GenomeNet

Database: PDB
Entry: 5MLW
LinkDB: 5MLW
Original site: 5MLW 
HEADER    HYDROLASE                               07-DEC-16   5MLW              
TITLE     CRYSTAL STRUCTURE OF HUMAN PCNA IN COMPLEX WITH ZRANB3 APIM MOTIF     
TITLE    2 PEPTIDE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;                        
COMPND   3 CHAIN: A, C, E;                                                      
COMPND   4 SYNONYM: PCNA,CYCLIN;                                                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: APIM MOTIF PEPTIDE;                                        
COMPND   8 CHAIN: B, D, F;                                                      
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PCNA;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    ENDONUCLEASE, METALLOPROTEIN, PCNA, DNA-BINDING, HYDROLASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.ARIZA                                                               
REVDAT   1   28-JUN-17 5MLW    0                                                
JRNL        AUTH   M.SEBESTA,C.D.O.COOPER,A.ARIZA,C.J.CARNIE,D.AHEL             
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE FUNCTION OF ZRANB3 IN           
JRNL        TITL 2 REPLICATION STRESS RESPONSE.                                 
JRNL        REF    NAT COMMUN                    V.   8 15847 2017              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   28621305                                                     
JRNL        DOI    10.1038/NCOMMS15847                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 73.29                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 30026                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1605                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.51                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2178                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.96                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3050                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 135                          
REMARK   3   BIN FREE R VALUE                    : 0.3630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6055                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 96                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 66.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.44000                                              
REMARK   3    B22 (A**2) : 2.44000                                              
REMARK   3    B33 (A**2) : -7.92000                                             
REMARK   3    B12 (A**2) : 1.22000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.645         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.303         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.280         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.410        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6346 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  6159 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8605 ; 1.420 ; 1.987       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 14257 ; 0.995 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   830 ; 8.362 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   276 ;46.319 ;25.580       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1196 ;18.096 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;20.167 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1021 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7129 ; 0.012 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1312 ; 0.008 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3198 ; 3.491 ; 2.561       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3197 ; 3.489 ; 2.559       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3996 ; 5.711 ; 3.805       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3997 ; 5.712 ; 3.807       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3148 ; 3.952 ; 3.049       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3121 ; 3.627 ; 2.994       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4543 ; 5.944 ; 4.305       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6509 ;10.599 ;19.294       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  6492 ;10.529 ;19.187       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 4                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     1    255       C     1    255   29742  0.07  0.05     
REMARK   3    2     A     1    255       E     1    255   29810  0.09  0.05     
REMARK   3    3     B  1069   1079       D  1069   1079     974  0.17  0.05     
REMARK   3    4     C     1    255       E     1    255   29486  0.09  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   255                          
REMARK   3    RESIDUE RANGE :   B  1069        B  1079                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.2440 -18.8240  19.6320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2897 T22:   0.1452                                     
REMARK   3      T33:   0.8985 T12:   0.0551                                     
REMARK   3      T13:   0.0513 T23:   0.0648                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7665 L22:   1.0243                                     
REMARK   3      L33:   0.1834 L12:   0.6758                                     
REMARK   3      L13:  -0.3110 L23:  -0.2299                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0117 S12:   0.0426 S13:  -0.2412                       
REMARK   3      S21:   0.0313 S22:  -0.0644 S23:  -0.1170                       
REMARK   3      S31:   0.0190 S32:   0.0888 S33:   0.0760                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   255                          
REMARK   3    RESIDUE RANGE :   D  1069        D  1079                          
REMARK   3    ORIGIN FOR THE GROUP (A): -58.4330   5.7510  15.3680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2218 T22:   0.2457                                     
REMARK   3      T33:   0.8632 T12:   0.0445                                     
REMARK   3      T13:   0.0621 T23:   0.0437                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8417 L22:   2.4147                                     
REMARK   3      L33:   0.0239 L12:   0.0177                                     
REMARK   3      L13:  -0.0861 L23:   0.0479                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0112 S12:   0.0111 S13:   0.0295                       
REMARK   3      S21:   0.0398 S22:   0.0987 S23:   0.2484                       
REMARK   3      S31:   0.0265 S32:   0.0131 S33:  -0.0875                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E   256                          
REMARK   3    RESIDUE RANGE :   F  1069        F  1078                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.6770  25.5750  16.8140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1007 T22:   0.4439                                     
REMARK   3      T33:   0.8696 T12:  -0.1084                                     
REMARK   3      T13:   0.0972 T23:   0.0111                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3587 L22:   1.3842                                     
REMARK   3      L33:   0.4022 L12:  -0.6080                                     
REMARK   3      L13:   0.7009 L23:  -0.6472                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3931 S12:  -0.2362 S13:  -0.0279                       
REMARK   3      S21:  -0.0929 S22:  -0.3199 S23:  -0.0837                       
REMARK   3      S31:   0.1062 S32:   0.0407 S33:  -0.0732                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5MLW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-DEC-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200002662.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2822                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31686                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 73.290                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.20                              
REMARK 200  R MERGE                    (I) : 0.10400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.29700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1VYM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM LITHIUM SULFATE + 30% (W/V)       
REMARK 280  POLYVINYLPYRROLIDONE + 100 MM HEPES PH 7.0, VAPOR DIFFUSION,        
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.25667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      134.51333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      134.51333            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       67.25667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASN A   187                                                      
REMARK 465     VAL A   188                                                      
REMARK 465     GLU A   256                                                      
REMARK 465     ASP A   257                                                      
REMARK 465     GLU A   258                                                      
REMARK 465     GLU A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     SER A   261                                                      
REMARK 465     SER C   186                                                      
REMARK 465     ASN C   187                                                      
REMARK 465     VAL C   188                                                      
REMARK 465     ASP C   189                                                      
REMARK 465     LYS C   190                                                      
REMARK 465     GLU C   191                                                      
REMARK 465     GLU C   192                                                      
REMARK 465     GLU C   256                                                      
REMARK 465     ASP C   257                                                      
REMARK 465     GLU C   258                                                      
REMARK 465     GLU C   259                                                      
REMARK 465     GLY C   260                                                      
REMARK 465     SER C   261                                                      
REMARK 465     LYS E   190                                                      
REMARK 465     GLU E   191                                                      
REMARK 465     GLU E   192                                                      
REMARK 465     ASP E   257                                                      
REMARK 465     GLU E   258                                                      
REMARK 465     GLU E   259                                                      
REMARK 465     GLY E   260                                                      
REMARK 465     SER E   261                                                      
REMARK 465     LYS F  1079                                                      
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   OE1  GLU C     3     NH1  ARG C    91              2.15            
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 A 108      -12.93     78.75                                   
REMARK 500    ASP A 122       47.26    -98.73                                   
REMARK 500    ALA A 163     -160.01   -106.72                                   
REMARK 500    MET A 244      -46.73   -146.75                                   
REMARK 500    GLN C 108      -13.61     79.76                                   
REMARK 500    ASP C 122       48.00    -98.18                                   
REMARK 500    ALA C 163     -159.87   -106.41                                   
REMARK 500    MET C 244      -45.86   -146.60                                   
REMARK 500    ASP D1071      115.89   -163.87                                   
REMARK 500    ARG D1074      -25.67    -39.56                                   
REMARK 500    GLN E   8       76.17   -100.76                                   
REMARK 500    GLN E 108      -13.23     79.83                                   
REMARK 500    ASP E 122       47.62    -98.73                                   
REMARK 500    GLU E 124       99.44    -69.96                                   
REMARK 500    ALA E 163     -159.91   -108.53                                   
REMARK 500    ASN E 187       77.08   -110.72                                   
REMARK 500    MET E 244      -49.61   -142.30                                   
REMARK 500    ASP F1071      119.89   -166.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN C   95     ALA C   96                 -130.11                    
REMARK 500 ALA E   96     ASP E   97                  148.09                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 303                 
DBREF  5MLW A    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  5MLW B 1069  1079  PDB    5MLW     5MLW          1069   1079             
DBREF  5MLW C    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  5MLW D 1069  1079  PDB    5MLW     5MLW          1069   1079             
DBREF  5MLW E    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  5MLW F 1069  1079  PDB    5MLW     5MLW          1069   1079             
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   11  GLY SER ASP ILE THR ARG PHE LEU VAL LYS LYS                  
SEQRES   1 C  261  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 C  261  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 C  261  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 C  261  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 C  261  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 C  261  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 C  261  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 C  261  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 C  261  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 C  261  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 C  261  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 C  261  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 C  261  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 C  261  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 C  261  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 C  261  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 C  261  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 C  261  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 C  261  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 C  261  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 C  261  SER                                                          
SEQRES   1 D   11  GLY SER ASP ILE THR ARG PHE LEU VAL LYS LYS                  
SEQRES   1 E  261  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 E  261  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 E  261  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 E  261  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 E  261  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 E  261  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 E  261  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 E  261  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 E  261  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 E  261  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 E  261  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 E  261  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 E  261  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 E  261  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 E  261  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 E  261  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 E  261  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 E  261  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 E  261  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 E  261  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 E  261  SER                                                          
SEQRES   1 F   11  GLY SER ASP ILE THR ARG PHE LEU VAL LYS LYS                  
HET    SO4  A 301       5                                                       
HET    SO4  A 302       5                                                       
HET    SO4  C 301       5                                                       
HET    SO4  C 302       5                                                       
HET    SO4  E 301       5                                                       
HET    SO4  E 302       5                                                       
HET    SO4  E 303       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   7  SO4    7(O4 S 2-)                                                   
FORMUL  14  HOH   *96(H2 O)                                                     
HELIX    1 AA1 GLY A    9  ASP A   21  1                                  13    
HELIX    2 AA2 GLU A   55  PHE A   57  5                                   3    
HELIX    3 AA3 LEU A   72  CYS A   81  1                                  10    
HELIX    4 AA4 SER A  141  HIS A  153  1                                  13    
HELIX    5 AA5 LEU A  209  THR A  216  1                                   8    
HELIX    6 AA6 LYS A  217  SER A  222  5                                   6    
HELIX    7 AA7 ILE B 1072  LEU B 1076  5                                   5    
HELIX    8 AA8 GLY C    9  ASP C   21  1                                  13    
HELIX    9 AA9 GLU C   55  PHE C   57  5                                   3    
HELIX   10 AB1 LEU C   72  CYS C   81  1                                  10    
HELIX   11 AB2 SER C  141  HIS C  153  1                                  13    
HELIX   12 AB3 LEU C  209  THR C  216  1                                   8    
HELIX   13 AB4 LYS C  217  SER C  222  5                                   6    
HELIX   14 AB5 ILE D 1072  LEU D 1076  5                                   5    
HELIX   15 AB6 GLY E    9  ASP E   21  1                                  13    
HELIX   16 AB7 GLU E   55  PHE E   57  5                                   3    
HELIX   17 AB8 LEU E   72  CYS E   81  1                                  10    
HELIX   18 AB9 SER E  141  HIS E  153  1                                  13    
HELIX   19 AC1 LEU E  209  THR E  216  1                                   8    
HELIX   20 AC2 LYS E  217  SER E  222  5                                   6    
HELIX   21 AC3 ILE F 1072  LEU F 1076  5                                   5    
SHEET    1 AA1 9 THR A  59  CYS A  62  0                                        
SHEET    2 AA1 9 PHE A   2  LEU A   6 -1  N  GLU A   3   O  ARG A  61           
SHEET    3 AA1 9 ILE A  87  ALA A  92 -1  O  ILE A  88   N  LEU A   6           
SHEET    4 AA1 9 THR A  98  GLU A 104 -1  O  ALA A 100   N  ARG A  91           
SHEET    5 AA1 9 LYS A 110  LYS A 117 -1  O  TYR A 114   N  LEU A 101           
SHEET    6 AA1 9 GLY C 176  SER C 183 -1  O  ASN C 177   N  GLU A 115           
SHEET    7 AA1 9 GLY C 166  GLY C 173 -1  N  PHE C 169   O  ILE C 180           
SHEET    8 AA1 9 ALA C 157  CYS C 162 -1  N  VAL C 159   O  SER C 170           
SHEET    9 AA1 9 VAL C 203  ALA C 208 -1  O  LEU C 205   N  ILE C 160           
SHEET    1 AA2 9 LEU A  66  ASN A  71  0                                        
SHEET    2 AA2 9 GLU A  25  SER A  31 -1  N  TRP A  28   O  MET A  68           
SHEET    3 AA2 9 GLY A  34  MET A  40 -1  O  ASN A  36   N  ASP A  29           
SHEET    4 AA2 9 SER A  46  ARG A  53 -1  O  VAL A  48   N  SER A  39           
SHEET    5 AA2 9 GLY A 245  LEU A 251 -1  O  LYS A 248   N  GLN A  49           
SHEET    6 AA2 9 LEU A 235  ILE A 241 -1  N  TYR A 239   O  LEU A 247           
SHEET    7 AA2 9 THR A 224  MET A 229 -1  N  THR A 226   O  GLU A 238           
SHEET    8 AA2 9 CYS A 135  PRO A 140 -1  N  CYS A 135   O  MET A 229           
SHEET    9 AA2 9 THR A 196  MET A 199 -1  O  THR A 196   N  LYS A 138           
SHEET    1 AA3 9 VAL A 203  ALA A 208  0                                        
SHEET    2 AA3 9 ALA A 157  CYS A 162 -1  N  ILE A 160   O  LEU A 205           
SHEET    3 AA3 9 GLY A 166  GLY A 173 -1  O  SER A 170   N  VAL A 159           
SHEET    4 AA3 9 GLY A 176  SER A 183 -1  O  LEU A 182   N  VAL A 167           
SHEET    5 AA3 9 LYS E 110  LYS E 117 -1  O  ASP E 113   N  ASN A 179           
SHEET    6 AA3 9 THR E  98  GLU E 104 -1  N  LEU E 101   O  TYR E 114           
SHEET    7 AA3 9 ILE E  87  ALA E  92 -1  N  ARG E  91   O  ALA E 100           
SHEET    8 AA3 9 PHE E   2  ARG E   5 -1  N  ALA E   4   O  LEU E  90           
SHEET    9 AA3 9 THR E  59  CYS E  62 -1  O  ARG E  61   N  GLU E   3           
SHEET    1 AA4 9 THR C  59  CYS C  62  0                                        
SHEET    2 AA4 9 PHE C   2  LEU C   6 -1  N  GLU C   3   O  ARG C  61           
SHEET    3 AA4 9 ILE C  87  ALA C  92 -1  O  ILE C  88   N  LEU C   6           
SHEET    4 AA4 9 THR C  98  GLU C 104 -1  O  ALA C 100   N  ARG C  91           
SHEET    5 AA4 9 LYS C 110  LYS C 117 -1  O  TYR C 114   N  LEU C 101           
SHEET    6 AA4 9 GLY E 176  SER E 183 -1  O  ASN E 177   N  GLU C 115           
SHEET    7 AA4 9 GLY E 166  GLY E 173 -1  N  PHE E 169   O  ILE E 180           
SHEET    8 AA4 9 ALA E 157  CYS E 162 -1  N  VAL E 159   O  SER E 170           
SHEET    9 AA4 9 VAL E 203  ALA E 208 -1  O  LEU E 205   N  ILE E 160           
SHEET    1 AA5 9 LEU C  66  ASN C  71  0                                        
SHEET    2 AA5 9 GLU C  25  ILE C  30 -1  N  TRP C  28   O  MET C  68           
SHEET    3 AA5 9 GLY C  34  MET C  40 -1  O  ASN C  36   N  ASP C  29           
SHEET    4 AA5 9 SER C  46  ARG C  53 -1  O  VAL C  48   N  SER C  39           
SHEET    5 AA5 9 GLY C 245  LEU C 251 -1  O  TYR C 250   N  LEU C  47           
SHEET    6 AA5 9 LEU C 235  ILE C 241 -1  N  TYR C 239   O  LEU C 247           
SHEET    7 AA5 9 THR C 224  MET C 229 -1  N  THR C 226   O  GLU C 238           
SHEET    8 AA5 9 CYS C 135  PRO C 140 -1  N  CYS C 135   O  MET C 229           
SHEET    9 AA5 9 THR C 196  MET C 199 -1  O  THR C 196   N  LYS C 138           
SHEET    1 AA6 9 LEU E  66  ASN E  71  0                                        
SHEET    2 AA6 9 GLU E  25  SER E  31 -1  N  TRP E  28   O  MET E  68           
SHEET    3 AA6 9 GLY E  34  MET E  40 -1  O  ASN E  36   N  ASP E  29           
SHEET    4 AA6 9 SER E  46  ARG E  53 -1  O  LEU E  50   N  LEU E  37           
SHEET    5 AA6 9 GLY E 245  LEU E 251 -1  O  TYR E 250   N  LEU E  47           
SHEET    6 AA6 9 LEU E 235  ILE E 241 -1  N  TYR E 239   O  LEU E 247           
SHEET    7 AA6 9 THR E 224  MET E 229 -1  N  SER E 228   O  VAL E 236           
SHEET    8 AA6 9 CYS E 135  PRO E 140 -1  N  CYS E 135   O  MET E 229           
SHEET    9 AA6 9 THR E 196  MET E 199 -1  O  THR E 196   N  LYS E 138           
SITE     1 AC1  5 ARG A  53  GLU A 238  LYS A 240  GLY A 245                    
SITE     2 AC1  5 HIS A 246                                                     
SITE     1 AC2  5 ALA A  82  GLY A  83  ASN A  84  GLU A  85                    
SITE     2 AC2  5 ARG C 146                                                     
SITE     1 AC3  7 LYS A 190  GLU A 191  ARG C  53  LYS C 240                    
SITE     2 AC3  7 GLY C 245  HIS C 246  HOH C 413                               
SITE     1 AC4  4 ALA C  82  GLY C  83  ASN C  84  ARG E 146                    
SITE     1 AC5  4 ARG E  53  LYS E 240  GLY E 245  HIS E 246                    
SITE     1 AC6  3 ARG A 146  ASN E  84  HOH E 412                               
SITE     1 AC7  5 SER E 152  ASP E 156  LEU E 209  ARG E 210                    
SITE     2 AC7  5 HOH E 416                                                     
CRYST1   84.631   84.631  201.770  90.00  90.00 120.00 P 31 2 1     18          
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      0.011816  0.006822  0.000000        0.00000                         
SCALE2      0.000000  0.013644  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004956        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system