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Database: PDB
Entry: 6GIS
LinkDB: 6GIS
Original site: 6GIS 
HEADER    DNA BINDING PROTEIN                     15-MAY-18   6GIS              
TITLE     STRUCTURAL BASIS OF HUMAN CLAMP SLIDING ON DNA                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;                        
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: PCNA,CYCLIN;                                                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA (5'-D(P*AP*TP*AP*CP*GP*AP*TP*GP*GP*G)-3');             
COMPND   9 CHAIN: D;                                                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: DNA (5'-D(P*CP*CP*CP*AP*TP*CP*GP*TP*AP*T)-3');             
COMPND  13 CHAIN: E;                                                            
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PCNA;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  11 ORGANISM_TAXID: 32630;                                               
SOURCE  12 MOL_ID: 3;                                                           
SOURCE  13 SYNTHETIC: YES;                                                      
SOURCE  14 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  15 ORGANISM_TAXID: 32630                                                
KEYWDS    STRUCTURAL ANALYSIS HUMAN PCNA DNA COMPLEX SLIDING, DNA BINDING       
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.DE MARCH,N.MERINO,S.BARRERA-VILARMAU,R.CREHUET,S.ONESTI,F.J.BLANCO, 
AUTHOR   2 A.DE BIASIO                                                          
REVDAT   2   02-OCT-19 6GIS    1       COMPND SOURCE REMARK DBREF               
REVDAT   2 2                   1       SEQADV SEQRES HELIX  SHEET               
REVDAT   2 3                   1       CRYST1 ATOM                              
REVDAT   1   30-MAY-18 6GIS    0                                                
SPRSDE     30-MAY-18 6GIS      5L7C                                             
JRNL        AUTH   M.DE MARCH,N.MERINO,S.BARRERA-VILARMAU,R.CREHUET,S.ONESTI,   
JRNL        AUTH 2 F.J.BLANCO,A.DE BIASIO                                       
JRNL        TITL   STRUCTURAL BASIS OF HUMAN PCNA SLIDING ON DNA.               
JRNL        REF    NAT COMMUN                    V.   8 13935 2017              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   28071730                                                     
JRNL        DOI    10.1038/NCOMMS13935                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.DE BIASIO,A.I.DE OPAKUA,G.B.MORTUZA,R.MOLINA,T.N.CORDEIRO, 
REMARK   1  AUTH 2 F.CASTILLO,M.VILLATE,N.MERINO,S.DELGADO,D.GIL-CARTON,        
REMARK   1  AUTH 3 I.LUQUE,T.DIERCKS,P.BERNADO,G.MONTOYA,F.J.BLANCO             
REMARK   1  TITL   STRUCTURE OF P15(PAF)-PCNA COMPLEX AND IMPLICATIONS FOR      
REMARK   1  TITL 2 CLAMP SLIDING DURING DNA REPLICATION AND REPAIR.             
REMARK   1  REF    NAT COMMUN                    V.   6  6439 2015              
REMARK   1  REFN                   ESSN 2041-1723                               
REMARK   1  PMID   25762514                                                     
REMARK   1  DOI    10.1038/NCOMMS7439                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.82 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0107                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 90.09                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 21184                          
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) : 0.248                           
REMARK   3   R VALUE            (WORKING SET) : 0.247                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1134                            
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) : 2.82                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.89                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1570                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.88                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 87                           
REMARK   3   BIN FREE R VALUE                    : 0.4160                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5293                                    
REMARK   3   NUCLEIC ACID ATOMS       : 410                                     
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 40                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.15000                                              
REMARK   3    B22 (A**2) : 0.15000                                              
REMARK   3    B33 (A**2) : -0.50000                                             
REMARK   3    B12 (A**2) : 0.08000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
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): 0.425         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.370         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 40.337        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.851                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.850                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5826 ; 0.016 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5244 ; 0.008 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8000 ; 1.818 ; 1.906       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11980 ; 1.455 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   738 ; 7.147 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   165 ;39.119 ;24.727       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   835 ;18.274 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;20.404 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   965 ; 0.099 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6374 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1219 ; 0.006 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  2970 ; 3.603 ; 4.997       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2969 ; 3.604 ; 4.997       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3702 ; 5.743 ; 7.497       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3703 ; 5.742 ; 7.497       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2856 ; 3.584 ; 7.357       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2855 ; 3.571 ; 7.354       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4299 ; 5.687 ;11.061       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6229 ;10.160 ;55.772       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  6228 ;10.143 ;55.755       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 3                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     1    254       B     1    254   24994  0.09  0.05     
REMARK   3    2     A     1    253       C     1    253   24772  0.08  0.05     
REMARK   3    3     B     1    253       C     1    253   24418  0.08  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   313                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.8133  69.9521  60.6321              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1913 T22:   0.1366                                     
REMARK   3      T33:   0.0337 T12:  -0.0809                                     
REMARK   3      T13:  -0.0300 T23:   0.0326                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0363 L22:   0.1509                                     
REMARK   3      L33:   0.0065 L12:   0.0718                                     
REMARK   3      L13:   0.0150 L23:   0.0302                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0224 S12:  -0.0145 S13:   0.0236                       
REMARK   3      S21:   0.0825 S22:  -0.0249 S23:   0.0432                       
REMARK   3      S31:   0.0177 S32:  -0.0111 S33:   0.0026                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: STRUCTURE REFINED USING NCS COSTRAINTS,   
REMARK   3  BABINET CORRECTION AND TLS.                                         
REMARK   4                                                                      
REMARK   4 6GIS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-MAY-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200010027.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-SEP-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-3                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9677                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 4M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22331                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.820                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 90.090                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.09300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.82                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 4D2G                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 3350 0.1M SODIUM ACETATE PH      
REMARK 280  4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       90.09450            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       52.01608            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       25.61067            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       90.09450            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       52.01608            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       25.61067            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       90.09450            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       52.01608            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       25.61067            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      104.03217            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       51.22133            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000      104.03217            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       51.22133            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000      104.03217            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       51.22133            
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: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5060 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
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     HIS A     0                                                      
REMARK 465     SER A   186                                                      
REMARK 465     ASN A   187                                                      
REMARK 465     VAL A   188                                                      
REMARK 465     ASP A   189                                                      
REMARK 465     LYS A   190                                                      
REMARK 465     GLU A   191                                                      
REMARK 465     ILE A   255                                                      
REMARK 465     GLU A   256                                                      
REMARK 465     ASP A   257                                                      
REMARK 465     GLU A   258                                                      
REMARK 465     GLU A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     SER A   261                                                      
REMARK 465     SER B   186                                                      
REMARK 465     ASN B   187                                                      
REMARK 465     VAL B   188                                                      
REMARK 465     ASP B   189                                                      
REMARK 465     LYS B   190                                                      
REMARK 465     ILE B   255                                                      
REMARK 465     GLU B   256                                                      
REMARK 465     ASP B   257                                                      
REMARK 465     GLU B   258                                                      
REMARK 465     GLU B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     SER B   261                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     SER C   186                                                      
REMARK 465     ASN C   187                                                      
REMARK 465     VAL C   188                                                      
REMARK 465     ASP C   189                                                      
REMARK 465     LYS C   190                                                      
REMARK 465     GLU C   191                                                      
REMARK 465     GLU C   192                                                      
REMARK 465     LYS C   254                                                      
REMARK 465     ILE C   255                                                      
REMARK 465     GLU C   256                                                      
REMARK 465     ASP C   257                                                      
REMARK 465     GLU C   258                                                      
REMARK 465     GLU C   259                                                      
REMARK 465     GLY C   260                                                      
REMARK 465     SER C   261                                                      
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     SER A  33    OG                                                  
REMARK 470     SER A  42    OG                                                  
REMARK 470     SER A  43    OG                                                  
REMARK 470     VAL A  70    CG1  CG2                                            
REMARK 470     GLU A  85    CD   OE1  OE2                                       
REMARK 470     ARG A  91    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A  93    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  94    CG   OD1  OD2                                       
REMARK 470     ASN A  95    CG   OD1  ND2                                       
REMARK 470     ASP A  97    CG   OD1  OD2                                       
REMARK 470     GLU A 104    CG   CD   OE1  OE2                                  
REMARK 470     PRO A 106    CB   CG   CD                                        
REMARK 470     GLN A 108    CD   OE1  NE2                                       
REMARK 470     GLU A 109    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 113    CG   OD1  OD2                                       
REMARK 470     GLU A 115    CD   OE1  OE2                                       
REMARK 470     LYS A 117    CD   CE   NZ                                        
REMARK 470     ASP A 122    CG   OD1  OD2                                       
REMARK 470     VAL A 123    CG1  CG2                                            
REMARK 470     GLU A 124    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 125    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 126    CG   CD1  CD2                                       
REMARK 470     ILE A 128    CG1  CG2  CD1                                       
REMARK 470     GLU A 130    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 132    CG   CD   OE1  OE2                                  
REMARK 470     CYS A 135    SG                                                  
REMARK 470     VAL A 136    CG1  CG2                                            
REMARK 470     LYS A 138    CD   CE   NZ                                        
REMARK 470     ASP A 156    CG   OD1  OD2                                       
REMARK 470     CYS A 162    SG                                                  
REMARK 470     LYS A 164    CG   CD   CE   NZ                                   
REMARK 470     ASP A 165    CG   OD1  OD2                                       
REMARK 470     GLU A 174    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 177    CG   OD1  ND2                                       
REMARK 470     LYS A 181    CD   CE   NZ                                        
REMARK 470     SER A 183    OG                                                  
REMARK 470     THR A 185    OG1  CG2                                            
REMARK 470     GLU A 192    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 193    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 198    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 201    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 210    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP A 232    CG   OD1  OD2                                       
REMARK 470     LYS A 240    CG   CD   CE   NZ                                   
REMARK 470     ASP A 243    CG   OD1  OD2                                       
REMARK 470     LYS A 254    CE   NZ                                             
REMARK 470     HIS B   0    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ILE B  11    CG1  CG2  CD1                                       
REMARK 470     GLU B  17    CG   CD   OE1  OE2                                  
REMARK 470     ASN B  24    CG   OD1  ND2                                       
REMARK 470     GLU B  25    CG   CD   OE1  OE2                                  
REMARK 470     CYS B  27    SG                                                  
REMARK 470     SER B  33    OG                                                  
REMARK 470     SER B  39    OG                                                  
REMARK 470     SER B  42    OG                                                  
REMARK 470     SER B  43    OG                                                  
REMARK 470     ARG B  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B  54    OG                                                  
REMARK 470     ASN B  84    CG   OD1  ND2                                       
REMARK 470     GLU B  85    CG   CD   OE1  OE2                                  
REMARK 470     ILE B  87    CD1                                                 
REMARK 470     ARG B  91    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  93    CG   CD   OE1  OE2                                  
REMARK 470     ASN B  95    CG   OD1  ND2                                       
REMARK 470     ASP B  97    CG   OD1  OD2                                       
REMARK 470     GLN B 108    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 110    NZ                                                  
REMARK 470     VAL B 111    CG1  CG2                                            
REMARK 470     GLU B 115    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 117    CG   CD   CE   NZ                                   
REMARK 470     ASP B 120    CG   OD1  OD2                                       
REMARK 470     LEU B 121    CG   CD1  CD2                                       
REMARK 470     ASP B 122    CG   OD1  OD2                                       
REMARK 470     VAL B 123    CG1  CG2                                            
REMARK 470     GLU B 124    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 125    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 126    CG   CD1  CD2                                       
REMARK 470     GLU B 132    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 138    CD   CE   NZ                                        
REMARK 470     ARG B 149    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 164    CG   CD   CE   NZ                                   
REMARK 470     GLU B 174    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 181    CG   CD   CE   NZ                                   
REMARK 470     THR B 185    OG1  CG2                                            
REMARK 470     GLU B 191    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 192    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 193    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 198    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 200    CG   OD1  ND2                                       
REMARK 470     GLU B 201    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 232    CG   OD1  OD2                                       
REMARK 470     LYS B 240    CG   CD   CE   NZ                                   
REMARK 470     ASP B 243    CG   OD1  OD2                                       
REMARK 470     LYS B 254    CG   CD   CE   NZ                                   
REMARK 470     ARG C   5    CZ   NH1  NH2                                       
REMARK 470     GLU C  25    CG   CD   OE1  OE2                                  
REMARK 470     ILE C  30    CD1                                                 
REMARK 470     SER C  32    OG                                                  
REMARK 470     SER C  43    OG                                                  
REMARK 470     VAL C  45    CG1  CG2                                            
REMARK 470     SER C  54    OG                                                  
REMARK 470     ARG C  61    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C  63    CG   OD1  OD2                                       
REMARK 470     LYS C  77    CG   CD   CE   NZ                                   
REMARK 470     ARG C  91    CZ   NH1  NH2                                       
REMARK 470     GLU C  93    CD   OE1  OE2                                       
REMARK 470     ASN C  95    CG   OD1  ND2                                       
REMARK 470     ASP C  97    CG   OD1  OD2                                       
REMARK 470     GLU C 104    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 108    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 109    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 110    CD   CE   NZ                                        
REMARK 470     LYS C 117    CG   CD   CE   NZ                                   
REMARK 470     ASP C 120    CG   OD1  OD2                                       
REMARK 470     LEU C 121    CG   CD1  CD2                                       
REMARK 470     ASP C 122    CG   OD1  OD2                                       
REMARK 470     VAL C 123    CG1  CG2                                            
REMARK 470     GLU C 124    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 125    CB   CG   CD   OE1  NE2                             
REMARK 470     LEU C 126    CG   CD1  CD2                                       
REMARK 470     GLU C 130    CG   CD   OE1  OE2                                  
REMARK 470     SER C 134    OG                                                  
REMARK 470     CYS C 135    SG                                                  
REMARK 470     LYS C 138    CD   CE   NZ                                        
REMARK 470     ARG C 149    NE   CZ   NH1  NH2                                  
REMARK 470     VAL C 158    CG1  CG2                                            
REMARK 470     VAL C 159    CG1  CG2                                            
REMARK 470     SER C 161    OG                                                  
REMARK 470     LYS C 164    CG   CD   CE   NZ                                   
REMARK 470     ASP C 165    CG   OD1  OD2                                       
REMARK 470     SER C 170    OG                                                  
REMARK 470     LYS C 181    CG   CD   CE   NZ                                   
REMARK 470     THR C 185    OG1  CG2                                            
REMARK 470     GLU C 193    CD   OE1  OE2                                       
REMARK 470     GLU C 198    CG   CD   OE1  OE2                                  
REMARK 470     ASN C 200    CG   OD1  ND2                                       
REMARK 470     VAL C 203    CG1  CG2                                            
REMARK 470     GLN C 204    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 217    NZ                                                  
REMARK 470     ASP C 232    CG   OD1  OD2                                       
REMARK 470     LYS C 240    CG   CD   CE   NZ                                   
REMARK 470     ASP C 243    CG   OD1  OD2                                       
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   CB   LEU A   126     O    HOH B   315     8655     2.09            
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    ARG A   5   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG B   5   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    GLN C 125   N   -  CA  -  C   ANGL. DEV. = -17.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  42      -37.22    -39.33                                   
REMARK 500    ASP A  94      118.83    -25.86                                   
REMARK 500    ASN A  95      -62.14    108.52                                   
REMARK 500    ASP A  97       60.28   -112.79                                   
REMARK 500    VAL A 123       61.28    -69.64                                   
REMARK 500    GLU A 124      -22.95    -31.97                                   
REMARK 500    ILE A 128       77.00     76.04                                   
REMARK 500    ASN A 179      108.40   -165.93                                   
REMARK 500    ALA A 242       75.61    -11.34                                   
REMARK 500    PRO A 253     -174.53    -63.42                                   
REMARK 500    SER B  42      -37.50    -39.82                                   
REMARK 500    ASP B  94      -39.76    -12.34                                   
REMARK 500    ALA B  96     -176.96     61.47                                   
REMARK 500    GLN B 108       22.86     80.02                                   
REMARK 500    VAL B 123      -70.09    -78.98                                   
REMARK 500    GLU B 124       91.84     53.76                                   
REMARK 500    LEU B 126     -179.04    -68.57                                   
REMARK 500    ASN B 179      104.29   -165.49                                   
REMARK 500    GLU B 192       89.36   -170.34                                   
REMARK 500    ALA B 242     -113.68     17.01                                   
REMARK 500    PRO B 253     -174.70    -69.29                                   
REMARK 500    SER C  42      -37.68    -39.44                                   
REMARK 500    ASP C  94      -46.83    -24.76                                   
REMARK 500    ASN C  95       71.37   -116.79                                   
REMARK 500    ASP C  97       58.36   -110.34                                   
REMARK 500    ASP C 122     -107.78    -58.78                                   
REMARK 500    VAL C 123      -30.67    174.84                                   
REMARK 500    ASN C 179      106.93   -168.02                                   
REMARK 500    ALA C 242       79.59    -13.34                                   
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 GLU C  124     GLN C  125                  135.07                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5L7C   RELATED DB: PDB                                   
REMARK 900 ERROR IN B-FACTOR DEPOSITION                                         
DBREF  6GIS A    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  6GIS B    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  6GIS C    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  6GIS D    1    10  PDB    6GIS     6GIS             1     10             
DBREF  6GIS E    1    10  PDB    6GIS     6GIS             1     10             
SEQADV 6GIS HIS A    0  UNP  P12004              EXPRESSION TAG                 
SEQADV 6GIS HIS B    0  UNP  P12004              EXPRESSION TAG                 
SEQADV 6GIS HIS C    0  UNP  P12004              EXPRESSION TAG                 
SEQRES   1 A  262  HIS MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU          
SEQRES   2 A  262  LYS LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU          
SEQRES   3 A  262  ALA CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN          
SEQRES   4 A  262  SER MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR          
SEQRES   5 A  262  LEU ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG          
SEQRES   6 A  262  ASN LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS          
SEQRES   7 A  262  ILE LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU          
SEQRES   8 A  262  ARG ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE          
SEQRES   9 A  262  GLU ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET          
SEQRES  10 A  262  LYS LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO          
SEQRES  11 A  262  GLU GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY          
SEQRES  12 A  262  GLU PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY          
SEQRES  13 A  262  ASP ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS          
SEQRES  14 A  262  PHE SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS          
SEQRES  15 A  262  LEU SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA          
SEQRES  16 A  262  VAL THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE          
SEQRES  17 A  262  ALA LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO          
SEQRES  18 A  262  LEU SER SER THR VAL THR LEU SER MET SER ALA ASP VAL          
SEQRES  19 A  262  PRO LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS          
SEQRES  20 A  262  LEU LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU          
SEQRES  21 A  262  GLY SER                                                      
SEQRES   1 B  262  HIS MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU          
SEQRES   2 B  262  LYS LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU          
SEQRES   3 B  262  ALA CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN          
SEQRES   4 B  262  SER MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR          
SEQRES   5 B  262  LEU ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG          
SEQRES   6 B  262  ASN LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS          
SEQRES   7 B  262  ILE LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU          
SEQRES   8 B  262  ARG ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE          
SEQRES   9 B  262  GLU ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET          
SEQRES  10 B  262  LYS LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO          
SEQRES  11 B  262  GLU GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY          
SEQRES  12 B  262  GLU PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY          
SEQRES  13 B  262  ASP ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS          
SEQRES  14 B  262  PHE SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS          
SEQRES  15 B  262  LEU SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA          
SEQRES  16 B  262  VAL THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE          
SEQRES  17 B  262  ALA LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO          
SEQRES  18 B  262  LEU SER SER THR VAL THR LEU SER MET SER ALA ASP VAL          
SEQRES  19 B  262  PRO LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS          
SEQRES  20 B  262  LEU LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU          
SEQRES  21 B  262  GLY SER                                                      
SEQRES   1 C  262  HIS MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU          
SEQRES   2 C  262  LYS LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU          
SEQRES   3 C  262  ALA CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN          
SEQRES   4 C  262  SER MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR          
SEQRES   5 C  262  LEU ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG          
SEQRES   6 C  262  ASN LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS          
SEQRES   7 C  262  ILE LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU          
SEQRES   8 C  262  ARG ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE          
SEQRES   9 C  262  GLU ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET          
SEQRES  10 C  262  LYS LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO          
SEQRES  11 C  262  GLU GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY          
SEQRES  12 C  262  GLU PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY          
SEQRES  13 C  262  ASP ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS          
SEQRES  14 C  262  PHE SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS          
SEQRES  15 C  262  LEU SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA          
SEQRES  16 C  262  VAL THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE          
SEQRES  17 C  262  ALA LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO          
SEQRES  18 C  262  LEU SER SER THR VAL THR LEU SER MET SER ALA ASP VAL          
SEQRES  19 C  262  PRO LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS          
SEQRES  20 C  262  LEU LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU          
SEQRES  21 C  262  GLY SER                                                      
SEQRES   1 D   10   DA  DT  DA  DC  DG  DA  DT  DG  DG  DG                      
SEQRES   1 E   10   DC  DC  DC  DA  DT  DC  DG  DT  DA  DT                      
FORMUL   6  HOH   *40(H2 O)                                                     
HELIX    1 AA1 GLN A    8  ASP A   21  1                                  14    
HELIX    2 AA2 GLU A   55  PHE A   57  5                                   3    
HELIX    3 AA3 LEU A   72  CYS A   81  1                                  10    
HELIX    4 AA4 SER A  141  HIS A  153  1                                  13    
HELIX    5 AA5 LEU A  209  THR A  216  1                                   8    
HELIX    6 AA6 LYS A  217  SER A  222  5                                   6    
HELIX    7 AA7 GLN B    8  ASP B   21  1                                  14    
HELIX    8 AA8 GLU B   55  PHE B   57  5                                   3    
HELIX    9 AA9 LEU B   72  CYS B   81  1                                  10    
HELIX   10 AB1 SER B  141  HIS B  153  1                                  13    
HELIX   11 AB2 LEU B  209  THR B  216  1                                   8    
HELIX   12 AB3 LYS B  217  SER B  222  5                                   6    
HELIX   13 AB4 GLN C    8  ASP C   21  1                                  14    
HELIX   14 AB5 GLU C   55  PHE C   57  5                                   3    
HELIX   15 AB6 LEU C   72  CYS C   81  1                                  10    
HELIX   16 AB7 SER C  141  HIS C  153  1                                  13    
HELIX   17 AB8 LEU C  209  THR C  216  1                                   8    
HELIX   18 AB9 LYS C  217  SER C  222  5                                   6    
SHEET    1 AA1 9 THR A  59  CYS A  62  0                                        
SHEET    2 AA1 9 PHE A   2  LEU A   6 -1  N  GLU A   3   O  ARG A  61           
SHEET    3 AA1 9 ILE A  87  ALA A  92 -1  O  ALA A  92   N  PHE A   2           
SHEET    4 AA1 9 THR A  98  GLU A 104 -1  O  ALA A 100   N  ARG A  91           
SHEET    5 AA1 9 LYS A 110  LYS A 117 -1  O  MET A 116   N  LEU A  99           
SHEET    6 AA1 9 GLY B 176  SER B 183 -1  O  LYS B 181   N  VAL A 111           
SHEET    7 AA1 9 GLY B 166  SER B 172 -1  N  PHE B 169   O  ILE B 180           
SHEET    8 AA1 9 ALA B 157  CYS B 162 -1  N  SER B 161   O  LYS B 168           
SHEET    9 AA1 9 VAL B 203  ALA B 208 -1  O  PHE B 207   N  VAL B 158           
SHEET    1 AA2 9 LEU A  66  ASN A  71  0                                        
SHEET    2 AA2 9 GLU A  25  SER A  31 -1  N  TRP A  28   O  MET A  68           
SHEET    3 AA2 9 GLY A  34  MET A  40 -1  O  ASN A  36   N  ASP A  29           
SHEET    4 AA2 9 SER A  46  ARG A  53 -1  O  VAL A  48   N  SER A  39           
SHEET    5 AA2 9 GLY A 245  LEU A 251 -1  O  TYR A 250   N  LEU A  47           
SHEET    6 AA2 9 LEU A 235  ILE A 241 -1  N  ILE A 241   O  GLY A 245           
SHEET    7 AA2 9 THR A 224  MET A 229 -1  N  SER A 228   O  VAL A 236           
SHEET    8 AA2 9 CYS A 135  PRO A 140 -1  N  CYS A 135   O  MET A 229           
SHEET    9 AA2 9 THR A 196  MET A 199 -1  O  GLU A 198   N  VAL A 136           
SHEET    1 AA3 9 VAL A 203  ALA A 208  0                                        
SHEET    2 AA3 9 ALA A 157  CYS A 162 -1  N  VAL A 158   O  PHE A 207           
SHEET    3 AA3 9 GLY A 166  SER A 172 -1  O  LYS A 168   N  SER A 161           
SHEET    4 AA3 9 GLY A 176  SER A 183 -1  O  ILE A 180   N  PHE A 169           
SHEET    5 AA3 9 VAL C 111  LYS C 117 -1  O  VAL C 111   N  LYS A 181           
SHEET    6 AA3 9 THR C  98  GLU C 104 -1  N  LEU C  99   O  MET C 116           
SHEET    7 AA3 9 ILE C  87  ALA C  92 -1  N  ARG C  91   O  ALA C 100           
SHEET    8 AA3 9 PHE C   2  LEU C   6 -1  N  PHE C   2   O  ALA C  92           
SHEET    9 AA3 9 THR C  59  CYS C  62 -1  O  ARG C  61   N  GLU C   3           
SHEET    1 AA4 9 THR B  59  CYS B  62  0                                        
SHEET    2 AA4 9 MET B   1  LEU B   6 -1  N  GLU B   3   O  ARG B  61           
SHEET    3 AA4 9 ILE B  87  GLU B  93 -1  O  ALA B  92   N  PHE B   2           
SHEET    4 AA4 9 THR B  98  GLU B 104 -1  O  ALA B 100   N  ARG B  91           
SHEET    5 AA4 9 LYS B 110  LYS B 117 -1  O  MET B 116   N  LEU B  99           
SHEET    6 AA4 9 GLY C 176  SER C 183 -1  O  LYS C 181   N  VAL B 111           
SHEET    7 AA4 9 GLY C 166  SER C 172 -1  N  PHE C 169   O  ILE C 180           
SHEET    8 AA4 9 ALA C 157  CYS C 162 -1  N  SER C 161   O  LYS C 168           
SHEET    9 AA4 9 VAL C 203  ALA C 208 -1  O  LEU C 205   N  ILE C 160           
SHEET    1 AA5 9 LEU B  66  ASN B  71  0                                        
SHEET    2 AA5 9 GLU B  25  SER B  31 -1  N  TRP B  28   O  MET B  68           
SHEET    3 AA5 9 GLY B  34  MET B  40 -1  O  ASN B  36   N  ASP B  29           
SHEET    4 AA5 9 SER B  46  ARG B  53 -1  O  VAL B  48   N  SER B  39           
SHEET    5 AA5 9 GLY B 245  LEU B 251 -1  O  TYR B 250   N  LEU B  47           
SHEET    6 AA5 9 LEU B 235  ILE B 241 -1  N  ILE B 241   O  GLY B 245           
SHEET    7 AA5 9 THR B 224  MET B 229 -1  N  THR B 226   O  GLU B 238           
SHEET    8 AA5 9 CYS B 135  PRO B 140 -1  N  CYS B 135   O  MET B 229           
SHEET    9 AA5 9 THR B 196  MET B 199 -1  O  GLU B 198   N  VAL B 136           
SHEET    1 AA6 9 LEU C  66  ASN C  71  0                                        
SHEET    2 AA6 9 GLU C  25  SER C  31 -1  N  TRP C  28   O  MET C  68           
SHEET    3 AA6 9 GLY C  34  MET C  40 -1  O  ASN C  36   N  ASP C  29           
SHEET    4 AA6 9 SER C  46  ARG C  53 -1  O  VAL C  48   N  SER C  39           
SHEET    5 AA6 9 GLY C 245  LEU C 251 -1  O  TYR C 250   N  LEU C  47           
SHEET    6 AA6 9 LEU C 235  ILE C 241 -1  N  ILE C 241   O  GLY C 245           
SHEET    7 AA6 9 THR C 224  MET C 229 -1  N  SER C 228   O  VAL C 236           
SHEET    8 AA6 9 CYS C 135  PRO C 140 -1  N  VAL C 137   O  LEU C 227           
SHEET    9 AA6 9 THR C 196  MET C 199 -1  O  GLU C 198   N  VAL C 136           
SSBOND   1 CYS B  135    CYS B  162                          1555   1555  2.11  
CRYST1  180.189  180.189   76.832  90.00  90.00 120.00 H 3          27          
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      0.005550  0.003204  0.000000        0.00000                         
SCALE2      0.000000  0.006408  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013015        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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