P*TP*TP*TP*TP*T)- 3');                                               
COMPND   5 CHAIN: B;                                                            
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA (5'-                                                   
COMPND   9 D(*AP*AP*AP*AP*AP*TP*TP*TP*TP*TP*CP*TP*AP*AP*GP*TP*C                 
COMPND  10 P*TP*TP*TP*TP*T)- 3');                                               
COMPND  11 CHAIN: C;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: TOPOISOMERASE I;                                           
COMPND  15 CHAIN: A;                                                            
COMPND  16 FRAGMENT: CORE DOMAIN AND C-TERMINAL DOMAIN;                         
COMPND  17 EC: 5.99.1.2;                                                        
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 MOL_ID: 2;                                                           
SOURCE   4 SYNTHETIC: YES;                                                      
SOURCE   5 MOL_ID: 3;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606;                                                
SOURCE   9 CELLULAR_LOCATION: NUCLEUS;                                          
SOURCE  10 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  11 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  13 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS                                
KEYWDS    COMPLEX (ISOMERASE/DNA), DNA, TOPOISOMERASE I                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.STEWART,M.R.REDINBO,X.QIU,J.J.CHAMPOUX,W.G.J.HOL                    
REVDAT   2   24-FEB-09 1A36    1       VERSN                                    
REVDAT   1   12-AUG-98 1A36    0                                                
JRNL        AUTH   L.STEWART,M.R.REDINBO,X.QIU,W.G.HOL,J.J.CHAMPOUX             
JRNL        TITL   A MODEL FOR THE MECHANISM OF HUMAN TOPOISOMERASE I.          
JRNL        REF    SCIENCE                       V. 279  1534 1998              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   9488652                                                      
JRNL        DOI    10.1126/SCIENCE.279.5356.1534                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 21217                          
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) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.312                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1445                            
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           : 25                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.84                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 710                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3220                       
REMARK   3   BIN FREE R VALUE                    : 0.4450                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 41                           
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            : 4332                                    
REMARK   3   NUCLEIC ACID ATOMS       : 896                                     
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 57                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.84000                                             
REMARK   3    B22 (A**2) : 1.35400                                              
REMARK   3    B33 (A**2) : 6.48600                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.05000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.58                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.51                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM_NDBX.DNA                                 
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOP_NDBX.DNA                                   
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1A36 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : MAY-95                             
REMARK 200  TEMPERATURE           (KELVIN) : 100.00                             
REMARK 200  PH                             : 7.70                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL1-5                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : UNKNOWN                            
REMARK 200  OPTICS                         : UNKNOWN                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : FUJI                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21217                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.05500                            
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) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30500                            
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: RIGID BODY REFINEMENT        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: RECONSTITUTED HUMAN TOPOISOMERASE I COVALENT         
REMARK 200  COMPLEX WITH 22 BASE PAIR DUPLEX DNA                                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.70                                  
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       59.20000            
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400                                                                      
REMARK 400 NOTE THAT RESIDUES 174 - 214 AND 634 - 640 OF CHAIN A ARE            
REMARK 400 DISORDERED AND ARE NOT PRESENT IN THE MODEL.  1-22 OF                
REMARK 400 CHAIN C COMPRISE THE SCISSILE STRAND OF THE DNA, 101-122 OF          
REMARK 400 CHAIN D THE INTACT DNA STRAND.                                       
REMARK 400                                                                      
REMARK 400 TER                                                                  
REMARK 400  PHE 765 A IS THE C-TERMINAL RESIDUE OF THE 70 KDA FRAGMENT          
REMARK 400  OF HUMAN TOPO I.                                                    
REMARK 400  THY 22 C IS THE 3' TERMINAL NUCLEOTIDE ON THE SCISSILE              
REMARK 400  STRAND OF THE DNA DUPLEX.                                           
REMARK 400  THY 122 D IS THE 3' TERMINAL NUCLEOTIDE ON THE INTACT               
REMARK 400  STRAND OF THE DNA DUPLEX.                                           
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A   175                                                      
REMARK 465     PRO A   176                                                      
REMARK 465     LYS A   177                                                      
REMARK 465     ASN A   178                                                      
REMARK 465     LYS A   179                                                      
REMARK 465     ASP A   180                                                      
REMARK 465     LYS A   181                                                      
REMARK 465     ASP A   182                                                      
REMARK 465     LYS A   183                                                      
REMARK 465     LYS A   184                                                      
REMARK 465     VAL A   185                                                      
REMARK 465     PRO A   186                                                      
REMARK 465     GLU A   187                                                      
REMARK 465     PRO A   188                                                      
REMARK 465     ASP A   189                                                      
REMARK 465     ASN A   190                                                      
REMARK 465     LYS A   191                                                      
REMARK 465     LYS A   192                                                      
REMARK 465     LYS A   193                                                      
REMARK 465     LYS A   194                                                      
REMARK 465     PRO A   195                                                      
REMARK 465     LYS A   196                                                      
REMARK 465     LYS A   197                                                      
REMARK 465     GLU A   198                                                      
REMARK 465     GLU A   199                                                      
REMARK 465     GLU A   200                                                      
REMARK 465     GLN A   201                                                      
REMARK 465     LYS A   202                                                      
REMARK 465     TRP A   203                                                      
REMARK 465     LYS A   204                                                      
REMARK 465     TRP A   205                                                      
REMARK 465     TRP A   206                                                      
REMARK 465     GLU A   207                                                      
REMARK 465     GLU A   208                                                      
REMARK 465     GLU A   209                                                      
REMARK 465     ARG A   210                                                      
REMARK 465     TYR A   211                                                      
REMARK 465     PRO A   212                                                      
REMARK 465     GLU A   213                                                      
REMARK 465     GLY A   214                                                      
REMARK 465     ARG A   634                                                      
REMARK 465     ALA A   635                                                      
REMARK 465     PRO A   636                                                      
REMARK 465     PRO A   637                                                      
REMARK 465     LYS A   638                                                      
REMARK 465     THR A   639                                                      
REMARK 465     PHE A   640                                                      
REMARK 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     LYS A 248    CG   CD   CE   NZ                                   
REMARK 470     LYS A 276    CG   CD   CE   NZ                                   
REMARK 470     GLU A 289    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 314    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 316    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 317    CG   CD   CE   NZ                                   
REMARK 470     GLN A 318    CG   CD   OE1  NE2                                  
REMARK 470     MET A 319    CG   SD   CE                                        
REMARK 470     LYS A 321    CG   CD   CE   NZ                                   
REMARK 470     GLU A 322    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 323    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 326    CG   CD   CE   NZ                                   
REMARK 470     GLU A 332    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 333    CG   CD   CE   NZ                                   
REMARK 470     ARG A 462    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 463    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 466    CG   CD   CE   NZ                                   
REMARK 470     LYS A 468    CG   CD   CE   NZ                                   
REMARK 470     LYS A 471    CG   CD   CE   NZ                                   
REMARK 470     LYS A 484    CG   CD   CE   NZ                                   
REMARK 470     GLU A 495    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 546    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 582    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 609    CG   OD1  OD2                                       
REMARK 470     GLU A 610    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 611    CG   OD1  ND2                                       
REMARK 470     GLN A 633    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 641    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 642    CG   CD   CE   NZ                                   
REMARK 470     SER A 643    OG                                                  
REMARK 470     MET A 644    CG   SD   CE                                        
REMARK 470     MET A 645    CG   SD   CE                                        
REMARK 470     ASN A 646    CG   OD1  ND2                                       
REMARK 470     ASP A 660    CG   OD1  OD2                                       
REMARK 470     VAL A 674    CG1  CG2                                            
REMARK 470     ARG A 693    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 696    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 712    CG   CD   CE   NZ                                   
REMARK 470     LYS A 735    CG   CD   CE   NZ                                   
REMARK 470     GLU A 741    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 742    CG   CD   CE   NZ                                   
REMARK 470     ASP A 760    CG   OD1  OD2                                       
REMARK 470     ASP A 762    CG   OD1  OD2                                       
REMARK 470     GLU A 764    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500     DA C 103   C3' -  C2' -  C1' ANGL. DEV. =  -5.8 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 265       31.23    -90.93                                   
REMARK 500    GLU A 272      -71.97    -62.50                                   
REMARK 500    ILE A 293      -61.55    -95.36                                   
REMARK 500    MET A 319      157.73    -45.10                                   
REMARK 500    ASP A 344     -127.85     55.54                                   
REMARK 500    ALA A 351      -72.84    -77.19                                   
REMARK 500    GLU A 403      141.44   -179.92                                   
REMARK 500    ASN A 459        1.43    -68.10                                   
REMARK 500    ASP A 519       38.19     39.27                                   
REMARK 500    PHE A 565       69.56   -108.02                                   
REMARK 500    CYS A 630        0.75    -68.85                                   
REMARK 500    LYS A 642       32.64    -74.63                                   
REMARK 500    LEU A 647      -74.26    -56.20                                   
REMARK 500    ASP A 677      -97.43    -47.90                                   
REMARK 500    ALA A 678      -50.80   -175.74                                   
REMARK 500    GLU A 696      -74.77    -56.37                                   
REMARK 500    ASP A 707      -71.01    -69.36                                   
REMARK 500    ASN A 711       45.69   -106.33                                   
REMARK 500    ASP A 762       31.85    -94.91                                   
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     DT C 108         0.08    SIDE_CHAIN                              
REMARK 500     DG C 115         0.07    SIDE_CHAIN                              
REMARK 500     DT C 121         0.08    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 A1025        DISTANCE =  7.26 ANGSTROMS                       
DBREF  1A36 A  175   765  UNP    P11387   TOP1_HUMAN     174    765             
DBREF  1A36 B    1    22  PDB    1A36     1A36             1     22             
DBREF  1A36 C  101   122  PDB    1A36     1A36           101    122             
SEQADV 1A36 PHE A  723  UNP  P11387    TYR   723 ENGINEERED                     
SEQRES   1 B   22   DA  DA  DA  DA  DA  DG  DA  DC  DT  DT  DA  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  DT  DA          
SEQRES   2 C   22   DA  DG  DT  DC  DT  DT  DT  DT  DT                          
SEQRES   1 A  591  LYS PRO LYS ASN LYS ASP LYS ASP LYS LYS VAL PRO GLU          
SEQRES   2 A  591  PRO ASP ASN LYS LYS LYS LYS PRO LYS LYS GLU GLU GLU          
SEQRES   3 A  591  GLN LYS TRP LYS TRP TRP GLU GLU GLU ARG TYR PRO GLU          
SEQRES   4 A  591  GLY ILE LYS TRP LYS PHE LEU GLU HIS LYS GLY PRO VAL          
SEQRES   5 A  591  PHE ALA PRO PRO TYR GLU PRO LEU PRO GLU ASN VAL LYS          
SEQRES   6 A  591  PHE TYR TYR ASP GLY LYS VAL MET LYS LEU SER PRO LYS          
SEQRES   7 A  591  ALA GLU GLU VAL ALA THR PHE PHE ALA LYS MET LEU ASP          
SEQRES   8 A  591  HIS GLU TYR THR THR LYS GLU ILE PHE ARG LYS ASN PHE          
SEQRES   9 A  591  PHE LYS ASP TRP ARG LYS GLU MET THR ASN GLU GLU LYS          
SEQRES  10 A  591  ASN ILE ILE THR ASN LEU SER LYS CYS ASP PHE THR GLN          
SEQRES  11 A  591  MET SER GLN TYR PHE LYS ALA GLN THR GLU ALA ARG LYS          
SEQRES  12 A  591  GLN MET SER LYS GLU GLU LYS LEU LYS ILE LYS GLU GLU          
SEQRES  13 A  591  ASN GLU LYS LEU LEU LYS GLU TYR GLY PHE CYS ILE MET          
SEQRES  14 A  591  ASP ASN HIS LYS GLU ARG ILE ALA ASN PHE LYS ILE GLU          
SEQRES  15 A  591  PRO PRO GLY LEU PHE ARG GLY ARG GLY ASN HIS PRO LYS          
SEQRES  16 A  591  MET GLY MET LEU LYS ARG ARG ILE MET PRO GLU ASP ILE          
SEQRES  17 A  591  ILE ILE ASN CYS SER LYS ASP ALA LYS VAL PRO SER PRO          
SEQRES  18 A  591  PRO PRO GLY HIS LYS TRP LYS GLU VAL ARG HIS ASP ASN          
SEQRES  19 A  591  LYS VAL THR TRP LEU VAL SER TRP THR GLU ASN ILE GLN          
SEQRES  20 A  591  GLY SER ILE LYS TYR ILE MET LEU ASN PRO SER SER ARG          
SEQRES  21 A  591  ILE LYS GLY GLU LYS ASP TRP GLN LYS TYR GLU THR ALA          
SEQRES  22 A  591  ARG ARG LEU LYS LYS CYS VAL ASP LYS ILE ARG ASN GLN          
SEQRES  23 A  591  TYR ARG GLU ASP TRP LYS SER LYS GLU MET LYS VAL ARG          
SEQRES  24 A  591  GLN ARG ALA VAL ALA LEU TYR PHE ILE ASP LYS LEU ALA          
SEQRES  25 A  591  LEU ARG ALA GLY ASN GLU LYS GLU GLU GLY GLU THR ALA          
SEQRES  26 A  591  ASP THR VAL GLY CYS CYS SER LEU ARG VAL GLU HIS ILE          
SEQRES  27 A  591  ASN LEU HIS PRO GLU LEU ASP GLY GLN GLU TYR VAL VAL          
SEQRES  28 A  591  GLU PHE ASP PHE LEU GLY LYS ASP SER ILE ARG TYR TYR          
SEQRES  29 A  591  ASN LYS VAL PRO VAL GLU LYS ARG VAL PHE LYS ASN LEU          
SEQRES  30 A  591  GLN LEU PHE MET GLU ASN LYS GLN PRO GLU ASP ASP LEU          
SEQRES  31 A  591  PHE ASP ARG LEU ASN THR GLY ILE LEU ASN LYS HIS LEU          
SEQRES  32 A  591  GLN ASP LEU MET GLU GLY LEU THR ALA LYS VAL PHE ARG          
SEQRES  33 A  591  THR TYR ASN ALA SER ILE THR LEU GLN GLN GLN LEU LYS          
SEQRES  34 A  591  GLU LEU THR ALA PRO ASP GLU ASN ILE PRO ALA LYS ILE          
SEQRES  35 A  591  LEU SER TYR ASN ARG ALA ASN ARG ALA VAL ALA ILE LEU          
SEQRES  36 A  591  CYS ASN HIS GLN ARG ALA PRO PRO LYS THR PHE GLU LYS          
SEQRES  37 A  591  SER MET MET ASN LEU GLN THR LYS ILE ASP ALA LYS LYS          
SEQRES  38 A  591  GLU GLN LEU ALA ASP ALA ARG ARG ASP LEU LYS SER ALA          
SEQRES  39 A  591  LYS ALA ASP ALA LYS VAL MET LYS ASP ALA LYS THR LYS          
SEQRES  40 A  591  LYS VAL VAL GLU SER LYS LYS LYS ALA VAL GLN ARG LEU          
SEQRES  41 A  591  GLU GLU GLN LEU MET LYS LEU GLU VAL GLN ALA THR ASP          
SEQRES  42 A  591  ARG GLU GLU ASN LYS GLN ILE ALA LEU GLY THR SER LYS          
SEQRES  43 A  591  LEU ASN PHE LEU ASP PRO ARG ILE THR VAL ALA TRP CYS          
SEQRES  44 A  591  LYS LYS TRP GLY VAL PRO ILE GLU LYS ILE TYR ASN LYS          
SEQRES  45 A  591  THR GLN ARG GLU LYS PHE ALA TRP ALA ILE ASP MET ALA          
SEQRES  46 A  591  ASP GLU ASP TYR GLU PHE                                      
FORMUL   4  HOH   *57(H2 O)                                                     
HELIX    1   1 PRO A  251  MET A  263  1                                  13    
HELIX    2   2 GLU A  267  THR A  270  5                                   4    
HELIX    3   3 GLU A  272  GLU A  285  1                                  14    
HELIX    4   4 ASN A  288  ILE A  293  1                                   6    
HELIX    5   5 THR A  303  GLN A  318  1                                  16    
HELIX    6   6 LYS A  321  TYR A  338  1                                  18    
HELIX    7   7 PRO A  379  ASP A  381  5                                   3    
HELIX    8   8 ARG A  434  ASP A  464  1                                  31    
HELIX    9   9 VAL A  472  LYS A  484  1                                  13    
HELIX   10  10 CYS A  504  SER A  506  5                                   3    
HELIX   11  11 VAL A  509  HIS A  511  5                                   3    
HELIX   12  12 LYS A  532  SER A  534  5                                   3    
HELIX   13  13 LYS A  545  MET A  555  1                                  11    
HELIX   14  14 THR A  570  LEU A  580  1                                  11    
HELIX   15  15 ALA A  586  LEU A  605  1                                  20    
HELIX   16  16 ILE A  612  LEU A  629  1                                  18    
HELIX   17  17 SER A  643  VAL A  674  1                                  32    
HELIX   18  18 LYS A  679  GLU A  710  1                                  32    
HELIX   19  19 SER A  719  ASN A  722  1                                   4    
HELIX   20  20 PRO A  726  TRP A  736  5                                  11    
HELIX   21  21 ILE A  740  LYS A  742  5                                   3    
HELIX   22  22 LYS A  746  LYS A  751  1                                   6    
HELIX   23  23 ALA A  753  ASP A  757  1                                   5    
SHEET    1   A 2 PHE A 240  TYR A 242  0                                        
SHEET    2   A 2 LYS A 245  MET A 247 -1  N  MET A 247   O  PHE A 240           
SHEET    1   B 2 PHE A 340  MET A 343  0                                        
SHEET    2   B 2 HIS A 346  ARG A 349 -1  N  GLU A 348   O  CYS A 341           
SHEET    1   C 2 ILE A 383  ASN A 385  0                                        
SHEET    2   C 2 GLU A 403  ARG A 405  1  N  GLU A 403   O  ILE A 384           
SHEET    1   D 2 VAL A 414  THR A 417  0                                        
SHEET    2   D 2 ILE A 424  ILE A 427 -1  N  ILE A 427   O  VAL A 414           
SHEET    1   E 3 ILE A 512  HIS A 515  0                                        
SHEET    2   E 3 VAL A 524  LEU A 530 -1  N  GLU A 526   O  ASN A 513           
SHEET    3   E 3 ARG A 536  PRO A 542 -1  N  VAL A 541   O  VAL A 525           
CRYST1   56.500  118.400   71.500  90.00 101.20  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      0.017699  0.000000  0.003505        0.00000                         
SCALE2      0.000000  0.008446  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014258        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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