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Database: PDB
Entry: 5MLO
LinkDB: 5MLO
Original site: 5MLO 
HEADER    HYDROLASE                               07-DEC-16   5MLO              
TITLE     CRYSTAL STRUCTURE OF HUMAN PCNA IN COMPLEX WITH ZRANB3 PIP BOX 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: ZRANB3 PIP BOX 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 5MLO    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.    1.96 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) : 1.96                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 78.34                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 64155                          
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) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3325                            
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) : 1.96                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.01                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4706                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.82                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3140                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 234                          
REMARK   3   BIN FREE R VALUE                    : 0.3390                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6175                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 385                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.95                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.27000                                             
REMARK   3    B22 (A**2) : -2.22000                                             
REMARK   3    B33 (A**2) : 2.49000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.179         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.167         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.142         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.139        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6419 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  6206 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8697 ; 1.401 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 14366 ; 1.091 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   836 ; 7.255 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   289 ;45.647 ;25.433       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1207 ;15.252 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    33 ;16.818 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1015 ; 0.097 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7273 ; 0.012 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1356 ; 0.007 ; 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):  3235 ; 2.452 ; 2.839       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3234 ; 2.450 ; 2.837       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4049 ; 3.904 ; 4.234       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  4050 ; 3.904 ; 4.236       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3184 ; 2.855 ; 3.296       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3185 ; 2.855 ; 3.297       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4629 ; 4.617 ; 4.799       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6945 ; 8.498 ;22.921       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  6828 ; 8.404 ;22.581       
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  : 3                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     1    255       C     1    255   29898  0.10  0.05     
REMARK   3    2     A     1    255       E     1    255   30064  0.10  0.05     
REMARK   3    3     C     1    255       E     1    255   30278  0.10  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   518        B   527                          
REMARK   3    ORIGIN FOR THE GROUP (A):  75.3730   2.3310  29.0090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1257 T22:   0.3595                                     
REMARK   3      T33:   0.0619 T12:  -0.0762                                     
REMARK   3      T13:   0.0406 T23:  -0.0534                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3059 L22:   0.9589                                     
REMARK   3      L33:   1.3350 L12:  -0.5097                                     
REMARK   3      L13:  -0.2259 L23:   0.7098                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0362 S12:  -0.0658 S13:  -0.0808                       
REMARK   3      S21:  -0.1031 S22:   0.1050 S23:   0.0856                       
REMARK   3      S31:  -0.2101 S32:   0.2672 S33:  -0.1412                       
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   517        D   527                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.9680  -9.7950  -9.9650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1277 T22:   0.2353                                     
REMARK   3      T33:   0.0265 T12:  -0.0154                                     
REMARK   3      T13:  -0.0129 T23:   0.0339                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6926 L22:   0.2023                                     
REMARK   3      L33:   0.4705 L12:  -0.3356                                     
REMARK   3      L13:   0.3341 L23:  -0.0710                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0292 S12:   0.0537 S13:   0.0314                       
REMARK   3      S21:   0.0047 S22:  -0.0316 S23:  -0.0070                       
REMARK   3      S31:   0.0509 S32:   0.0633 S33:   0.0024                       
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   518        F   528                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.0450  24.6860  11.7930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1663 T22:   0.2529                                     
REMARK   3      T33:   0.0378 T12:   0.0705                                     
REMARK   3      T13:   0.0577 T23:  -0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4647 L22:   0.4184                                     
REMARK   3      L33:   0.9495 L12:   0.1605                                     
REMARK   3      L13:   0.6153 L23:  -0.0002                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0791 S12:  -0.1008 S13:   0.0504                       
REMARK   3      S21:   0.1028 S22:   0.0442 S23:   0.0932                       
REMARK   3      S31:  -0.1501 S32:  -0.1657 S33:   0.0349                       
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 5MLO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-DEC-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200002644.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-FEB-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1402                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67566                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.960                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 78.340                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.00                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.76300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1VYM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NACL + 8% (V/V) DMSO + 31%        
REMARK 280  PENTAERYTHITOL PROPOXYLATE (5/4 PO/OH), VAPOR DIFFUSION, SITTING    
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       34.06800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       78.33950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.40100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       78.33950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.06800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.40100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 1470 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 1560 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 1540 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
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     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     GLU B   515                                                      
REMARK 465     LYS B   516                                                      
REMARK 465     GLU B   517                                                      
REMARK 465     PRO B   528                                                      
REMARK 465     GLN B   529                                                      
REMARK 465     GLU C   256                                                      
REMARK 465     ASP C   257                                                      
REMARK 465     GLU C   258                                                      
REMARK 465     GLU C   259                                                      
REMARK 465     GLY C   260                                                      
REMARK 465     SER C   261                                                      
REMARK 465     GLU D   515                                                      
REMARK 465     LYS D   516                                                      
REMARK 465     PRO D   528                                                      
REMARK 465     GLN D   529                                                      
REMARK 465     GLU E   256                                                      
REMARK 465     ASP E   257                                                      
REMARK 465     GLU E   258                                                      
REMARK 465     GLU E   259                                                      
REMARK 465     GLY E   260                                                      
REMARK 465     SER E   261                                                      
REMARK 465     GLU F   515                                                      
REMARK 465     LYS F   516                                                      
REMARK 465     GLU F   517                                                      
REMARK 465     GLN F   529                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A  16   CA  -  CB  -  CG  ANGL. DEV. = -17.0 DEGREES          
REMARK 500    LEU C  16   CA  -  CB  -  CG  ANGL. DEV. = -18.2 DEGREES          
REMARK 500    LEU E  16   CA  -  CB  -  CG  ANGL. DEV. = -17.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  94      -38.65    -38.25                                   
REMARK 500    ASN A  95       32.13   -141.87                                   
REMARK 500    ASP A 243       -3.21     74.87                                   
REMARK 500    ASP C 189      -17.13     89.23                                   
REMARK 500    ASP C 243      -11.53     75.79                                   
REMARK 500    SER E 186      -66.32    -99.29                                   
REMARK 500    ASP E 243       -2.49     76.80                                   
REMARK 500    MET E 244      -44.39   -132.71                                   
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                              NA A 301  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A 105   O                                                      
REMARK 620 2 GLN A 108   O    77.6                                              
REMARK 620 3 HOH A 435   O   160.3  84.2                                        
REMARK 620 4 HOH A 464   O    82.6  95.2  91.8                                  
REMARK 620 5 HOH A 510   O    99.4 173.0  99.6  90.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 302  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS A 164   O                                                      
REMARK 620 2 GLN A 184   OE1  87.8                                              
REMARK 620 3 SER C  32   OG  100.0  13.2                                        
REMARK 620 4 HOH C 471   O   168.5  84.3  73.1                                  
REMARK 620 5 HOH C 452   O   108.3  99.5  90.6  81.2                            
REMARK 620 6 HOH C 483   O    94.3  83.4  87.8  76.6 157.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 301  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN C 108   O                                                      
REMARK 620 2 HOH C 515   O    70.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA E 301  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA E 105   O                                                      
REMARK 620 2 GLN E 108   O    60.8                                              
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 NA A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA E 301                  
DBREF  5MLO A    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  5MLO B  515   529  PDB    5MLO     5MLO           515    529             
DBREF  5MLO C    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  5MLO D  515   529  PDB    5MLO     5MLO           515    529             
DBREF  5MLO E    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  5MLO F  515   529  PDB    5MLO     5MLO           515    529             
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   15  GLU LYS GLU LYS GLN HIS ASP ILE ARG SER PHE PHE VAL          
SEQRES   2 B   15  PRO GLN                                                      
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   15  GLU LYS GLU LYS GLN HIS ASP ILE ARG SER PHE PHE VAL          
SEQRES   2 D   15  PRO GLN                                                      
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   15  GLU LYS GLU LYS GLN HIS ASP ILE ARG SER PHE PHE VAL          
SEQRES   2 F   15  PRO GLN                                                      
HET     NA  A 301       1                                                       
HET     NA  A 302       1                                                       
HET     NA  C 301       1                                                       
HET     NA  E 301       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   7   NA    4(NA 1+)                                                     
FORMUL  11  HOH   *385(H2 O)                                                    
HELIX    1 AA1 GLY A    9  LYS A   20  1                                  12    
HELIX    2 AA2 GLU A   55  PHE A   57  5                                   3    
HELIX    3 AA3 LEU A   72  LYS A   80  1                                   9    
HELIX    4 AA4 SER A  141  HIS A  153  1                                  13    
HELIX    5 AA5 LYS A  190  ALA A  194  5                                   5    
HELIX    6 AA6 LEU A  209  THR A  216  1                                   8    
HELIX    7 AA7 LYS A  217  SER A  222  5                                   6    
HELIX    8 AA8 ASP B  521  PHE B  525  5                                   5    
HELIX    9 AA9 GLY C    9  ALA C   18  1                                  10    
HELIX   10 AB1 GLU C   55  PHE C   57  5                                   3    
HELIX   11 AB2 LEU C   72  LYS C   80  1                                   9    
HELIX   12 AB3 SER C  141  HIS C  153  1                                  13    
HELIX   13 AB4 LEU C  209  THR C  216  1                                   8    
HELIX   14 AB5 LYS C  217  SER C  222  5                                   6    
HELIX   15 AB6 ILE D  522  VAL D  527  1                                   6    
HELIX   16 AB7 GLY E    9  LYS E   20  1                                  12    
HELIX   17 AB8 GLU E   55  PHE E   57  5                                   3    
HELIX   18 AB9 LEU E   72  LYS E   80  1                                   9    
HELIX   19 AC1 SER E  141  HIS E  153  1                                  13    
HELIX   20 AC2 LYS E  190  ALA E  194  5                                   5    
HELIX   21 AC3 LEU E  209  THR E  216  1                                   8    
HELIX   22 AC4 LYS E  217  SER E  222  5                                   6    
HELIX   23 AC5 ASP F  521  PHE F  526  5                                   6    
SHEET    1 AA1 9 THR A  59  CYS A  62  0                                        
SHEET    2 AA1 9 PHE A   2  LEU A   6 -1  N  GLU A   3   O  ARG A  61           
SHEET    3 AA1 9 ILE A  87  ALA A  92 -1  O  ILE A  88   N  LEU A   6           
SHEET    4 AA1 9 THR A  98  GLU A 104 -1  O  ALA A 100   N  ARG A  91           
SHEET    5 AA1 9 LYS A 110  LYS A 117 -1  O  MET A 116   N  LEU A  99           
SHEET    6 AA1 9 GLY C 176  SER C 183 -1  O  LYS C 181   N  VAL A 111           
SHEET    7 AA1 9 GLY C 166  GLY C 173 -1  N  VAL C 167   O  LEU C 182           
SHEET    8 AA1 9 ALA C 157  ALA C 163 -1  N  SER C 161   O  LYS C 168           
SHEET    9 AA1 9 VAL C 203  ALA C 208 -1  O  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  ALA A  26   O  VAL A  70           
SHEET    3 AA2 9 GLY A  34  MET A  40 -1  O  ASN A  36   N  ASP A  29           
SHEET    4 AA2 9 SER A  46  ARG A  53 -1  O  LEU A  50   N  LEU A  37           
SHEET    5 AA2 9 GLY A 245  LEU A 251 -1  O  TYR A 250   N  LEU A  47           
SHEET    6 AA2 9 LEU A 235  ILE A 241 -1  N  VAL A 237   O  TYR A 249           
SHEET    7 AA2 9 THR A 224  MET A 229 -1  N  THR A 226   O  GLU A 238           
SHEET    8 AA2 9 CYS A 135  PRO A 140 -1  N  VAL A 137   O  LEU A 227           
SHEET    9 AA2 9 THR A 196  MET A 199 -1  O  THR A 196   N  LYS A 138           
SHEET    1 AA3 9 GLN A 204  ALA A 208  0                                        
SHEET    2 AA3 9 ALA A 157  ALA A 163 -1  N  ILE A 160   O  LEU A 205           
SHEET    3 AA3 9 GLY A 166  GLY A 173 -1  O  LYS A 168   N  SER A 161           
SHEET    4 AA3 9 GLY A 176  SER A 183 -1  O  ILE A 180   N  PHE A 169           
SHEET    5 AA3 9 LYS E 110  LYS E 117 -1  O  VAL E 111   N  LYS A 181           
SHEET    6 AA3 9 THR E  98  GLU E 104 -1  N  LEU E  99   O  MET E 116           
SHEET    7 AA3 9 ILE E  87  ALA E  92 -1  N  ARG E  91   O  ALA E 100           
SHEET    8 AA3 9 PHE E   2  LEU E   6 -1  N  LEU E   6   O  ILE E  88           
SHEET    9 AA3 9 THR E  59  CYS E  62 -1  O  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  MET C 116   N  LEU C  99           
SHEET    6 AA4 9 GLY E 176  SER E 183 -1  O  LYS E 181   N  VAL C 111           
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  SER E 161   O  LYS E 168           
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  SER C  31 -1  N  ALA C  26   O  VAL C  70           
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  LEU C  50   N  LEU C  37           
SHEET    5 AA5 9 GLY C 245  LEU C 251 -1  O  TYR C 250   N  LEU C  47           
SHEET    6 AA5 9 LEU C 235  ILE C 241 -1  N  VAL C 237   O  TYR C 249           
SHEET    7 AA5 9 THR C 224  MET C 229 -1  N  THR C 226   O  GLU C 238           
SHEET    8 AA5 9 CYS C 135  PRO C 140 -1  N  VAL C 137   O  LEU C 227           
SHEET    9 AA5 9 THR C 196  MET C 199 -1  O  THR C 196   N  LYS C 138           
SHEET    1 AA6 9 LEU E  66  ASN E  71  0                                        
SHEET    2 AA6 9 GLU E  25  SER E  31 -1  N  TRP E  28   O  MET E  68           
SHEET    3 AA6 9 GLY E  34  MET E  40 -1  O  ASN E  36   N  ASP E  29           
SHEET    4 AA6 9 SER E  46  ARG E  53 -1  O  LEU E  52   N  VAL E  35           
SHEET    5 AA6 9 GLY E 245  LEU E 251 -1  O  TYR E 250   N  LEU E  47           
SHEET    6 AA6 9 LEU E 235  ILE E 241 -1  N  VAL E 237   O  TYR E 249           
SHEET    7 AA6 9 THR E 224  MET E 229 -1  N  THR E 226   O  GLU E 238           
SHEET    8 AA6 9 CYS E 135  PRO E 140 -1  N  VAL E 137   O  LEU E 227           
SHEET    9 AA6 9 THR E 196  MET E 199 -1  O  THR E 196   N  LYS E 138           
LINK         O   ALA A 105                NA    NA A 301     1555   1555  2.17  
LINK         O   GLN A 108                NA    NA A 301     1555   1555  2.44  
LINK         O   LYS A 164                NA    NA A 302     1555   1555  2.35  
LINK         OE1 GLN A 184                NA    NA A 302     1555   1555  2.35  
LINK         O   GLN C 108                NA    NA C 301     1555   1555  2.92  
LINK         O   ALA E 105                NA    NA E 301     1555   1555  2.43  
LINK         O   GLN E 108                NA    NA E 301     1555   1555  2.82  
LINK        NA    NA A 301                 O   HOH A 435     1555   1555  2.28  
LINK        NA    NA A 301                 O   HOH A 464     1555   1555  2.46  
LINK        NA    NA A 301                 O   HOH A 510     1555   1555  2.27  
LINK        NA    NA C 301                 O   HOH C 515     1555   1555  2.40  
LINK         OG  SER C  32                NA    NA A 302     1555   2654  2.33  
LINK        NA    NA A 302                 O   HOH C 471     1555   2655  2.51  
LINK        NA    NA A 302                 O   HOH C 452     1555   2655  2.40  
LINK        NA    NA A 302                 O   HOH C 483     1555   2655  2.59  
SITE     1 AC1  5 ALA A 105  GLN A 108  HOH A 435  HOH A 464                    
SITE     2 AC1  5 HOH A 510                                                     
SITE     1 AC2  7 LYS A 164  GLN A 184  SER C  32  CYS C  62                    
SITE     2 AC2  7 HOH C 452  HOH C 471  HOH C 483                               
SITE     1 AC3  2 GLN C 108  HOH C 515                                          
SITE     1 AC4  3 ALA E 105  GLN E 108  LYS E 110                               
CRYST1   68.136   86.802  156.679  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      0.014677  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011520  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006382        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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