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Database: PDB
Entry: 6CBI
LinkDB: 6CBI
Original site: 6CBI 
HEADER    CELL CYCLE                              03-FEB-18   6CBI              
TITLE     PCNA IN COMPLEX WITH INHIBITOR                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;                        
COMPND   3 CHAIN: A, C, E, B, D, F;                                             
COMPND   4 SYNONYM: PCNA,CYCLIN;                                                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: GLY-ARG-LYS-ARG-ARG-GLN-DAB-SER-MET-THR-GLU-PHE-TYR-HIS;   
COMPND   8 CHAIN: H, I, J, K;                                                   
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 OTHER_DETAILS: PEPTIDE MIMETIC WITH COVALENT LACTAM BRIDGE BETWEEN   
COMPND  11 DAB AND GLU SIDE CHAINS                                              
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 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606                                                 
KEYWDS    PCNA, SLIDING CLAMP, PROLIFERATING CELL NUCLEAR ANTIGEN, CELL CYCLE   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.B.BRUNING,K.L.WEGENER                                               
REVDAT   3   29-AUG-18 6CBI    1       JRNL                                     
REVDAT   2   01-AUG-18 6CBI    1       JRNL                                     
REVDAT   1   04-JUL-18 6CBI    0                                                
JRNL        AUTH   K.L.WEGENER,A.E.MCGRATH,N.E.DIXON,A.J.OAKLEY,D.B.SCANLON,    
JRNL        AUTH 2 A.D.ABELL,J.B.BRUNING                                        
JRNL        TITL   RATIONAL DESIGN OF A 310-HELICAL PIP-BOX MIMETIC TARGETING   
JRNL        TITL 2 PCNA, THE HUMAN SLIDING CLAMP.                               
JRNL        REF    CHEMISTRY                     V.  24 11325 2018              
JRNL        REFN                   ISSN 1521-3765                               
JRNL        PMID   29917264                                                     
JRNL        DOI    10.1002/CHEM.201801734                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.09                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 46931                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.960                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2328                            
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 41.0904 -  7.0599    0.91     2837   151  0.1966 0.2199        
REMARK   3     2  7.0599 -  5.6082    0.95     2845   140  0.2147 0.2243        
REMARK   3     3  5.6082 -  4.9006    0.96     2826   149  0.1573 0.1915        
REMARK   3     4  4.9006 -  4.4531    0.96     2831   140  0.1393 0.1968        
REMARK   3     5  4.4531 -  4.1342    0.95     2797   140  0.1636 0.1992        
REMARK   3     6  4.1342 -  3.8907    0.95     2799   128  0.1844 0.2324        
REMARK   3     7  3.8907 -  3.6960    0.94     2763   147  0.1984 0.2293        
REMARK   3     8  3.6960 -  3.5352    0.94     2705   147  0.2123 0.2410        
REMARK   3     9  3.5352 -  3.3991    0.92     2673   138  0.2228 0.2863        
REMARK   3    10  3.3991 -  3.2819    0.91     2667   122  0.2407 0.3267        
REMARK   3    11  3.2819 -  3.1793    0.89     2565   154  0.2670 0.3344        
REMARK   3    12  3.1793 -  3.0885    0.87     2494   135  0.2922 0.3398        
REMARK   3    13  3.0885 -  3.0072    0.85     2419   144  0.2990 0.3825        
REMARK   3    14  3.0072 -  2.9338    0.82     2369   121  0.3121 0.3445        
REMARK   3    15  2.9338 -  2.8672    0.82     2353   132  0.3252 0.3807        
REMARK   3    16  2.8672 -  2.8062    0.81     2338   128  0.3267 0.3975        
REMARK   3    17  2.8062 -  2.7500    0.80     2322   112  0.3421 0.3577        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.450            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.370           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 57.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.006          11893                                  
REMARK   3   ANGLE     :  1.011          16059                                  
REMARK   3   CHIRALITY :  0.052           1909                                  
REMARK   3   PLANARITY :  0.009           2038                                  
REMARK   3   DIHEDRAL  : 13.790           7331                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6CBI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000232496.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUL-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : DOUBLE SI WITH SAGITTALY BENT      
REMARK 200                                   SECOND CRYSTAL                     
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.3.11                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47028                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.680                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.19600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.89900                            
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: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE 0.1M TRIS PH8.0,     
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 289K                                   
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       39.13000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       87.24000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.41000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       87.24000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.13000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       72.41000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7270 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, H, J                         
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, D, F, I, K                         
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     PRO A   106                                                      
REMARK 465     ASN A   107                                                      
REMARK 465     VAL A   123                                                      
REMARK 465     GLU A   124                                                      
REMARK 465     ASN A   187                                                      
REMARK 465     VAL A   188                                                      
REMARK 465     ASP A   189                                                      
REMARK 465     LYS A   190                                                      
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     LEU C   126                                                      
REMARK 465     GLY C   127                                                      
REMARK 465     ILE C   128                                                      
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   256                                                      
REMARK 465     ASP C   257                                                      
REMARK 465     GLU C   258                                                      
REMARK 465     GLU C   259                                                      
REMARK 465     GLY C   260                                                      
REMARK 465     SER C   261                                                      
REMARK 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 465     PRO B   106                                                      
REMARK 465     ASN B   107                                                      
REMARK 465     ASP B   122                                                      
REMARK 465     VAL B   123                                                      
REMARK 465     GLU B   124                                                      
REMARK 465     ASN B   187                                                      
REMARK 465     VAL B   188                                                      
REMARK 465     ASP B   189                                                      
REMARK 465     LYS B   190                                                      
REMARK 465     GLU B   256                                                      
REMARK 465     ASP B   257                                                      
REMARK 465     GLU B   258                                                      
REMARK 465     GLU B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     SER B   261                                                      
REMARK 465     GLU D   124                                                      
REMARK 465     GLN D   125                                                      
REMARK 465     SER D   186                                                      
REMARK 465     ASN D   187                                                      
REMARK 465     VAL D   188                                                      
REMARK 465     ASP D   189                                                      
REMARK 465     GLU D   256                                                      
REMARK 465     ASP D   257                                                      
REMARK 465     GLU D   258                                                      
REMARK 465     GLU D   259                                                      
REMARK 465     GLY D   260                                                      
REMARK 465     SER D   261                                                      
REMARK 465     ASN F   107                                                      
REMARK 465     GLN F   108                                                      
REMARK 465     GLU F   256                                                      
REMARK 465     ASP F   257                                                      
REMARK 465     GLU F   258                                                      
REMARK 465     GLU F   259                                                      
REMARK 465     GLY F   260                                                      
REMARK 465     SER F   261                                                      
REMARK 465     GLY H   139                                                      
REMARK 465     ARG H   140                                                      
REMARK 465     LYS H   141                                                      
REMARK 465     GLY I   139                                                      
REMARK 465     ARG I   140                                                      
REMARK 465     LYS I   141                                                      
REMARK 465     ARG I   142                                                      
REMARK 465     ARG I   143                                                      
REMARK 465     HIS I   152                                                      
REMARK 465     GLY J   139                                                      
REMARK 465     ARG J   140                                                      
REMARK 465     LYS J   141                                                      
REMARK 465     GLY K   139                                                      
REMARK 465     ARG K   140                                                      
REMARK 465     LYS K   141                                                      
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     GLN A 108    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 109    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 122    CG   OD1  OD2                                       
REMARK 470     GLN A 125    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 126    CG   CD1  CD2                                       
REMARK 470     GLU A 191    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 198    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 255    CG1  CG2  CD1                                       
REMARK 470     ASP C  94    CG   OD1  OD2                                       
REMARK 470     GLU C 109    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 124    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 125    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 191    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 192    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 193    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 198    CG   CD   OE1  OE2                                  
REMARK 470     ASN E 107    CG   OD1  ND2                                       
REMARK 470     GLN E 108    CG   CD   OE1  NE2                                  
REMARK 470     GLU E 109    CG   CD   OE1  OE2                                  
REMARK 470     ASP E 122    CG   OD1  OD2                                       
REMARK 470     GLU E 124    CG   CD   OE1  OE2                                  
REMARK 470     ILE E 128    CG1  CG2  CD1                                       
REMARK 470     ARG E 146    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER E 186    OG                                                  
REMARK 470     ASN E 187    CG   OD1  ND2                                       
REMARK 470     VAL E 188    CG1  CG2                                            
REMARK 470     ASP E 189    CG   OD1  OD2                                       
REMARK 470     LYS E 190    CG   CD   CE   NZ                                   
REMARK 470     ILE E 255    CG1  CG2  CD1                                       
REMARK 470     ASN B  24    CG   OD1  ND2                                       
REMARK 470     ARG B  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 109    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 125    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 126    CG   CD1  CD2                                       
REMARK 470     GLU B 191    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 193    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 255    CG1  CG2  CD1                                       
REMARK 470     ASN D  95    CG   OD1  ND2                                       
REMARK 470     ASN D 107    CG   OD1  ND2                                       
REMARK 470     GLN D 108    CG   CD   OE1  NE2                                  
REMARK 470     VAL D 123    CG1  CG2                                            
REMARK 470     ILE D 128    CG1  CG2  CD1                                       
REMARK 470     GLU D 193    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 210    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE D 255    CG1  CG2  CD1                                       
REMARK 470     ARG F  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU F 109    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 124    CG   CD   OE1  OE2                                  
REMARK 470     LEU F 126    CG   CD1  CD2                                       
REMARK 470     SER F 186    OG                                                  
REMARK 470     ASP F 189    CG   OD1  OD2                                       
REMARK 470     LYS F 190    CG   CD   CE   NZ                                   
REMARK 470     GLU F 191    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 198    CG   CD   OE1  OE2                                  
REMARK 470     TYR H 151    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     HIS H 152    O                                                   
REMARK 470     TYR I 151    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     HIS J 152    O    CG   ND1  CD2  CE1  NE2                        
REMARK 470     HIS K 152    O                                                   
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   C    ALA C   105     CD   PRO C   106              1.70            
REMARK 500   OD1  ASP F    58     O    HOH F   301              1.84            
REMARK 500   O    ASN C   107     N    GLU C   109              1.87            
REMARK 500   OE2  GLU B   198     O    HOH B   401              1.91            
REMARK 500   O    GLU A   256     N    GLN I   144              1.99            
REMARK 500   OG1  THR C    59     O    HOH C   301              2.01            
REMARK 500   CG   DAB I   145     CD   GLU I   149              2.02            
REMARK 500   NZ   LYS E    80     O    HOH E   301              2.07            
REMARK 500   O    HOH E   324     O    HOH K   203              2.10            
REMARK 500   OD2  ASP E   232     O    HOH E   302              2.11            
REMARK 500   NE   ARG A    91     O    HOH A   301              2.11            
REMARK 500   O    HOH E   324     O    HOH K   204              2.11            
REMARK 500   OD2  ASP C    29     O    HOH C   302              2.12            
REMARK 500   N    GLN A   184     O    HOH A   302              2.12            
REMARK 500   O    MET C   119     O    HOH C   303              2.12            
REMARK 500   OE1  GLU F    25     O    HOH F   302              2.13            
REMARK 500   CG   DAB I   145     OE1  GLU I   149              2.13            
REMARK 500   OD1  ASP B   150     O    HOH B   402              2.13            
REMARK 500   OH   TYR D   114     O    HOH D   401              2.14            
REMARK 500   OE1  GLU A   143     NH2  ARG A   146              2.14            
REMARK 500   O    CYS A   162     O    HOH A   303              2.15            
REMARK 500   OE2  GLU B    25     O    HOH B   403              2.15            
REMARK 500   O    THR F   216     OG1  THR F   219              2.16            
REMARK 500   OG1  THR F    59     O    HOH F   303              2.16            
REMARK 500   O    MET C   199     O    HOH C   304              2.16            
REMARK 500   ND   DAB K   145     CG   GLU K   149              2.16            
REMARK 500   O    SER B   172     O    HOH B   404              2.17            
REMARK 500   OH   TYR C   114     O    HOH C   305              2.17            
REMARK 500   O    LEU D   121     O    HOH D   402              2.17            
REMARK 500   OG1  THR B    59     O    HOH B   405              2.17            
REMARK 500   O    GLY E    34     O    HOH E   303              2.17            
REMARK 500   OE2  GLU E   132     ND2  ASN E   200              2.18            
REMARK 500   OD1  ASP E    58     O    HOH E   304              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   NH1  ARG C    53     OD1  ASN F   187     1655     2.04            
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    PRO C 106   C   -  N   -  CD  ANGL. DEV. = -53.1 DEGREES          
REMARK 500    PRO C 106   CA  -  N   -  CD  ANGL. DEV. =  -9.4 DEGREES          
REMARK 500    ASP C 122   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    PRO F 106   C   -  N   -  CD  ANGL. DEV. = -16.3 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    ASN A  95       42.89    -93.30                                   
REMARK 500    GLU A 109       65.25     -6.83                                   
REMARK 500    PRO A 129     -144.68    -71.67                                   
REMARK 500    GLN A 204      116.83   -162.92                                   
REMARK 500    SER A 230     -101.32    -60.91                                   
REMARK 500    ALA A 231      -64.87    167.13                                   
REMARK 500    ASP A 232       50.02   -157.35                                   
REMARK 500    ASP A 243      -12.93     69.88                                   
REMARK 500    ILE A 255       66.44   -108.40                                   
REMARK 500    ASN C  95       57.98    -94.42                                   
REMARK 500    PRO C 106      -85.32      1.46                                   
REMARK 500    ASN C 107       79.43    -52.70                                   
REMARK 500    GLN C 108       41.12    -37.20                                   
REMARK 500    ASP C 122      139.99     71.30                                   
REMARK 500    GLU C 124      -64.60    -98.09                                   
REMARK 500    ASP C 243      -18.28     70.36                                   
REMARK 500    ASN E  95      -86.20    -83.86                                   
REMARK 500    ALA E  96      116.21     52.56                                   
REMARK 500    GLN E 108        7.51     85.96                                   
REMARK 500    VAL E 123       99.27    -63.96                                   
REMARK 500    ASN E 187      136.65     73.18                                   
REMARK 500    VAL E 188     -159.84   -118.13                                   
REMARK 500    GLN E 204      115.51   -161.80                                   
REMARK 500    ASP E 243      -16.21     68.41                                   
REMARK 500    ASN B  95       38.42    -88.83                                   
REMARK 500    GLU B 109      -34.65     64.97                                   
REMARK 500    LEU B 126       85.26   -155.25                                   
REMARK 500    ILE B 128       97.77     78.58                                   
REMARK 500    PRO B 129     -151.58    -41.12                                   
REMARK 500    GLN B 204      116.03   -160.84                                   
REMARK 500    ASP B 243      -17.08     67.73                                   
REMARK 500    PHE D   2      116.88   -166.51                                   
REMARK 500    ASN D  95       59.78    -93.43                                   
REMARK 500    ALA D  96     -111.33     20.37                                   
REMARK 500    ASP D  97      -48.74     68.57                                   
REMARK 500    PRO D 106      -51.44    -28.10                                   
REMARK 500    ASN D 107       49.56   -179.34                                   
REMARK 500    GLU D 191     -131.69   -162.08                                   
REMARK 500    GLN D 204      115.47   -161.54                                   
REMARK 500    ASP D 243      -17.14     67.03                                   
REMARK 500    ASN F  95       52.59    -97.40                                   
REMARK 500    GLU F 124       45.80    -85.61                                   
REMARK 500    LEU F 126     -119.81    -91.93                                   
REMARK 500    ASN F 187       91.62    -62.47                                   
REMARK 500    ALA F 242       57.93      9.90                                   
REMARK 500    PHE H 150     -109.83    -70.54                                   
REMARK 500    PHE J 150      -82.72    -77.89                                   
REMARK 500    TYR J 151       98.74    -69.44                                   
REMARK 500    PHE K 150      -75.54    -86.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH F 347        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH F 348        DISTANCE =  7.62 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLN H 144 and DAB H    
REMARK 800  145                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DAB H 145 and SER H    
REMARK 800  146                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DAB H 145 and GLU H    
REMARK 800  149                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLN I 144 and DAB I    
REMARK 800  145                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DAB I 145 and SER I    
REMARK 800  146                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DAB I 145 and GLU I    
REMARK 800  149                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLN J 144 and DAB J    
REMARK 800  145                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DAB J 145 and GLU J    
REMARK 800  149                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DAB J 145 and SER J    
REMARK 800  146                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLN K 144 and DAB K    
REMARK 800  145                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DAB K 145 and GLU K    
REMARK 800  149                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DAB K 145 and SER K    
REMARK 800  146                                                                 
DBREF  6CBI A    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  6CBI C    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  6CBI E    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  6CBI B    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  6CBI D    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  6CBI F    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  6CBI H  139   152  PDB    6CBI     6CBI           139    152             
DBREF  6CBI I  139   152  PDB    6CBI     6CBI           139    152             
DBREF  6CBI J  139   152  PDB    6CBI     6CBI           139    152             
DBREF  6CBI K  139   152  PDB    6CBI     6CBI           139    152             
SEQRES   1 A  261  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 A  261  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 A  261  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 A  261  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 A  261  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 A  261  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 A  261  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 A  261  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 A  261  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 A  261  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 A  261  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 A  261  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 A  261  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 A  261  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 A  261  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 A  261  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 A  261  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 A  261  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 A  261  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 A  261  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 A  261  SER                                                          
SEQRES   1 C  261  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 C  261  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 C  261  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 C  261  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 C  261  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 C  261  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 C  261  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 C  261  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 C  261  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 C  261  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 C  261  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 C  261  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 C  261  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 C  261  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 C  261  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 C  261  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 C  261  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 C  261  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 C  261  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 C  261  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 C  261  SER                                                          
SEQRES   1 E  261  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 E  261  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 E  261  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 E  261  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 E  261  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 E  261  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 E  261  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 E  261  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 E  261  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 E  261  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 E  261  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 E  261  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 E  261  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 E  261  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 E  261  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 E  261  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 E  261  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 E  261  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 E  261  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 E  261  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 E  261  SER                                                          
SEQRES   1 B  261  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 B  261  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 B  261  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 B  261  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 B  261  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 B  261  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 B  261  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 B  261  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 B  261  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 B  261  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 B  261  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 B  261  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 B  261  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 B  261  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 B  261  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 B  261  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 B  261  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 B  261  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 B  261  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 B  261  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 B  261  SER                                                          
SEQRES   1 D  261  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 D  261  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 D  261  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 D  261  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 D  261  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 D  261  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 D  261  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 D  261  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 D  261  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 D  261  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 D  261  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 D  261  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 D  261  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 D  261  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 D  261  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 D  261  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 D  261  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 D  261  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 D  261  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 D  261  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 D  261  SER                                                          
SEQRES   1 F  261  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 F  261  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 F  261  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 F  261  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 F  261  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 F  261  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 F  261  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 F  261  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 F  261  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 F  261  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 F  261  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 F  261  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 F  261  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 F  261  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 F  261  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 F  261  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 F  261  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 F  261  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 F  261  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 F  261  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 F  261  SER                                                          
SEQRES   1 H   14  GLY ARG LYS ARG ARG GLN DAB SER MET THR GLU PHE TYR          
SEQRES   2 H   14  HIS                                                          
SEQRES   1 I   14  GLY ARG LYS ARG ARG GLN DAB SER MET THR GLU PHE TYR          
SEQRES   2 I   14  HIS                                                          
SEQRES   1 J   14  GLY ARG LYS ARG ARG GLN DAB SER MET THR GLU PHE TYR          
SEQRES   2 J   14  HIS                                                          
SEQRES   1 K   14  GLY ARG LYS ARG ARG GLN DAB SER MET THR GLU PHE TYR          
SEQRES   2 K   14  HIS                                                          
HET    DAB  H 145       7                                                       
HET    DAB  I 145       7                                                       
HET    DAB  J 145       7                                                       
HET    DAB  K 145       7                                                       
HET    SO4  B 301       5                                                       
HET    SO4  D 301       5                                                       
HETNAM     DAB 2,4-DIAMINOBUTYRIC ACID                                          
HETNAM     SO4 SULFATE ION                                                      
FORMUL   7  DAB    4(C4 H10 N2 O2)                                              
FORMUL  11  SO4    2(O4 S 2-)                                                   
FORMUL  13  HOH   *212(H2 O)                                                    
HELIX    1 AA1 GLY A    9  LYS A   20  1                                  12    
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  SER A  152  1                                  12    
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  LYS C   20  1                                  13    
HELIX    8 AA8 GLU C   55  PHE C   57  5                                   3    
HELIX    9 AA9 LEU C   72  LYS C   80  1                                   9    
HELIX   10 AB1 SER C  141  HIS C  153  1                                  13    
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  LYS E   20  1                                  13    
HELIX   14 AB5 GLU E   55  PHE E   57  5                                   3    
HELIX   15 AB6 LEU E   72  LYS E   80  1                                   9    
HELIX   16 AB7 SER E  141  HIS E  153  1                                  13    
HELIX   17 AB8 LYS E  190  ALA E  194  5                                   5    
HELIX   18 AB9 LEU E  209  THR E  216  1                                   8    
HELIX   19 AC1 LYS E  217  SER E  222  5                                   6    
HELIX   20 AC2 GLN B    8  LYS B   20  1                                  13    
HELIX   21 AC3 GLU B   55  PHE B   57  5                                   3    
HELIX   22 AC4 LEU B   72  LYS B   80  1                                   9    
HELIX   23 AC5 SER B  141  SER B  152  1                                  12    
HELIX   24 AC6 LEU B  209  THR B  216  1                                   8    
HELIX   25 AC7 LYS B  217  SER B  222  5                                   6    
HELIX   26 AC8 GLY D    9  LYS D   20  1                                  12    
HELIX   27 AC9 GLU D   55  PHE D   57  5                                   3    
HELIX   28 AD1 LEU D   72  CYS D   81  1                                  10    
HELIX   29 AD2 SER D  141  HIS D  153  1                                  13    
HELIX   30 AD3 LEU D  209  THR D  216  1                                   8    
HELIX   31 AD4 LYS D  217  SER D  222  5                                   6    
HELIX   32 AD5 GLY F    9  LYS F   20  1                                  12    
HELIX   33 AD6 GLU F   55  PHE F   57  5                                   3    
HELIX   34 AD7 LEU F   72  LYS F   80  1                                   9    
HELIX   35 AD8 SER F  141  HIS F  153  1                                  13    
HELIX   36 AD9 LYS F  190  ALA F  194  5                                   5    
HELIX   37 AE1 LEU F  209  THR F  216  1                                   8    
HELIX   38 AE2 LYS F  217  SER F  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  ARG A   5   O  THR A  59           
SHEET    3 AA1 9 ILE A  87  ALA A  92 -1  O  ALA A  92   N  PHE A   2           
SHEET    4 AA1 9 THR A  98  GLU A 104 -1  O  GLU A 104   N  ILE A  87           
SHEET    5 AA1 9 LYS A 110  LYS A 117 -1  O  MET A 116   N  LEU A  99           
SHEET    6 AA1 9 GLY C 176  LEU C 182 -1  O  ASN C 179   N  ASP A 113           
SHEET    7 AA1 9 GLY C 166  GLY C 173 -1  N  GLY C 173   O  GLY C 176           
SHEET    8 AA1 9 ALA C 157  ALA C 163 -1  N  SER C 161   O  LYS C 168           
SHEET    9 AA1 9 VAL C 203  ALA C 208 -1  O  VAL C 203   N  CYS C 162           
SHEET    1 AA2 9 LEU A  66  ASN A  71  0                                        
SHEET    2 AA2 9 GLU A  25  SER A  31 -1  N  ALA A  26   O  VAL A  70           
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  HIS A 246   N  THR A  51           
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  CYS A 135   O  MET A 229           
SHEET    9 AA2 9 THR A 196  MET A 199 -1  O  THR A 196   N  LYS A 138           
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  LEU A 182 -1  O  GLY A 176   N  GLY A 173           
SHEET    5 AA3 9 LYS E 110  LYS E 117 -1  O  GLU E 115   N  ASN A 177           
SHEET    6 AA3 9 THR E  98  GLU E 104 -1  N  LEU E  99   O  MET E 116           
SHEET    7 AA3 9 ILE E  87  ALA E  92 -1  N  ARG E  91   O  ALA E 100           
SHEET    8 AA3 9 PHE E   2  LEU E   6 -1  N  LEU E   6   O  ILE E  88           
SHEET    9 AA3 9 THR E  59  CYS E  62 -1  O  THR E  59   N  ARG E   5           
SHEET    1 AA4 9 THR C  59  CYS C  62  0                                        
SHEET    2 AA4 9 PHE C   2  LEU C   6 -1  N  ARG C   5   O  THR C  59           
SHEET    3 AA4 9 ILE C  87  ALA C  92 -1  O  ILE C  88   N  LEU C   6           
SHEET    4 AA4 9 THR C  98  ALA C 105 -1  O  ALA C 100   N  ARG C  91           
SHEET    5 AA4 9 LYS C 110  LYS C 117 -1  O  MET C 116   N  LEU C  99           
SHEET    6 AA4 9 GLY E 176  SER E 183 -1  O  ASN E 177   N  GLU C 115           
SHEET    7 AA4 9 GLY E 166  GLY E 173 -1  N  GLY E 173   O  GLY E 176           
SHEET    8 AA4 9 ALA E 157  ALA E 163 -1  N  SER E 161   O  LYS E 168           
SHEET    9 AA4 9 VAL E 203  ALA E 208 -1  O  VAL E 203   N  CYS E 162           
SHEET    1 AA5 9 LEU C  66  ASN C  71  0                                        
SHEET    2 AA5 9 GLU C  25  SER C  31 -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  HIS C 246   N  THR C  51           
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 LEU E  66  ASN E  71  0                                        
SHEET    2 AA6 9 GLU E  25  SER E  31 -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  LEU E  52   N  VAL E  35           
SHEET    5 AA6 9 GLY E 245  LEU E 251 -1  O  HIS E 246   N  THR E  51           
SHEET    6 AA6 9 LEU E 235  ILE E 241 -1  N  TYR E 239   O  LEU E 247           
SHEET    7 AA6 9 THR E 224  MET E 229 -1  N  SER E 228   O  VAL E 236           
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           
SHEET    1 AA7 9 THR B  59  CYS B  62  0                                        
SHEET    2 AA7 9 PHE B   2  LEU B   6 -1  N  ARG B   5   O  THR B  59           
SHEET    3 AA7 9 ILE B  87  ALA B  92 -1  O  ILE B  88   N  LEU B   6           
SHEET    4 AA7 9 THR B  98  GLU B 104 -1  O  GLU B 104   N  ILE B  87           
SHEET    5 AA7 9 LYS B 110  LYS B 117 -1  O  MET B 116   N  LEU B  99           
SHEET    6 AA7 9 GLY D 176  SER D 183 -1  O  ASN D 177   N  GLU B 115           
SHEET    7 AA7 9 GLY D 166  GLY D 173 -1  N  VAL D 167   O  LEU D 182           
SHEET    8 AA7 9 ALA D 157  ALA D 163 -1  N  ALA D 163   O  GLY D 166           
SHEET    9 AA7 9 VAL D 203  ALA D 208 -1  O  PHE D 207   N  VAL D 158           
SHEET    1 AA8 9 LEU B  66  ASN B  71  0                                        
SHEET    2 AA8 9 GLU B  25  SER B  31 -1  N  TRP B  28   O  MET B  68           
SHEET    3 AA8 9 GLY B  34  MET B  40 -1  O  ASN B  36   N  ASP B  29           
SHEET    4 AA8 9 SER B  46  ARG B  53 -1  O  LEU B  52   N  VAL B  35           
SHEET    5 AA8 9 GLY B 245  LEU B 251 -1  O  HIS B 246   N  THR B  51           
SHEET    6 AA8 9 LEU B 235  ILE B 241 -1  N  VAL B 237   O  TYR B 249           
SHEET    7 AA8 9 THR B 224  MET B 229 -1  N  THR B 226   O  GLU B 238           
SHEET    8 AA8 9 CYS B 135  PRO B 140 -1  N  MET B 139   O  VAL B 225           
SHEET    9 AA8 9 THR B 196  MET B 199 -1  O  THR B 196   N  LYS B 138           
SHEET    1 AA9 8 VAL B 203  ALA B 208  0                                        
SHEET    2 AA9 8 ALA B 157  ALA B 163 -1  N  CYS B 162   O  VAL B 203           
SHEET    3 AA9 8 GLY B 166  GLY B 173 -1  O  LYS B 168   N  SER B 161           
SHEET    4 AA9 8 GLY B 176  SER B 183 -1  O  GLY B 176   N  GLY B 173           
SHEET    5 AA9 8 LYS F 110  LYS F 117 -1  O  ASP F 113   N  ASN B 179           
SHEET    6 AA9 8 THR F  98  GLU F 104 -1  N  LEU F  99   O  MET F 116           
SHEET    7 AA9 8 ILE F  87  ALA F  92 -1  N  ARG F  91   O  ALA F 100           
SHEET    8 AA9 8 PHE F   2  LEU F   6 -1  N  LEU F   6   O  ILE F  88           
SHEET    1 AB1 8 GLU D   3  LEU D   6  0                                        
SHEET    2 AB1 8 ILE D  87  ARG D  91 -1  O  ILE D  88   N  LEU D   6           
SHEET    3 AB1 8 THR D  98  GLU D 104 -1  O  ALA D 100   N  ARG D  91           
SHEET    4 AB1 8 LYS D 110  LYS D 117 -1  O  MET D 116   N  LEU D  99           
SHEET    5 AB1 8 GLY F 176  SER F 183 -1  O  ASN F 179   N  ASP D 113           
SHEET    6 AB1 8 GLY F 166  GLY F 173 -1  N  PHE F 169   O  ILE F 180           
SHEET    7 AB1 8 ALA F 157  CYS F 162 -1  N  VAL F 159   O  SER F 170           
SHEET    8 AB1 8 VAL F 203  ALA F 208 -1  O  VAL F 203   N  CYS F 162           
SHEET    1 AB2 9 LEU D  66  ASN D  71  0                                        
SHEET    2 AB2 9 GLU D  25  SER D  31 -1  N  ALA D  26   O  VAL D  70           
SHEET    3 AB2 9 GLY D  34  MET D  40 -1  O  ASN D  36   N  ASP D  29           
SHEET    4 AB2 9 SER D  46  ARG D  53 -1  O  VAL D  48   N  SER D  39           
SHEET    5 AB2 9 GLY D 245  LEU D 251 -1  O  HIS D 246   N  THR D  51           
SHEET    6 AB2 9 LEU D 235  ILE D 241 -1  N  TYR D 239   O  LEU D 247           
SHEET    7 AB2 9 THR D 224  MET D 229 -1  N  THR D 226   O  GLU D 238           
SHEET    8 AB2 9 CYS D 135  PRO D 140 -1  N  MET D 139   O  VAL D 225           
SHEET    9 AB2 9 THR D 196  MET D 199 -1  O  GLU D 198   N  VAL D 136           
SHEET    1 AB3 9 LEU F  66  ASN F  71  0                                        
SHEET    2 AB3 9 GLU F  25  SER F  31 -1  N  TRP F  28   O  MET F  68           
SHEET    3 AB3 9 GLY F  34  MET F  40 -1  O  ASN F  36   N  ASP F  29           
SHEET    4 AB3 9 SER F  46  ARG F  53 -1  O  LEU F  52   N  VAL F  35           
SHEET    5 AB3 9 GLY F 245  LEU F 251 -1  O  HIS F 246   N  THR F  51           
SHEET    6 AB3 9 LEU F 235  ILE F 241 -1  N  VAL F 237   O  TYR F 249           
SHEET    7 AB3 9 THR F 224  MET F 229 -1  N  THR F 226   O  GLU F 238           
SHEET    8 AB3 9 CYS F 135  PRO F 140 -1  N  MET F 139   O  VAL F 225           
SHEET    9 AB3 9 THR F 196  MET F 199 -1  O  THR F 196   N  LYS F 138           
SSBOND   1 CYS A  135    CYS A  162                          1555   1555  2.05  
SSBOND   2 CYS C  135    CYS C  162                          1555   1555  2.03  
SSBOND   3 CYS E  135    CYS E  162                          1555   1555  2.03  
SSBOND   4 CYS B  135    CYS B  162                          1555   1555  2.03  
SSBOND   5 CYS D  135    CYS D  162                          1555   1555  2.04  
SSBOND   6 CYS F  135    CYS F  162                          1555   1555  2.03  
LINK         C   GLN H 144                 N   DAB H 145     1555   1555  1.33  
LINK         C   DAB H 145                 N   SER H 146     1555   1555  1.33  
LINK         ND  DAB H 145                 CD  GLU H 149     1555   1555  1.36  
LINK         C   GLN I 144                 N   DAB I 145     1555   1555  1.32  
LINK         C   DAB I 145                 N   SER I 146     1555   1555  1.33  
LINK         ND  DAB I 145                 CD  GLU I 149     1555   1555  1.35  
LINK         C   GLN J 144                 N   DAB J 145     1555   1555  1.33  
LINK         C   DAB J 145                 N   SER J 146     1555   1555  1.33  
LINK         ND  DAB J 145                 CD  GLU J 149     1555   1555  1.37  
LINK         C   GLN K 144                 N   DAB K 145     1555   1555  1.33  
LINK         C   DAB K 145                 N   SER K 146     1555   1555  1.33  
LINK         ND  DAB K 145                 CD  GLU K 149     1555   1555  1.29  
SITE     1 AC1  3 MET B  40  LEU B  47  PRO B 234                               
SITE     1 AC2  1 SER D  42                                                     
SITE     1 AC3 10 GLU B 174  VAL C  45  ALA C 252  PRO C 253                    
SITE     2 AC3 10 LYS C 254  HOH C 315  ARG H 143  SER H 146                    
SITE     3 AC3 10 GLU H 149  PHE H 150                                          
SITE     1 AC4  8 HIS C  44  ALA C 252  PRO C 253  GLN H 144                    
SITE     2 AC4  8 MET H 147  THR H 148  GLU H 149  PHE H 150                    
SITE     1 AC5  8 ALA C 252  PRO C 253  GLN H 144  SER H 146                    
SITE     2 AC5  8 MET H 147  THR H 148  PHE H 150  HIS H 152                    
SITE     1 AC6  8 VAL A  45  ALA A 252  PRO A 253  LYS A 254                    
SITE     2 AC6  8 GLU A 256  SER I 146  GLU I 149  PHE I 150                    
SITE     1 AC7  8 HIS A  44  ALA A 252  PRO A 253  GLN I 144                    
SITE     2 AC7  8 MET I 147  THR I 148  GLU I 149  PHE I 150                    
SITE     1 AC8  7 ALA A 252  PRO A 253  GLN I 144  SER I 146                    
SITE     2 AC8  7 MET I 147  THR I 148  PHE I 150                               
SITE     1 AC9  8 VAL D  45  ALA D 252  PRO D 253  LYS D 254                    
SITE     2 AC9  8 ARG J 143  SER J 146  GLU J 149  PHE J 150                    
SITE     1 AD1  7 ALA D 252  PRO D 253  GLN J 144  SER J 146                    
SITE     2 AD1  7 MET J 147  THR J 148  PHE J 150                               
SITE     1 AD2  8 HIS D  44  ALA D 252  PRO D 253  GLN J 144                    
SITE     2 AD2  8 MET J 147  THR J 148  GLU J 149  PHE J 150                    
SITE     1 AD3  9 VAL E  45  ALA E 252  PRO E 253  GLU F 174                    
SITE     2 AD3  9 ARG K 143  SER K 146  GLU K 149  PHE K 150                    
SITE     3 AD3  9 HOH K 201                                                     
SITE     1 AD4  8 ALA E 252  PRO E 253  GLN K 144  SER K 146                    
SITE     2 AD4  8 MET K 147  THR K 148  PHE K 150  HIS K 152                    
SITE     1 AD5  9 HIS E  44  ALA E 252  PRO E 253  GLN K 144                    
SITE     2 AD5  9 MET K 147  THR K 148  GLU K 149  PHE K 150                    
SITE     3 AD5  9 HOH K 202                                                     
CRYST1   78.260  144.820  174.480  90.00  90.00  90.00 P 21 21 21   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      0.012778  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006905  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005731        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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