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Database: PDB
Entry: 2ZVM
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HEADER    TRANSFERASE                             11-NOV-08   2ZVM              
TITLE     CRYSTAL STRUCTURE OF PCNA IN COMPLEX WITH DNA POLYMERASE IOTA 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 IOTA;                                       
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: T7;                                   
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, COMPLEX, PIP-BOX, DNA POLYMERASE IOTA, TRANSFERASE       
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 2ZVM    1       VERSN                                    
REVDAT   2   21-APR-09 2ZVM    1       JRNL                                     
REVDAT   1   10-FEB-09 2ZVM    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.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 42715                          
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2249                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2700                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2250                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 143                          
REMARK   3   BIN FREE R VALUE                    : 0.2820                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5985                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 225                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.51                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.53000                                             
REMARK   3    B22 (A**2) : 0.40000                                              
REMARK   3    B33 (A**2) : 0.20000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.43000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.261         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.222         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.171         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.736        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5948 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3961 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8027 ; 1.790 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9729 ; 4.420 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   765 ; 7.385 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   226 ;44.167 ;25.265       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1079 ;16.580 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;19.853 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   955 ; 0.105 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6526 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1093 ; 0.009 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1050 ; 0.211 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3711 ; 0.241 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2728 ; 0.177 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3101 ; 0.118 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   229 ; 0.173 ; 0.200       
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):    16 ; 0.240 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    38 ; 0.385 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.242 ; 0.200       
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):  4907 ; 1.533 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1565 ; 0.027 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6151 ; 1.780 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2410 ; 2.841 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1876 ; 4.241 ; 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):  24.7990  15.9700  43.8850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0962 T22:  -0.0420                                     
REMARK   3      T33:  -0.0185 T12:  -0.0319                                     
REMARK   3      T13:   0.0776 T23:  -0.0326                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7060 L22:   0.4347                                     
REMARK   3      L33:   1.0103 L12:   0.2747                                     
REMARK   3      L13:  -0.1803 L23:   0.2843                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0133 S12:  -0.0757 S13:   0.1231                       
REMARK   3      S21:  -0.0079 S22:  -0.0217 S23:   0.0880                       
REMARK   3      S31:  -0.1705 S32:   0.0345 S33:   0.0084                       
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   420        U   432                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.4220  16.2060  62.4170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0035 T22:   0.2116                                     
REMARK   3      T33:  -0.0336 T12:  -0.0572                                     
REMARK   3      T13:   0.0731 T23:  -0.0166                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.4356 L22:  13.0791                                     
REMARK   3      L33:   9.2921 L12: -12.3148                                     
REMARK   3      L13:  -6.8168 L23:  10.2030                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3380 S12:  -1.1585 S13:   0.3278                       
REMARK   3      S21:   0.8656 S22:   0.4714 S23:  -0.2447                       
REMARK   3      S31:   0.4211 S32:   0.8108 S33:  -0.1334                       
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   255                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.2680 -14.1400  15.3050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1232 T22:  -0.0003                                     
REMARK   3      T33:   0.0038 T12:  -0.0679                                     
REMARK   3      T13:   0.0655 T23:  -0.0663                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1325 L22:   0.8634                                     
REMARK   3      L33:   1.9414 L12:  -0.3301                                     
REMARK   3      L13:  -1.1142 L23:   0.8677                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0612 S12:   0.0679 S13:  -0.0196                       
REMARK   3      S21:  -0.1253 S22:   0.0381 S23:   0.0065                       
REMARK   3      S31:  -0.0464 S32:  -0.0786 S33:   0.0232                       
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   420        V   429                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.1530 -25.9390  26.8200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1030 T22:   0.0355                                     
REMARK   3      T33:  -0.0038 T12:  -0.0971                                     
REMARK   3      T13:   0.1152 T23:  -0.0361                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  18.8645 L22:   9.3994                                     
REMARK   3      L33:   8.5497 L12:   6.3544                                     
REMARK   3      L13:   3.0119 L23:  -0.4611                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4631 S12:   0.1496 S13:  -0.9224                       
REMARK   3      S21:  -0.2327 S22:   0.2700 S23:  -0.1616                       
REMARK   3      S31:   1.0366 S32:  -0.2867 S33:   0.1931                       
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   256                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.4730  -2.4720  15.5320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1386 T22:   0.0190                                     
REMARK   3      T33:  -0.0535 T12:  -0.0442                                     
REMARK   3      T13:   0.0708 T23:   0.0235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4401 L22:   1.3526                                     
REMARK   3      L33:   0.9559 L12:   0.8142                                     
REMARK   3      L13:   0.0118 L23:   0.6618                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0380 S12:  -0.0442 S13:  -0.1366                       
REMARK   3      S21:  -0.0635 S22:  -0.0079 S23:  -0.0673                       
REMARK   3      S31:   0.0017 S32:   0.0969 S33:   0.0460                       
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   421        W   429                          
REMARK   3    ORIGIN FOR THE GROUP (A):  62.2970 -19.2740  14.1400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0378 T22:   0.0129                                     
REMARK   3      T33:  -0.0034 T12:   0.1519                                     
REMARK   3      T13:   0.0898 T23:   0.0529                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  18.6810 L22:   9.0376                                     
REMARK   3      L33:   4.3300 L12:   2.9902                                     
REMARK   3      L13:   4.0195 L23:   4.9182                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0398 S12:   0.2651 S13:  -0.3136                       
REMARK   3      S21:   0.6810 S22:  -0.1068 S23:  -0.2054                       
REMARK   3      S31:   0.7453 S32:   0.9669 S33:   0.0669                       
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 2ZVM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-NOV-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB028481.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-FEB-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.4                                
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44815                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
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   (%): 55.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH6.4, HANGING DROP VAPOR DIFFUSION,     
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       83.81000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.41000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       83.81000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.41000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.3 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     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     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     ALA U   415                                                      
REMARK 465     LEU U   416                                                      
REMARK 465     ASN U   417                                                      
REMARK 465     THR U   418                                                      
REMARK 465     ALA U   419                                                      
REMARK 465     SER U   433                                                      
REMARK 465     THR U   434                                                      
REMARK 465     THR U   435                                                      
REMARK 465     SER U   436                                                      
REMARK 465     ARG U   437                                                      
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     GLU B   193                                                      
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     ALA V   415                                                      
REMARK 465     LEU V   416                                                      
REMARK 465     ASN V   417                                                      
REMARK 465     THR V   418                                                      
REMARK 465     ALA V   419                                                      
REMARK 465     PRO V   430                                                      
REMARK 465     SER V   431                                                      
REMARK 465     LEU V   432                                                      
REMARK 465     SER V   433                                                      
REMARK 465     THR V   434                                                      
REMARK 465     THR V   435                                                      
REMARK 465     SER V   436                                                      
REMARK 465     ARG V   437                                                      
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     ASP C   257                                                      
REMARK 465     GLU C   258                                                      
REMARK 465     GLU C   259                                                      
REMARK 465     GLY C   260                                                      
REMARK 465     SER C   261                                                      
REMARK 465     ALA W   415                                                      
REMARK 465     LEU W   416                                                      
REMARK 465     ASN W   417                                                      
REMARK 465     THR W   418                                                      
REMARK 465     ALA W   419                                                      
REMARK 465     LYS W   420                                                      
REMARK 465     PRO W   430                                                      
REMARK 465     SER W   431                                                      
REMARK 465     LEU W   432                                                      
REMARK 465     SER W   433                                                      
REMARK 465     THR W   434                                                      
REMARK 465     THR W   435                                                      
REMARK 465     SER W   436                                                      
REMARK 465     ARG W   437                                                      
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     LYS A   80   NZ                                                  
REMARK 480     ASN A  107   CA   CB   CG   OD1  ND2                             
REMARK 480     GLU A  109   CB   CG   CD   OE1  OE2                             
REMARK 480     VAL A  123   CB   CG1  CG2                                       
REMARK 480     GLN A  125   CG   CD   OE1  NE2                                  
REMARK 480     LYS A  138   CD   CE   NZ                                        
REMARK 480     LYS A  240   CD   CE   NZ                                        
REMARK 480     GLU B   93   CD   OE1  OE2                                       
REMARK 480     ASN B  107   CB   CG   OD1  ND2                                  
REMARK 480     GLN B  108   CG   CD   OE1  NE2                                  
REMARK 480     GLU B  109   CB   CG   CD   OE1  OE2                             
REMARK 480     GLN B  125   CG   CD   OE1  NE2                                  
REMARK 480     GLU B  132   CB   CG   CD   OE1  OE2                             
REMARK 480     ARG B  146   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS B  164   CB   CG   CD   CE   NZ                              
REMARK 480     ASP B  165   CB   CG   OD1  OD2                                  
REMARK 480     GLU B  198   CG   CD   OE1  OE2                                  
REMARK 480     LYS V  421   CE   NZ                                             
REMARK 480     PRO C  106   CB                                                  
REMARK 480     ASN C  107   CB   CG   OD1  ND2                                  
REMARK 480     GLU C  109   CG   CD   OE1  OE2                                  
REMARK 480     ASP C  120   CB   CG   OD1  OD2                                  
REMARK 480     ASP C  122   CB   CG   OD1  OD2                                  
REMARK 480     GLU C  124   CB   CG   CD   OE1  OE2                             
REMARK 480     GLU C  132   CG   CD   OE1  OE2                                  
REMARK 480     LYS C  138   CE   NZ                                             
REMARK 480     LYS C  164   CG   CD   CE   NZ                                   
REMARK 480     ASP C  165   CG   OD1  OD2                                       
REMARK 480     GLU C  198   CD   OE1  OE2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LYS A  80   CD  -  CE  -  NZ  ANGL. DEV. =  16.5 DEGREES          
REMARK 500    LEU B  66   CA  -  CB  -  CG  ANGL. DEV. =  16.9 DEGREES          
REMARK 500    GLN B 125   CA  -  CB  -  CG  ANGL. DEV. =  31.4 DEGREES          
REMARK 500    GLU B 132   CB  -  CA  -  C   ANGL. DEV. =  17.0 DEGREES          
REMARK 500    GLU B 132   N   -  CA  -  CB  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    GLU B 132   CA  -  CB  -  CG  ANGL. DEV. =  14.5 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    HIS A  44       17.17     58.97                                   
REMARK 500    ASN A  95       40.90   -102.99                                   
REMARK 500    ASN A 107      -61.32    -91.12                                   
REMARK 500    ASP A 122       71.47   -107.73                                   
REMARK 500    MET A 244      -38.49   -151.90                                   
REMARK 500    ASP U 425      -35.76    -39.15                                   
REMARK 500    GLN B 108     -172.42     84.68                                   
REMARK 500    LYS B 217       -8.01    -59.63                                   
REMARK 500    ALA B 242     -132.49     51.92                                   
REMARK 500    ASP B 243       75.09   -114.78                                   
REMARK 500    MET B 244      -10.14   -172.23                                   
REMARK 500    GLU C 109       75.50   -104.70                                   
REMARK 500    VAL C 123      -98.45    -54.75                                   
REMARK 500    GLU C 124       74.36     64.49                                   
REMARK 500    MET C 244      -17.48   -166.05                                   
REMARK 500    ILE C 255      -70.62    -94.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLU B 132        10.9      L          L   OUTSIDE RANGE           
REMARK 500    LYS B 164        24.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ZVK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2ZVL   RELATED DB: PDB                                   
DBREF  2ZVM A    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  2ZVM U  415   437  PDB    2ZVM     2ZVM           415    437             
DBREF  2ZVM B    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  2ZVM V  415   437  PDB    2ZVM     2ZVM           415    437             
DBREF  2ZVM C    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  2ZVM W  415   437  PDB    2ZVM     2ZVM           415    437             
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   23  ALA LEU ASN THR ALA LYS LYS GLY LEU ILE ASP TYR TYR          
SEQRES   2 U   23  LEU MET PRO SER LEU SER THR THR SER ARG                      
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   23  ALA LEU ASN THR ALA LYS LYS GLY LEU ILE ASP TYR TYR          
SEQRES   2 V   23  LEU MET PRO SER LEU SER THR THR SER ARG                      
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   23  ALA LEU ASN THR ALA LYS LYS GLY LEU ILE ASP TYR TYR          
SEQRES   2 W   23  LEU MET PRO SER LEU SER THR THR SER ARG                      
FORMUL   7  HOH   *225(H2 O)                                                    
HELIX    1   1 GLY A    9  ALA A   18  1                                  10    
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 LEU U  423  TYR U  427  5                                   5    
HELIX    8   8 GLY B    9  LYS B   20  1                                  12    
HELIX    9   9 GLU B   55  PHE B   57  5                                   3    
HELIX   10  10 LEU B   72  CYS B   81  1                                  10    
HELIX   11  11 SER B  141  SER B  152  1                                  12    
HELIX   12  12 LEU B  209  THR B  216  1                                   8    
HELIX   13  13 LYS B  217  SER B  222  5                                   6    
HELIX   14  14 LEU V  423  LEU V  428  5                                   6    
HELIX   15  15 GLY C    9  ALA C   18  1                                  10    
HELIX   16  16 GLU C   55  PHE C   57  5                                   3    
HELIX   17  17 LEU C   72  LYS C   80  1                                   9    
HELIX   18  18 SER C  141  GLY C  155  1                                  15    
HELIX   19  19 LEU C  209  THR C  216  1                                   8    
HELIX   20  20 LYS C  217  SER C  222  5                                   6    
HELIX   21  21 LEU W  423  LEU W  428  5                                   6    
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  87  ALA A  92 -1  O  ILE A  88   N  LEU A   6           
SHEET    4   A 9 THR A  98  GLU A 104 -1  O  GLU A 104   N  ILE A  87           
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  SER B 183 -1  O  LYS B 181   N  VAL A 111           
SHEET    7   A 9 GLY B 166  SER B 172 -1  N  PHE B 169   O  ILE B 180           
SHEET    8   A 9 ALA B 157  CYS B 162 -1  N  SER B 161   O  LYS B 168           
SHEET    9   A 9 VAL B 203  ALA B 208 -1  O  LEU B 205   N  ILE B 160           
SHEET    1   B 9 LEU A  66  ASN A  71  0                                        
SHEET    2   B 9 GLU A  25  SER A  31 -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  52   N  VAL A  35           
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  VAL A 137   O  LEU A 227           
SHEET    9   B 9 THR A 196  MET A 199 -1  O  THR A 196   N  LYS A 138           
SHEET    1   C 9 VAL A 203  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  SER A 170   N  VAL A 159           
SHEET    4   C 9 GLY A 176  SER A 183 -1  O  GLY A 176   N  GLY A 173           
SHEET    5   C 9 LYS C 110  LYS C 117 -1  O  VAL C 111   N  LYS A 181           
SHEET    6   C 9 THR C  98  GLU C 104 -1  N  LEU C 101   O  TYR C 114           
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  PHE C   2   O  ALA C  92           
SHEET    9   C 9 THR C  59  CYS C  62 -1  O  ARG C  61   N  GLU C   3           
SHEET    1   D 9 THR B  59  CYS B  62  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  GLU B 104   N  ILE B  87           
SHEET    5   D 9 LYS B 110  LYS B 117 -1  O  TYR B 114   N  LEU B 101           
SHEET    6   D 9 GLY C 176  SER C 183 -1  O  LYS C 181   N  VAL B 111           
SHEET    7   D 9 GLY C 166  GLY C 173 -1  N  GLY C 173   O  GLY C 176           
SHEET    8   D 9 ALA C 157  CYS C 162 -1  N  SER C 161   O  LYS C 168           
SHEET    9   D 9 VAL C 203  ALA C 208 -1  O  LEU C 205   N  ILE C 160           
SHEET    1   E 9 LEU B  66  ASN B  71  0                                        
SHEET    2   E 9 GLU B  25  SER B  31 -1  N  ILE B  30   O  LEU B  66           
SHEET    3   E 9 GLY B  34  MET B  40 -1  O  ASN B  36   N  ASP B  29           
SHEET    4   E 9 SER B  46  ARG B  53 -1  O  LEU B  52   N  VAL B  35           
SHEET    5   E 9 GLY B 245  LEU B 251 -1  O  LYS B 248   N  GLN B  49           
SHEET    6   E 9 LEU B 235  ILE B 241 -1  N  ILE B 241   O  GLY B 245           
SHEET    7   E 9 THR B 224  MET B 229 -1  N  SER B 228   O  VAL B 236           
SHEET    8   E 9 CYS B 135  PRO B 140 -1  N  VAL B 137   O  LEU B 227           
SHEET    9   E 9 THR B 196  MET B 199 -1  O  THR B 196   N  LYS B 138           
SHEET    1   F 9 LEU C  66  ASN C  71  0                                        
SHEET    2   F 9 GLU C  25  SER C  31 -1  N  ILE C  30   O  LEU C  66           
SHEET    3   F 9 GLY C  34  MET C  40 -1  O  ASN C  36   N  ASP C  29           
SHEET    4   F 9 SER C  46  ARG C  53 -1  O  LEU C  52   N  VAL C  35           
SHEET    5   F 9 GLY C 245  LEU C 251 -1  O  TYR C 250   N  LEU C  47           
SHEET    6   F 9 LEU C 235  ILE C 241 -1  N  TYR C 239   O  LEU C 247           
SHEET    7   F 9 THR C 224  MET C 229 -1  N  SER C 228   O  VAL C 236           
SHEET    8   F 9 CYS C 135  PRO C 140 -1  N  VAL C 137   O  LEU C 227           
SHEET    9   F 9 THR C 196  MET C 199 -1  O  THR C 196   N  LYS C 138           
CISPEP   1 MET U  429    PRO U  430          0        -7.75                     
CRYST1  167.620   68.820   90.180  90.00  95.05  90.00 C 1 2 1      12          
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      0.005966  0.000000  0.000527        0.00000                         
SCALE2      0.000000  0.014531  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011132        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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