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Database: PDB
Entry: 5MOM
LinkDB: 5MOM
Original site: 5MOM 
HEADER    DNA BINDING PROTEIN                     14-DEC-16   5MOM              
TITLE     CRYSTAL STRUCTURE OF PCNA ENCODING THE HYPOMORPHIC MUTATION S228I     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;                        
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: PCNA,CYCLIN;                                                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
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: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: STAR;                                     
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    PCNA, DNA BINDING PROTEIN                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.J.BIASUTTO,E.J.MANCINI,C.M.GREEN,R.H.C.WILSON                       
REVDAT   3   13-SEP-17 5MOM    1       REMARK                                   
REVDAT   2   01-FEB-17 5MOM    1       JRNL                                     
REVDAT   1   25-JAN-17 5MOM    0                                                
JRNL        AUTH   R.H.WILSON,A.J.BIASUTTO,L.WANG,R.FISCHER,E.L.BAPLE,          
JRNL        AUTH 2 A.H.CROSBY,E.J.MANCINI,C.M.GREEN                             
JRNL        TITL   PCNA DEPENDENT CELLULAR ACTIVITIES TOLERATE DRAMATIC         
JRNL        TITL 2 PERTURBATIONS IN PCNA CLIENT INTERACTIONS.                   
JRNL        REF    DNA REPAIR (AMST.)            V.  50    22 2017              
JRNL        REFN                   ISSN 1568-7856                               
JRNL        PMID   28073635                                                     
JRNL        DOI    10.1016/J.DNAREP.2016.12.003                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.27 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10.1_2155                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.27                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 89.07                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 87369                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.120                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4470                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 89.1373 -  7.0524    1.00     3003   174  0.2007 0.1869        
REMARK   3     2  7.0524 -  5.5979    1.00     2856   165  0.2181 0.2385        
REMARK   3     3  5.5979 -  4.8904    1.00     2850   133  0.1678 0.1700        
REMARK   3     4  4.8904 -  4.4433    1.00     2784   177  0.1384 0.1572        
REMARK   3     5  4.4433 -  4.1248    1.00     2805   145  0.1534 0.1697        
REMARK   3     6  4.1248 -  3.8816    1.00     2805   137  0.1722 0.2030        
REMARK   3     7  3.8816 -  3.6872    1.00     2791   130  0.1817 0.1991        
REMARK   3     8  3.6872 -  3.5267    1.00     2757   159  0.1974 0.2254        
REMARK   3     9  3.5267 -  3.3909    1.00     2771   149  0.2005 0.2135        
REMARK   3    10  3.3909 -  3.2739    1.00     2787   139  0.2184 0.2276        
REMARK   3    11  3.2739 -  3.1715    1.00     2729   161  0.2232 0.2193        
REMARK   3    12  3.1715 -  3.0809    1.00     2727   182  0.2182 0.2368        
REMARK   3    13  3.0809 -  2.9998    1.00     2756   135  0.2158 0.2743        
REMARK   3    14  2.9998 -  2.9266    1.00     2753   154  0.2252 0.2771        
REMARK   3    15  2.9266 -  2.8600    1.00     2743   139  0.2268 0.2770        
REMARK   3    16  2.8600 -  2.7992    1.00     2739   148  0.2424 0.2393        
REMARK   3    17  2.7992 -  2.7432    1.00     2759   144  0.2317 0.2946        
REMARK   3    18  2.7432 -  2.6914    1.00     2722   147  0.2184 0.2450        
REMARK   3    19  2.6914 -  2.6433    1.00     2749   150  0.2171 0.2387        
REMARK   3    20  2.6433 -  2.5985    1.00     2720   162  0.2225 0.2429        
REMARK   3    21  2.5985 -  2.5566    1.00     2729   148  0.2237 0.2501        
REMARK   3    22  2.5566 -  2.5173    1.00     2717   162  0.2317 0.2709        
REMARK   3    23  2.5173 -  2.4802    1.00     2759   141  0.2354 0.3000        
REMARK   3    24  2.4802 -  2.4453    1.00     2732   128  0.2514 0.2537        
REMARK   3    25  2.4453 -  2.4123    1.00     2732   150  0.2552 0.2714        
REMARK   3    26  2.4123 -  2.3809    1.00     2721   147  0.2606 0.3240        
REMARK   3    27  2.3809 -  2.3512    1.00     2715   151  0.2725 0.3079        
REMARK   3    28  2.3512 -  2.3228    1.00     2745   131  0.2874 0.2803        
REMARK   3    29  2.3228 -  2.2958    1.00     2738   144  0.3004 0.3457        
REMARK   3    30  2.2958 -  2.2700    1.00     2705   138  0.3072 0.3249        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.140           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 48.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 62.53                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           5654                                  
REMARK   3   ANGLE     :  1.126           7656                                  
REMARK   3   CHIRALITY :  0.065            935                                  
REMARK   3   PLANARITY :  0.007            965                                  
REMARK   3   DIHEDRAL  : 16.071           3460                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.2864  30.6718 -29.7998              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3922 T22:   0.3256                                     
REMARK   3      T33:   0.3293 T12:  -0.0446                                     
REMARK   3      T13:  -0.0514 T23:  -0.0276                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1978 L22:   0.6863                                     
REMARK   3      L33:   0.6166 L12:  -0.1641                                     
REMARK   3      L13:  -0.0627 L23:  -0.2678                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0280 S12:  -0.0593 S13:  -0.0289                       
REMARK   3      S21:   0.0425 S22:   0.0172 S23:  -0.0689                       
REMARK   3      S31:   0.0231 S32:   0.0459 S33:  -0.0390                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND (RESSEQ 2:23 OR RESSEQ 25:57   
REMARK   3                          OR (RESID 58 AND (NAME N OR NAME CA OR      
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESSEQ    
REMARK   3                          59:60 OR (RESID 61 AND (NAME N OR NAME CA   
REMARK   3                          OR NAME C OR NAME O OR NAME CB )) OR        
REMARK   3                          RESSEQ 62:76 OR (RESID 77 AND (NAME N OR    
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB OR   
REMARK   3                          NAME CG OR NAME CD )) OR RESSEQ 78:90 OR    
REMARK   3                          (RESID 91 AND (NAME N OR NAME CA OR NAME    
REMARK   3                          C OR NAME O OR NAME CB OR NAME CG )) OR     
REMARK   3                          RESSEQ 92:116 OR (RESID 117 AND (NAME N     
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB   
REMARK   3                          OR NAME CG )) OR RESSEQ 118 OR RESSEQ 120:  
REMARK   3                          121 OR (RESID 123 AND (NAME N OR NAME CA    
REMARK   3                          OR NAME C OR NAME O OR NAME CB )) OR        
REMARK   3                          RESSEQ 126:128 OR RESSEQ 130:137 OR         
REMARK   3                          (RESID 138 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          C OR NAME O OR NAME CB OR NAME CG OR NAME   
REMARK   3                          CD )) OR RESSEQ 139:145 OR RESSEQ 147:148   
REMARK   3                          OR (RESID 149 AND (NAME N OR NAME CA OR     
REMARK   3                          NAME C OR NAME O OR NAME CB OR NAME CG ))   
REMARK   3                          OR RESSEQ 150:185 OR RESSEQ 193:209 OR      
REMARK   3                          RESSEQ 211:242 OR (RESID 243 AND (NAME N    
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB   
REMARK   3                          )) OR RESSEQ 244:253))                      
REMARK   3     SELECTION          : (CHAIN B AND (RESSEQ 2:23 OR RESSEQ 25:57   
REMARK   3                          OR (RESID 58 AND (NAME N OR NAME CA OR      
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESSEQ    
REMARK   3                          59:60 OR (RESID 61 AND (NAME N OR NAME CA   
REMARK   3                          OR NAME C OR NAME O OR NAME CB )) OR        
REMARK   3                          RESSEQ 62:63 OR (RESID 64 AND (NAME N OR    
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB OR   
REMARK   3                          NAME CG OR NAME CD )) OR RESSEQ 65:76 OR    
REMARK   3                          (RESID 77 AND (NAME N OR NAME CA OR NAME    
REMARK   3                          C OR NAME O OR NAME CB OR NAME CG OR NAME   
REMARK   3                          CD )) OR RESSEQ 78:79 OR (RESID 80 AND      
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O OR   
REMARK   3                          NAME CB OR NAME CG OR NAME CD OR NAME CE )  
REMARK   3                          ) OR RESSEQ 81:84 OR (RESID 85 AND (NAME    
REMARK   3                          N OR NAME CA OR NAME C OR NAME O OR NAME    
REMARK   3                          CB OR NAME CG )) OR RESSEQ 86:90 OR         
REMARK   3                          (RESID 91 AND (NAME N OR NAME CA OR NAME    
REMARK   3                          C OR NAME O OR NAME CB OR NAME CG )) OR     
REMARK   3                          RESSEQ 92:106 OR (RESID 107 AND (NAME N     
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB   
REMARK   3                          )) OR RESSEQ 108:116 OR (RESID 117 AND      
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O OR   
REMARK   3                          NAME CB OR NAME CG )) OR RESSEQ 118 OR      
REMARK   3                          RESSEQ 120:121 OR (RESID 123 AND (NAME N    
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB   
REMARK   3                          )) OR (RESID 126 AND (NAME N OR NAME CA     
REMARK   3                          OR NAME C OR NAME O OR NAME CB )) OR        
REMARK   3                          RESSEQ 127:128 OR (RESID 130 AND (NAME N    
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB   
REMARK   3                          )) OR RESSEQ 131:137 OR (RESID 138 AND      
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O OR   
REMARK   3                          NAME CB OR NAME CG OR NAME CD )) OR         
REMARK   3                          RESSEQ 139:145 OR RESSEQ 147:163 OR         
REMARK   3                          (RESID 164 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          C OR NAME O OR NAME CB )) OR RESSEQ 165:    
REMARK   3                          173 OR (RESID 174 AND (NAME N OR NAME CA    
REMARK   3                          OR NAME C OR NAME O OR NAME CB OR NAME CG   
REMARK   3                          )) OR RESSEQ 175:185 OR RESSEQ 193:197 OR   
REMARK   3                          (RESID 198 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          C OR NAME O OR NAME CB OR NAME CG )) OR     
REMARK   3                          RESSEQ 199:209 OR RESSEQ 211:231 OR         
REMARK   3                          (RESID 232 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          C OR NAME O OR NAME CB )) OR RESSEQ 233:    
REMARK   3                          253))                                       
REMARK   3     ATOM PAIRS NUMBER  : 3043                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND (RESSEQ 2:23 OR RESSEQ 25:57   
REMARK   3                          OR (RESID 58 AND (NAME N OR NAME CA OR      
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESSEQ    
REMARK   3                          59:60 OR (RESID 61 AND (NAME N OR NAME CA   
REMARK   3                          OR NAME C OR NAME O OR NAME CB )) OR        
REMARK   3                          RESSEQ 62:76 OR (RESID 77 AND (NAME N OR    
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB OR   
REMARK   3                          NAME CG OR NAME CD )) OR RESSEQ 78:90 OR    
REMARK   3                          (RESID 91 AND (NAME N OR NAME CA OR NAME    
REMARK   3                          C OR NAME O OR NAME CB OR NAME CG )) OR     
REMARK   3                          RESSEQ 92:116 OR (RESID 117 AND (NAME N     
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB   
REMARK   3                          OR NAME CG )) OR RESSEQ 118 OR RESSEQ 120:  
REMARK   3                          121 OR (RESID 123 AND (NAME N OR NAME CA    
REMARK   3                          OR NAME C OR NAME O OR NAME CB )) OR        
REMARK   3                          RESSEQ 126:128 OR RESSEQ 130:137 OR         
REMARK   3                          (RESID 138 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          C OR NAME O OR NAME CB OR NAME CG OR NAME   
REMARK   3                          CD )) OR RESSEQ 139:145 OR RESSEQ 147:148   
REMARK   3                          OR (RESID 149 AND (NAME N OR NAME CA OR     
REMARK   3                          NAME C OR NAME O OR NAME CB OR NAME CG ))   
REMARK   3                          OR RESSEQ 150:185 OR RESSEQ 193:209 OR      
REMARK   3                          RESSEQ 211:242 OR (RESID 243 AND (NAME N    
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB   
REMARK   3                          )) OR RESSEQ 244:253))                      
REMARK   3     SELECTION          : (CHAIN C AND (RESSEQ 2:23 OR RESSEQ 25:84   
REMARK   3                          OR (RESID 85 AND (NAME N OR NAME CA OR      
REMARK   3                          NAME C OR NAME O OR NAME CB OR NAME CG ))   
REMARK   3                          OR RESSEQ 86:106 OR (RESID 107 AND (NAME    
REMARK   3                          N OR NAME CA OR NAME C OR NAME O OR NAME    
REMARK   3                          CB )) OR RESSEQ 108:118 OR RESSEQ 120:121   
REMARK   3                          OR RESSEQ 123 OR (RESID 126 AND (NAME N     
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB   
REMARK   3                          )) OR RESSEQ 127:128 OR (RESID 130 AND      
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O OR   
REMARK   3                          NAME CB )) OR RESSEQ 131:145 OR RESSEQ      
REMARK   3                          147:173 OR (RESID 174 AND (NAME N OR NAME   
REMARK   3                          CA OR NAME C OR NAME O OR NAME CB OR NAME   
REMARK   3                          CG )) OR RESSEQ 175:185 OR RESSEQ 193:197   
REMARK   3                          OR (RESID 198 AND (NAME N OR NAME CA OR     
REMARK   3                          NAME C OR NAME O OR NAME CB OR NAME CG ))   
REMARK   3                          OR RESSEQ 199:209 OR RESSEQ 211:253))       
REMARK   3     ATOM PAIRS NUMBER  : 3043                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5MOM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-DEC-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200002499.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97625                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 87453                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.270                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 89.070                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.40                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.20                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.6.0                                          
REMARK 200 STARTING MODEL: 1VYM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 77.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NAACO, 2M (NH4)2SO4, PH 4.5,        
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.20000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       81.47500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       81.47500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       35.10000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       81.47500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       81.47500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      105.30000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       81.47500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       81.47500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       35.10000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       81.47500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       81.47500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      105.30000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       70.20000            
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, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   186                                                      
REMARK 465     ASN A   187                                                      
REMARK 465     VAL A   188                                                      
REMARK 465     ASP A   189                                                      
REMARK 465     LYS A   190                                                      
REMARK 465     GLU A   191                                                      
REMARK 465     GLU A   192                                                      
REMARK 465     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     ASP B   257                                                      
REMARK 465     GLU B   258                                                      
REMARK 465     SER C   186                                                      
REMARK 465     ASN C   187                                                      
REMARK 465     VAL C   188                                                      
REMARK 465     ASP C   189                                                      
REMARK 465     LYS C   190                                                      
REMARK 465     GLU C   191                                                      
REMARK 465     GLU C   192                                                      
REMARK 465     GLU C   256                                                      
REMARK 465     ASP C   257                                                      
REMARK 465     GLU C   258                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  64    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A  80    NZ                                                  
REMARK 470     GLU A  85    CD   OE1  OE2                                       
REMARK 470     ARG A  91    NE   CZ   NH1  NH2                                  
REMARK 470     ASP A  94    CG   OD1  OD2                                       
REMARK 470     ASN A  95    CG   OD1  ND2                                       
REMARK 470     ASN A 107    CG   OD1  ND2                                       
REMARK 470     GLN A 108    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 109    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 125    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 126    CG   CD1  CD2                                       
REMARK 470     GLU A 130    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 164    CG   CD   CE   NZ                                   
REMARK 470     ASP A 165    CG   OD1  OD2                                       
REMARK 470     GLU A 174    CD   OE1  OE2                                       
REMARK 470     GLU A 193    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 198    CD   OE1  OE2                                       
REMARK 470     ASP A 232    CG   OD1  OD2                                       
REMARK 470     LYS A 240    CD   CE   NZ                                        
REMARK 470     GLU A 256    CD   OE1  OE2                                       
REMARK 470     ARG B  91    NE   CZ   NH1  NH2                                  
REMARK 470     ASP B  94    CG   OD1  OD2                                       
REMARK 470     ASN B  95    CG   OD1  ND2                                       
REMARK 470     GLN B 108    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 109    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 130    CD   OE1  OE2                                       
REMARK 470     ARG B 149    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP B 165    CG   OD1  OD2                                       
REMARK 470     GLU B 193    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 240    CD   CE   NZ                                        
REMARK 470     ASP B 243    CG   OD1  OD2                                       
REMARK 470     ASP C  58    CG   OD1  OD2                                       
REMARK 470     ARG C  61    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C  64    NE   CZ   NH1  NH2                                  
REMARK 470     LYS C  77    CE   NZ                                             
REMARK 470     LYS C  80    NZ                                                  
REMARK 470     ARG C  91    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP C  94    CG   OD1  OD2                                       
REMARK 470     ASN C  95    CG   OD1  ND2                                       
REMARK 470     GLN C 108    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 109    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 117    CD   CE   NZ                                        
REMARK 470     ASP C 122    CG   OD1  OD2                                       
REMARK 470     VAL C 123    CG1  CG2                                            
REMARK 470     GLU C 124    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 125    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 138    CE   NZ                                             
REMARK 470     ARG C 149    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS C 164    CG   CD   CE   NZ                                   
REMARK 470     ASP C 165    CG   OD1  OD2                                       
REMARK 470     GLU C 193    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 232    CG   OD1  OD2                                       
REMARK 470     LYS C 240    CD   CE   NZ                                        
REMARK 470     ASP C 243    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER C   230     O    HOH C   301              1.80            
REMARK 500   OE1  GLN A   131     O    HOH A   301              1.99            
REMARK 500   O    HOH B   323     O    HOH B   361              2.04            
REMARK 500   O    HOH B   343     O    HOH B   371              2.05            
REMARK 500   OG1  THR B    73     O    HOH B   301              2.13            
REMARK 500   OD1  ASP A    41     N    SER A    46              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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   O    HOH A   328     O    HOH C   329     8554     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 175   CA  -  CB  -  CG  ANGL. DEV. =  20.6 DEGREES          
REMARK 500    LEU C 121   CA  -  CB  -  CG  ANGL. DEV. =  13.9 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    ALA A  96     -131.91     50.01                                   
REMARK 500    ASP A  97      -36.62     81.66                                   
REMARK 500    GLN A 108        3.18     88.46                                   
REMARK 500    TYR A 133       63.35   -101.55                                   
REMARK 500    LEU A 175      -37.82     74.22                                   
REMARK 500    MET A 244      -43.62   -155.18                                   
REMARK 500    ALA B  96     -130.94     51.41                                   
REMARK 500    ASP B  97      -38.76     82.72                                   
REMARK 500    GLN B 108        6.75     90.10                                   
REMARK 500    GLN B 125      109.95     79.03                                   
REMARK 500    TYR B 133       63.56   -101.18                                   
REMARK 500    ASP B 232      -10.33     75.70                                   
REMARK 500    MET B 244      -42.86   -156.65                                   
REMARK 500    ALA C  96     -130.56     50.28                                   
REMARK 500    ASP C  97      -36.94     81.74                                   
REMARK 500    GLN C 108        3.49     90.44                                   
REMARK 500    TYR C 133       62.17   -101.77                                   
REMARK 500    MET C 244      -42.19   -154.65                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5MOM A    1   258  UNP    P12004   PCNA_HUMAN       1    258             
DBREF  5MOM B    1   258  UNP    P12004   PCNA_HUMAN       1    258             
DBREF  5MOM C    1   258  UNP    P12004   PCNA_HUMAN       1    258             
SEQADV 5MOM ILE A  228  UNP  P12004    SER   228 ENGINEERED MUTATION            
SEQADV 5MOM ILE B  228  UNP  P12004    SER   228 ENGINEERED MUTATION            
SEQADV 5MOM ILE C  228  UNP  P12004    SER   228 ENGINEERED MUTATION            
SEQRES   1 A  258  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 A  258  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 A  258  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 A  258  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 A  258  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 A  258  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 A  258  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 A  258  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 A  258  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 A  258  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 A  258  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 A  258  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 A  258  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 A  258  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 A  258  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 A  258  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 A  258  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 A  258  SER SER THR VAL THR LEU ILE MET SER ALA ASP VAL PRO          
SEQRES  19 A  258  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 A  258  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU                  
SEQRES   1 B  258  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 B  258  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 B  258  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 B  258  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 B  258  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 B  258  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 B  258  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 B  258  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 B  258  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 B  258  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 B  258  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 B  258  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 B  258  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 B  258  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 B  258  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 B  258  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 B  258  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 B  258  SER SER THR VAL THR LEU ILE MET SER ALA ASP VAL PRO          
SEQRES  19 B  258  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 B  258  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU                  
SEQRES   1 C  258  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 C  258  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 C  258  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 C  258  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 C  258  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 C  258  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 C  258  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 C  258  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 C  258  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 C  258  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 C  258  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 C  258  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 C  258  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 C  258  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 C  258  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 C  258  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 C  258  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 C  258  SER SER THR VAL THR LEU ILE MET SER ALA ASP VAL PRO          
SEQRES  19 C  258  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 C  258  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU                  
FORMUL   4  HOH   *152(H2 O)                                                    
HELIX    1 AA1 GLY A    9  ASP A   21  1                                  13    
HELIX    2 AA2 GLU A   55  PHE A   57  5                                   3    
HELIX    3 AA3 LEU A   72  LYS A   80  1                                   9    
HELIX    4 AA4 SER A  141  HIS A  153  1                                  13    
HELIX    5 AA5 LEU A  209  THR A  216  1                                   8    
HELIX    6 AA6 LYS A  217  SER A  222  5                                   6    
HELIX    7 AA7 GLY B    9  LYS B   20  1                                  12    
HELIX    8 AA8 GLU B   55  PHE B   57  5                                   3    
HELIX    9 AA9 LEU B   72  LYS B   80  1                                   9    
HELIX   10 AB1 SER B  141  HIS B  153  1                                  13    
HELIX   11 AB2 LEU B  209  THR B  216  1                                   8    
HELIX   12 AB3 LYS B  217  SER B  222  5                                   6    
HELIX   13 AB4 GLY C    9  ASP C   21  1                                  13    
HELIX   14 AB5 GLU C   55  PHE C   57  5                                   3    
HELIX   15 AB6 LEU C   72  LYS C   80  1                                   9    
HELIX   16 AB7 SER C  141  HIS C  153  1                                  13    
HELIX   17 AB8 LEU C  209  THR C  216  1                                   8    
HELIX   18 AB9 LYS C  217  SER C  222  5                                   6    
SHEET    1 AA1 9 THR A  59  CYS A  62  0                                        
SHEET    2 AA1 9 PHE A   2  LEU A   6 -1  N  GLU A   3   O  ARG A  61           
SHEET    3 AA1 9 ILE A  87  ALA A  92 -1  O  ILE A  88   N  LEU A   6           
SHEET    4 AA1 9 THR A  98  GLU A 104 -1  O  ALA A 100   N  ARG A  91           
SHEET    5 AA1 9 LYS A 110  LYS A 117 -1  O  SER A 112   N  PHE A 103           
SHEET    6 AA1 9 GLY B 176  SER B 183 -1  O  ASN B 177   N  GLU A 115           
SHEET    7 AA1 9 GLY B 166  GLY B 173 -1  N  VAL B 167   O  LEU B 182           
SHEET    8 AA1 9 ALA B 157  CYS B 162 -1  N  SER B 161   O  LYS B 168           
SHEET    9 AA1 9 VAL B 203  ALA B 208 -1  O  LEU B 205   N  ILE B 160           
SHEET    1 AA2 9 LEU A  66  ASN A  71  0                                        
SHEET    2 AA2 9 GLU A  25  SER A  31 -1  N  ILE A  30   O  LEU A  66           
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  LEU A  52   N  VAL A  35           
SHEET    5 AA2 9 GLY A 245  LEU A 251 -1  O  LYS A 248   N  GLN A  49           
SHEET    6 AA2 9 LEU A 235  ILE A 241 -1  N  TYR A 239   O  LEU A 247           
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  GLU A 198   N  VAL A 136           
SHEET    1 AA3 9 VAL A 203  ALA A 208  0                                        
SHEET    2 AA3 9 ALA A 157  ALA A 163 -1  N  CYS A 162   O  VAL A 203           
SHEET    3 AA3 9 GLY A 166  GLY A 173 -1  O  LYS A 168   N  SER A 161           
SHEET    4 AA3 9 GLY A 176  SER A 183 -1  O  LEU A 182   N  VAL A 167           
SHEET    5 AA3 9 LYS C 110  LYS C 117 -1  O  VAL C 111   N  LYS A 181           
SHEET    6 AA3 9 THR C  98  GLU C 104 -1  N  LEU C  99   O  MET C 116           
SHEET    7 AA3 9 ILE C  87  ALA C  92 -1  N  ARG C  91   O  ALA C 100           
SHEET    8 AA3 9 PHE C   2  LEU C   6 -1  N  LEU C   6   O  ILE C  88           
SHEET    9 AA3 9 THR C  59  CYS C  62 -1  O  ARG C  61   N  GLU C   3           
SHEET    1 AA4 9 THR B  59  CYS B  62  0                                        
SHEET    2 AA4 9 PHE B   2  LEU B   6 -1  N  GLU B   3   O  ARG B  61           
SHEET    3 AA4 9 ILE B  87  ALA B  92 -1  O  ILE B  88   N  LEU B   6           
SHEET    4 AA4 9 THR B  98  GLU B 104 -1  O  ALA B 100   N  ARG B  91           
SHEET    5 AA4 9 LYS B 110  LYS B 117 -1  O  MET B 116   N  LEU B  99           
SHEET    6 AA4 9 GLY C 176  SER C 183 -1  O  ASN C 177   N  GLU B 115           
SHEET    7 AA4 9 GLY C 166  GLY C 173 -1  N  VAL C 167   O  LEU C 182           
SHEET    8 AA4 9 ALA C 157  ALA C 163 -1  N  VAL C 159   O  SER C 170           
SHEET    9 AA4 9 VAL C 203  ALA C 208 -1  O  LEU C 205   N  ILE C 160           
SHEET    1 AA5 9 LEU B  66  ASN B  71  0                                        
SHEET    2 AA5 9 GLU B  25  SER B  31 -1  N  ILE B  30   O  LEU B  66           
SHEET    3 AA5 9 GLY B  34  MET B  40 -1  O  ASN B  36   N  ASP B  29           
SHEET    4 AA5 9 LEU B  47  ARG B  53 -1  O  LEU B  50   N  LEU B  37           
SHEET    5 AA5 9 GLY B 245  LEU B 251 -1  O  LYS B 248   N  GLN B  49           
SHEET    6 AA5 9 LEU B 235  ILE B 241 -1  N  TYR B 239   O  LEU B 247           
SHEET    7 AA5 9 THR B 224  MET B 229 -1  N  THR B 226   O  GLU B 238           
SHEET    8 AA5 9 CYS B 135  PRO B 140 -1  N  VAL B 137   O  LEU B 227           
SHEET    9 AA5 9 THR B 196  MET B 199 -1  O  GLU B 198   N  VAL B 136           
SHEET    1 AA6 9 LEU C  66  ASN C  71  0                                        
SHEET    2 AA6 9 GLU C  25  SER C  31 -1  N  ILE C  30   O  LEU C  66           
SHEET    3 AA6 9 GLY C  34  MET C  40 -1  O  ASN C  36   N  ASP C  29           
SHEET    4 AA6 9 SER C  46  ARG C  53 -1  O  LEU C  52   N  VAL C  35           
SHEET    5 AA6 9 GLY C 245  LEU C 251 -1  O  LYS C 248   N  GLN C  49           
SHEET    6 AA6 9 LEU C 235  ILE C 241 -1  N  TYR C 239   O  LEU C 247           
SHEET    7 AA6 9 THR C 224  MET C 229 -1  N  THR C 226   O  GLU C 238           
SHEET    8 AA6 9 CYS C 135  PRO C 140 -1  N  VAL C 137   O  LEU C 227           
SHEET    9 AA6 9 THR C 196  MET C 199 -1  O  GLU C 198   N  VAL C 136           
CRYST1  162.950  162.950  140.400  90.00  90.00  90.00 P 41 21 2    24          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006137  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006137  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007123        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system