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Database: PDB
Entry: 3V61
LinkDB: 3V61
Original site: 3V61 
HEADER    PROTEIN BINDING/DNA BINDING PROTEIN     18-DEC-11   3V61              
TITLE     STRUCTURE OF S. CEREVISIAE PCNA CONJUGATED TO SUMO ON LYSINE 164      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN-LIKE PROTEIN SMT3;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 20-98;                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;                        
COMPND   8 CHAIN: B;                                                            
COMPND   9 SYNONYM: PCNA;                                                       
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 559292;                                              
SOURCE   5 STRAIN: W3031A;                                                      
SOURCE   6 GENE: D9719.15, SMT3, YDR510W;                                       
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYSS;                           
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET28B;                                   
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  14 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  15 ORGANISM_TAXID: 559292;                                              
SOURCE  16 STRAIN: W3031A;                                                      
SOURCE  17 GENE: POL30, YBR0811, YBR088C;                                       
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  20 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CP RIL;                           
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PET21B                                    
KEYWDS    UBIQUITIN-LIKE PROTEIN PCNA, POST-TRANSLATIONAL MODIFICATION, DNA     
KEYWDS   2 REPLICATION, DNA DAMAGE RESPONSE, SRS2, NEM MODIFICATION ON PCNA     
KEYWDS   3 CYS22 AND CYS81, NUCLEAR, PROTEIN BINDING-DNA BINDING PROTEIN        
KEYWDS   4 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.A.ARMSTRONG,F.MOHIDEEN,C.D.LIMA                                     
REVDAT   5   25-OCT-17 3V61    1       REMARK                                   
REVDAT   4   18-SEP-13 3V61    1       REMARK                                   
REVDAT   3   03-APR-13 3V61    1       JRNL                                     
REVDAT   2   07-MAR-12 3V61    1       JRNL                                     
REVDAT   1   29-FEB-12 3V61    0                                                
JRNL        AUTH   A.A.ARMSTRONG,F.MOHIDEEN,C.D.LIMA                            
JRNL        TITL   RECOGNITION OF SUMO-MODIFIED PCNA REQUIRES TANDEM RECEPTOR   
JRNL        TITL 2 MOTIFS IN SRS2.                                              
JRNL        REF    NATURE                        V. 483    59 2012              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   22382979                                                     
JRNL        DOI    10.1038/NATURE10883                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 12550                          
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) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.214                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 617                             
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 842                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.79                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3090                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 49                           
REMARK   3   BIN FREE R VALUE                    : 0.3820                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2604                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 90                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.14000                                             
REMARK   3    B22 (A**2) : -2.14000                                             
REMARK   3    B33 (A**2) : 4.27000                                              
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): 0.997         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.347         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.187         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.592         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2663 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3581 ; 1.289 ; 1.995       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   329 ; 5.807 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   120 ;36.634 ;25.250       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   505 ;19.093 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;17.472 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   413 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1978 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  1647 ; 0.608 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2663 ; 1.147 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1016 ; 1.251 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   918 ; 2.178 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.00                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  NEM MOLECULE HAS OCCUPANCY OF 1 AS MASS SPEC SUGGESTED THAT THIS    
REMARK   3  LIGAND IS                                                           
REMARK   3  FULLY MODIFIED IN THE STUDIED SAMPLES.                              
REMARK   4                                                                      
REMARK   4 3V61 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000069639.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-AUG-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23649                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 1PLQ AND 1EUV                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 21% MPD, 100 MM BACL2, 100 MM BIS        
REMARK 280  -TRIS, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y,Z                                                 
REMARK 290       7555   -Y+1/2,X,Z+3/4                                          
REMARK 290       8555   Y,-X+1/2,Z+1/4                                          
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       70.03000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       70.03000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       26.05950            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       70.03000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       13.02975            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       70.03000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       39.08925            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       70.03000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       70.03000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       26.05950            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       70.03000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       39.08925            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       70.03000            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       13.02975            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: PCNA IS NORMALLY A TRIMER BUT NEM MODIFICATION DISRUPTS THE  
REMARK 300 TRIMER AND CAUSES PCNA TO RUN AS A MONOMER ON GEL FILTRATION THIS    
REMARK 300 SUMO-PCNA MONOMER CRYSTALLIZES BY REFORMING THE PCNA:PCNA PROTOMER   
REMARK 300 BUT WITH A RIGHT HANDED HELICAL SCREW COINCIDENT WITH THE I41 SCREW  
REMARK 300 AXIS THE UNIT CELL CONTAINS ONE TURN OF THIS HELICAL SCREW           
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THERE IS AN ISOPEPTIDE LINKAGE BETWEEN RESIDUES A98 AND B164         
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     GLY A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     HIS A    17                                                      
REMARK 465     MET A    18                                                      
REMARK 465     ARG A    19                                                      
REMARK 465     PRO A    20                                                      
REMARK 465     GLU A    21                                                      
REMARK 465     ASN B   255                                                      
REMARK 465     ASP B   256                                                      
REMARK 465     GLU B   257                                                      
REMARK 465     GLU B   258                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  84    CG   CD   OE1  OE2                                  
REMARK 470     PHE B 254    CG   CD1  CD2  CE1  CE2  CZ                         
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   O    GLY A    98     NZ   LYS B   164              1.92            
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  30     -127.74   -102.50                                   
REMARK 500    LYS B 107      -13.60     83.92                                   
REMARK 500    LYS B 108       37.93     91.58                                   
REMARK 500    ASP B 109      -79.75    -79.43                                   
REMARK 500    ALA B 123      132.89    -39.97                                   
REMARK 500    LEU B 126       43.24   -106.98                                   
REMARK 500    GLU B 130      112.05     42.85                                   
REMARK 500    GLU B 165       19.24     52.12                                   
REMARK 500    PHE B 185      117.96   -164.12                                   
REMARK 500    GLN B 201      135.87   -177.30                                   
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                              BA A   2  BA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  82   OD2                                                    
REMARK 620 2 ASP A  82   O    50.0                                              
REMARK 620 3 HOH A 100   O    86.0  64.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              BA B 260  BA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU B 241   O                                                      
REMARK 620 2 ASP B 240   OD2  75.8                                              
REMARK 620 3 HOH B 270   O    67.2 102.2                                        
REMARK 620 4 HOH B 322   O    51.2 105.1 100.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              BA B 264  BA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  93   OD1                                                    
REMARK 620 2 THR B  95   OG1  88.6                                              
REMARK 620 3 THR B  95   O   100.0  49.4                                        
REMARK 620 4 HOH B 340   O   158.2  84.1  60.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              BA A   3  BA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  87   OD1                                                    
REMARK 620 2 HOH A   6   O   125.8                                              
REMARK 620 3 HOH A 104   O   134.9  92.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              BA B 267  BA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG B  80   O                                                      
REMARK 620 2 GLY B  82   O    62.4                                              
REMARK 620 3 HOH B 274   O    76.0  74.4                                        
REMARK 620 4 HOH B 276   O   147.0  86.5  85.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              BA B 261  BA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE B  57   O                                                      
REMARK 620 2 HOH B 294   O   129.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              BA B 259  BA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 214   OD1                                                    
REMARK 620 2 ASP B  21   O    99.4                                              
REMARK 620 3 HOH B 323   O   145.1  73.8                                        
REMARK 620 4 HOH B 280   O    91.5  89.2  54.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              BA B 262  BA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  55   O                                                      
REMARK 620 2 HOH B 279   O   111.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              BA B 263  BA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B  85   O                                                      
REMARK 620 2 GLU B   7   O    94.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              BA B 265  BA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 108   O                                                      
REMARK 620 2 HOH B 271   O   134.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              BA A  11  BA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 113   O                                                      
REMARK 620 2 HOH B 293   O    95.7                                              
REMARK 620 3 HOH B 277   O    49.7  46.2                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BA A 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BA A 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BA A 4                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BA A 11                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BA B 259                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BA B 260                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BA B 261                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BA B 262                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BA B 263                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BA B 264                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BA B 265                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BA B 266                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BA B 267                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NEQ B 268                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NEQ B 269                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3V60   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3V62   RELATED DB: PDB                                   
DBREF  3V61 A   20    98  UNP    Q12306   SMT3_YEAST      20     98             
DBREF  3V61 B    1   258  UNP    P15873   PCNA_YEAST       1    258             
SEQADV 3V61 GLY A   15  UNP  Q12306              EXPRESSION TAG                 
SEQADV 3V61 SER A   16  UNP  Q12306              EXPRESSION TAG                 
SEQADV 3V61 HIS A   17  UNP  Q12306              EXPRESSION TAG                 
SEQADV 3V61 MET A   18  UNP  Q12306              EXPRESSION TAG                 
SEQADV 3V61 ARG A   19  UNP  Q12306              EXPRESSION TAG                 
SEQADV 3V61 GLY B  127  UNP  P15873    LYS   127 ENGINEERED MUTATION            
SEQRES   1 A   84  GLY SER HIS MET ARG PRO GLU THR HIS ILE ASN LEU LYS          
SEQRES   2 A   84  VAL SER ASP GLY SER SER GLU ILE PHE PHE LYS ILE LYS          
SEQRES   3 A   84  LYS THR THR PRO LEU ARG ARG LEU MET GLU ALA PHE ALA          
SEQRES   4 A   84  LYS ARG GLN GLY LYS GLU MET ASP SER LEU ARG PHE LEU          
SEQRES   5 A   84  TYR ASP GLY ILE ARG ILE GLN ALA ASP GLN THR PRO GLU          
SEQRES   6 A   84  ASP LEU ASP MET GLU ASP ASN ASP ILE ILE GLU ALA HIS          
SEQRES   7 A   84  ARG GLU GLN ILE GLY GLY                                      
SEQRES   1 B  258  MET LEU GLU ALA LYS PHE GLU GLU ALA SER LEU PHE LYS          
SEQRES   2 B  258  ARG ILE ILE ASP GLY PHE LYS ASP CYS VAL GLN LEU VAL          
SEQRES   3 B  258  ASN PHE GLN CYS LYS GLU ASP GLY ILE ILE ALA GLN ALA          
SEQRES   4 B  258  VAL ASP ASP SER ARG VAL LEU LEU VAL SER LEU GLU ILE          
SEQRES   5 B  258  GLY VAL GLU ALA PHE GLN GLU TYR ARG CYS ASP HIS PRO          
SEQRES   6 B  258  VAL THR LEU GLY MET ASP LEU THR SER LEU SER LYS ILE          
SEQRES   7 B  258  LEU ARG CYS GLY ASN ASN THR ASP THR LEU THR LEU ILE          
SEQRES   8 B  258  ALA ASP ASN THR PRO ASP SER ILE ILE LEU LEU PHE GLU          
SEQRES   9 B  258  ASP THR LYS LYS ASP ARG ILE ALA GLU TYR SER LEU LYS          
SEQRES  10 B  258  LEU MET ASP ILE ASP ALA ASP PHE LEU GLY ILE GLU GLU          
SEQRES  11 B  258  LEU GLN TYR ASP SER THR LEU SER LEU PRO SER SER GLU          
SEQRES  12 B  258  PHE SER LYS ILE VAL ARG ASP LEU SER GLN LEU SER ASP          
SEQRES  13 B  258  SER ILE ASN ILE MET ILE THR LYS GLU THR ILE LYS PHE          
SEQRES  14 B  258  VAL ALA ASP GLY ASP ILE GLY SER GLY SER VAL ILE ILE          
SEQRES  15 B  258  LYS PRO PHE VAL ASP MET GLU HIS PRO GLU THR SER ILE          
SEQRES  16 B  258  LYS LEU GLU MET ASP GLN PRO VAL ASP LEU THR PHE GLY          
SEQRES  17 B  258  ALA LYS TYR LEU LEU ASP ILE ILE LYS GLY SER SER LEU          
SEQRES  18 B  258  SER ASP ARG VAL GLY ILE ARG LEU SER SER GLU ALA PRO          
SEQRES  19 B  258  ALA LEU PHE GLN PHE ASP LEU LYS SER GLY PHE LEU GLN          
SEQRES  20 B  258  PHE PHE LEU ALA PRO LYS PHE ASN ASP GLU GLU                  
HET     BA  A   2       1                                                       
HET     BA  A   3       1                                                       
HET     BA  A   4       1                                                       
HET     BA  A  11       1                                                       
HET     BA  B 259       1                                                       
HET     BA  B 260       1                                                       
HET     BA  B 261       1                                                       
HET     BA  B 262       1                                                       
HET     BA  B 263       1                                                       
HET     BA  B 264       1                                                       
HET     BA  B 265       1                                                       
HET     BA  B 266       1                                                       
HET     BA  B 267       1                                                       
HET    NEQ  B 268       9                                                       
HET    NEQ  B 269       9                                                       
HETNAM      BA BARIUM ION                                                       
HETNAM     NEQ N-ETHYLMALEIMIDE                                                 
FORMUL   3   BA    13(BA 2+)                                                    
FORMUL  16  NEQ    2(C6 H7 N O2)                                                
FORMUL  18  HOH   *90(H2 O)                                                     
HELIX    1   1 LEU A   45  ARG A   55  1                                  11    
HELIX    2   2 GLU A   59  ASP A   61  5                                   3    
HELIX    3   3 THR A   77  ASP A   82  1                                   6    
HELIX    4   4 GLU B    8  VAL B   23  1                                  16    
HELIX    5   5 GLU B   55  PHE B   57  5                                   3    
HELIX    6   6 LEU B   72  GLY B   82  1                                  11    
HELIX    7   7 THR B  106  ASP B  109  5                                   4    
HELIX    8   8 SER B  141  GLN B  153  1                                  13    
HELIX    9   9 HIS B  190  SER B  194  5                                   5    
HELIX   10  10 ALA B  209  LYS B  217  1                                   9    
HELIX   11  11 GLY B  218  LEU B  221  5                                   4    
SHEET    1   A 5 GLU A  34  LYS A  38  0                                        
SHEET    2   A 5 ASN A  25  SER A  29 -1  N  VAL A  28   O  ILE A  35           
SHEET    3   A 5 ILE A  88  ARG A  93  1  O  ALA A  91   N  SER A  29           
SHEET    4   A 5 LEU A  63  TYR A  67 -1  N  ARG A  64   O  HIS A  92           
SHEET    5   A 5 ILE A  70  ARG A  71 -1  O  ILE A  70   N  TYR A  67           
SHEET    1   B 5 GLU B  59  CYS B  62  0                                        
SHEET    2   B 5 LEU B   2  PHE B   6 -1  N  GLU B   3   O  ARG B  61           
SHEET    3   B 5 THR B  87  ALA B  92 -1  O  ALA B  92   N  LEU B   2           
SHEET    4   B 5 SER B  98  GLU B 104 -1  O  ILE B 100   N  ILE B  91           
SHEET    5   B 5 ILE B 111  LYS B 117 -1  O  ALA B 112   N  PHE B 103           
SHEET    1   C 9 VAL B  66  ASP B  71  0                                        
SHEET    2   C 9 LEU B  25  LYS B  31 -1  N  CYS B  30   O  VAL B  66           
SHEET    3   C 9 GLY B  34  VAL B  40 -1  O  GLY B  34   N  LYS B  31           
SHEET    4   C 9 LEU B  46  GLY B  53 -1  O  LEU B  50   N  ALA B  37           
SHEET    5   C 9 GLY B 244  LEU B 250 -1  O  PHE B 245   N  GLU B  51           
SHEET    6   C 9 ALA B 235  ASP B 240 -1  N  ALA B 235   O  LEU B 250           
SHEET    7   C 9 ARG B 224  LEU B 229 -1  N  GLY B 226   O  GLN B 238           
SHEET    8   C 9 SER B 135  PRO B 140 -1  N  LEU B 137   O  ILE B 227           
SHEET    9   C 9 LYS B 196  MET B 199 -1  O  LYS B 196   N  SER B 138           
SHEET    1   D 4 SER B 177  ILE B 182  0                                        
SHEET    2   D 4 THR B 166  ASP B 172 -1  N  ALA B 171   O  GLY B 178           
SHEET    3   D 4 SER B 157  THR B 163 -1  N  ASN B 159   O  VAL B 170           
SHEET    4   D 4 VAL B 203  GLY B 208 -1  O  PHE B 207   N  ILE B 158           
LINK         OD2 ASP A  82                BA    BA A   2     1555   1555  2.62  
LINK         O   LEU B 241                BA    BA B 260     1555   1555  2.83  
LINK         OD1 ASP B  93                BA    BA B 264     1555   1555  2.89  
LINK         OD1 ASP A  87                BA    BA A   3     1555   1555  2.89  
LINK         O   ARG B  80                BA    BA B 267     1555   1555  2.98  
LINK         O   PHE B  57                BA    BA B 261     1555   1555  2.98  
LINK         OD2 ASP B 240                BA    BA B 260     1555   1555  3.01  
LINK         OD1 ASP B 214                BA    BA B 259     1555   1555  3.06  
LINK         O   GLU B  55                BA    BA B 262     1555   1555  3.08  
LINK         O   THR B  85                BA    BA B 263     1555   1555  3.10  
LINK         OD2 ASP A  82                BA    BA A   4     1555   1555  3.11  
LINK         O   ASP B  21                BA    BA B 259     1555   1555  3.13  
LINK         O   GLU B   7                BA    BA B 263     1555   1555  3.14  
LINK         OG1 THR B  95                BA    BA B 264     1555   1555  3.15  
LINK         O   ASP A  82                BA    BA A   2     1555   1555  3.20  
LINK         O   THR B  95                BA    BA B 264     1555   1555  3.23  
LINK         O   GLY B  82                BA    BA B 267     1555   1555  3.30  
LINK         SG  CYS B  81                 C3  NEQ B 269     1555   1555  1.66  
LINK         SG  CYS B  22                 C3  NEQ B 268     1555   1555  1.69  
LINK         C   GLY A  98                 NZ  LYS B 164     1555   1555  1.35  
LINK        BA    BA B 264                 O   HOH B 340     1555   1555  2.55  
LINK        BA    BA A   2                 O   HOH A 100     1555   1555  2.61  
LINK        BA    BA B 267                 O   HOH B 274     1555   1555  2.82  
LINK        BA    BA B 259                 O   HOH B 323     1555   1555  2.86  
LINK        BA    BA B 265                 O   HOH A 108     1555   1555  2.87  
LINK        BA    BA B 260                 O   HOH B 270     1555   1555  2.91  
LINK        BA    BA B 260                 O   HOH B 322     1555   1555  2.92  
LINK        BA    BA B 259                 O   HOH B 280     1555   1555  2.96  
LINK        BA    BA A  11                 O   HOH A 113     1555   1555  2.99  
LINK        BA    BA B 267                 O   HOH B 276     1555   1555  3.00  
LINK        BA    BA A  11                 O   HOH B 293     1555   1555  3.29  
LINK        BA    BA B 261                 O   HOH B 294     1555   1555  3.32  
LINK        BA    BA A   3                 O   HOH A   6     1555   1555  3.34  
LINK        BA    BA B 265                 O   HOH B 271     1555   1555  3.34  
LINK        BA    BA B 262                 O   HOH B 279     1555   1555  3.35  
LINK        BA    BA A   3                 O   HOH A 104     1555   1555  3.36  
LINK        BA    BA A  11                 O   HOH B 277     1555   1555  3.40  
CISPEP   1 GLY A   97    GLY A   98          0        -3.98                     
SITE     1 AC1  4 HOH A   6  ASP A  82  ASP A  85  HOH A 100                    
SITE     1 AC2  1 ASP A  87                                                     
SITE     1 AC3  3 HIS A  23  ASP A  82  ASP A  85                               
SITE     1 AC4  2 HOH A 113  ASP B  33                                          
SITE     1 AC5  5 ASP B  21  ASP B 214  HOH B 275  HOH B 280                    
SITE     2 AC5  5 HOH B 323                                                     
SITE     1 AC6  5 ASP B 240  LEU B 241  HOH B 270  HOH B 273                    
SITE     2 AC6  5 HOH B 322                                                     
SITE     1 AC7  3 PHE B  57   BA B 262  HOH B 299                               
SITE     1 AC8  2 GLU B  55   BA B 261                                          
SITE     1 AC9  3 GLU B   7  THR B  85  THR B  87                               
SITE     1 BC1  4 ASP B  93  ASN B  94  THR B  95  HOH B 340                    
SITE     1 BC2  2 HOH A 108  HOH B 293                                          
SITE     1 BC3  1 ASP B 172                                                     
SITE     1 BC4  4 ARG B  80  GLY B  82  HOH B 274  HOH B 276                    
SITE     1 BC5  5 GLY B  18  PHE B  19  CYS B  22  VAL B  48                    
SITE     2 BC5  5 ASP B 214                                                     
SITE     1 BC6  6 ILE B  78  CYS B  81  ASP B 150  GLN B 153                    
SITE     2 BC6  6 LEU B 154  HOH B 324                                          
CRYST1  140.060  140.060   52.119  90.00  90.00  90.00 I 41          8          
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      0.007140  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007140  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019187        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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