GenomeNet

Database: PDB
Entry: 2ZVK
LinkDB: 2ZVK
Original site: 2ZVK 
HEADER    TRANSFERASE                             11-NOV-08   2ZVK              
TITLE     CRYSTAL STRUCTURE OF PCNA IN COMPLEX WITH DNA POLYMERASE ETA FRAGMENT 
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 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: DNA POLYMERASE ETA;                                        
COMPND   8 CHAIN: U, V, W;                                                      
COMPND   9 EC: 2.7.7.7;                                                         
COMPND  10 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;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT7;                                      
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: CHEMICALLY SYNTHESIZED PEPTIDE                        
KEYWDS    DNA REPLICATION, PCNA, CLAMP, TRANSLESION SYNTHESIS, TLS, DNA         
KEYWDS   2 POLYMERASE, TLS POLYMERASE, COMPLEX, PIP-BOX, DNA POLYMERASE ETA,    
KEYWDS   3 TRANSFERASE, DNA-BINDING, NUCLEUS, SYSTEMIC LUPUS ERYTHEMATOSUS,     
KEYWDS   4 DISEASE MUTATION, DNA DAMAGE, DNA REPAIR, DNA SYNTHESIS, DNA-        
KEYWDS   5 DIRECTED DNA POLYMERASE, MAGNESIUM, METAL-BINDING, MUTATOR PROTEIN,  
KEYWDS   6 NUCLEOTIDYLTRANSFERASE, PHOSPHOPROTEIN, SCHIFF BASE, XERODERMA       
KEYWDS   7 PIGMENTOSUM                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.HISHIKI,H.HASHIMOTO,T.HANAFUSA,K.KAMEI,E.OHASHI,T.SHIMIZU,H.OHMORI, 
AUTHOR   2 M.SATO                                                               
REVDAT   3   13-JUL-11 2ZVK    1       VERSN                                    
REVDAT   2   21-APR-09 2ZVK    1       JRNL                                     
REVDAT   1   10-FEB-09 2ZVK    0                                                
JRNL        AUTH   A.HISHIKI,H.HASHIMOTO,T.HANAFUSA,K.KAMEI,E.OHASHI,T.SHIMIZU, 
JRNL        AUTH 2 H.OHMORI,M.SATO                                              
JRNL        TITL   STRUCTURAL BASIS FOR NOVEL INTERACTIONS BETWEEN HUMAN        
JRNL        TITL 2 TRANSLESION SYNTHESIS POLYMERASES AND PROLIFERATING CELL     
JRNL        TITL 3 NUCLEAR ANTIGEN                                              
JRNL        REF    J.BIOL.CHEM.                  V. 284 10552 2009              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   19208623                                                     
JRNL        DOI    10.1074/JBC.M809745200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0066                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 26440                          
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) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1398                            
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1634                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 81                           
REMARK   3   BIN FREE R VALUE                    : 0.4090                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6003                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 18                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 59.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : 0.03000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
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): 0.776         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.367         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.300         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 33.735        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.880                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5839 ; 0.019 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  5418 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7899 ; 1.902 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 12563 ; 1.273 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   767 ; 7.874 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   208 ;42.829 ;25.337       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1004 ;22.066 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;27.632 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   950 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6454 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1076 ; 0.007 ; 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):  3844 ; 0.822 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1580 ; 0.005 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6149 ; 1.412 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1995 ; 2.000 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1750 ; 3.278 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
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   255                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.5020  -0.7540  65.7330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2183 T22:   0.2315                                     
REMARK   3      T33:   0.0780 T12:  -0.0096                                     
REMARK   3      T13:   0.0007 T23:   0.0523                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5366 L22:   3.4729                                     
REMARK   3      L33:   2.6138 L12:   1.0473                                     
REMARK   3      L13:  -0.1377 L23:  -0.1104                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0069 S12:  -0.1613 S13:  -0.0542                       
REMARK   3      S21:   0.1526 S22:  -0.1452 S23:  -0.2253                       
REMARK   3      S31:  -0.0442 S32:   0.4278 S33:   0.1382                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   U   693        U   712                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.4750  -2.6030  68.4060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8156 T22:   0.5741                                     
REMARK   3      T33:   0.6479 T12:   0.1020                                     
REMARK   3      T13:  -0.1322 T23:   0.1706                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2089 L22:   0.1007                                     
REMARK   3      L33:   0.7369 L12:  -0.8976                                     
REMARK   3      L13:  -2.4469 L23:   0.2651                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0485 S12:   0.0072 S13:  -0.4842                       
REMARK   3      S21:  -0.0123 S22:  -0.0240 S23:   0.0916                       
REMARK   3      S31:  -0.0308 S32:  -0.0626 S33:   0.0725                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   254                          
REMARK   3    ORIGIN FOR THE GROUP (A):  64.8960  26.4520  35.5820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3111 T22:   0.1557                                     
REMARK   3      T33:   0.1434 T12:  -0.1182                                     
REMARK   3      T13:  -0.0556 T23:   0.0577                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4394 L22:   1.1946                                     
REMARK   3      L33:   5.0110 L12:  -0.3268                                     
REMARK   3      L13:  -1.6649 L23:   0.4564                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1099 S12:  -0.1280 S13:  -0.0656                       
REMARK   3      S21:   0.2387 S22:  -0.1743 S23:  -0.0505                       
REMARK   3      S31:  -0.4458 S32:   0.3341 S33:   0.0643                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   V   701        V   710                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.7570  42.2160  38.1430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7473 T22:   0.3375                                     
REMARK   3      T33:   0.3207 T12:  -0.1637                                     
REMARK   3      T13:   0.2395 T23:  -0.1617                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  18.1330 L22:   7.7672                                     
REMARK   3      L33:  19.2919 L12:  -6.9565                                     
REMARK   3      L13:   9.7469 L23:   4.7159                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2530 S12:   0.3210 S13:  -0.3877                       
REMARK   3      S21:  -0.1436 S22:  -0.2126 S23:   0.5993                       
REMARK   3      S31:  -0.6533 S32:   0.1181 S33:   0.4656                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   257                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.8880 -13.3280  23.9310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3133 T22:   0.1559                                     
REMARK   3      T33:   0.1126 T12:   0.0102                                     
REMARK   3      T13:  -0.0118 T23:  -0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0867 L22:   2.7577                                     
REMARK   3      L33:   2.2555 L12:   0.3937                                     
REMARK   3      L13:  -0.5691 L23:  -1.0639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1616 S12:   0.0939 S13:  -0.2074                       
REMARK   3      S21:   0.0325 S22:   0.0854 S23:  -0.0641                       
REMARK   3      S31:   0.3513 S32:   0.0812 S33:   0.0762                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   W   700        W   710                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.1480 -11.2360   8.4700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1963 T22:   0.2725                                     
REMARK   3      T33:   0.0366 T12:  -0.0389                                     
REMARK   3      T13:   0.0156 T23:   0.0123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9306 L22:  28.2543                                     
REMARK   3      L33:   3.0531 L12:   6.0340                                     
REMARK   3      L13:  -0.7419 L23:  -8.2617                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0181 S12:  -0.3605 S13:  -0.1284                       
REMARK   3      S21:   0.7601 S22:   0.1820 S23:   0.2833                       
REMARK   3      S31:  -0.3045 S32:  -0.3118 S33:  -0.2001                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2ZVK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-NOV-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB028479.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-OCT-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 3.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NUMERICAL LINK TYPE SI(111)        
REMARK 200                                   DOUBLE CRYSTAL MONOCHROMATOR,      
REMARK 200                                   LIQUID NITROGEN COOLING            
REMARK 200  OPTICS                         : RHODIUM COATED SILICON SINGLE      
REMARK 200                                   CRYSTAL MIRRORS                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27933                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -0.400                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.1                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : 0.09300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
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: PDB ENTRY 1VYM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH3.6, HANGING DROP VAPOR DIFFUSION,     
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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      155.22150            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       41.01350            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       41.01350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      232.83225            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       41.01350            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       41.01350            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       77.61075            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       41.01350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       41.01350            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      232.83225            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       41.01350            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       41.01350            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       77.61075            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      155.22150            
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7980 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, U, B, V, C, W                      
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     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     GLU A   192                                                      
REMARK 465     GLU A   193                                                      
REMARK 465     ALA A   194                                                      
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     HIS U   713                                                      
REMARK 465     ALA B   163                                                      
REMARK 465     LYS B   164                                                      
REMARK 465     ASP B   165                                                      
REMARK 465     GLY B   166                                                      
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     GLU B   191                                                      
REMARK 465     GLU B   192                                                      
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     CYS V   693                                                      
REMARK 465     LYS V   694                                                      
REMARK 465     ARG V   695                                                      
REMARK 465     PRO V   696                                                      
REMARK 465     ARG V   697                                                      
REMARK 465     PRO V   698                                                      
REMARK 465     GLU V   699                                                      
REMARK 465     GLY V   700                                                      
REMARK 465     LEU V   711                                                      
REMARK 465     THR V   712                                                      
REMARK 465     HIS V   713                                                      
REMARK 465     GLN C   184                                                      
REMARK 465     THR C   185                                                      
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     GLU C   193                                                      
REMARK 465     GLU C   258                                                      
REMARK 465     GLU C   259                                                      
REMARK 465     GLY C   260                                                      
REMARK 465     SER C   261                                                      
REMARK 465     CYS W   693                                                      
REMARK 465     LYS W   694                                                      
REMARK 465     ARG W   695                                                      
REMARK 465     PRO W   696                                                      
REMARK 465     ARG W   697                                                      
REMARK 465     PRO W   698                                                      
REMARK 465     GLU W   699                                                      
REMARK 465     LEU W   711                                                      
REMARK 465     THR W   712                                                      
REMARK 465     HIS W   713                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A   64   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ARG A   91   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ASP A   94   CB   CG   OD1  OD2                                  
REMARK 480     ASN A  107   CB   CG   OD1  ND2                                  
REMARK 480     GLN A  108   CB   CG   CD   OE1  NE2                             
REMARK 480     GLU A  109   CG   CD   OE1  OE2                                  
REMARK 480     LYS A  110   CG   CD   CE   NZ                                   
REMARK 480     LYS A  117   CG   CD   CE   NZ                                   
REMARK 480     ASP A  122   CB   CG   OD1  OD2                                  
REMARK 480     GLU A  132   CB   CG   CD   OE1  OE2                             
REMARK 480     LYS A  138   CD   CE   NZ                                        
REMARK 480     GLU A  143   CD   OE1  OE2                                       
REMARK 480     ARG A  149   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS A  164   CB   CG   CD   CE   NZ                              
REMARK 480     ASP A  165   CB   CG   OD1  OD2                                  
REMARK 480     GLU A  174   CG   CD   OE1  OE2                                  
REMARK 480     LYS A  181   CG   CD   CE   NZ                                   
REMARK 480     GLU A  198   CG   CD   OE1  OE2                                  
REMARK 480     GLU A  201   CD   OE1  OE2                                       
REMARK 480     ARG A  210   NE   CZ   NH1  NH2                                  
REMARK 480     LYS A  240   CG   CD   CE   NZ                                   
REMARK 480     LYS U  694   CB   CG   CD   CE   NZ                              
REMARK 480     GLU U  699   CB   CG   CD   OE1  OE2                             
REMARK 480     ARG B   64   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLU B   85   CB   CG   CD   OE1  OE2                             
REMARK 480     ARG B   91   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLU B   93   CD   OE1  OE2                                       
REMARK 480     GLU B  104   CG   CD   OE1  OE2                                  
REMARK 480     GLN B  108   CG   CD   OE1  NE2                                  
REMARK 480     GLU B  109   CB   CG   CD   OE1  OE2                             
REMARK 480     LYS B  117   NZ                                                  
REMARK 480     ASP B  120   CG   OD1  OD2                                       
REMARK 480     ASP B  122   CG   OD1  OD2                                       
REMARK 480     VAL B  123   CB   CG1  CG2                                       
REMARK 480     GLN B  125   CG   CD   OE1  NE2                                  
REMARK 480     GLU B  130   CD   OE1  OE2                                       
REMARK 480     GLU B  132   CB   CG   CD   OE1  OE2                             
REMARK 480     LYS B  138   CD   CE   NZ                                        
REMARK 480     ARG B  149   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLU B  174   CG   CD   OE1  OE2                                  
REMARK 480     GLU B  193   CG   CD   OE1  OE2                                  
REMARK 480     GLU B  201   CG   CD   OE1  OE2                                  
REMARK 480     ASP B  232   CB   CG   OD1  OD2                                  
REMARK 480     LYS B  240   CG   CD   CE   NZ                                   
REMARK 480     ASP B  243   CG   OD1  OD2                                       
REMARK 480     LYS B  254   CE   NZ                                             
REMARK 480     GLU C   55   CD   OE1  OE2                                       
REMARK 480     ARG C   64   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     LYS C   80   CG   CD   CE   NZ                                   
REMARK 480     GLU C   85   CG   CD   OE1  OE2                                  
REMARK 480     GLU C  104   CD   OE1  OE2                                       
REMARK 480     GLN C  108   CB   CG   CD   OE1  NE2                             
REMARK 480     ASP C  122   CB   CG   OD1  OD2                                  
REMARK 480     GLU C  124   CG   CD   OE1  OE2                                  
REMARK 480     GLU C  132   CG   CD   OE1  OE2                                  
REMARK 480     ARG C  149   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS C  164   CG   CD   CE   NZ                                   
REMARK 480     GLU C  174   CG   CD   OE1  OE2                                  
REMARK 480     GLU C  198   CD   OE1  OE2                                       
REMARK 480     LYS C  217   CE   NZ                                             
REMARK 480     LYS C  240   CE   NZ                                             
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    GLN A   8       62.41   -100.28                                   
REMARK 500    SER A  10      -44.96    -29.08                                   
REMARK 500    ASP A  58       -9.91    -56.41                                   
REMARK 500    LEU A  66      119.52   -161.11                                   
REMARK 500    ASN A  71       96.96    -58.73                                   
REMARK 500    ASP A  94       51.48    -67.26                                   
REMARK 500    ASN A  95      -80.90    162.90                                   
REMARK 500    ALA A  96      139.60    -11.92                                   
REMARK 500    THR A  98      116.55   -163.51                                   
REMARK 500    ALA A 105     -151.02   -144.85                                   
REMARK 500    PRO A 106      -97.98    -76.63                                   
REMARK 500    GLN A 108       59.12    -38.09                                   
REMARK 500    ASP A 120      109.25    -53.13                                   
REMARK 500    ASP A 122       34.74    -96.48                                   
REMARK 500    GLN A 184      111.45     -5.76                                   
REMARK 500    MET A 244      -34.43   -146.36                                   
REMARK 500    THR U 703      152.24    -46.06                                   
REMARK 500    GLN B   8       71.91   -100.71                                   
REMARK 500    ALA B  26      153.63    179.45                                   
REMARK 500    CYS B  62      108.91   -174.91                                   
REMARK 500    ASN B  65      171.74    -58.28                                   
REMARK 500    ASP B  94      -70.77      0.35                                   
REMARK 500    PRO B 106      -97.16    -17.50                                   
REMARK 500    ASN B 107       94.98    -66.10                                   
REMARK 500    GLN B 108       79.49     -6.26                                   
REMARK 500    GLU B 109      -55.10   -138.12                                   
REMARK 500    GLU B 124      147.98    -36.08                                   
REMARK 500    SER B 161       81.26   -161.26                                   
REMARK 500    GLN B 184     -175.03     54.97                                   
REMARK 500    PRO B 202      135.73    -38.90                                   
REMARK 500    ALA B 231      160.28    -49.07                                   
REMARK 500    ASP B 232       32.90     39.02                                   
REMARK 500    MET B 244      -15.53   -166.61                                   
REMARK 500    GLN C   8       76.09   -103.04                                   
REMARK 500    SER C  32      -53.32    -20.16                                   
REMARK 500    ASP C  41     -177.13    -68.36                                   
REMARK 500    GLU C  55       -0.44    -56.25                                   
REMARK 500    ASN C  65      153.14    -47.61                                   
REMARK 500    ASN C  95      -81.93    -38.33                                   
REMARK 500    ALA C  96       86.90     96.14                                   
REMARK 500    ASP C  97       42.26   -149.03                                   
REMARK 500    THR C  98      105.98    165.74                                   
REMARK 500    PRO C 106        5.24    -64.00                                   
REMARK 500    LEU C 118     -155.13    -93.20                                   
REMARK 500    CYS C 135      135.66    175.14                                   
REMARK 500    ASP C 150      -69.39    -23.31                                   
REMARK 500    LYS C 164       36.48    -84.05                                   
REMARK 500    ASP C 165       40.80    163.13                                   
REMARK 500    PRO C 202      150.99    -47.60                                   
REMARK 500    THR C 216       -7.20    -51.67                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      54 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ZVL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2ZVM   RELATED DB: PDB                                   
DBREF  2ZVK A    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  2ZVK U  693   713  PDB    2ZVK     2ZVK           693    713             
DBREF  2ZVK B    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  2ZVK V  693   713  PDB    2ZVK     2ZVK           693    713             
DBREF  2ZVK C    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  2ZVK W  693   713  PDB    2ZVK     2ZVK           693    713             
SEQRES   1 A  261  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 A  261  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 A  261  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 A  261  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 A  261  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 A  261  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 A  261  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 A  261  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 A  261  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 A  261  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 A  261  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 A  261  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 A  261  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 A  261  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 A  261  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 A  261  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 A  261  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 A  261  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 A  261  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 A  261  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 A  261  SER                                                          
SEQRES   1 U   21  CYS LYS ARG PRO ARG PRO GLU GLY MET GLN THR LEU GLU          
SEQRES   2 U   21  SER PHE PHE LYS PRO LEU THR HIS                              
SEQRES   1 B  261  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 B  261  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 B  261  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 B  261  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 B  261  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 B  261  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 B  261  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 B  261  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 B  261  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 B  261  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 B  261  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 B  261  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 B  261  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 B  261  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 B  261  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 B  261  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 B  261  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 B  261  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 B  261  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 B  261  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 B  261  SER                                                          
SEQRES   1 V   21  CYS LYS ARG PRO ARG PRO GLU GLY MET GLN THR LEU GLU          
SEQRES   2 V   21  SER PHE PHE LYS PRO LEU THR HIS                              
SEQRES   1 C  261  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 C  261  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 C  261  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 C  261  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 C  261  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 C  261  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 C  261  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 C  261  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 C  261  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 C  261  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 C  261  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 C  261  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 C  261  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 C  261  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 C  261  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 C  261  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 C  261  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 C  261  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 C  261  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 C  261  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 C  261  SER                                                          
SEQRES   1 W   21  CYS LYS ARG PRO ARG PRO GLU GLY MET GLN THR LEU GLU          
SEQRES   2 W   21  SER PHE PHE LYS PRO LEU THR HIS                              
FORMUL   7  HOH   *18(H2 O)                                                     
HELIX    1   1 GLY A    9  ASP A   21  1                                  13    
HELIX    2   2 GLU A   55  PHE A   57  5                                   3    
HELIX    3   3 LEU A   72  LYS A   80  1                                   9    
HELIX    4   4 SER A  141  SER A  152  1                                  12    
HELIX    5   5 LEU A  209  THR A  216  1                                   8    
HELIX    6   6 LYS A  217  SER A  222  5                                   6    
HELIX    7   7 THR U  703  PHE U  707  5                                   5    
HELIX    8   8 GLY B    9  ASP B   21  1                                  13    
HELIX    9   9 LEU B   72  LYS B   80  1                                   9    
HELIX   10  10 SER B  141  HIS B  153  1                                  13    
HELIX   11  11 LEU B  209  THR B  216  1                                   8    
HELIX   12  12 LYS B  217  SER B  222  5                                   6    
HELIX   13  13 GLY C    9  ASP C   21  1                                  13    
HELIX   14  14 GLU C   55  PHE C   57  5                                   3    
HELIX   15  15 LEU C   72  LYS C   80  1                                   9    
HELIX   16  16 SER C  141  HIS C  153  1                                  13    
HELIX   17  17 LEU C  209  THR C  216  1                                   8    
HELIX   18  18 LYS C  217  SER C  222  5                                   6    
HELIX   19  19 THR W  703  PHE W  707  5                                   5    
SHEET    1   A 9 THR A  59  CYS A  62  0                                        
SHEET    2   A 9 PHE A   2  LEU A   6 -1  N  GLU A   3   O  ARG A  61           
SHEET    3   A 9 ILE A  88  ALA A  92 -1  O  LEU A  90   N  ALA A   4           
SHEET    4   A 9 THR A  98  PHE A 103 -1  O  ALA A 100   N  ARG A  91           
SHEET    5   A 9 LYS A 110  LYS A 117 -1  O  MET A 116   N  LEU A  99           
SHEET    6   A 9 GLY B 176  LEU B 182 -1  O  ASN B 179   N  ASP A 113           
SHEET    7   A 9 LYS B 168  GLY B 173 -1  N  ALA B 171   O  GLY B 178           
SHEET    8   A 9 ALA B 157  ILE B 160 -1  N  VAL B 159   O  SER B 170           
SHEET    9   A 9 THR B 206  ALA B 208 -1  O  PHE B 207   N  VAL B 158           
SHEET    1   B 9 LEU A  66  ASN A  71  0                                        
SHEET    2   B 9 GLU A  25  ILE A  30 -1  N  ILE A  30   O  LEU A  66           
SHEET    3   B 9 GLY A  34  MET A  40 -1  O  ASN A  36   N  ASP A  29           
SHEET    4   B 9 SER A  46  ARG A  53 -1  O  LEU A  50   N  LEU A  37           
SHEET    5   B 9 GLY A 245  LEU A 251 -1  O  TYR A 250   N  LEU A  47           
SHEET    6   B 9 LEU A 235  ILE A 241 -1  N  VAL A 237   O  TYR A 249           
SHEET    7   B 9 THR A 224  MET A 229 -1  N  THR A 226   O  GLU A 238           
SHEET    8   B 9 CYS A 135  PRO A 140 -1  N  MET A 139   O  VAL A 225           
SHEET    9   B 9 THR A 196  MET A 199 -1  O  THR A 196   N  LYS A 138           
SHEET    1   C 9 GLN A 204  ALA A 208  0                                        
SHEET    2   C 9 ALA A 157  ALA A 163 -1  N  VAL A 158   O  PHE A 207           
SHEET    3   C 9 GLY A 166  GLY A 173 -1  O  LYS A 168   N  SER A 161           
SHEET    4   C 9 GLY A 176  SER A 183 -1  O  ILE A 180   N  PHE A 169           
SHEET    5   C 9 LYS C 110  MET C 116 -1  O  ASP C 113   N  ASN A 179           
SHEET    6   C 9 LEU C  99  GLU C 104 -1  N  LEU C  99   O  MET C 116           
SHEET    7   C 9 ILE C  87  ALA C  92 -1  N  ARG C  91   O  ALA C 100           
SHEET    8   C 9 PHE C   2  LEU C   6 -1  N  LEU C   6   O  ILE C  88           
SHEET    9   C 9 THR C  59  ARG C  61 -1  O  THR C  59   N  ARG C   5           
SHEET    1   D 9 THR B  59  ARG B  61  0                                        
SHEET    2   D 9 PHE B   2  LEU B   6 -1  N  GLU B   3   O  ARG B  61           
SHEET    3   D 9 ILE B  87  ALA B  92 -1  O  ILE B  88   N  LEU B   6           
SHEET    4   D 9 THR B  98  GLU B 104 -1  O  VAL B 102   N  THR B  89           
SHEET    5   D 9 LYS B 110  LYS B 117 -1  O  MET B 116   N  LEU B  99           
SHEET    6   D 9 GLY C 176  LEU C 182 -1  O  LYS C 181   N  VAL B 111           
SHEET    7   D 9 GLY C 166  GLY C 173 -1  N  VAL C 167   O  LEU C 182           
SHEET    8   D 9 ALA C 157  ALA C 163 -1  N  VAL C 159   O  SER C 170           
SHEET    9   D 9 VAL C 203  ALA C 208 -1  O  PHE C 207   N  VAL C 158           
SHEET    1   E 6 LEU B  66  ASN B  71  0                                        
SHEET    2   E 6 GLU B  25  SER B  31 -1  N  TRP B  28   O  MET B  68           
SHEET    3   E 6 GLY B  34  MET B  40 -1  O  ASN B  36   N  ASP B  29           
SHEET    4   E 6 SER B  46  ARG B  53 -1  O  LEU B  50   N  LEU B  37           
SHEET    5   E 6 GLY B 245  LEU B 251 -1  O  TYR B 250   N  LEU B  47           
SHEET    6   E 6 LEU B 235  ILE B 241 -1  N  VAL B 237   O  TYR B 249           
SHEET    1   F 3 THR B 196  MET B 199  0                                        
SHEET    2   F 3 CYS B 135  PRO B 140 -1  N  LYS B 138   O  THR B 196           
SHEET    3   F 3 THR B 224  MET B 229 -1  O  MET B 229   N  CYS B 135           
SHEET    1   G 9 LEU C  66  ASN C  71  0                                        
SHEET    2   G 9 GLU C  25  ILE C  30 -1  N  ALA C  26   O  VAL C  70           
SHEET    3   G 9 GLY C  34  MET C  40 -1  O  ASN C  36   N  ASP C  29           
SHEET    4   G 9 SER C  46  ARG C  53 -1  O  VAL C  48   N  SER C  39           
SHEET    5   G 9 GLY C 245  LEU C 251 -1  O  HIS C 246   N  THR C  51           
SHEET    6   G 9 VAL C 233  ILE C 241 -1  N  LEU C 235   O  LEU C 251           
SHEET    7   G 9 THR C 224  SER C 230 -1  N  SER C 228   O  VAL C 236           
SHEET    8   G 9 VAL C 136  PRO C 140 -1  N  MET C 139   O  VAL C 225           
SHEET    9   G 9 THR C 196  GLU C 198 -1  O  THR C 196   N  LYS C 138           
SSBOND   1 CYS U  693    CYS B   27                          1555   6455  2.02  
SSBOND   2 CYS C  135    CYS C  162                          1555   1555  2.59  
CRYST1   82.027   82.027  310.443  90.00  90.00  90.00 P 43 21 2    24          
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      0.012191  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012191  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003221        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system