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Database: PDB
Entry: 1R49
LinkDB: 1R49
Original site: 1R49 
HEADER    ISOMERASE/DNA                           03-OCT-03   1R49              
TITLE     HUMAN TOPOISOMERASE I (TOPO70) DOUBLE MUTANT K532R/Y723F              
CAVEAT     1R49    CHIRALITY ERRORS AT LYS204A AND GLU208A                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-                                                        
COMPND   3 D(*AP*AP*AP*AP*AP*GP*AP*CP*TP*TP*AP*GP*AP*AP*AP*AP*AP*TP*TP          
COMPND   4 *TP*TP*T)-3';                                                        
COMPND   5 CHAIN: B;                                                            
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: 5'-                                                        
COMPND   9 D(P*AP*AP*AP*AP*AP*TP*TP*TP*TP*TP*CP*TP*AP*AP*GP*TP*CP*TP*T          
COMPND  10 P*TP*TP*T)-3';                                                       
COMPND  11 CHAIN: C;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: DNA TOPOISOMERASE I;                                       
COMPND  15 CHAIN: A;                                                            
COMPND  16 FRAGMENT: TOPO70;                                                    
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 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_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    PROTEIN, DNA, TOPOISOMERASE I, ISOMERASE/DNA COMPLEX                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.INTERTHAL,P.M.QUIGLEY,W.G.HOL,J.J.CHAMPOUX                          
REVDAT   3   24-FEB-09 1R49    1       VERSN                                    
REVDAT   2   30-MAR-04 1R49    1       JRNL                                     
REVDAT   1   16-DEC-03 1R49    0                                                
JRNL        AUTH   H.INTERTHAL,P.M.QUIGLEY,W.G.HOL,J.J.CHAMPOUX                 
JRNL        TITL   THE ROLE OF LYSINE 532 IN THE CATALYTIC MECHANISM            
JRNL        TITL 2 OF HUMAN TOPOISOMERASE I.                                    
JRNL        REF    J.BIOL.CHEM.                  V. 279  2984 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   14594810                                                     
JRNL        DOI    10.1074/JBC.M309959200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.13 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.13                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 14675                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.280                           
REMARK   3   R VALUE            (WORKING SET) : 0.277                           
REMARK   3   FREE R VALUE                     : 0.339                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 821                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.13                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 621                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3570                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 28                           
REMARK   3   BIN FREE R VALUE                    : 0.5360                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4527                                    
REMARK   3   NUCLEIC ACID ATOMS       : 897                                     
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 29                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.23000                                             
REMARK   3    B22 (A**2) : -0.37000                                             
REMARK   3    B33 (A**2) : 0.59000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.04000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.656         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.887                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.841                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5560 ; 0.004 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7645 ; 0.763 ; 2.162       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   540 ; 4.590 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   774 ; 0.060 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3872 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2682 ; 0.223 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   285 ; 0.216 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    54 ; 0.235 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.267 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2725 ; 5.686 ; 3.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4394 ; 9.138 ; 6.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2835 ;14.551 ; 8.800       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3251 ;19.426 ;12.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1R49 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB020417.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15514                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.130                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.13                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 64.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.28000                            
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350 MME, MAGNESIUM CHLORIDE,        
REMARK 280  MES, TCEP, PH 7.5, VAPOR DIFFUSION, TEMPERATURE 298K                
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       59.31900            
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A   174                                                      
REMARK 465     LYS A   175                                                      
REMARK 465     PRO A   176                                                      
REMARK 465     LYS A   177                                                      
REMARK 465     ASN A   178                                                      
REMARK 465     LYS A   179                                                      
REMARK 465     ASP A   180                                                      
REMARK 465     LYS A   181                                                      
REMARK 465     ASP A   182                                                      
REMARK 465     LYS A   183                                                      
REMARK 465     LYS A   184                                                      
REMARK 465     VAL A   185                                                      
REMARK 465     PRO A   186                                                      
REMARK 465     GLU A   187                                                      
REMARK 465     PRO A   188                                                      
REMARK 465     ASP A   189                                                      
REMARK 465     ASN A   190                                                      
REMARK 465     LYS A   191                                                      
REMARK 465     LYS A   192                                                      
REMARK 465     LYS A   193                                                      
REMARK 465     LYS A   194                                                      
REMARK 465     PRO A   195                                                      
REMARK 465     LYS A   196                                                      
REMARK 465     LYS A   197                                                      
REMARK 465     GLU A   198                                                      
REMARK 465     GLU A   199                                                      
REMARK 465     GLU A   200                                                      
REMARK 465     GLN A   201                                                      
REMARK 465     LYS A   388                                                      
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 465     GLU A   641                                                      
REMARK 465     LYS A   642                                                      
REMARK 465     SER A   643                                                      
REMARK 465     ILE A   714                                                      
REMARK 465     ALA A   715                                                      
REMARK 465     LEU A   716                                                      
REMARK 465     GLY A   717                                                      
REMARK 465     THR A   718                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470      DT B  20    C7                                                  
REMARK 470      DT C 112    C7                                                  
REMARK 470     LYS A 202    CG   CD   CE   NZ                                   
REMARK 470     TRP A 203    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 203    CZ3  CH2                                            
REMARK 470     ILE A 273    CD1                                                 
REMARK 470     ILE A 293    CD1                                                 
REMARK 470     ILE A 294    CD1                                                 
REMARK 470     ILE A 327    CD1                                                 
REMARK 470     ILE A 342    CD1                                                 
REMARK 470     ILE A 350    CD1                                                 
REMARK 470     ILE A 355    CD1                                                 
REMARK 470     ILE A 377    CD1                                                 
REMARK 470     ILE A 382    CD1                                                 
REMARK 470     ILE A 383    CD1                                                 
REMARK 470     ILE A 384    CD1                                                 
REMARK 470     ILE A 420    CD1                                                 
REMARK 470     ILE A 424    CD1                                                 
REMARK 470     ILE A 427    CD1                                                 
REMARK 470     ILE A 435    CD1                                                 
REMARK 470     ILE A 457    CD1                                                 
REMARK 470     ILE A 482    CD1                                                 
REMARK 470     ILE A 512    CD1                                                 
REMARK 470     ILE A 535    CD1                                                 
REMARK 470     ILE A 572    CD1                                                 
REMARK 470     ILE A 612    CD1                                                 
REMARK 470     ILE A 616    CD1                                                 
REMARK 470     ILE A 628    CD1                                                 
REMARK 470     ILE A 651    CD1                                                 
REMARK 470     ILE A 728    CD1                                                 
REMARK 470     ILE A 740    CD1                                                 
REMARK 470     ILE A 743    CD1                                                 
REMARK 470     ILE A 756    CD1                                                 
REMARK 470     PHE A 765    O                                                   
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A  202   C     O     CB                                      
REMARK 480     TRP A  203   N     C                                             
REMARK 480     LYS A  204   CB    CG    CD    CE    NZ                          
REMARK 480     TRP A  205   CB    CG    CD1   CD2   NE1   CE2   CE3             
REMARK 480     TRP A  205   CZ3   CH2                                           
REMARK 480     TRP A  206   CA    CB    CG    CD1   CD2   NE1   CE2             
REMARK 480     TRP A  206   CE3   CZ2   CZ3   CH2                               
REMARK 480     GLU A  207   CB    CG    CD    OE1   OE2                         
REMARK 480     GLU A  208   CB    CG    CD    OE1   OE2                         
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   O    GLU A   255     OG1  THR A   258              2.04            
REMARK 500   O    ARG A   532     N    SER A   534              2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS A   204     OE2  GLU A   272     1455     0.42            
REMARK 500   NZ   LYS A   204     CD   GLU A   272     1455     1.23            
REMARK 500   CE   LYS A   204     OE2  GLU A   272     1455     1.54            
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     DT B   9   C5     DT B   9   C7     -0.096                       
REMARK 500     DT B  10   C5     DT B  10   C7     -0.096                       
REMARK 500     DT B  18   C5     DT B  18   C7     -0.097                       
REMARK 500     DT B  19   C5     DT B  19   C7     -0.097                       
REMARK 500     DT B  21   C5     DT B  21   C7     -0.097                       
REMARK 500     DT B  22   C5     DT B  22   C7     -0.096                       
REMARK 500     DT C 106   C5     DT C 106   C7     -0.096                       
REMARK 500     DT C 107   C5     DT C 107   C7     -0.097                       
REMARK 500     DT C 108   C5     DT C 108   C7     -0.097                       
REMARK 500     DT C 109   C5     DT C 109   C7     -0.097                       
REMARK 500     DT C 110   C5     DT C 110   C7     -0.097                       
REMARK 500     DT C 116   C5     DT C 116   C7     -0.096                       
REMARK 500     DT C 118   C5     DT C 118   C7     -0.097                       
REMARK 500     DT C 119   C5     DT C 119   C7     -0.097                       
REMARK 500     DT C 120   C5     DT C 120   C7     -0.097                       
REMARK 500     DT C 121   C5     DT C 121   C7     -0.096                       
REMARK 500     DT C 122   C5     DT C 122   C7     -0.097                       
REMARK 500    TRP A 203   N     TRP A 203   CA      0.214                       
REMARK 500    TRP A 203   CA    TRP A 203   C       0.660                       
REMARK 500    TRP A 203   C     TRP A 203   O       0.271                       
REMARK 500    LYS A 204   CA    LYS A 204   CB     -0.272                       
REMARK 500    TRP A 203   C     LYS A 204   N       0.276                       
REMARK 500    TRP A 205   CH2   TRP A 205   CZ2     0.197                       
REMARK 500    GLU A 208   CA    GLU A 208   CB     -0.187                       
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     DT B   9   C4  -  C5  -  C7  ANGL. DEV. =   4.4 DEGREES          
REMARK 500     DT B   9   C6  -  C5  -  C7  ANGL. DEV. =  -5.5 DEGREES          
REMARK 500     DT B  10   C4  -  C5  -  C7  ANGL. DEV. =   4.4 DEGREES          
REMARK 500     DT B  10   C6  -  C5  -  C7  ANGL. DEV. =  -5.5 DEGREES          
REMARK 500     DT B  18   C4  -  C5  -  C7  ANGL. DEV. =   4.4 DEGREES          
REMARK 500     DT B  18   C6  -  C5  -  C7  ANGL. DEV. =  -5.5 DEGREES          
REMARK 500     DT B  19   C4  -  C5  -  C7  ANGL. DEV. =   4.4 DEGREES          
REMARK 500     DT B  19   C6  -  C5  -  C7  ANGL. DEV. =  -5.7 DEGREES          
REMARK 500     DT B  21   C4  -  C5  -  C7  ANGL. DEV. =   4.4 DEGREES          
REMARK 500     DT B  21   C6  -  C5  -  C7  ANGL. DEV. =  -5.6 DEGREES          
REMARK 500     DT B  22   C4  -  C5  -  C7  ANGL. DEV. =   4.6 DEGREES          
REMARK 500     DT B  22   C6  -  C5  -  C7  ANGL. DEV. =  -5.4 DEGREES          
REMARK 500     DT C 106   C4  -  C5  -  C7  ANGL. DEV. =   4.6 DEGREES          
REMARK 500     DT C 106   C6  -  C5  -  C7  ANGL. DEV. =  -5.3 DEGREES          
REMARK 500     DT C 107   C4  -  C5  -  C7  ANGL. DEV. =   4.5 DEGREES          
REMARK 500     DT C 107   C6  -  C5  -  C7  ANGL. DEV. =  -5.5 DEGREES          
REMARK 500     DT C 108   C4  -  C5  -  C7  ANGL. DEV. =   4.4 DEGREES          
REMARK 500     DT C 108   C6  -  C5  -  C7  ANGL. DEV. =  -5.5 DEGREES          
REMARK 500     DT C 109   C4  -  C5  -  C7  ANGL. DEV. =   4.5 DEGREES          
REMARK 500     DT C 109   C6  -  C5  -  C7  ANGL. DEV. =  -5.5 DEGREES          
REMARK 500     DT C 110   C4  -  C5  -  C7  ANGL. DEV. =   4.5 DEGREES          
REMARK 500     DT C 110   C6  -  C5  -  C7  ANGL. DEV. =  -5.5 DEGREES          
REMARK 500     DC C 111   O4' -  C1' -  N1  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DT C 112   O4' -  C1' -  N1  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DT C 116   C4  -  C5  -  C7  ANGL. DEV. =   4.5 DEGREES          
REMARK 500     DT C 116   C6  -  C5  -  C7  ANGL. DEV. =  -5.1 DEGREES          
REMARK 500     DT C 118   C4  -  C5  -  C7  ANGL. DEV. =   4.3 DEGREES          
REMARK 500     DT C 118   C6  -  C5  -  C7  ANGL. DEV. =  -5.8 DEGREES          
REMARK 500     DT C 119   C4  -  C5  -  C7  ANGL. DEV. =   4.3 DEGREES          
REMARK 500     DT C 119   C6  -  C5  -  C7  ANGL. DEV. =  -5.6 DEGREES          
REMARK 500     DT C 120   C4  -  C5  -  C7  ANGL. DEV. =   4.4 DEGREES          
REMARK 500     DT C 120   C6  -  C5  -  C7  ANGL. DEV. =  -5.6 DEGREES          
REMARK 500     DT C 121   C4  -  C5  -  C7  ANGL. DEV. =   4.6 DEGREES          
REMARK 500     DT C 121   C6  -  C5  -  C7  ANGL. DEV. =  -5.5 DEGREES          
REMARK 500     DT C 122   C4  -  C5  -  C7  ANGL. DEV. =   4.3 DEGREES          
REMARK 500     DT C 122   C6  -  C5  -  C7  ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    LYS A 202   CB  -  CA  -  C   ANGL. DEV. =  16.3 DEGREES          
REMARK 500    TRP A 203   CB  -  CA  -  C   ANGL. DEV. = -35.7 DEGREES          
REMARK 500    TRP A 203   N   -  CA  -  CB  ANGL. DEV. = -27.8 DEGREES          
REMARK 500    TRP A 203   N   -  CA  -  C   ANGL. DEV. = -37.0 DEGREES          
REMARK 500    TRP A 203   C   -  N   -  CA  ANGL. DEV. = -24.9 DEGREES          
REMARK 500    LYS A 204   CB  -  CA  -  C   ANGL. DEV. =  28.6 DEGREES          
REMARK 500    LYS A 204   CA  -  CB  -  CG  ANGL. DEV. =  26.3 DEGREES          
REMARK 500    TRP A 203   CA  -  C   -  N   ANGL. DEV. =  13.9 DEGREES          
REMARK 500    TRP A 203   O   -  C   -  N   ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    LYS A 204   C   -  N   -  CA  ANGL. DEV. =  20.7 DEGREES          
REMARK 500    TRP A 205   N   -  CA  -  CB  ANGL. DEV. =  23.9 DEGREES          
REMARK 500    TRP A 205   CD2 -  CE2 -  CZ2 ANGL. DEV. = -15.1 DEGREES          
REMARK 500    TRP A 205   CG  -  CD2 -  CE3 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    TRP A 205   CZ3 -  CH2 -  CZ2 ANGL. DEV. = -18.4 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      56 ANGLE DEVIATIONS.                             
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    TRP A 203     -168.60    170.74                                   
REMARK 500    LYS A 204     -143.74    -57.68                                   
REMARK 500    TRP A 205      -36.18    172.90                                   
REMARK 500    ARG A 210      105.13     -5.12                                   
REMARK 500    ASN A 237       21.20    -79.12                                   
REMARK 500    ASP A 243       24.34     82.86                                   
REMARK 500    LEU A 264       20.20    -78.36                                   
REMARK 500    LYS A 321      -36.18    -39.73                                   
REMARK 500    ASP A 344     -110.22     46.14                                   
REMARK 500    ALA A 351      -86.11    -72.28                                   
REMARK 500    PRO A 397      114.03    -35.95                                   
REMARK 500    LYS A 468       32.56    -92.56                                   
REMARK 500    ASP A 519       20.12     43.53                                   
REMARK 500    GLN A 521      124.58    176.63                                   
REMARK 500    GLU A 522      108.54    134.81                                   
REMARK 500    ARG A 532     -148.24    -36.92                                   
REMARK 500    ASP A 533       77.75    -23.49                                   
REMARK 500    SER A 534       45.45     13.39                                   
REMARK 500    PRO A 560      -32.24    -33.14                                   
REMARK 500    GLN A 578        4.38    -68.31                                   
REMARK 500    ASN A 631     -177.11     43.64                                   
REMARK 500    LYS A 676       46.62    -87.27                                   
REMARK 500    ASP A 677     -104.49    -77.65                                   
REMARK 500    ALA A 678      -53.28   -164.45                                   
REMARK 500    GLU A 696      -71.00    -66.94                                   
REMARK 500    ASN A 722      -52.61   -142.64                                   
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 TRP A  205     TRP A  206                  149.31                    
REMARK 500 TRP A  206     GLU A  207                  143.35                    
REMARK 500 GLU A  522     TYR A  523                  -34.29                    
REMARK 500 ALA A  594     SER A  595                  148.33                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    TRP A 203         15.08                                           
REMARK 500    TRP A 206        -24.58                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500   M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                
REMARK 500     LYS A 204       160.4                     ALPHA-CARBON           
REMARK 500     GLU A 208       159.5                     ALPHA-CARBON           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1A36   RELATED DB: PDB                                   
REMARK 900 HUMAN DNA TOPOISOMERASE I (70 KDA) IN NON-COVALENT COMPLEX           
REMARK 900 WITH A 22 BASE PAIR DNA DUPLEX                                       
REMARK 900 RELATED ID: 1EJ9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TOPOISOMERASE I DNA COMPLEX               
REMARK 900 RELATED ID: 1K4S   RELATED DB: PDB                                   
REMARK 900 HUMAN DNA TOPOISOMERASE I IN COVALENT COMPLEX WITH A 22              
REMARK 900 BASE PAIR DNA DUPLEX                                                 
REMARK 900 RELATED ID: 1K4T   RELATED DB: PDB                                   
REMARK 900 HUMAN DNA TOPOISOMERASE I (70 KDA) IN COMPLEX WITH THE               
REMARK 900 POISON TOPOTECAN AND COVALENT COMPLEX WITH A 22 BASE PAIR            
REMARK 900 DNA DUPLEX                                                           
REMARK 900 RELATED ID: 1LPQ   RELATED DB: PDB                                   
REMARK 900 HUMAN DNA TOPOISOMERASE I (70 KDA) IN NON-COVALENT COMPLEX           
REMARK 900 WITH A 22 BASE PAIR DNA DUPLEX CONTAINING AN 8-OXOG LESION           
REMARK 900 RELATED ID: 1TMC   RELATED DB: PDB                                   
REMARK 900 THE THREE-DIMENSIONAL STRUCTURE OF A CLASS I MAJOR                   
REMARK 900 HISTOCOMPATIBILITY COMPLEX MOLECULE MISSING THE 3 DOMAIN OF          
REMARK 900 THE HEAVY CHAIN                                                      
DBREF  1R49 A  174   765  UNP    P11387   TOP1_HUMAN     174    765             
DBREF  1R49 B    1    22  PDB    1R49     1R49             1     22             
DBREF  1R49 C  101   122  PDB    1R49     1R49           101    122             
SEQADV 1R49 ARG A  532  UNP  P11387    LYS   532 ENGINEERED                     
SEQADV 1R49 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  592  LYS LYS PRO LYS ASN LYS ASP LYS ASP LYS LYS VAL PRO          
SEQRES   2 A  592  GLU PRO ASP ASN LYS LYS LYS LYS PRO LYS LYS GLU GLU          
SEQRES   3 A  592  GLU GLN LYS TRP LYS TRP TRP GLU GLU GLU ARG TYR PRO          
SEQRES   4 A  592  GLU GLY ILE LYS TRP LYS PHE LEU GLU HIS LYS GLY PRO          
SEQRES   5 A  592  VAL PHE ALA PRO PRO TYR GLU PRO LEU PRO GLU ASN VAL          
SEQRES   6 A  592  LYS PHE TYR TYR ASP GLY LYS VAL MET LYS LEU SER PRO          
SEQRES   7 A  592  LYS ALA GLU GLU VAL ALA THR PHE PHE ALA LYS MET LEU          
SEQRES   8 A  592  ASP HIS GLU TYR THR THR LYS GLU ILE PHE ARG LYS ASN          
SEQRES   9 A  592  PHE PHE LYS ASP TRP ARG LYS GLU MET THR ASN GLU GLU          
SEQRES  10 A  592  LYS ASN ILE ILE THR ASN LEU SER LYS CYS ASP PHE THR          
SEQRES  11 A  592  GLN MET SER GLN TYR PHE LYS ALA GLN THR GLU ALA ARG          
SEQRES  12 A  592  LYS GLN MET SER LYS GLU GLU LYS LEU LYS ILE LYS GLU          
SEQRES  13 A  592  GLU ASN GLU LYS LEU LEU LYS GLU TYR GLY PHE CYS ILE          
SEQRES  14 A  592  MET ASP ASN HIS LYS GLU ARG ILE ALA ASN PHE LYS ILE          
SEQRES  15 A  592  GLU PRO PRO GLY LEU PHE ARG GLY ARG GLY ASN HIS PRO          
SEQRES  16 A  592  LYS MET GLY MET LEU LYS ARG ARG ILE MET PRO GLU ASP          
SEQRES  17 A  592  ILE ILE ILE ASN CYS SER LYS ASP ALA LYS VAL PRO SER          
SEQRES  18 A  592  PRO PRO PRO GLY HIS LYS TRP LYS GLU VAL ARG HIS ASP          
SEQRES  19 A  592  ASN LYS VAL THR TRP LEU VAL SER TRP THR GLU ASN ILE          
SEQRES  20 A  592  GLN GLY SER ILE LYS TYR ILE MET LEU ASN PRO SER SER          
SEQRES  21 A  592  ARG ILE LYS GLY GLU LYS ASP TRP GLN LYS TYR GLU THR          
SEQRES  22 A  592  ALA ARG ARG LEU LYS LYS CYS VAL ASP LYS ILE ARG ASN          
SEQRES  23 A  592  GLN TYR ARG GLU ASP TRP LYS SER LYS GLU MET LYS VAL          
SEQRES  24 A  592  ARG GLN ARG ALA VAL ALA LEU TYR PHE ILE ASP LYS LEU          
SEQRES  25 A  592  ALA LEU ARG ALA GLY ASN GLU LYS GLU GLU GLY GLU THR          
SEQRES  26 A  592  ALA ASP THR VAL GLY CYS CYS SER LEU ARG VAL GLU HIS          
SEQRES  27 A  592  ILE ASN LEU HIS PRO GLU LEU ASP GLY GLN GLU TYR VAL          
SEQRES  28 A  592  VAL GLU PHE ASP PHE LEU GLY ARG ASP SER ILE ARG TYR          
SEQRES  29 A  592  TYR ASN LYS VAL PRO VAL GLU LYS ARG VAL PHE LYS ASN          
SEQRES  30 A  592  LEU GLN LEU PHE MET GLU ASN LYS GLN PRO GLU ASP ASP          
SEQRES  31 A  592  LEU PHE ASP ARG LEU ASN THR GLY ILE LEU ASN LYS HIS          
SEQRES  32 A  592  LEU GLN ASP LEU MET GLU GLY LEU THR ALA LYS VAL PHE          
SEQRES  33 A  592  ARG THR TYR ASN ALA SER ILE THR LEU GLN GLN GLN LEU          
SEQRES  34 A  592  LYS GLU LEU THR ALA PRO ASP GLU ASN ILE PRO ALA LYS          
SEQRES  35 A  592  ILE LEU SER TYR ASN ARG ALA ASN ARG ALA VAL ALA ILE          
SEQRES  36 A  592  LEU CYS ASN HIS GLN ARG ALA PRO PRO LYS THR PHE GLU          
SEQRES  37 A  592  LYS SER MET MET ASN LEU GLN THR LYS ILE ASP ALA LYS          
SEQRES  38 A  592  LYS GLU GLN LEU ALA ASP ALA ARG ARG ASP LEU LYS SER          
SEQRES  39 A  592  ALA LYS ALA ASP ALA LYS VAL MET LYS ASP ALA LYS THR          
SEQRES  40 A  592  LYS LYS VAL VAL GLU SER LYS LYS LYS ALA VAL GLN ARG          
SEQRES  41 A  592  LEU GLU GLU GLN LEU MET LYS LEU GLU VAL GLN ALA THR          
SEQRES  42 A  592  ASP ARG GLU GLU ASN LYS GLN ILE ALA LEU GLY THR SER          
SEQRES  43 A  592  LYS LEU ASN PHE LEU ASP PRO ARG ILE THR VAL ALA TRP          
SEQRES  44 A  592  CYS LYS LYS TRP GLY VAL PRO ILE GLU LYS ILE TYR ASN          
SEQRES  45 A  592  LYS THR GLN ARG GLU LYS PHE ALA TRP ALA ILE ASP MET          
SEQRES  46 A  592  ALA ASP GLU ASP TYR GLU PHE                                  
FORMUL   4  HOH   *29(H2 O)                                                     
HELIX    1   1 SER A  250  MET A  263  1                                  14    
HELIX    2   2 GLU A  267  THR A  270  5                                   4    
HELIX    3   3 LYS A  271  GLU A  285  1                                  15    
HELIX    4   4 THR A  287  ILE A  294  1                                   8    
HELIX    5   5 PHE A  302  GLN A  318  1                                  17    
HELIX    6   6 SER A  320  GLY A  339  1                                  20    
HELIX    7   7 SER A  433  ARG A  462  1                                  30    
HELIX    8   8 GLU A  463  SER A  467  5                                   5    
HELIX    9   9 GLU A  469  LEU A  485  1                                  17    
HELIX   10  10 ARG A  508  GLU A  510  5                                   3    
HELIX   11  11 GLU A  544  PHE A  554  1                                  11    
HELIX   12  12 ASN A  569  MET A  581  1                                  13    
HELIX   13  13 LYS A  587  GLU A  604  1                                  18    
HELIX   14  14 ASN A  611  ALA A  627  1                                  17    
HELIX   15  15 LEU A  647  ASP A  660  1                                  14    
HELIX   16  16 ALA A  661  MET A  675  1                                  15    
HELIX   17  17 ALA A  678  ASN A  711  1                                  34    
HELIX   18  18 ASP A  725  TRP A  736  1                                  12    
HELIX   19  19 PRO A  739  ILE A  743  5                                   5    
HELIX   20  20 ASN A  745  PHE A  752  1                                   8    
HELIX   21  21 PHE A  752  MET A  758  1                                   7    
SHEET    1   A 3 LEU A 220  GLU A 221  0                                        
SHEET    2   A 3 PHE A 340  MET A 343 -1  O  ILE A 342   N  GLU A 221           
SHEET    3   A 3 HIS A 346  ARG A 349 -1  O  HIS A 346   N  MET A 343           
SHEET    1   B 3 LYS A 245  MET A 247  0                                        
SHEET    2   B 3 PHE A 240  TYR A 242 -1  N  TYR A 242   O  LYS A 245           
SHEET    3   B 3 CYS A 300  ASP A 301 -1  O  ASP A 301   N  TYR A 241           
SHEET    1   C 2 GLY A 359  LEU A 360  0                                        
SHEET    2   C 2 LEU A 373  LYS A 374 -1  O  LYS A 374   N  GLY A 359           
SHEET    1   D 4 GLU A 403  ARG A 405  0                                        
SHEET    2   D 4 ILE A 383  ASN A 385  1  N  ILE A 384   O  ARG A 405           
SHEET    3   D 4 VAL A 414  THR A 417 -1  O  SER A 415   N  ILE A 383           
SHEET    4   D 4 ILE A 424  ILE A 427 -1  O  LYS A 425   N  TRP A 416           
SHEET    1   E 3 ILE A 512  HIS A 515  0                                        
SHEET    2   E 3 VAL A 524  LEU A 530 -1  O  GLU A 526   N  ASN A 513           
SHEET    3   E 3 ARG A 536  PRO A 542 -1  O  ASN A 539   N  PHE A 527           
CISPEP   1 LYS A  204    TRP A  205          0        -4.46                     
CISPEP   2 GLN A  521    GLU A  522          0         8.04                     
CISPEP   3 MET A  644    MET A  645          0        -0.89                     
CRYST1   56.944  118.638   71.651  90.00  98.33  90.00 P 1 21 1      2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017561  0.000000  0.002570        0.00000                         
SCALE2      0.000000  0.008429  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014105        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system