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Database: PDB
Entry: 6CA8
LinkDB: 6CA8
Original site: 6CA8 
HEADER    ISOMERASE                               29-JAN-18   6CA8              
TITLE     CRYSTAL STRUCTURE OF PLASMODIUM FALCIPARUM TOPOISOMERASE II DNA-      
TITLE    2 BINDING, CLEAVAGE AND RE-LIGATION DOMAIN                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA TOPOISOMERASE 2;                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 5.99.1.3;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;                          
SOURCE   3 ORGANISM_COMMON: MALARIA PARASITE P. FALCIPARUM;                     
SOURCE   4 ORGANISM_TAXID: 5833;                                                
SOURCE   5 GENE: TOPOII;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TOPOISOMERASE, DNA-BINDING DOMAIN, ISOMERASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.KUMAR,P.KANDAVELU,P.K.RATHOD                                        
REVDAT   3   18-DEC-19 6CA8    1       REMARK                                   
REVDAT   2   20-FEB-19 6CA8    1       REMARK                                   
REVDAT   1   06-FEB-19 6CA8    0                                                
JRNL        AUTH   S.KUMAR,P.KANDAVELU,P.K.RATHOD                               
JRNL        TITL   CRYSTAL STRUCTURE OF PLASMODIUM FALCIPARUM TOPOISOMERASE II  
JRNL        TITL 2 DNA-BINDING, CLEAVAGE AND RE-LIGATION DOMAIN                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.33 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.33                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.22                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 42388                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2135                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 44.2255 -  5.7443    1.00     2938   144  0.1666 0.1649        
REMARK   3     2  5.7443 -  4.5609    1.00     2793   153  0.1556 0.1673        
REMARK   3     3  4.5609 -  3.9848    1.00     2777   138  0.1523 0.1746        
REMARK   3     4  3.9848 -  3.6206    1.00     2732   157  0.1692 0.2121        
REMARK   3     5  3.6206 -  3.3612    1.00     2731   153  0.1890 0.2316        
REMARK   3     6  3.3612 -  3.1631    1.00     2728   144  0.1921 0.2634        
REMARK   3     7  3.1631 -  3.0047    1.00     2726   147  0.2042 0.2495        
REMARK   3     8  3.0047 -  2.8740    1.00     2708   139  0.2077 0.2121        
REMARK   3     9  2.8740 -  2.7633    1.00     2692   166  0.2009 0.2658        
REMARK   3    10  2.7633 -  2.6680    1.00     2692   145  0.2086 0.2526        
REMARK   3    11  2.6680 -  2.5846    1.00     2732   128  0.2194 0.2731        
REMARK   3    12  2.5846 -  2.5107    0.98     2642   152  0.2202 0.2778        
REMARK   3    13  2.5107 -  2.4446    0.95     2563   126  0.2190 0.2591        
REMARK   3    14  2.4446 -  2.3850    0.91     2452   124  0.2309 0.2735        
REMARK   3    15  2.3850 -  2.3308    0.86     2347   119  0.2372 0.2863        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.330           
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) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           6042                                  
REMARK   3   ANGLE     :  1.186           8141                                  
REMARK   3   CHIRALITY :  0.056            889                                  
REMARK   3   PLANARITY :  0.006           1036                                  
REMARK   3   DIHEDRAL  : 16.819           2286                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6CA8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JAN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000232397.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-OCT-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 94                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42437                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.330                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 26.40                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.33                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM FORMATE, 19% PEG3350,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       41.51700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.24100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       41.51700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.24100            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 63420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350   BIOMT1   2 -1.000000  0.000000  0.000000       83.03400            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A1580  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1665  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1729  LIES ON A SPECIAL POSITION.                          
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     MET A   468                                                      
REMARK 465     ALA A   469                                                      
REMARK 465     ILE A  1112                                                      
REMARK 465     LYS A  1113                                                      
REMARK 465     LYS A  1114                                                      
REMARK 465     LEU A  1123                                                      
REMARK 465     ASP A  1124                                                      
REMARK 465     ALA A  1125                                                      
REMARK 465     ALA A  1126                                                      
REMARK 465     ASP A  1127                                                      
REMARK 465     ASN A  1128                                                      
REMARK 465     PRO A  1129                                                      
REMARK 465     SER A  1211                                                      
REMARK 465     ASN A  1212                                                      
REMARK 465     HIS A  1213                                                      
REMARK 465     HIS A  1214                                                      
REMARK 465     HIS A  1215                                                      
REMARK 465     HIS A  1216                                                      
REMARK 465     HIS A  1217                                                      
REMARK 465     HIS A  1218                                                      
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     ARG A 470    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 491    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 559    CG   CD   CE   NZ                                   
REMARK 470     ASP A 562    CG   OD1  OD2                                       
REMARK 470     ASP A 563    CG   OD1  OD2                                       
REMARK 470     ILE A 564    CG1  CG2  CD1                                       
REMARK 470     LYS A 565    CG   CD   CE   NZ                                   
REMARK 470     LYS A 619    CG   CD   CE   NZ                                   
REMARK 470     SER A 621    OG                                                  
REMARK 470     GLN A 622    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 640    CG   OD1  ND2                                       
REMARK 470     LEU A 641    CG   CD1  CD2                                       
REMARK 470     LEU A 642    CG   CD1  CD2                                       
REMARK 470     LYS A 668    CG   CD   CE   NZ                                   
REMARK 470     LYS A 713    CG   CD   CE   NZ                                   
REMARK 470     GLU A 970    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 971    CG   CD   CE   NZ                                   
REMARK 470     ASN A1110    CG   OD1  ND2                                       
REMARK 470     LYS A1111    CG   CD   CE   NZ                                   
REMARK 470     GLU A1115    CG   CD   OE1  OE2                                  
REMARK 470     LEU A1122    CG   CD1  CD2                                       
REMARK 470     GLU A1130    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1133    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1142    CG   CD   CE   NZ                                   
REMARK 470     GLU A1209    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1210    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   NZ   LYS A  1066     OE1  GLU A  1171              1.94            
REMARK 500   OE2  GLU A   924     O    HOH A  1301              2.03            
REMARK 500   OG   SER A  1149     O    HOH A  1302              2.17            
REMARK 500   NZ   LYS A   561     O    LYS A   565              2.17            
REMARK 500   O    HOH A  1545     O    HOH A  1788              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 706   CA  -  CB  -  CG  ANGL. DEV. =  16.0 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    ASN A 560       -2.89     72.32                                   
REMARK 500    GLN A 622       61.27     60.52                                   
REMARK 500    GLU A 726      -54.05   -128.55                                   
REMARK 500    SER A 802     -126.16    -98.48                                   
REMARK 500    ILE A 860     -157.06   -112.78                                   
REMARK 500    LYS A 928      -70.04   -132.98                                   
REMARK 500    GLU A1121       42.93   -107.37                                   
REMARK 500    ASP A1131      165.17     82.95                                   
REMARK 500    ILE A1136      146.81    152.26                                   
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 LEU A  642     GLY A  643                  -64.24                    
REMARK 500 ILE A 1136     ALA A 1137                  -38.28                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6CA8 A  469  1212  UNP    Q7Z2D0   Q7Z2D0_PLAFA   469   1212             
SEQADV 6CA8 MET A  468  UNP  Q7Z2D0              INITIATING METHIONINE          
SEQADV 6CA8 HIS A 1213  UNP  Q7Z2D0              EXPRESSION TAG                 
SEQADV 6CA8 HIS A 1214  UNP  Q7Z2D0              EXPRESSION TAG                 
SEQADV 6CA8 HIS A 1215  UNP  Q7Z2D0              EXPRESSION TAG                 
SEQADV 6CA8 HIS A 1216  UNP  Q7Z2D0              EXPRESSION TAG                 
SEQADV 6CA8 HIS A 1217  UNP  Q7Z2D0              EXPRESSION TAG                 
SEQADV 6CA8 HIS A 1218  UNP  Q7Z2D0              EXPRESSION TAG                 
SEQRES   1 A  751  MET ALA ARG GLU ARG ILE ILE GLY ILE PRO LYS LEU GLU          
SEQRES   2 A  751  ASP ALA ASN ASP ALA GLY SER LYS TYR SER GLN GLU CYS          
SEQRES   3 A  751  THR LEU ILE LEU THR GLU GLY ASP SER ALA LYS THR SER          
SEQRES   4 A  751  CYS LEU ALA GLY LEU SER ILE VAL GLY ARG ASP LYS TYR          
SEQRES   5 A  751  GLY VAL PHE PRO LEU LYS GLY LYS LEU LEU ASN VAL ARG          
SEQRES   6 A  751  ASP ALA SER PHE LYS GLN LEU MET ASP ASN LYS GLU ILE          
SEQRES   7 A  751  GLN ASN ILE PHE ARG ILE MET GLY LEU ASP ILE THR ASP          
SEQRES   8 A  751  LYS ASN LYS ASP ASP ILE LYS GLY LEU ARG TYR GLY SER          
SEQRES   9 A  751  LEU MET ILE MET THR ASP GLN ASP TYR ASP GLY SER HIS          
SEQRES  10 A  751  ILE LYS GLY LEU LEU ILE ASN MET ILE HIS LYS PHE TRP          
SEQRES  11 A  751  PRO SER LEU LEU LYS HIS LYS GLY PHE LEU SER GLU PHE          
SEQRES  12 A  751  VAL THR PRO ILE VAL LYS VAL GLN LYS GLY SER GLN GLU          
SEQRES  13 A  751  TYR SER PHE PHE THR ILE ALA GLU TYR GLU GLN TRP LYS          
SEQRES  14 A  751  GLU ASN THR ASN LEU LEU GLY TRP LYS ILE LYS TYR TYR          
SEQRES  15 A  751  LYS GLY LEU GLY THR SER THR ASP ARG GLU PHE LYS GLN          
SEQRES  16 A  751  TYR PHE SER ASP ILE LYS ASN HIS LYS ILE MET PHE LEU          
SEQRES  17 A  751  TRP THR GLY ASP ARG ASP GLY ASP SER ILE ASP MET ALA          
SEQRES  18 A  751  PHE SER LYS LYS ARG ILE GLU ASP ARG LYS LEU TRP LEU          
SEQRES  19 A  751  GLN ASN PHE ILE LEU GLY SER TYR VAL ASP HIS LYS GLU          
SEQRES  20 A  751  LYS ASP LEU SER TYR TYR ASP PHE VAL ASN LYS GLU LEU          
SEQRES  21 A  751  ILE TYR TYR SER ARG TYR ASP THR GLU ARG SER ILE PRO          
SEQRES  22 A  751  ASN ILE MET ASP GLY TRP LYS PRO GLY GLN ARG LYS VAL          
SEQRES  23 A  751  LEU TYR GLY CYS PHE LYS ARG ASN LEU ARG ASN GLU CYS          
SEQRES  24 A  751  LYS VAL ALA GLN LEU VAL GLY TYR ILE ALA GLU HIS SER          
SEQRES  25 A  751  ALA TYR HIS HIS GLY GLU SER SER LEU GLN GLN THR ILE          
SEQRES  26 A  751  ILE ASN MET ALA GLN THR PHE VAL GLY SER ASN ASN ILE          
SEQRES  27 A  751  ASN PHE LEU GLU PRO CYS GLY GLN PHE GLY SER ARG LYS          
SEQRES  28 A  751  GLU GLY GLY LYS ASP ALA SER ALA ALA ARG TYR ILE PHE          
SEQRES  29 A  751  THR LYS LEU ALA SER SER THR ARG SER ILE PHE ASN GLU          
SEQRES  30 A  751  TYR ASP ASP PRO ILE LEU LYS TYR LEU ASN GLU GLU GLY          
SEQRES  31 A  751  GLN LYS ILE GLU PRO GLN TYR TYR ILE PRO VAL ILE PRO          
SEQRES  32 A  751  THR ILE LEU VAL ASN GLY CYS GLU GLY ILE GLY THR GLY          
SEQRES  33 A  751  TYR SER SER PHE ILE PRO ASN TYR ASN TYR LYS ASP ILE          
SEQRES  34 A  751  ILE ASP ASN ILE LYS ARG TYR ILE ASN LYS GLU PRO LEU          
SEQRES  35 A  751  ILE PRO MET VAL PRO TRP TYR LYS ASP PHE LYS GLY ARG          
SEQRES  36 A  751  ILE GLU SER ASN GLY LYS THR GLY TYR GLU THR ILE GLY          
SEQRES  37 A  751  ILE ILE ASN LYS ILE ASP ASN ASP THR LEU GLU ILE THR          
SEQRES  38 A  751  GLU LEU PRO ILE LYS LYS TRP THR GLN ASP TYR LYS GLU          
SEQRES  39 A  751  PHE LEU GLU GLU LEU LEU THR ASP GLU LYS HIS GLN LEU          
SEQRES  40 A  751  ILE LEU ASP TYR ILE ASP ASN SER SER HIS GLU ASP ILE          
SEQRES  41 A  751  CYS PHE THR ILE LYS MET ASP PRO ALA LYS LEU GLN LYS          
SEQRES  42 A  751  ALA GLU GLU GLU GLY LEU GLU LYS VAL PHE LYS LEU LYS          
SEQRES  43 A  751  SER THR LEU THR THR THR ASN MET THR LEU PHE ASP PRO          
SEQRES  44 A  751  ASN LEU LYS LEU GLN ARG TYR SER THR GLU LEU ASP ILE          
SEQRES  45 A  751  LEU LYS GLU PHE CYS TYR GLN ARG LEU LYS ALA TYR GLU          
SEQRES  46 A  751  ASN ARG LYS SER TYR LEU ILE SER LYS LEU GLU LYS GLU          
SEQRES  47 A  751  LYS ARG ILE ILE SER ASN LYS THR LYS PHE ILE LEU ALA          
SEQRES  48 A  751  ILE VAL ASN ASN GLU LEU ILE VAL ASN LYS LYS LYS LYS          
SEQRES  49 A  751  LYS VAL LEU VAL GLU GLU LEU TYR ARG LYS GLY TYR ASP          
SEQRES  50 A  751  PRO TYR LYS ASP ILE ASN LYS ILE LYS LYS GLU GLU ILE          
SEQRES  51 A  751  PHE GLU GLN GLU LEU LEU ASP ALA ALA ASP ASN PRO GLU          
SEQRES  52 A  751  ASP ASN GLU GLU ILE ILE ALA GLY ILE THR VAL LYS ASP          
SEQRES  53 A  751  TYR ASP TYR LEU LEU SER MET PRO ILE PHE SER LEU THR          
SEQRES  54 A  751  LEU GLU LYS VAL GLU ASP LEU LEU THR GLN LEU LYS GLU          
SEQRES  55 A  751  LYS GLU ARG GLU LEU GLU ILE LEU ARG ASN ILE THR VAL          
SEQRES  56 A  751  GLU THR MET TRP LEU LYS ASP ILE GLU LYS VAL GLU GLU          
SEQRES  57 A  751  ALA ILE GLU PHE GLN ARG ASN VAL GLU LEU SER ASN ARG          
SEQRES  58 A  751  GLU GLU SER ASN HIS HIS HIS HIS HIS HIS                      
FORMUL   2  HOH   *536(H2 O)                                                    
HELIX    1 AA1 TYR A  489  GLU A  492  5                                   4    
HELIX    2 AA2 GLY A  500  GLY A  515  1                                  16    
HELIX    3 AA3 SER A  535  ASN A  542  1                                   8    
HELIX    4 AA4 ASN A  542  GLY A  553  1                                  12    
HELIX    5 AA5 ASP A  579  TRP A  597  1                                  19    
HELIX    6 AA6 TRP A  597  HIS A  603  1                                   7    
HELIX    7 AA7 THR A  628  ASN A  638  1                                  11    
HELIX    8 AA8 GLY A  651  SER A  655  5                                   5    
HELIX    9 AA9 THR A  656  ASP A  666  1                                  11    
HELIX   10 AB1 ILE A  667  ASN A  669  5                                   3    
HELIX   11 AB2 GLY A  678  SER A  690  1                                  13    
HELIX   12 AB3 ARG A  693  ASN A  703  1                                  11    
HELIX   13 AB4 TYR A  719  GLU A  726  1                                   8    
HELIX   14 AB5 GLU A  726  ILE A  739  1                                  14    
HELIX   15 AB6 LYS A  747  ASN A  761  1                                  15    
HELIX   16 AB7 VAL A  768  SER A  779  1                                  12    
HELIX   17 AB8 GLY A  784  GLN A  797  1                                  14    
HELIX   18 AB9 SER A  837  PHE A  842  1                                   6    
HELIX   19 AC1 ASN A  843  LEU A  850  5                                   8    
HELIX   20 AC2 PRO A  870  GLY A  876  1                                   7    
HELIX   21 AC3 ASN A  892  ASN A  905  1                                  14    
HELIX   22 AC4 TRP A  955  THR A  968  1                                  14    
HELIX   23 AC5 ASP A  969  HIS A  972  5                                   4    
HELIX   24 AC6 ASP A  994  GLY A 1005  1                                  12    
HELIX   25 AC7 GLY A 1005  PHE A 1010  1                                   6    
HELIX   26 AC8 THR A 1035  ASN A 1081  1                                  47    
HELIX   27 AC9 LYS A 1090  LYS A 1101  1                                  12    
HELIX   28 AD1 PRO A 1105  ASN A 1110  1                                   6    
HELIX   29 AD2 VAL A 1141  ASP A 1143  5                                   3    
HELIX   30 AD3 TYR A 1144  SER A 1149  1                                   6    
HELIX   31 AD4 PRO A 1151  LEU A 1155  5                                   5    
HELIX   32 AD5 THR A 1156  ILE A 1180  1                                  25    
HELIX   33 AD6 THR A 1181  GLU A 1209  1                                  29    
SHEET    1 AA1 6 TYR A 519  LEU A 524  0                                        
SHEET    2 AA1 6 THR A 494  GLU A 499  1  N  ILE A 496   O  GLY A 520           
SHEET    3 AA1 6 SER A 571  MET A 575  1  O  MET A 575   N  LEU A 497           
SHEET    4 AA1 6 LEU A 607  PHE A 610  1  O  SER A 608   N  ILE A 574           
SHEET    5 AA1 6 LYS A 671  LEU A 675 -1  O  PHE A 674   N  LEU A 607           
SHEET    6 AA1 6 ASP A 716  SER A 718  1  O  LEU A 717   N  MET A 673           
SHEET    1 AA2 3 TYR A 624  PHE A 626  0                                        
SHEET    2 AA2 3 VAL A 615  GLN A 618 -1  N  VAL A 615   O  PHE A 626           
SHEET    3 AA2 3 LYS A 645  TYR A 648 -1  O  LYS A 645   N  GLN A 618           
SHEET    1 AA3 2 CYS A 766  LYS A 767  0                                        
SHEET    2 AA3 2 PHE A 831  THR A 832 -1  O  THR A 832   N  CYS A 766           
SHEET    1 AA4 2 TYR A 852  GLU A 855  0                                        
SHEET    2 AA4 2 GLN A 858  PRO A 862 -1  O  GLN A 858   N  GLU A 855           
SHEET    1 AA5 2 CYS A 877  ILE A 880  0                                        
SHEET    2 AA5 2 SER A 885  ILE A 888 -1  O  SER A 886   N  GLY A 879           
SHEET    1 AA6 3 ARG A 922  SER A 925  0                                        
SHEET    2 AA6 3 GLY A 930  ILE A 934 -1  O  GLU A 932   N  GLU A 924           
SHEET    3 AA6 3 LYS A1013  THR A1017 -1  O  SER A1014   N  THR A 933           
SHEET    1 AA7 4 ILE A 936  LYS A 939  0                                        
SHEET    2 AA7 4 THR A 944  GLU A 949 -1  O  GLU A 946   N  ASN A 938           
SHEET    3 AA7 4 PHE A 989  LYS A 992 -1  O  ILE A 991   N  LEU A 945           
SHEET    4 AA7 4 ASP A 977  ASP A 980 -1  N  ASP A 977   O  LYS A 992           
SHEET    1 AA8 2 MET A1021  PHE A1024  0                                        
SHEET    2 AA8 2 LEU A1030  TYR A1033 -1  O  TYR A1033   N  MET A1021           
CISPEP   1 LYS A  565    GLY A  566          0       -12.93                     
CRYST1   83.034  104.482  114.523  90.00  90.00  90.00 P 21 21 2     4          
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      0.012043  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009571  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008732        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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