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Database: PDB
Entry: 1UL1
LinkDB: 1UL1
Original site: 1UL1 
HEADER    HYDROLASE/DNA BINDING PROTEIN           05-SEP-03   1UL1              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN FEN1-PCNA COMPLEX                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FLAP ENDONUCLEASE-1;                                       
COMPND   3 CHAIN: X, Y, Z;                                                      
COMPND   4 SYNONYM: MATURATION FACTOR 1, MF1;                                   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;                        
COMPND   8 CHAIN: A, B, C;                                                      
COMPND   9 SYNONYM: PCNA, CYCLIN;                                               
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-22B(+);                               
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PGEMEX-1                                  
KEYWDS    PROTEIN COMPLEX, DNA-BINDING PROTEIN, FLAP DNA, FLAP                  
KEYWDS   2 ENDONUCLEASE, SLIDING CLAMP, DNA CLAMP, REPLICATION, DNA             
KEYWDS   3 REPAIR, HYDROLASE/DNA BINDING PROTEIN COMPLEX                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SAKURAI,K.KITANO,H.YAMAGUCHI,K.HAMADA,K.OKADA,K.FUKUDA,             
AUTHOR   2 M.UCHIDA,E.OHTSUKA,H.MORIOKA,T.HAKOSHIMA                             
REVDAT   2   24-FEB-09 1UL1    1       VERSN                                    
REVDAT   1   01-MAR-05 1UL1    0                                                
JRNL        AUTH   S.SAKURAI,K.KITANO,H.YAMAGUCHI,K.OKADA,K.HAMADA,             
JRNL        AUTH 2 K.FUKUDA,M.UCHIDA,E.OHTSUKA,H.MORIOKA,T.HAKOSHIMA            
JRNL        TITL   STRUCTURAL BASIS FOR RECRUITMENT OF HUMAN FLAP               
JRNL        TITL 2 ENDONUCLEASE 1 TO PCNA                                       
JRNL        REF    EMBO J.                       V.  24   683 2005              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   15616578                                                     
JRNL        DOI    10.1038/SJ.EMBOJ.7600519                                     
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 55716                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2821                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13157                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 1                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.30                          
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1UL1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-SEP-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB005944.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JAN-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL38B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55775                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG1000, 50MM MES, 50MM SODIUM        
REMARK 280  CHLORIDE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE        
REMARK 280  283K                                                                
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       41.10150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      123.32950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       71.69150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      123.32950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       41.10150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       71.69150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X, Y, Z, 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     ARG X    47                                                      
REMARK 465     GLN X    48                                                      
REMARK 465     GLY X    49                                                      
REMARK 465     GLY X    50                                                      
REMARK 465     ASP X    51                                                      
REMARK 465     VAL X    52                                                      
REMARK 465     LEU X    53                                                      
REMARK 465     GLN X    54                                                      
REMARK 465     ASN X    55                                                      
REMARK 465     GLU X    56                                                      
REMARK 465     GLU X    57                                                      
REMARK 465     GLY X    58                                                      
REMARK 465     GLU X    59                                                      
REMARK 465     ARG X   100                                                      
REMARK 465     SER X   101                                                      
REMARK 465     GLU X   102                                                      
REMARK 465     ARG X   103                                                      
REMARK 465     ARG X   104                                                      
REMARK 465     ALA X   105                                                      
REMARK 465     GLU X   106                                                      
REMARK 465     ALA X   107                                                      
REMARK 465     GLU X   108                                                      
REMARK 465     LYS X   109                                                      
REMARK 465     GLN X   110                                                      
REMARK 465     LEU X   111                                                      
REMARK 465     GLN X   112                                                      
REMARK 465     GLN X   113                                                      
REMARK 465     ALA X   114                                                      
REMARK 465     GLN X   115                                                      
REMARK 465     ALA X   116                                                      
REMARK 465     ALA X   117                                                      
REMARK 465     GLY X   118                                                      
REMARK 465     ALA X   119                                                      
REMARK 465     GLU X   120                                                      
REMARK 465     GLN X   121                                                      
REMARK 465     GLU X   122                                                      
REMARK 465     VAL X   123                                                      
REMARK 465     GLU X   124                                                      
REMARK 465     LYS X   125                                                      
REMARK 465     PHE X   126                                                      
REMARK 465     THR X   127                                                      
REMARK 465     LYS X   128                                                      
REMARK 465     ALA X   199                                                      
REMARK 465     PRO X   358                                                      
REMARK 465     GLU X   359                                                      
REMARK 465     PRO X   360                                                      
REMARK 465     LYS X   361                                                      
REMARK 465     GLY X   362                                                      
REMARK 465     SER X   363                                                      
REMARK 465     THR X   364                                                      
REMARK 465     LYS X   365                                                      
REMARK 465     LYS X   366                                                      
REMARK 465     LYS X   367                                                      
REMARK 465     ALA X   368                                                      
REMARK 465     LYS X   369                                                      
REMARK 465     THR X   370                                                      
REMARK 465     GLY X   371                                                      
REMARK 465     ALA X   372                                                      
REMARK 465     ALA X   373                                                      
REMARK 465     GLY X   374                                                      
REMARK 465     LYS X   375                                                      
REMARK 465     PHE X   376                                                      
REMARK 465     LYS X   377                                                      
REMARK 465     ARG X   378                                                      
REMARK 465     GLY X   379                                                      
REMARK 465     LYS X   380                                                      
REMARK 465     ALA Y    45                                                      
REMARK 465     VAL Y    46                                                      
REMARK 465     ARG Y    47                                                      
REMARK 465     GLN Y    48                                                      
REMARK 465     GLY Y    49                                                      
REMARK 465     GLY Y    50                                                      
REMARK 465     ASP Y    51                                                      
REMARK 465     VAL Y    52                                                      
REMARK 465     LEU Y    53                                                      
REMARK 465     GLN Y    54                                                      
REMARK 465     ASN Y    55                                                      
REMARK 465     GLU Y    56                                                      
REMARK 465     GLU Y    57                                                      
REMARK 465     GLY Y    58                                                      
REMARK 465     GLU Y    59                                                      
REMARK 465     ARG Y   103                                                      
REMARK 465     ARG Y   104                                                      
REMARK 465     ALA Y   105                                                      
REMARK 465     GLU Y   106                                                      
REMARK 465     ALA Y   107                                                      
REMARK 465     GLU Y   108                                                      
REMARK 465     LYS Y   109                                                      
REMARK 465     GLN Y   110                                                      
REMARK 465     LEU Y   111                                                      
REMARK 465     GLN Y   112                                                      
REMARK 465     GLN Y   113                                                      
REMARK 465     ALA Y   114                                                      
REMARK 465     GLN Y   115                                                      
REMARK 465     ALA Y   116                                                      
REMARK 465     ALA Y   117                                                      
REMARK 465     GLY Y   118                                                      
REMARK 465     ALA Y   119                                                      
REMARK 465     GLU Y   120                                                      
REMARK 465     GLN Y   121                                                      
REMARK 465     GLU Y   122                                                      
REMARK 465     VAL Y   123                                                      
REMARK 465     GLU Y   124                                                      
REMARK 465     LYS Y   125                                                      
REMARK 465     PHE Y   126                                                      
REMARK 465     THR Y   127                                                      
REMARK 465     LYS Y   128                                                      
REMARK 465     ARG Y   129                                                      
REMARK 465     LEU Y   130                                                      
REMARK 465     VAL Y   131                                                      
REMARK 465     LYS Y   132                                                      
REMARK 465     VAL Y   133                                                      
REMARK 465     PRO Y   360                                                      
REMARK 465     LYS Y   361                                                      
REMARK 465     GLY Y   362                                                      
REMARK 465     SER Y   363                                                      
REMARK 465     THR Y   364                                                      
REMARK 465     LYS Y   365                                                      
REMARK 465     LYS Y   366                                                      
REMARK 465     LYS Y   367                                                      
REMARK 465     ALA Y   368                                                      
REMARK 465     LYS Y   369                                                      
REMARK 465     THR Y   370                                                      
REMARK 465     GLY Y   371                                                      
REMARK 465     ALA Y   372                                                      
REMARK 465     ALA Y   373                                                      
REMARK 465     GLY Y   374                                                      
REMARK 465     LYS Y   375                                                      
REMARK 465     PHE Y   376                                                      
REMARK 465     LYS Y   377                                                      
REMARK 465     ARG Y   378                                                      
REMARK 465     GLY Y   379                                                      
REMARK 465     LYS Y   380                                                      
REMARK 465     ALA Z   114                                                      
REMARK 465     GLN Z   115                                                      
REMARK 465     ALA Z   116                                                      
REMARK 465     ALA Z   117                                                      
REMARK 465     GLY Z   118                                                      
REMARK 465     ALA Z   119                                                      
REMARK 465     GLU Z   357                                                      
REMARK 465     PRO Z   358                                                      
REMARK 465     GLU Z   359                                                      
REMARK 465     PRO Z   360                                                      
REMARK 465     LYS Z   361                                                      
REMARK 465     GLY Z   362                                                      
REMARK 465     SER Z   363                                                      
REMARK 465     THR Z   364                                                      
REMARK 465     LYS Z   365                                                      
REMARK 465     LYS Z   366                                                      
REMARK 465     LYS Z   367                                                      
REMARK 465     ALA Z   368                                                      
REMARK 465     LYS Z   369                                                      
REMARK 465     THR Z   370                                                      
REMARK 465     GLY Z   371                                                      
REMARK 465     ALA Z   372                                                      
REMARK 465     ALA Z   373                                                      
REMARK 465     GLY Z   374                                                      
REMARK 465     LYS Z   375                                                      
REMARK 465     PHE Z   376                                                      
REMARK 465     LYS Z   377                                                      
REMARK 465     ARG Z   378                                                      
REMARK 465     GLY Z   379                                                      
REMARK 465     LYS Z   380                                                      
REMARK 465     ASN A   187                                                      
REMARK 465     VAL A   188                                                      
REMARK 465     ASP A   189                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     SER A   261                                                      
REMARK 465     GLU B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     SER B   261                                                      
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 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     LYS X   8    CG   CD   CE   NZ                                   
REMARK 470     VAL X  13    CG1  CG2                                            
REMARK 470     TYR X  40    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL X  46    CG1  CG2                                            
REMARK 470     MET X  65    CG   SD   CE                                        
REMARK 470     GLU X  96    CG   CD   OE1  OE2                                  
REMARK 470     LEU X  97    CG   CD1  CD2                                       
REMARK 470     ARG X 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU X 130    CG   CD1  CD2                                       
REMARK 470     VAL X 131    CG1  CG2                                            
REMARK 470     LYS X 132    CG   CD   CE   NZ                                   
REMARK 470     VAL X 133    CG1  CG2                                            
REMARK 470     THR X 134    OG1  CG2                                            
REMARK 470     LYS X 135    CG   CD   CE   NZ                                   
REMARK 470     LYS X 200    CG   CD   CE   NZ                                   
REMARK 470     LYS X 201    CG   CD   CE   NZ                                   
REMARK 470     ARG X 245    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS X 252    CG   CD   CE   NZ                                   
REMARK 470     LYS X 277    CG   CD   CE   NZ                                   
REMARK 470     GLU X 285    CG   CD   OE1  OE2                                  
REMARK 470     LYS X 314    CG   CD   CE   NZ                                   
REMARK 470     GLN X 315    CG   CD   OE1  NE2                                  
REMARK 470     GLU X 319    CG   CD   OE1  OE2                                  
REMARK 470     LYS X 326    CG   CD   CE   NZ                                   
REMARK 470     ARG X 339    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU X 357    CG   CD   OE1  OE2                                  
REMARK 470     LYS Y   8    CG   CD   CE   NZ                                   
REMARK 470     ARG Y  19    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE Y  44    CG1  CG2  CD1                                       
REMARK 470     LYS Y  93    CG   CD   CE   NZ                                   
REMARK 470     GLU Y  96    CG   CD   OE1  OE2                                  
REMARK 470     LEU Y  97    CG   CD1  CD2                                       
REMARK 470     LYS Y  99    CG   CD   CE   NZ                                   
REMARK 470     ARG Y 100    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER Y 101    OG                                                  
REMARK 470     GLU Y 102    CG   CD   OE1  OE2                                  
REMARK 470     CYS Y 141    SG                                                  
REMARK 470     HIS Y 143    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU Y 147    CG   CD1  CD2                                       
REMARK 470     TYR Y 152    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS Y 168    CG   CD   CE   NZ                                   
REMARK 470     GLN Y 214    CG   CD   OE1  NE2                                  
REMARK 470     ASN Y 219    CG   OD1  ND2                                       
REMARK 470     ILE Y 256    CG1  CG2  CD1                                       
REMARK 470     GLU Y 257    CG   CD   OE1  OE2                                  
REMARK 470     ILE Y 259    CG1  CG2  CD1                                       
REMARK 470     LYS Y 267    CG   CD   CE   NZ                                   
REMARK 470     TYR Y 268    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS Y 277    CG   CD   CE   NZ                                   
REMARK 470     GLU Y 285    CG   CD   OE1  OE2                                  
REMARK 470     LEU Y 296    CG   CD1  CD2                                       
REMARK 470     LYS Y 297    CG   CD   CE   NZ                                   
REMARK 470     GLU Y 303    CG   CD   OE1  OE2                                  
REMARK 470     LEU Y 306    CG   CD1  CD2                                       
REMARK 470     PHE Y 309    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     MET Y 310    CG   SD   CE                                        
REMARK 470     LYS Y 314    CG   CD   CE   NZ                                   
REMARK 470     LYS Y 326    CG   CD   CE   NZ                                   
REMARK 470     GLN Y 333    CG   CD   OE1  NE2                                  
REMARK 470     GLU Y 359    CG   CD   OE1  OE2                                  
REMARK 470     LYS Z   8    CG   CD   CE   NZ                                   
REMARK 470     LEU Z   9    CG   CD1  CD2                                       
REMARK 470     ASP Z  12    CG   OD1  OD2                                       
REMARK 470     VAL Z  13    CG1  CG2                                            
REMARK 470     ILE Z  39    CG1  CG2  CD1                                       
REMARK 470     ILE Z  44    CG1  CG2  CD1                                       
REMARK 470     GLU Z  56    CG   CD   OE1  OE2                                  
REMARK 470     ILE Z  72    CG1  CG2  CD1                                       
REMARK 470     LYS Z  93    CG   CD   CE   NZ                                   
REMARK 470     ARG Z 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS Z 109    CG   CD   CE   NZ                                   
REMARK 470     GLN Z 113    CG   CD   OE1  NE2                                  
REMARK 470     GLU Z 120    CG   CD   OE1  OE2                                  
REMARK 470     GLN Z 121    CG   CD   OE1  NE2                                  
REMARK 470     GLU Z 122    CG   CD   OE1  OE2                                  
REMARK 470     VAL Z 123    CG1  CG2                                            
REMARK 470     GLU Z 124    CG   CD   OE1  OE2                                  
REMARK 470     PHE Z 126    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG Z 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU Z 140    CG   CD   OE1  OE2                                  
REMARK 470     MET Z 148    CG   SD   CE                                        
REMARK 470     GLU Z 158    CG   CD   OE1  OE2                                  
REMARK 470     GLU Z 160    CG   CD   OE1  OE2                                  
REMARK 470     GLU Z 198    CG   CD   OE1  OE2                                  
REMARK 470     ILE Z 228    CG1  CG2  CD1                                       
REMARK 470     LEU Z 229    CG   CD1  CD2                                       
REMARK 470     TYR Z 234    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE Z 241    CG1  CG2  CD1                                       
REMARK 470     ARG Z 245    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU Z 257    CG   CD   OE1  OE2                                  
REMARK 470     GLU Z 272    CG   CD   OE1  OE2                                  
REMARK 470     ASN Z 273    CG   OD1  ND2                                       
REMARK 470     LYS Z 277    CG   CD   CE   NZ                                   
REMARK 470     PHE Z 283    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU Z 285    CG   CD   OE1  OE2                                  
REMARK 470     GLU Z 295    CG   CD   OE1  OE2                                  
REMARK 470     LEU Z 306    CG   CD1  CD2                                       
REMARK 470     ILE Z 307    CG1  CG2  CD1                                       
REMARK 470     LYS Z 308    CG   CD   CE   NZ                                   
REMARK 470     GLU Z 319    CG   CD   OE1  OE2                                  
REMARK 470     GLN Z 333    CG   CD   OE1  NE2                                  
REMARK 470     LYS Z 345    CG   CD   CE   NZ                                   
REMARK 470     LYS Z 354    CG   CD   CE   NZ                                   
REMARK 470     LYS Z 356    CG   CD   CE   NZ                                   
REMARK 470     ASN A 107    CG   OD1  ND2                                       
REMARK 470     GLU A 109    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 164    CG   CD   CE   NZ                                   
REMARK 470     LYS A 190    CG   CD   CE   NZ                                   
REMARK 470     ARG B  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 138    CG   CD   CE   NZ                                   
REMARK 470     GLU B 174    CG   CD   OE1  OE2                                  
REMARK 470     SER B 186    OG                                                  
REMARK 470     VAL B 188    CG1  CG2                                            
REMARK 470     ASP B 189    CG   OD1  OD2                                       
REMARK 470     GLU B 193    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 210    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN C 107    CG   OD1  ND2                                       
REMARK 470     GLU C 109    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 122    CG   OD1  OD2                                       
REMARK 470     LYS C 138    CG   CD   CE   NZ                                   
REMARK 470     LYS C 164    CG   CD   CE   NZ                                   
REMARK 470     LYS C 181    CG   CD   CE   NZ                                   
REMARK 470     ASP C 189    CG   OD1  OD2                                       
REMARK 470     GLU C 191    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 240    CG   CD   CE   NZ                                   
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   OG1  THR Z    71     OH   TYR Z    83              2.17            
REMARK 500   O    ASN C   107     N    GLU C   109              2.19            
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    GLN X   4      116.85    -33.89                                   
REMARK 500    ASP X  12     -110.94    -74.90                                   
REMARK 500    VAL X  13      -42.82    -17.81                                   
REMARK 500    THR X  61       26.68   -148.53                                   
REMARK 500    GLU X  96       85.99    -61.58                                   
REMARK 500    LEU X  97      156.09    -49.95                                   
REMARK 500    ALA X  98      -95.25    -89.68                                   
REMARK 500    VAL X 133       87.93   -156.65                                   
REMARK 500    THR X 134      106.75    -57.65                                   
REMARK 500    GLN X 136       19.11     56.01                                   
REMARK 500    ASN X 138      -60.99    -24.16                                   
REMARK 500    PRO X 156      -72.65    -70.00                                   
REMARK 500    SER X 157     -115.40   -100.38                                   
REMARK 500    ASP X 181        8.18    -68.24                                   
REMARK 500    HIS X 193       29.63     95.27                                   
REMARK 500    THR X 195      -36.80   -140.49                                   
REMARK 500    ALA X 196       -1.83    -49.36                                   
REMARK 500    SER X 197      102.07    -52.00                                   
REMARK 500    LYS X 201       77.44   -161.43                                   
REMARK 500    GLN X 220      -54.81    -24.21                                   
REMARK 500    GLU X 221      -70.38    -50.26                                   
REMARK 500    CYS X 235      132.76   -175.45                                   
REMARK 500    GLU X 236      152.50    -42.88                                   
REMARK 500    LYS X 254      -23.83    -31.92                                   
REMARK 500    ARG X 262       41.52    102.06                                   
REMARK 500    LEU X 263     -125.76   -177.59                                   
REMARK 500    ASP X 264       -7.40     61.65                                   
REMARK 500    ASN X 266      -43.70    -12.86                                   
REMARK 500    TYR X 268       68.54   -111.27                                   
REMARK 500    GLU X 272     -128.88    -53.66                                   
REMARK 500    HIS X 280      -37.44    -35.88                                   
REMARK 500    GLU X 285       77.65   -112.06                                   
REMARK 500    GLU X 304      -71.29    -43.60                                   
REMARK 500    GLN X 315      108.57    -24.89                                   
REMARK 500    ARG X 332      -52.48    -24.56                                   
REMARK 500    GLN X 333       86.84    -62.78                                   
REMARK 500    SER X 335      101.37    -41.51                                   
REMARK 500    LEU X 340       -6.12    -55.22                                   
REMARK 500    ALA X 353      151.56    -42.76                                   
REMARK 500    ALA Y  14       60.23   -167.87                                   
REMARK 500    SER Y  25       -6.22    -59.58                                   
REMARK 500    SER Y  36      -76.54    -42.13                                   
REMARK 500    PHE Y  68      -84.94    -93.45                                   
REMARK 500    LYS Y  93      -92.38    -37.39                                   
REMARK 500    GLU Y  96       53.93    -92.60                                   
REMARK 500    LYS Y 135        2.72    -63.51                                   
REMARK 500    LYS Y 142        1.34    -59.11                                   
REMARK 500    PRO Y 151      171.97    -53.90                                   
REMARK 500    SER Y 157     -103.99   -166.45                                   
REMARK 500    LYS Y 168       36.06    -87.93                                   
REMARK 500    MET Y 180       -9.27    -56.11                                   
REMARK 500    PHE Y 185        1.60    -63.58                                   
REMARK 500    HIS Y 193        2.01     86.03                                   
REMARK 500    ALA Y 199      -80.71    -63.76                                   
REMARK 500    LYS Y 200       94.95    -37.44                                   
REMARK 500    LYS Y 201       26.91    -66.91                                   
REMARK 500    LEU Y 216        3.67    -59.51                                   
REMARK 500    SER Y 237     -169.73    -79.67                                   
REMARK 500    ARG Y 239      -24.48    -36.95                                   
REMARK 500    VAL Y 247      -70.35    -62.14                                   
REMARK 500    LYS Y 254       36.52    -62.44                                   
REMARK 500    SER Y 255      153.60    174.82                                   
REMARK 500    ARG Y 262      -93.17    -78.57                                   
REMARK 500    ASP Y 264      -11.86   -140.58                                   
REMARK 500    TYR Y 268       66.20   -150.80                                   
REMARK 500    PRO Y 271      163.68    -29.91                                   
REMARK 500    GLU Y 272      -98.60    -58.72                                   
REMARK 500    LEU Y 275       39.68    -98.53                                   
REMARK 500    HIS Y 276       -8.74    -52.20                                   
REMARK 500    LYS Y 277      -65.48    -96.59                                   
REMARK 500    LEU Y 284      -76.46    -93.10                                   
REMARK 500    SER Y 293      -32.62    -38.07                                   
REMARK 500    GLU Y 304      -76.43    -61.01                                   
REMARK 500    GLU Y 305      -37.46    -32.58                                   
REMARK 500    MET Y 310      -85.42   -136.89                                   
REMARK 500    GLN Y 315      112.23     40.50                                   
REMARK 500    PHE Y 316      141.64   -170.91                                   
REMARK 500    SER Y 317      109.25    -26.23                                   
REMARK 500    ILE Y 321       -6.93    -54.80                                   
REMARK 500    SER Y 335       30.69    -90.71                                   
REMARK 500    THR Y 336      -18.27   -140.05                                   
REMARK 500    ASP Y 342      -14.75    -48.99                                   
REMARK 500    LYS Y 356     -159.01    -61.52                                   
REMARK 500    PRO Y 358       78.35    -43.33                                   
REMARK 500    ASP Z  12      -72.00    -76.67                                   
REMARK 500    GLU Z  20       51.62   -117.19                                   
REMARK 500    PHE Z  27      154.67    -49.36                                   
REMARK 500    ALA Z  45      -60.73   -156.91                                   
REMARK 500    VAL Z  46       36.06    -72.07                                   
REMARK 500    ARG Z  47       77.84   -111.57                                   
REMARK 500    ASN Z  55      -75.69    -51.95                                   
REMARK 500    PHE Z  68      -90.47    -58.46                                   
REMARK 500    GLN Z  91       43.90    -70.10                                   
REMARK 500    SER Z  94      161.90    -40.37                                   
REMARK 500    GLU Z  96      -61.87   -163.33                                   
REMARK 500    ALA Z  98       -8.78     67.29                                   
REMARK 500    ARG Z 103       44.04    -91.75                                   
REMARK 500    ARG Z 104       41.45    -96.50                                   
REMARK 500    GLN Z 110      -23.80   -157.17                                   
REMARK 500    GLN Z 112      -65.73     64.19                                   
REMARK 500    PHE Z 126       33.93    -79.29                                   
REMARK 500    VAL Z 131       49.56   -100.85                                   
REMARK 500    VAL Z 133       65.23    -59.58                                   
REMARK 500    LYS Z 135     -125.85     26.92                                   
REMARK 500    SER Z 157     -129.75   -124.74                                   
REMARK 500    LYS Z 171        6.95    -69.79                                   
REMARK 500    ASP Z 181        4.23    -60.98                                   
REMARK 500    SER Z 187      104.86    -33.39                                   
REMARK 500    THR Z 195       17.67    -66.98                                   
REMARK 500    ALA Z 196     -142.39    -57.04                                   
REMARK 500    LYS Z 201       63.15     39.82                                   
REMARK 500    ILE Z 212      -74.17    -73.70                                   
REMARK 500    LEU Z 213      -16.50    -45.30                                   
REMARK 500    GLU Z 215      -31.17   -146.68                                   
REMARK 500    LEU Z 218      176.72    -35.36                                   
REMARK 500    SER Z 232     -148.94    -89.59                                   
REMARK 500    ASP Z 233       10.64   -146.60                                   
REMARK 500    CYS Z 235     -145.70   -130.34                                   
REMARK 500    PRO Z 243     -105.45    -42.60                                   
REMARK 500    ARG Z 245        4.75    -66.39                                   
REMARK 500    ALA Z 246       29.04   -149.18                                   
REMARK 500    HIS Z 253       -0.45     89.01                                   
REMARK 500    LYS Z 254       77.40    -21.09                                   
REMARK 500    SER Z 255      119.14    171.91                                   
REMARK 500    ILE Z 256       12.37    -56.01                                   
REMARK 500    GLU Z 257      -53.26   -121.41                                   
REMARK 500    LEU Z 263       73.56     56.34                                   
REMARK 500    ASP Z 264       97.46   -167.01                                   
REMARK 500    PRO Z 265       20.62    -61.82                                   
REMARK 500    ASN Z 266       -3.22     52.57                                   
REMARK 500    PRO Z 271      154.24    -43.09                                   
REMARK 500    ASN Z 273       52.00     32.44                                   
REMARK 500    PHE Z 283       30.80    -63.93                                   
REMARK 500    LEU Z 284      -35.46   -147.63                                   
REMARK 500    LEU Z 289      176.85    -58.93                                   
REMARK 500    SER Z 293        5.07    -56.62                                   
REMARK 500    LYS Z 297       87.65   -151.06                                   
REMARK 500    SER Z 299     -141.35   -101.97                                   
REMARK 500    GLU Z 303     -110.84     41.63                                   
REMARK 500    LYS Z 308      -73.15    -59.37                                   
REMARK 500    MET Z 310     -101.45    -73.89                                   
REMARK 500    CYS Z 311       93.35    -66.61                                   
REMARK 500    GLN Z 315      121.43    -23.53                                   
REMARK 500    SER Z 317       99.83    -42.57                                   
REMARK 500    LYS Z 330       -4.14    -59.88                                   
REMARK 500    ASP Z 342       13.84    -61.69                                   
REMARK 500    GLN A   8       38.80    -87.78                                   
REMARK 500    LEU A  37      113.81   -163.41                                   
REMARK 500    HIS A  44       14.31     55.34                                   
REMARK 500    ARG A  64      117.63   -172.92                                   
REMARK 500    ASP A  94      -96.61    -51.77                                   
REMARK 500    ASN A 107       80.82    -64.80                                   
REMARK 500    GLN A 108       84.59    -31.20                                   
REMARK 500    GLU A 109      -45.25   -157.16                                   
REMARK 500    SER A 134       39.80    -91.73                                   
REMARK 500    CYS A 135      122.12    166.82                                   
REMARK 500    ALA A 163     -164.70   -108.74                                   
REMARK 500    GLU A 192     -102.17    -53.42                                   
REMARK 500    GLU A 198       71.84   -114.90                                   
REMARK 500    ASN A 200      -63.78    -92.97                                   
REMARK 500    ALA A 231     -102.76    -17.50                                   
REMARK 500    ALA A 242     -139.79     54.47                                   
REMARK 500    ASP A 257      100.68    -58.11                                   
REMARK 500    GLU A 258       11.11   -143.66                                   
REMARK 500    PHE B   2      128.92   -172.35                                   
REMARK 500    SER B  42      -19.28    -45.74                                   
REMARK 500    ARG B  61      102.50    179.09                                   
REMARK 500    ASN B  84      -17.67    -40.85                                   
REMARK 500    ASP B  94      -75.78    -49.84                                   
REMARK 500    ASN B  95       53.56    -93.35                                   
REMARK 500    ASN B 107        2.02    -59.24                                   
REMARK 500    GLN B 108       12.17     50.93                                   
REMARK 500    ASN B 187       52.29    -66.78                                   
REMARK 500    VAL B 188      -96.78     64.32                                   
REMARK 500    ASP B 189      -13.99   -142.71                                   
REMARK 500    GLU B 191     -159.18     81.91                                   
REMARK 500    ALA B 194     -172.54    -32.09                                   
REMARK 500    GLN B 204       90.23   -160.10                                   
REMARK 500    THR B 216       -5.45    -58.74                                   
REMARK 500    PRO B 220       -4.68    -55.08                                   
REMARK 500    ASP B 232       26.14     38.77                                   
REMARK 500    ALA B 242     -127.60     28.17                                   
REMARK 500    PRO B 253     -171.02    -64.61                                   
REMARK 500    ILE B 255       89.25    -64.21                                   
REMARK 500    GLU B 256       59.60    -68.46                                   
REMARK 500    GLN C   8       71.84   -106.72                                   
REMARK 500    LYS C  20      -45.70    -26.14                                   
REMARK 500    SER C  31      170.79    165.21                                   
REMARK 500    LEU C  37      119.05   -162.94                                   
REMARK 500    SER C  39      155.76    179.90                                   
REMARK 500    ASP C  63      -67.11   -104.43                                   
REMARK 500    ASN C  84      -15.96    -48.04                                   
REMARK 500    ASN C 107       26.12    -79.74                                   
REMARK 500    GLN C 108      -36.36     32.90                                   
REMARK 500    LEU C 175       52.86   -117.30                                   
REMARK 500    THR C 185       76.45    -67.86                                   
REMARK 500    SER C 186      -74.93    -81.47                                   
REMARK 500    VAL C 188       38.32    -69.00                                   
REMARK 500    ASP C 189      102.22    -59.23                                   
REMARK 500    LYS C 190       59.39   -144.35                                   
REMARK 500    GLU C 191      -89.11     38.83                                   
REMARK 500    GLU C 192      -72.22    -57.96                                   
REMARK 500    GLU C 193       38.27    -66.04                                   
REMARK 500    ASN C 200      -84.20   -100.66                                   
REMARK 500    GLN C 204      110.91    179.10                                   
REMARK 500    ASN C 213       12.46    -68.50                                   
REMARK 500    LYS C 217       -5.82    -58.81                                   
REMARK 500    ASP C 232       -5.34     68.49                                   
REMARK 500    ALA C 242     -134.16     36.75                                   
REMARK 500    PRO C 253      176.69    -55.27                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG X1002  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU X 158   OE1                                                    
REMARK 620 2 GLU X 160   OE1  87.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG Y1004  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP Y 181   OD1                                                    
REMARK 620 2 GLU Y 160   OE2  78.2                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 1001                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 1002                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Y 1003                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Y 1004                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1B43   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1A76   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1AXC   RELATED DB: PDB                                   
DBREF  1UL1 X    2   380  UNP    P39748   FEN1_HUMAN       2    380             
DBREF  1UL1 Y    2   380  UNP    P39748   FEN1_HUMAN       2    380             
DBREF  1UL1 Z    2   380  UNP    P39748   FEN1_HUMAN       2    380             
DBREF  1UL1 A    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  1UL1 B    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  1UL1 C    1   261  UNP    P12004   PCNA_HUMAN       1    261             
SEQRES   1 X  379  GLY ILE GLN GLY LEU ALA LYS LEU ILE ALA ASP VAL ALA          
SEQRES   2 X  379  PRO SER ALA ILE ARG GLU ASN ASP ILE LYS SER TYR PHE          
SEQRES   3 X  379  GLY ARG LYS VAL ALA ILE ASP ALA SER MET SER ILE TYR          
SEQRES   4 X  379  GLN PHE LEU ILE ALA VAL ARG GLN GLY GLY ASP VAL LEU          
SEQRES   5 X  379  GLN ASN GLU GLU GLY GLU THR THR SER HIS LEU MET GLY          
SEQRES   6 X  379  MET PHE TYR ARG THR ILE ARG MET MET GLU ASN GLY ILE          
SEQRES   7 X  379  LYS PRO VAL TYR VAL PHE ASP GLY LYS PRO PRO GLN LEU          
SEQRES   8 X  379  LYS SER GLY GLU LEU ALA LYS ARG SER GLU ARG ARG ALA          
SEQRES   9 X  379  GLU ALA GLU LYS GLN LEU GLN GLN ALA GLN ALA ALA GLY          
SEQRES  10 X  379  ALA GLU GLN GLU VAL GLU LYS PHE THR LYS ARG LEU VAL          
SEQRES  11 X  379  LYS VAL THR LYS GLN HIS ASN ASP GLU CYS LYS HIS LEU          
SEQRES  12 X  379  LEU SER LEU MET GLY ILE PRO TYR LEU ASP ALA PRO SER          
SEQRES  13 X  379  GLU ALA GLU ALA SER CYS ALA ALA LEU VAL LYS ALA GLY          
SEQRES  14 X  379  LYS VAL TYR ALA ALA ALA THR GLU ASP MET ASP CYS LEU          
SEQRES  15 X  379  THR PHE GLY SER PRO VAL LEU MET ARG HIS LEU THR ALA          
SEQRES  16 X  379  SER GLU ALA LYS LYS LEU PRO ILE GLN GLU PHE HIS LEU          
SEQRES  17 X  379  SER ARG ILE LEU GLN GLU LEU GLY LEU ASN GLN GLU GLN          
SEQRES  18 X  379  PHE VAL ASP LEU CYS ILE LEU LEU GLY SER ASP TYR CYS          
SEQRES  19 X  379  GLU SER ILE ARG GLY ILE GLY PRO LYS ARG ALA VAL ASP          
SEQRES  20 X  379  LEU ILE GLN LYS HIS LYS SER ILE GLU GLU ILE VAL ARG          
SEQRES  21 X  379  ARG LEU ASP PRO ASN LYS TYR PRO VAL PRO GLU ASN TRP          
SEQRES  22 X  379  LEU HIS LYS GLU ALA HIS GLN LEU PHE LEU GLU PRO GLU          
SEQRES  23 X  379  VAL LEU ASP PRO GLU SER VAL GLU LEU LYS TRP SER GLU          
SEQRES  24 X  379  PRO ASN GLU GLU GLU LEU ILE LYS PHE MET CYS GLY GLU          
SEQRES  25 X  379  LYS GLN PHE SER GLU GLU ARG ILE ARG SER GLY VAL LYS          
SEQRES  26 X  379  ARG LEU SER LYS SER ARG GLN GLY SER THR GLN GLY ARG          
SEQRES  27 X  379  LEU ASP ASP PHE PHE LYS VAL THR GLY SER LEU SER SER          
SEQRES  28 X  379  ALA LYS ARG LYS GLU PRO GLU PRO LYS GLY SER THR LYS          
SEQRES  29 X  379  LYS LYS ALA LYS THR GLY ALA ALA GLY LYS PHE LYS ARG          
SEQRES  30 X  379  GLY LYS                                                      
SEQRES   1 Y  379  GLY ILE GLN GLY LEU ALA LYS LEU ILE ALA ASP VAL ALA          
SEQRES   2 Y  379  PRO SER ALA ILE ARG GLU ASN ASP ILE LYS SER TYR PHE          
SEQRES   3 Y  379  GLY ARG LYS VAL ALA ILE ASP ALA SER MET SER ILE TYR          
SEQRES   4 Y  379  GLN PHE LEU ILE ALA VAL ARG GLN GLY GLY ASP VAL LEU          
SEQRES   5 Y  379  GLN ASN GLU GLU GLY GLU THR THR SER HIS LEU MET GLY          
SEQRES   6 Y  379  MET PHE TYR ARG THR ILE ARG MET MET GLU ASN GLY ILE          
SEQRES   7 Y  379  LYS PRO VAL TYR VAL PHE ASP GLY LYS PRO PRO GLN LEU          
SEQRES   8 Y  379  LYS SER GLY GLU LEU ALA LYS ARG SER GLU ARG ARG ALA          
SEQRES   9 Y  379  GLU ALA GLU LYS GLN LEU GLN GLN ALA GLN ALA ALA GLY          
SEQRES  10 Y  379  ALA GLU GLN GLU VAL GLU LYS PHE THR LYS ARG LEU VAL          
SEQRES  11 Y  379  LYS VAL THR LYS GLN HIS ASN ASP GLU CYS LYS HIS LEU          
SEQRES  12 Y  379  LEU SER LEU MET GLY ILE PRO TYR LEU ASP ALA PRO SER          
SEQRES  13 Y  379  GLU ALA GLU ALA SER CYS ALA ALA LEU VAL LYS ALA GLY          
SEQRES  14 Y  379  LYS VAL TYR ALA ALA ALA THR GLU ASP MET ASP CYS LEU          
SEQRES  15 Y  379  THR PHE GLY SER PRO VAL LEU MET ARG HIS LEU THR ALA          
SEQRES  16 Y  379  SER GLU ALA LYS LYS LEU PRO ILE GLN GLU PHE HIS LEU          
SEQRES  17 Y  379  SER ARG ILE LEU GLN GLU LEU GLY LEU ASN GLN GLU GLN          
SEQRES  18 Y  379  PHE VAL ASP LEU CYS ILE LEU LEU GLY SER ASP TYR CYS          
SEQRES  19 Y  379  GLU SER ILE ARG GLY ILE GLY PRO LYS ARG ALA VAL ASP          
SEQRES  20 Y  379  LEU ILE GLN LYS HIS LYS SER ILE GLU GLU ILE VAL ARG          
SEQRES  21 Y  379  ARG LEU ASP PRO ASN LYS TYR PRO VAL PRO GLU ASN TRP          
SEQRES  22 Y  379  LEU HIS LYS GLU ALA HIS GLN LEU PHE LEU GLU PRO GLU          
SEQRES  23 Y  379  VAL LEU ASP PRO GLU SER VAL GLU LEU LYS TRP SER GLU          
SEQRES  24 Y  379  PRO ASN GLU GLU GLU LEU ILE LYS PHE MET CYS GLY GLU          
SEQRES  25 Y  379  LYS GLN PHE SER GLU GLU ARG ILE ARG SER GLY VAL LYS          
SEQRES  26 Y  379  ARG LEU SER LYS SER ARG GLN GLY SER THR GLN GLY ARG          
SEQRES  27 Y  379  LEU ASP ASP PHE PHE LYS VAL THR GLY SER LEU SER SER          
SEQRES  28 Y  379  ALA LYS ARG LYS GLU PRO GLU PRO LYS GLY SER THR LYS          
SEQRES  29 Y  379  LYS LYS ALA LYS THR GLY ALA ALA GLY LYS PHE LYS ARG          
SEQRES  30 Y  379  GLY LYS                                                      
SEQRES   1 Z  379  GLY ILE GLN GLY LEU ALA LYS LEU ILE ALA ASP VAL ALA          
SEQRES   2 Z  379  PRO SER ALA ILE ARG GLU ASN ASP ILE LYS SER TYR PHE          
SEQRES   3 Z  379  GLY ARG LYS VAL ALA ILE ASP ALA SER MET SER ILE TYR          
SEQRES   4 Z  379  GLN PHE LEU ILE ALA VAL ARG GLN GLY GLY ASP VAL LEU          
SEQRES   5 Z  379  GLN ASN GLU GLU GLY GLU THR THR SER HIS LEU MET GLY          
SEQRES   6 Z  379  MET PHE TYR ARG THR ILE ARG MET MET GLU ASN GLY ILE          
SEQRES   7 Z  379  LYS PRO VAL TYR VAL PHE ASP GLY LYS PRO PRO GLN LEU          
SEQRES   8 Z  379  LYS SER GLY GLU LEU ALA LYS ARG SER GLU ARG ARG ALA          
SEQRES   9 Z  379  GLU ALA GLU LYS GLN LEU GLN GLN ALA GLN ALA ALA GLY          
SEQRES  10 Z  379  ALA GLU GLN GLU VAL GLU LYS PHE THR LYS ARG LEU VAL          
SEQRES  11 Z  379  LYS VAL THR LYS GLN HIS ASN ASP GLU CYS LYS HIS LEU          
SEQRES  12 Z  379  LEU SER LEU MET GLY ILE PRO TYR LEU ASP ALA PRO SER          
SEQRES  13 Z  379  GLU ALA GLU ALA SER CYS ALA ALA LEU VAL LYS ALA GLY          
SEQRES  14 Z  379  LYS VAL TYR ALA ALA ALA THR GLU ASP MET ASP CYS LEU          
SEQRES  15 Z  379  THR PHE GLY SER PRO VAL LEU MET ARG HIS LEU THR ALA          
SEQRES  16 Z  379  SER GLU ALA LYS LYS LEU PRO ILE GLN GLU PHE HIS LEU          
SEQRES  17 Z  379  SER ARG ILE LEU GLN GLU LEU GLY LEU ASN GLN GLU GLN          
SEQRES  18 Z  379  PHE VAL ASP LEU CYS ILE LEU LEU GLY SER ASP TYR CYS          
SEQRES  19 Z  379  GLU SER ILE ARG GLY ILE GLY PRO LYS ARG ALA VAL ASP          
SEQRES  20 Z  379  LEU ILE GLN LYS HIS LYS SER ILE GLU GLU ILE VAL ARG          
SEQRES  21 Z  379  ARG LEU ASP PRO ASN LYS TYR PRO VAL PRO GLU ASN TRP          
SEQRES  22 Z  379  LEU HIS LYS GLU ALA HIS GLN LEU PHE LEU GLU PRO GLU          
SEQRES  23 Z  379  VAL LEU ASP PRO GLU SER VAL GLU LEU LYS TRP SER GLU          
SEQRES  24 Z  379  PRO ASN GLU GLU GLU LEU ILE LYS PHE MET CYS GLY GLU          
SEQRES  25 Z  379  LYS GLN PHE SER GLU GLU ARG ILE ARG SER GLY VAL LYS          
SEQRES  26 Z  379  ARG LEU SER LYS SER ARG GLN GLY SER THR GLN GLY ARG          
SEQRES  27 Z  379  LEU ASP ASP PHE PHE LYS VAL THR GLY SER LEU SER SER          
SEQRES  28 Z  379  ALA LYS ARG LYS GLU PRO GLU PRO LYS GLY SER THR LYS          
SEQRES  29 Z  379  LYS LYS ALA LYS THR GLY ALA ALA GLY LYS PHE LYS ARG          
SEQRES  30 Z  379  GLY LYS                                                      
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 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 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                                                          
HET     MG  X1001       1                                                       
HET     MG  X1002       1                                                       
HET     MG  Y1003       1                                                       
HET     MG  Y1004       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   7   MG    4(MG 2+)                                                     
FORMUL  11  HOH   *(H2 O)                                                       
HELIX    1   1 GLY X    5  ASP X   12  1                                   8    
HELIX    2   2 ASP X   22  PHE X   27  5                                   6    
HELIX    3   3 ALA X   35  ILE X   44  1                                  10    
HELIX    4   4 THR X   61  ASN X   77  1                                  17    
HELIX    5   5 HIS X  137  GLY X  149  1                                  13    
HELIX    6   6 GLU X  158  GLY X  170  1                                  13    
HELIX    7   7 MET X  180  PHE X  185  1                                   6    
HELIX    8   8 LEU X  209  GLY X  217  1                                   9    
HELIX    9   9 ASN X  219  SER X  232  1                                  14    
HELIX   10  10 GLY X  242  HIS X  253  1                                  12    
HELIX   11  11 SER X  255  ARG X  261  1                                   7    
HELIX   12  12 LEU X  275  GLU X  285  1                                  11    
HELIX   13  13 ASP X  290  VAL X  294  5                                   5    
HELIX   14  14 ASN X  302  MET X  310  1                                   9    
HELIX   15  15 SER X  317  GLN X  333  1                                  17    
HELIX   16  16 ARG X  339  PHE X  344  1                                   6    
HELIX   17  17 GLY Y    5  ALA Y   14  1                                  10    
HELIX   18  18 ASP Y   22  PHE Y   27  5                                   6    
HELIX   19  19 ALA Y   35  ILE Y   44  1                                  10    
HELIX   20  20 THR Y   61  ASN Y   77  1                                  17    
HELIX   21  21 SER Y   94  SER Y  101  5                                   8    
HELIX   22  22 LYS Y  135  GLU Y  140  1                                   6    
HELIX   23  23 GLU Y  140  LEU Y  145  1                                   6    
HELIX   24  24 GLU Y  158  LYS Y  168  1                                  11    
HELIX   25  25 MET Y  180  PHE Y  185  1                                   6    
HELIX   26  26 LEU Y  209  LEU Y  216  1                                   8    
HELIX   27  27 ASN Y  219  SER Y  232  1                                  14    
HELIX   28  28 GLY Y  242  HIS Y  253  1                                  12    
HELIX   29  29 SER Y  255  LEU Y  263  1                                   9    
HELIX   30  30 LYS Y  277  PHE Y  283  1                                   7    
HELIX   31  31 ASN Y  302  LYS Y  308  1                                   7    
HELIX   32  32 SER Y  317  ARG Y  332  1                                  16    
HELIX   33  33 GLY Z    5  ALA Z   14  1                                  10    
HELIX   34  34 ASP Z   22  PHE Z   27  5                                   6    
HELIX   35  35 ALA Z   35  ILE Z   44  1                                  10    
HELIX   36  36 THR Z   61  GLU Z   76  1                                  16    
HELIX   37  37 LYS Z   93  LEU Z   97  5                                   5    
HELIX   38  38 ARG Z  104  LYS Z  109  1                                   6    
HELIX   39  39 HIS Z  137  GLY Z  149  1                                  13    
HELIX   40  40 GLU Z  158  ALA Z  169  1                                  12    
HELIX   41  41 ASP Z  179  LEU Z  183  5                                   5    
HELIX   42  42 LEU Z  209  GLY Z  217  1                                   9    
HELIX   43  43 ASN Z  219  SER Z  232  1                                  14    
HELIX   44  44 PRO Z  243  VAL Z  247  5                                   5    
HELIX   45  45 LEU Z  275  PHE Z  283  1                                   9    
HELIX   46  46 GLU Z  303  MET Z  310  1                                   8    
HELIX   47  47 SER Z  317  LYS Z  330  1                                  14    
HELIX   48  48 GLY A    9  ALA A   18  1                                  10    
HELIX   49  49 GLU A   55  PHE A   57  5                                   3    
HELIX   50  50 LEU A   72  LYS A   80  1                                   9    
HELIX   51  51 SER A  141  GLY A  155  1                                  15    
HELIX   52  52 LEU A  209  THR A  216  1                                   8    
HELIX   53  53 LYS A  217  SER A  222  5                                   6    
HELIX   54  54 GLY B    9  ASP B   21  1                                  13    
HELIX   55  55 ASN B   71  LYS B   80  1                                  10    
HELIX   56  56 SER B  141  SER B  152  1                                  12    
HELIX   57  57 LEU B  209  THR B  216  1                                   8    
HELIX   58  58 LYS B  217  SER B  222  5                                   6    
HELIX   59  59 GLY C    9  ASP C   21  1                                  13    
HELIX   60  60 GLU C   55  PHE C   57  5                                   3    
HELIX   61  61 ASN C   71  CYS C   81  1                                  11    
HELIX   62  62 SER C  141  SER C  152  1                                  12    
HELIX   63  63 LYS C  190  ALA C  194  5                                   5    
HELIX   64  64 LEU C  209  THR C  216  1                                   8    
HELIX   65  65 LYS C  217  SER C  222  5                                   6    
SHEET    1   A 7 GLU X  20  ASN X  21  0                                        
SHEET    2   A 7 ILE X 204  HIS X 208 -1  O  ILE X 204   N  ASN X  21           
SHEET    3   A 7 VAL X 189  ARG X 192 -1  N  ARG X 192   O  GLN X 205           
SHEET    4   A 7 ALA X 174  ALA X 176  1  N  ALA X 175   O  MET X 191           
SHEET    5   A 7 VAL X  31  ASP X  34  1  N  ALA X  32   O  ALA X 176           
SHEET    6   A 7 PRO X  81  PHE X  85  1  O  VAL X  84   N  ILE X  33           
SHEET    7   A 7 TYR X 152  ASP X 154  1  O  LEU X 153   N  PHE X  85           
SHEET    1   B 2 LYS X 345  SER X 351  0                                        
SHEET    2   B 2 ASP A 122  GLY A 127 -1  O  VAL A 123   N  LEU X 350           
SHEET    1   C 7 ILE Y  18  ASN Y  21  0                                        
SHEET    2   C 7 ILE Y 204  HIS Y 208 -1  O  GLU Y 206   N  ARG Y  19           
SHEET    3   C 7 VAL Y 189  ARG Y 192 -1  N  ARG Y 192   O  GLN Y 205           
SHEET    4   C 7 ALA Y 174  ALA Y 176  1  N  ALA Y 175   O  MET Y 191           
SHEET    5   C 7 LYS Y  30  ASP Y  34  1  N  ALA Y  32   O  ALA Y 176           
SHEET    6   C 7 LYS Y  80  PHE Y  85  1  O  VAL Y  82   N  ILE Y  33           
SHEET    7   C 7 TYR Y 152  ASP Y 154  1  O  LEU Y 153   N  PHE Y  85           
SHEET    1   D 2 GLY Y 348  SER Y 351  0                                        
SHEET    2   D 2 ASP B 122  GLN B 125 -1  O  VAL B 123   N  LEU Y 350           
SHEET    1   E 7 ILE Z  18  ARG Z  19  0                                        
SHEET    2   E 7 GLN Z 205  HIS Z 208 -1  O  GLU Z 206   N  ARG Z  19           
SHEET    3   E 7 VAL Z 189  ARG Z 192 -1  N  LEU Z 190   O  PHE Z 207           
SHEET    4   E 7 ALA Z 174  ALA Z 176  1  N  ALA Z 175   O  MET Z 191           
SHEET    5   E 7 LYS Z  30  ASP Z  34  1  N  ALA Z  32   O  ALA Z 176           
SHEET    6   E 7 LYS Z  80  PHE Z  85  1  O  VAL Z  84   N  ILE Z  33           
SHEET    7   E 7 TYR Z 152  ASP Z 154  1  O  LEU Z 153   N  PHE Z  85           
SHEET    1   F 2 SER Z 349  SER Z 351  0                                        
SHEET    2   F 2 ASP C 122  GLU C 124 -1  O  VAL C 123   N  LEU Z 350           
SHEET    1   G 9 THR A  59  CYS A  62  0                                        
SHEET    2   G 9 PHE A   2  LEU A   6 -1  N  ARG A   5   O  THR A  59           
SHEET    3   G 9 ILE A  87  ALA A  92 -1  O  ILE A  88   N  LEU A   6           
SHEET    4   G 9 THR A  98  GLU A 104 -1  O  VAL A 102   N  THR A  89           
SHEET    5   G 9 LYS A 110  LYS A 117 -1  O  SER A 112   N  PHE A 103           
SHEET    6   G 9 GLY B 176  SER B 183 -1  O  ASN B 179   N  ASP A 113           
SHEET    7   G 9 GLY B 166  GLY B 173 -1  N  GLY B 173   O  GLY B 176           
SHEET    8   G 9 ALA B 157  SER B 161 -1  N  VAL B 159   O  SER B 170           
SHEET    9   G 9 GLN B 204  ALA B 208 -1  O  PHE B 207   N  VAL B 158           
SHEET    1   H 9 LEU A  66  ASN A  71  0                                        
SHEET    2   H 9 GLU A  25  ILE A  30 -1  N  ALA A  26   O  VAL A  70           
SHEET    3   H 9 GLY A  34  MET A  40 -1  O  ASN A  36   N  ASP A  29           
SHEET    4   H 9 SER A  46  ARG A  53 -1  O  LEU A  50   N  LEU A  37           
SHEET    5   H 9 GLY A 245  LEU A 251 -1  O  TYR A 250   N  LEU A  47           
SHEET    6   H 9 LEU A 235  ILE A 241 -1  N  LEU A 235   O  LEU A 251           
SHEET    7   H 9 THR A 224  SER A 228 -1  N  SER A 228   O  VAL A 236           
SHEET    8   H 9 VAL A 136  PRO A 140 -1  N  MET A 139   O  VAL A 225           
SHEET    9   H 9 THR A 196  ILE A 197 -1  O  THR A 196   N  LYS A 138           
SHEET    1   I 9 VAL A 203  ALA A 208  0                                        
SHEET    2   I 9 ALA A 157  CYS A 162 -1  N  VAL A 158   O  PHE A 207           
SHEET    3   I 9 GLY A 166  GLY A 173 -1  O  SER A 170   N  VAL A 159           
SHEET    4   I 9 GLY A 176  SER A 183 -1  O  GLY A 176   N  GLY A 173           
SHEET    5   I 9 LYS C 110  LYS C 117 -1  O  GLU C 115   N  ASN A 177           
SHEET    6   I 9 THR C  98  GLU C 104 -1  N  LEU C  99   O  MET C 116           
SHEET    7   I 9 ILE C  87  ALA C  92 -1  N  ILE C  87   O  GLU C 104           
SHEET    8   I 9 PHE C   2  LEU C   6 -1  N  LEU C   6   O  ILE C  88           
SHEET    9   I 9 THR C  59  CYS C  62 -1  O  THR C  59   N  ARG C   5           
SHEET    1   J 6 PHE B   2  LEU B   6  0                                        
SHEET    2   J 6 ILE B  88  ALA B  92 -1  O  ALA B  92   N  PHE B   2           
SHEET    3   J 6 THR B  98  LEU B 101 -1  O  ALA B 100   N  ARG B  91           
SHEET    4   J 6 LYS B 110  LYS B 117 -1  O  MET B 116   N  LEU B  99           
SHEET    5   J 6 GLY C 176  SER C 183 -1  O  ASN C 177   N  GLU B 115           
SHEET    6   J 6 GLY C 166  GLY C 173 -1  N  PHE C 169   O  ILE C 180           
SHEET    1   K 9 LEU B  66  VAL B  70  0                                        
SHEET    2   K 9 ALA B  26  ILE B  30 -1  N  ALA B  26   O  VAL B  70           
SHEET    3   K 9 GLY B  34  MET B  40 -1  O  ASN B  36   N  ASP B  29           
SHEET    4   K 9 SER B  46  ARG B  53 -1  O  LEU B  52   N  VAL B  35           
SHEET    5   K 9 GLY B 245  LEU B 251 -1  O  LYS B 248   N  GLN B  49           
SHEET    6   K 9 LEU B 235  ILE B 241 -1  N  TYR B 239   O  LEU B 247           
SHEET    7   K 9 THR B 224  MET B 229 -1  N  SER B 228   O  VAL B 236           
SHEET    8   K 9 CYS B 135  PRO B 140 -1  N  CYS B 135   O  MET B 229           
SHEET    9   K 9 THR B 196  MET B 199 -1  O  GLU B 198   N  VAL B 136           
SHEET    1   L 9 ALA C  67  VAL C  70  0                                        
SHEET    2   L 9 ALA C  26  ASP C  29 -1  N  TRP C  28   O  MET C  68           
SHEET    3   L 9 GLY C  34  MET C  40 -1  O  ASN C  36   N  ASP C  29           
SHEET    4   L 9 SER C  46  ARG C  53 -1  O  LEU C  52   N  VAL C  35           
SHEET    5   L 9 GLY C 245  LEU C 251 -1  O  LYS C 248   N  GLN C  49           
SHEET    6   L 9 LEU C 235  ILE C 241 -1  N  VAL C 237   O  TYR C 249           
SHEET    7   L 9 THR C 224  MET C 229 -1  N  THR C 226   O  GLU C 238           
SHEET    8   L 9 CYS C 135  PRO C 140 -1  N  VAL C 137   O  LEU C 227           
SHEET    9   L 9 THR C 196  MET C 199 -1  O  THR C 196   N  LYS C 138           
SHEET    1   M 2 ALA C 157  ILE C 160  0                                        
SHEET    2   M 2 LEU C 205  ALA C 208 -1  O  LEU C 205   N  ILE C 160           
SSBOND   1 CYS B  135    CYS B  162                          1555   1555  2.04  
LINK        MG    MG X1001                 OE2 GLU X 160     1555   1555  3.06  
LINK        MG    MG X1002                 OE1 GLU X 158     1555   1555  3.00  
LINK        MG    MG X1002                 OE1 GLU X 160     1555   1555  2.58  
LINK        MG    MG Y1004                 OD1 ASP Y 181     1555   1555  2.97  
LINK        MG    MG Y1004                 OE2 GLU Y 160     1555   1555  3.10  
SITE     1 AC1  5 ASP X  34  ASP X  86  GLU X 158  GLU X 160                    
SITE     2 AC1  5  MG X1002                                                     
SITE     1 AC2  5 GLU X 158  GLU X 160  ASP X 181  TYR X 234                    
SITE     2 AC2  5  MG X1001                                                     
SITE     1 AC3  2 GLU Y 158   MG Y1004                                          
SITE     1 AC4  4 GLU Y 160  ASP Y 181  ASP Y 233   MG Y1003                    
CRYST1   82.203  143.383  246.659  90.00  90.00  90.00 P 21 21 21   12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012165  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006974  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004054        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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