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Database: PDB
Entry: 6FCN
LinkDB: 6FCN
Original site: 6FCN 
HEADER    NUCLEAR PROTEIN                         20-DEC-17   6FCN              
TITLE     CRYSTAL STRUCTURE OF HUMAN PCNA SOAKED WITH P47PHOX(106-127) PEPTIDE  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;                        
COMPND   3 CHAIN: A, C, E;                                                      
COMPND   4 SYNONYM: PCNA,CYCLIN;                                                
COMPND   5 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                                         
KEYWDS    PROLIFERATING CELL NUCLEAR ANTIGEN, NUCLEAR PROTEIN                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.HOUSSET,P.FRACHET                                                   
REVDAT   3   13-NOV-19 6FCN    1       JRNL                                     
REVDAT   2   18-SEP-19 6FCN    1       JRNL                                     
REVDAT   1   30-JAN-19 6FCN    0                                                
JRNL        AUTH   D.OHAYON,A.DE CHIARA,P.M.DANG,N.THIEBLEMONT,S.CHATFIELD,     
JRNL        AUTH 2 V.MARZAIOLI,S.S.BURGENER,J.MOCEK,C.CANDALH,C.PINTARD,        
JRNL        AUTH 3 P.TACNET-DELORME,G.RENAULT,I.LAGOUTTE,M.FAVIER,F.WALKER,     
JRNL        AUTH 4 M.HURTADO-NEDELEC,D.DESPLANCQ,E.WEISS,C.BENARAFA,D.HOUSSET,  
JRNL        AUTH 5 J.C.MARIE,P.FRACHET,J.EL-BENNA,V.WITKO-SARSAT                
JRNL        TITL   CYTOSOLIC PCNA INTERACTS WITH P47PHOX AND CONTROLS NADPH     
JRNL        TITL 2 OXIDASE NOX2 ACTIVATION IN NEUTROPHILS.                      
JRNL        REF    J.EXP.MED.                    V. 216  2669 2019              
JRNL        REFN                   ESSN 1540-9538                               
JRNL        PMID   31492810                                                     
JRNL        DOI    10.1084/JEM.20180371                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.22 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.22                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 14362                          
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) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 733                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.22                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.30                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 808                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 70.87                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4250                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 46                           
REMARK   3   BIN FREE R VALUE                    : 0.4260                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5777                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 7                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 118.1                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.15000                                              
REMARK   3    B22 (A**2) : -0.15000                                             
REMARK   3    B33 (A**2) : 0.00000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.581         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.480         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.719        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.902                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5852 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5546 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7903 ; 1.233 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 12903 ; 0.855 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   749 ; 6.655 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   239 ;45.814 ;25.607       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1081 ;16.483 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;13.856 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   940 ; 0.072 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6436 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1064 ; 0.002 ; 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):  3014 ; 5.926 ;11.873       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3013 ; 5.921 ;11.872       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3757 ; 9.537 ;17.807       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3758 ; 9.536 ;17.808       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2838 ; 5.729 ;12.378       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2838 ; 5.727 ;12.378       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4146 ; 9.317 ;18.368       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5789 ;13.532 ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5788 ;13.532 ;  NULL       
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 : 5                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A C E                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      3       A      92      2                      
REMARK   3           1     C      3       C      92      2                      
REMARK   3           1     E      3       E      92      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    822 ;  0.01 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):    822 ;  0.01 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    E    (A):    822 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):    535 ; 10.68 ;  0.50           
REMARK   3   TIGHT THERMAL      1    C (A**2):    535 ; 11.34 ;  0.50           
REMARK   3   TIGHT THERMAL      1    E (A**2):    535 ; 17.97 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    822 ; 11.57 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):    822 ; 10.89 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    E (A**2):    822 ; 17.47 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A C E                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     96       A     105      2                      
REMARK   3           1     C     96       C     105      2                      
REMARK   3           1     E     96       E     105      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):     84 ;  0.02 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    C    (A):     84 ;  0.03 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    E    (A):     84 ;  0.03 ;  0.50           
REMARK   3   TIGHT THERMAL      2    A (A**2):     60 ; 14.65 ;  0.50           
REMARK   3   TIGHT THERMAL      2    C (A**2):     60 ;  5.35 ;  0.50           
REMARK   3   TIGHT THERMAL      2    E (A**2):     60 ; 15.73 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    A (A**2):     84 ; 13.83 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    C (A**2):     84 ;  6.64 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    E (A**2):     84 ; 13.32 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A C E                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    110       A     121      2                      
REMARK   3           1     C    110       C     121      2                      
REMARK   3           1     E    110       E     121      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  3    A    (A):    129 ;  0.01 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    C    (A):    129 ;  0.02 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    E    (A):    129 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL      3    A (A**2):     72 ; 12.89 ;  0.50           
REMARK   3   TIGHT THERMAL      3    C (A**2):     72 ;  8.05 ;  0.50           
REMARK   3   TIGHT THERMAL      3    E (A**2):     72 ; 12.81 ;  0.50           
REMARK   3   MEDIUM THERMAL     3    A (A**2):    129 ; 12.65 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    C (A**2):    129 ;  8.90 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    E (A**2):    129 ; 13.35 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : A C E                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    132       A     185      2                      
REMARK   3           1     C    132       C     185      2                      
REMARK   3           1     E    132       E     185      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  4    A    (A):    454 ;  0.01 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  4    C    (A):    454 ;  0.01 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  4    E    (A):    454 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL      4    A (A**2):    317 ; 10.03 ;  0.50           
REMARK   3   TIGHT THERMAL      4    C (A**2):    317 ; 15.57 ;  0.50           
REMARK   3   TIGHT THERMAL      4    E (A**2):    317 ; 16.84 ;  0.50           
REMARK   3   MEDIUM THERMAL     4    A (A**2):    454 ; 10.28 ;  2.00           
REMARK   3   MEDIUM THERMAL     4    C (A**2):    454 ; 14.20 ;  2.00           
REMARK   3   MEDIUM THERMAL     4    E (A**2):    454 ; 14.53 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : A C E                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    192       A     255      2                      
REMARK   3           1     C    192       C     255      2                      
REMARK   3           1     E    192       E     255      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  5    A    (A):    601 ;  0.01 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  5    C    (A):    601 ;  0.01 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  5    E    (A):    601 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL      5    A (A**2):    379 ;  7.37 ;  0.50           
REMARK   3   TIGHT THERMAL      5    C (A**2):    379 ; 16.66 ;  0.50           
REMARK   3   TIGHT THERMAL      5    E (A**2):    379 ; 19.98 ;  0.50           
REMARK   3   MEDIUM THERMAL     5    A (A**2):    601 ;  7.90 ;  2.00           
REMARK   3   MEDIUM THERMAL     5    C (A**2):    601 ; 16.01 ;  2.00           
REMARK   3   MEDIUM THERMAL     5    E (A**2):    601 ; 18.79 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 6FCN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200008086.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-OCT-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-1                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96600                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 2M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS VERSION MAY 1, 2016            
REMARK 200                                   BUILT=20160617                     
REMARK 200  DATA SCALING SOFTWARE          : XSCALE VERSION MAY 1, 2016         
REMARK 200                                   BUILT=20160617                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16369                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.220                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 5.710                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.22                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.61                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.71000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.6.1                                          
REMARK 200 STARTING MODEL: 1AXC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 19 TO 23% PEG 3350, 0.2 TO 0.3 M NACL,   
REMARK 280  0.1 M TRIS-HCL PH 8.5 12H PRIOR TO CRYSTAL FREEZING, 100 UM OF      
REMARK 280  P47PHOX(106-127) PEPTIDE WAS ADDED TO THE CRYSTALLIZATION DROP,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       19.94000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       85.88500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       70.33500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       85.88500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.94000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       70.33500            
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -20                                                      
REMARK 465     GLY A   -19                                                      
REMARK 465     SER A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     LEU A    -7                                                      
REMARK 465     VAL A    -6                                                      
REMARK 465     PRO A    -5                                                      
REMARK 465     ARG A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     SER A   186                                                      
REMARK 465     ASN A   187                                                      
REMARK 465     VAL A   188                                                      
REMARK 465     ASP A   189                                                      
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     MET C   -20                                                      
REMARK 465     GLY C   -19                                                      
REMARK 465     SER C   -18                                                      
REMARK 465     SER C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     SER C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     GLY C    -8                                                      
REMARK 465     LEU C    -7                                                      
REMARK 465     VAL C    -6                                                      
REMARK 465     PRO C    -5                                                      
REMARK 465     ARG C    -4                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     HIS C    -1                                                      
REMARK 465     MET C     0                                                      
REMARK 465     VAL C   188                                                      
REMARK 465     ASP C   189                                                      
REMARK 465     LYS C   190                                                      
REMARK 465     GLU C   191                                                      
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     MET E   -20                                                      
REMARK 465     GLY E   -19                                                      
REMARK 465     SER E   -18                                                      
REMARK 465     SER E   -17                                                      
REMARK 465     HIS E   -16                                                      
REMARK 465     HIS E   -15                                                      
REMARK 465     HIS E   -14                                                      
REMARK 465     HIS E   -13                                                      
REMARK 465     HIS E   -12                                                      
REMARK 465     HIS E   -11                                                      
REMARK 465     SER E   -10                                                      
REMARK 465     SER E    -9                                                      
REMARK 465     GLY E    -8                                                      
REMARK 465     LEU E    -7                                                      
REMARK 465     VAL E    -6                                                      
REMARK 465     PRO E    -5                                                      
REMARK 465     ARG E    -4                                                      
REMARK 465     GLY E    -3                                                      
REMARK 465     SER E    -2                                                      
REMARK 465     HIS E    -1                                                      
REMARK 465     MET E     0                                                      
REMARK 465     ASN E   187                                                      
REMARK 465     VAL E   188                                                      
REMARK 465     ASP E   189                                                      
REMARK 465     LYS E   190                                                      
REMARK 465     GLU E   256                                                      
REMARK 465     ASP E   257                                                      
REMARK 465     GLU E   258                                                      
REMARK 465     GLU E   259                                                      
REMARK 465     GLY E   260                                                      
REMARK 465     SER E   261                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 198    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 232    CG   OD1  OD2                                       
REMARK 470     GLU A 256    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 198    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 232    CG   OD1  OD2                                       
REMARK 470     GLU C 256    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 191    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 198    CG   CD   OE1  OE2                                  
REMARK 470     ASP E 232    CG   OD1  OD2                                       
REMARK 470     ILE E 255    CG1  CG2  CD1                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CB   SER A    43     OE2  GLU A   192     1655     2.10            
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    ASP A 122       67.80   -109.75                                   
REMARK 500    GLU A 191      -71.72    -16.96                                   
REMARK 500    ASP A 243       37.75     70.06                                   
REMARK 500    MET A 244      -49.71   -169.40                                   
REMARK 500    ASP C  94      -73.89    -62.46                                   
REMARK 500    GLU C 130      111.11    -23.52                                   
REMARK 500    ASP C 243       37.92     70.30                                   
REMARK 500    MET C 244      -52.13   -169.83                                   
REMARK 500    ASP E  94      -33.34    -37.27                                   
REMARK 500    GLN E 108       36.18     73.72                                   
REMARK 500    VAL E 123       78.06    -67.02                                   
REMARK 500    GLU E 124       58.50   -103.55                                   
REMARK 500    MET E 244      -49.76   -169.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AXC   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN, IN COMPLEX WITH P21 PEPTIDE                            
REMARK 900 RELATED ID: 6FCM   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH PEPTIDE                                            
DBREF  6FCN A    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  6FCN C    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  6FCN E    1   261  UNP    P12004   PCNA_HUMAN       1    261             
SEQADV 6FCN MET A  -20  UNP  P12004              INITIATING METHIONINE          
SEQADV 6FCN GLY A  -19  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN SER A  -18  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN SER A  -17  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS A  -16  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS A  -15  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS A  -14  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS A  -13  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS A  -12  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS A  -11  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN SER A  -10  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN SER A   -9  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN GLY A   -8  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN LEU A   -7  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN VAL A   -6  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN PRO A   -5  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN ARG A   -4  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN GLY A   -3  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN SER A   -2  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS A   -1  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN MET A    0  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN MET C  -20  UNP  P12004              INITIATING METHIONINE          
SEQADV 6FCN GLY C  -19  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN SER C  -18  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN SER C  -17  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS C  -16  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS C  -15  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS C  -14  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS C  -13  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS C  -12  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS C  -11  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN SER C  -10  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN SER C   -9  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN GLY C   -8  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN LEU C   -7  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN VAL C   -6  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN PRO C   -5  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN ARG C   -4  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN GLY C   -3  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN SER C   -2  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS C   -1  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN MET C    0  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN MET E  -20  UNP  P12004              INITIATING METHIONINE          
SEQADV 6FCN GLY E  -19  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN SER E  -18  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN SER E  -17  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS E  -16  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS E  -15  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS E  -14  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS E  -13  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS E  -12  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS E  -11  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN SER E  -10  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN SER E   -9  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN GLY E   -8  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN LEU E   -7  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN VAL E   -6  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN PRO E   -5  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN ARG E   -4  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN GLY E   -3  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN SER E   -2  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN HIS E   -1  UNP  P12004              EXPRESSION TAG                 
SEQADV 6FCN MET E    0  UNP  P12004              EXPRESSION TAG                 
SEQRES   1 A  282  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  282  LEU VAL PRO ARG GLY SER HIS MET MET PHE GLU ALA ARG          
SEQRES   3 A  282  LEU VAL GLN GLY SER ILE LEU LYS LYS VAL LEU GLU ALA          
SEQRES   4 A  282  LEU LYS ASP LEU ILE ASN GLU ALA CYS TRP ASP ILE SER          
SEQRES   5 A  282  SER SER GLY VAL ASN LEU GLN SER MET ASP SER SER HIS          
SEQRES   6 A  282  VAL SER LEU VAL GLN LEU THR LEU ARG SER GLU GLY PHE          
SEQRES   7 A  282  ASP THR TYR ARG CYS ASP ARG ASN LEU ALA MET GLY VAL          
SEQRES   8 A  282  ASN LEU THR SER MET SER LYS ILE LEU LYS CYS ALA GLY          
SEQRES   9 A  282  ASN GLU ASP ILE ILE THR LEU ARG ALA GLU ASP ASN ALA          
SEQRES  10 A  282  ASP THR LEU ALA LEU VAL PHE GLU ALA PRO ASN GLN GLU          
SEQRES  11 A  282  LYS VAL SER ASP TYR GLU MET LYS LEU MET ASP LEU ASP          
SEQRES  12 A  282  VAL GLU GLN LEU GLY ILE PRO GLU GLN GLU TYR SER CYS          
SEQRES  13 A  282  VAL VAL LYS MET PRO SER GLY GLU PHE ALA ARG ILE CYS          
SEQRES  14 A  282  ARG ASP LEU SER HIS ILE GLY ASP ALA VAL VAL ILE SER          
SEQRES  15 A  282  CYS ALA LYS ASP GLY VAL LYS PHE SER ALA SER GLY GLU          
SEQRES  16 A  282  LEU GLY ASN GLY ASN ILE LYS LEU SER GLN THR SER ASN          
SEQRES  17 A  282  VAL ASP LYS GLU GLU GLU ALA VAL THR ILE GLU MET ASN          
SEQRES  18 A  282  GLU PRO VAL GLN LEU THR PHE ALA LEU ARG TYR LEU ASN          
SEQRES  19 A  282  PHE PHE THR LYS ALA THR PRO LEU SER SER THR VAL THR          
SEQRES  20 A  282  LEU SER MET SER ALA ASP VAL PRO LEU VAL VAL GLU TYR          
SEQRES  21 A  282  LYS ILE ALA ASP MET GLY HIS LEU LYS TYR TYR LEU ALA          
SEQRES  22 A  282  PRO LYS ILE GLU ASP GLU GLU GLY SER                          
SEQRES   1 C  282  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  282  LEU VAL PRO ARG GLY SER HIS MET MET PHE GLU ALA ARG          
SEQRES   3 C  282  LEU VAL GLN GLY SER ILE LEU LYS LYS VAL LEU GLU ALA          
SEQRES   4 C  282  LEU LYS ASP LEU ILE ASN GLU ALA CYS TRP ASP ILE SER          
SEQRES   5 C  282  SER SER GLY VAL ASN LEU GLN SER MET ASP SER SER HIS          
SEQRES   6 C  282  VAL SER LEU VAL GLN LEU THR LEU ARG SER GLU GLY PHE          
SEQRES   7 C  282  ASP THR TYR ARG CYS ASP ARG ASN LEU ALA MET GLY VAL          
SEQRES   8 C  282  ASN LEU THR SER MET SER LYS ILE LEU LYS CYS ALA GLY          
SEQRES   9 C  282  ASN GLU ASP ILE ILE THR LEU ARG ALA GLU ASP ASN ALA          
SEQRES  10 C  282  ASP THR LEU ALA LEU VAL PHE GLU ALA PRO ASN GLN GLU          
SEQRES  11 C  282  LYS VAL SER ASP TYR GLU MET LYS LEU MET ASP LEU ASP          
SEQRES  12 C  282  VAL GLU GLN LEU GLY ILE PRO GLU GLN GLU TYR SER CYS          
SEQRES  13 C  282  VAL VAL LYS MET PRO SER GLY GLU PHE ALA ARG ILE CYS          
SEQRES  14 C  282  ARG ASP LEU SER HIS ILE GLY ASP ALA VAL VAL ILE SER          
SEQRES  15 C  282  CYS ALA LYS ASP GLY VAL LYS PHE SER ALA SER GLY GLU          
SEQRES  16 C  282  LEU GLY ASN GLY ASN ILE LYS LEU SER GLN THR SER ASN          
SEQRES  17 C  282  VAL ASP LYS GLU GLU GLU ALA VAL THR ILE GLU MET ASN          
SEQRES  18 C  282  GLU PRO VAL GLN LEU THR PHE ALA LEU ARG TYR LEU ASN          
SEQRES  19 C  282  PHE PHE THR LYS ALA THR PRO LEU SER SER THR VAL THR          
SEQRES  20 C  282  LEU SER MET SER ALA ASP VAL PRO LEU VAL VAL GLU TYR          
SEQRES  21 C  282  LYS ILE ALA ASP MET GLY HIS LEU LYS TYR TYR LEU ALA          
SEQRES  22 C  282  PRO LYS ILE GLU ASP GLU GLU GLY SER                          
SEQRES   1 E  282  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 E  282  LEU VAL PRO ARG GLY SER HIS MET MET PHE GLU ALA ARG          
SEQRES   3 E  282  LEU VAL GLN GLY SER ILE LEU LYS LYS VAL LEU GLU ALA          
SEQRES   4 E  282  LEU LYS ASP LEU ILE ASN GLU ALA CYS TRP ASP ILE SER          
SEQRES   5 E  282  SER SER GLY VAL ASN LEU GLN SER MET ASP SER SER HIS          
SEQRES   6 E  282  VAL SER LEU VAL GLN LEU THR LEU ARG SER GLU GLY PHE          
SEQRES   7 E  282  ASP THR TYR ARG CYS ASP ARG ASN LEU ALA MET GLY VAL          
SEQRES   8 E  282  ASN LEU THR SER MET SER LYS ILE LEU LYS CYS ALA GLY          
SEQRES   9 E  282  ASN GLU ASP ILE ILE THR LEU ARG ALA GLU ASP ASN ALA          
SEQRES  10 E  282  ASP THR LEU ALA LEU VAL PHE GLU ALA PRO ASN GLN GLU          
SEQRES  11 E  282  LYS VAL SER ASP TYR GLU MET LYS LEU MET ASP LEU ASP          
SEQRES  12 E  282  VAL GLU GLN LEU GLY ILE PRO GLU GLN GLU TYR SER CYS          
SEQRES  13 E  282  VAL VAL LYS MET PRO SER GLY GLU PHE ALA ARG ILE CYS          
SEQRES  14 E  282  ARG ASP LEU SER HIS ILE GLY ASP ALA VAL VAL ILE SER          
SEQRES  15 E  282  CYS ALA LYS ASP GLY VAL LYS PHE SER ALA SER GLY GLU          
SEQRES  16 E  282  LEU GLY ASN GLY ASN ILE LYS LEU SER GLN THR SER ASN          
SEQRES  17 E  282  VAL ASP LYS GLU GLU GLU ALA VAL THR ILE GLU MET ASN          
SEQRES  18 E  282  GLU PRO VAL GLN LEU THR PHE ALA LEU ARG TYR LEU ASN          
SEQRES  19 E  282  PHE PHE THR LYS ALA THR PRO LEU SER SER THR VAL THR          
SEQRES  20 E  282  LEU SER MET SER ALA ASP VAL PRO LEU VAL VAL GLU TYR          
SEQRES  21 E  282  LYS ILE ALA ASP MET GLY HIS LEU LYS TYR TYR LEU ALA          
SEQRES  22 E  282  PRO LYS ILE GLU ASP GLU GLU GLY SER                          
FORMUL   4  HOH   *7(H2 O)                                                      
HELIX    1 AA1 GLN A    8  ASP A   21  1                                  14    
HELIX    2 AA2 GLU A   55  PHE A   57  5                                   3    
HELIX    3 AA3 LEU A   72  CYS A   81  1                                  10    
HELIX    4 AA4 SER A  141  GLY A  155  1                                  15    
HELIX    5 AA5 LEU A  209  THR A  216  1                                   8    
HELIX    6 AA6 LYS A  217  SER A  222  5                                   6    
HELIX    7 AA7 GLN C    8  ASP C   21  1                                  14    
HELIX    8 AA8 GLU C   55  PHE C   57  5                                   3    
HELIX    9 AA9 LEU C   72  CYS C   81  1                                  10    
HELIX   10 AB1 SER C  141  GLY C  155  1                                  15    
HELIX   11 AB2 LEU C  209  THR C  216  1                                   8    
HELIX   12 AB3 LYS C  217  SER C  222  5                                   6    
HELIX   13 AB4 GLN E    8  ASP E   21  1                                  14    
HELIX   14 AB5 GLU E   55  PHE E   57  5                                   3    
HELIX   15 AB6 LEU E   72  CYS E   81  1                                  10    
HELIX   16 AB7 SER E  141  GLY E  155  1                                  15    
HELIX   17 AB8 LEU E  209  THR E  216  1                                   8    
HELIX   18 AB9 LYS E  217  SER E  222  5                                   6    
SHEET    1 AA1 8 PHE A   2  LEU A   6  0                                        
SHEET    2 AA1 8 ILE A  87  ALA A  92 -1  O  ILE A  88   N  LEU A   6           
SHEET    3 AA1 8 THR A  98  GLU A 104 -1  O  ALA A 100   N  ARG A  91           
SHEET    4 AA1 8 LYS A 110  LYS A 117 -1  O  MET A 116   N  LEU A  99           
SHEET    5 AA1 8 GLY C 176  SER C 183 -1  O  ASN C 177   N  GLU A 115           
SHEET    6 AA1 8 GLY C 166  SER C 172 -1  N  PHE C 169   O  ILE C 180           
SHEET    7 AA1 8 ALA C 157  CYS C 162 -1  N  SER C 161   O  LYS C 168           
SHEET    8 AA1 8 VAL C 203  ALA C 208 -1  O  VAL C 203   N  CYS C 162           
SHEET    1 AA2 9 ALA A  67  ASN A  71  0                                        
SHEET    2 AA2 9 GLU A  25  ILE A  30 -1  N  TRP A  28   O  MET A  68           
SHEET    3 AA2 9 GLY A  34  MET A  40 -1  O  ASN A  36   N  ASP A  29           
SHEET    4 AA2 9 SER A  46  ARG A  53 -1  O  VAL A  48   N  SER A  39           
SHEET    5 AA2 9 GLY A 245  LEU A 251 -1  O  TYR A 250   N  LEU A  47           
SHEET    6 AA2 9 LEU A 235  ILE A 241 -1  N  VAL A 237   O  TYR A 249           
SHEET    7 AA2 9 THR A 224  MET A 229 -1  N  THR A 226   O  GLU A 238           
SHEET    8 AA2 9 CYS A 135  PRO A 140 -1  N  MET A 139   O  VAL A 225           
SHEET    9 AA2 9 THR A 196  MET A 199 -1  O  THR A 196   N  LYS A 138           
SHEET    1 AA3 8 VAL A 203  ALA A 208  0                                        
SHEET    2 AA3 8 ALA A 157  CYS A 162 -1  N  CYS A 162   O  VAL A 203           
SHEET    3 AA3 8 GLY A 166  GLY A 173 -1  O  LYS A 168   N  SER A 161           
SHEET    4 AA3 8 GLY A 176  SER A 183 -1  O  LEU A 182   N  VAL A 167           
SHEET    5 AA3 8 LYS E 110  LYS E 117 -1  O  GLU E 115   N  ASN A 177           
SHEET    6 AA3 8 THR E  98  GLU E 104 -1  N  LEU E 101   O  TYR E 114           
SHEET    7 AA3 8 ILE E  87  ALA E  92 -1  N  ILE E  87   O  GLU E 104           
SHEET    8 AA3 8 PHE E   2  LEU E   6 -1  N  LEU E   6   O  ILE E  88           
SHEET    1 AA4 8 PHE C   2  LEU C   6  0                                        
SHEET    2 AA4 8 ILE C  87  ALA C  92 -1  O  ILE C  88   N  LEU C   6           
SHEET    3 AA4 8 THR C  98  GLU C 104 -1  O  ALA C 100   N  ARG C  91           
SHEET    4 AA4 8 LYS C 110  LYS C 117 -1  O  MET C 116   N  LEU C  99           
SHEET    5 AA4 8 GLY E 176  SER E 183 -1  O  ASN E 177   N  GLU C 115           
SHEET    6 AA4 8 GLY E 166  GLY E 173 -1  N  VAL E 167   O  LEU E 182           
SHEET    7 AA4 8 ALA E 157  CYS E 162 -1  N  SER E 161   O  LYS E 168           
SHEET    8 AA4 8 VAL E 203  ALA E 208 -1  O  VAL E 203   N  CYS E 162           
SHEET    1 AA5 9 ALA C  67  ASN C  71  0                                        
SHEET    2 AA5 9 GLU C  25  ILE C  30 -1  N  TRP C  28   O  MET C  68           
SHEET    3 AA5 9 GLY C  34  MET C  40 -1  O  ASN C  36   N  ASP C  29           
SHEET    4 AA5 9 SER C  46  ARG C  53 -1  O  VAL C  48   N  SER C  39           
SHEET    5 AA5 9 GLY C 245  LEU C 251 -1  O  TYR C 250   N  LEU C  47           
SHEET    6 AA5 9 LEU C 235  ILE C 241 -1  N  VAL C 237   O  TYR C 249           
SHEET    7 AA5 9 THR C 224  MET C 229 -1  N  THR C 226   O  GLU C 238           
SHEET    8 AA5 9 CYS C 135  PRO C 140 -1  N  MET C 139   O  VAL C 225           
SHEET    9 AA5 9 THR C 196  MET C 199 -1  O  THR C 196   N  LYS C 138           
SHEET    1 AA6 9 ALA E  67  ASN E  71  0                                        
SHEET    2 AA6 9 GLU E  25  ILE E  30 -1  N  TRP E  28   O  MET E  68           
SHEET    3 AA6 9 GLY E  34  MET E  40 -1  O  ASN E  36   N  ASP E  29           
SHEET    4 AA6 9 SER E  46  ARG E  53 -1  O  VAL E  48   N  SER E  39           
SHEET    5 AA6 9 GLY E 245  LEU E 251 -1  O  TYR E 250   N  LEU E  47           
SHEET    6 AA6 9 LEU E 235  ILE E 241 -1  N  VAL E 237   O  TYR E 249           
SHEET    7 AA6 9 THR E 224  MET E 229 -1  N  THR E 226   O  GLU E 238           
SHEET    8 AA6 9 CYS E 135  PRO E 140 -1  N  MET E 139   O  VAL E 225           
SHEET    9 AA6 9 THR E 196  MET E 199 -1  O  THR E 196   N  LYS E 138           
CRYST1   39.880  140.670  171.770  90.00  90.00  90.00 P 21 21 21   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      0.025075  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007109  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005822        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2  0.982072  0.140338  0.125860        2.52553    1                    
MTRIX2   2 -0.043213 -0.482282  0.874950       18.48782    1                    
MTRIX3   2  0.183488 -0.864702 -0.467571      -32.57957    1                    
MTRIX1   3  0.984523 -0.054899  0.166436        3.80108    1                    
MTRIX2   3  0.115890 -0.508471 -0.853245      -19.64861    1                    
MTRIX3   3  0.131470  0.859327 -0.494239      -32.58945    1                    
MTRIX1   4  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   4  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   4  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   5  0.973509  0.164680  0.158623        2.45214    1                    
MTRIX2   5 -0.091943 -0.353235  0.931005       15.85979    1                    
MTRIX3   5  0.209349 -0.920926 -0.328736      -28.70097    1                    
MTRIX1   6  0.984806  0.029343  0.171162        5.20913    1                    
MTRIX2   6  0.169473 -0.377484 -0.910376      -17.24378    1                    
MTRIX3   6  0.037897  0.925551 -0.376721      -31.61068    1                    
MTRIX1   7  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   7  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   7  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   8  0.979602  0.158824  0.123108        1.99300    1                    
MTRIX2   8 -0.037067 -0.459304  0.887506       17.90472    1                    
MTRIX3   8  0.197501 -0.873965 -0.444048      -32.09895    1                    
MTRIX1   9  0.977287 -0.076373  0.197679        3.27276    1                    
MTRIX2   9  0.125668 -0.542239 -0.830773      -20.35778    1                    
MTRIX3   9  0.170638  0.836746 -0.520326      -33.49889    1                    
MTRIX1  10  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  10  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  10  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  11  0.983994  0.132479  0.119184        2.49889    1                    
MTRIX2  11 -0.036206 -0.506241  0.861632       18.33656    1                    
MTRIX3  11  0.174484 -0.852156 -0.493341      -33.63534    1                    
MTRIX1  12  0.985538 -0.051808  0.161338        3.79609    1                    
MTRIX2  12  0.115021 -0.494647 -0.861449      -19.62603    1                    
MTRIX3  12  0.124435  0.867548 -0.481535      -32.69951    1                    
MTRIX1  13  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  13  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  13  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  14  0.985609  0.123935  0.114954        2.38291    1                    
MTRIX2  14 -0.038048 -0.499943  0.865222       18.54349    1                    
MTRIX3  14  0.164702 -0.857145 -0.488033      -33.35170    1                    
MTRIX1  15  0.986657 -0.051145  0.154572        3.74096    1                    
MTRIX2  15  0.108611 -0.500514 -0.858889      -19.47413    1                    
MTRIX3  15  0.121293  0.864216 -0.488281      -32.62668    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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