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Database: PDB
Entry: 3V62
LinkDB: 3V62
Original site: 3V62 
HEADER    PROTEIN BINDING/DNA BINDING PROTEIN     18-DEC-11   3V62              
TITLE     STRUCTURE OF THE S. CEREVISIAE SRS2 C-TERMINAL DOMAIN IN COMPLEX WITH 
TITLE    2 PCNA CONJUGATED TO SUMO ON LYSINE 164                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN-LIKE PROTEIN SMT3;                               
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 20-98;                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;                        
COMPND   9 CHAIN: B, E;                                                         
COMPND  10 SYNONYM: PCNA;                                                       
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES;                                                       
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: ATP-DEPENDENT DNA HELICASE SRS2;                           
COMPND  15 CHAIN: C, F;                                                         
COMPND  16 FRAGMENT: UNP RESIDUES 1107-1174;                                    
COMPND  17 EC: 3.6.4.12;                                                        
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 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;                                   
SOURCE  23 MOL_ID: 3;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  25 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  26 ORGANISM_TAXID: 559292;                                              
SOURCE  27 STRAIN: W3031A;                                                      
SOURCE  28 GENE: HPR5, J0913, RADH, SRS2, YJL092W;                              
SOURCE  29 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  30 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  31 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CP RIL;                           
SOURCE  32 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  33 EXPRESSION_SYSTEM_PLASMID: PSMT3                                     
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 REDUCTIVE METHYLATION OF ALL LYSINE RESIDUES ON      
KEYWDS   4 SMT3, NUCLEAR, PROTEIN BINDING-DNA BINDING PROTEIN COMPLEX           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.A.ARMSTRONG,F.MOHIDEEN,C.D.LIMA                                     
REVDAT   4   25-OCT-17 3V62    1       REMARK                                   
REVDAT   3   03-APR-13 3V62    1       JRNL                                     
REVDAT   2   07-MAR-12 3V62    1       JRNL                                     
REVDAT   1   29-FEB-12 3V62    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.    2.90 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) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 25191                          
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) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1342                            
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) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1652                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.61                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3440                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 84                           
REMARK   3   BIN FREE R VALUE                    : 0.3530                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5616                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 51                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 88.56                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.62000                                             
REMARK   3    B22 (A**2) : 4.61000                                              
REMARK   3    B33 (A**2) : -4.39000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -3.11000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.862         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.334         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.274         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.141        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5750 ; 0.008 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7726 ; 1.697 ; 2.009       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   702 ; 6.360 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   260 ;39.894 ;25.308       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1044 ;20.123 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;17.792 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   896 ; 0.157 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4234 ; 0.005 ; 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):  3526 ; 0.743 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5696 ; 1.429 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2224 ; 1.661 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2030 ; 2.989 ; 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 : 4                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : B E                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     255      2                      
REMARK   3           1     D      1       D     255      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    B    (A):   1020 ; 0.080 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    979 ; 0.180 ; 0.500           
REMARK   3   TIGHT THERMAL      1    B (A**2):   1020 ; 0.160 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    B (A**2):    979 ; 0.280 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     20       A      98      2                      
REMARK   3           1     D     20       D      98      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    A    (A):    316 ; 0.010 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    328 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      2    A (A**2):    316 ; 0.020 ; 0.500           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    328 ; 0.040 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : C F                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C   1148       C    1161      2                      
REMARK   3           1     F   1148       F    1161      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    C    (A):     56 ; 0.010 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  3    C    (A):     57 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      3    C (A**2):     56 ; 0.010 ; 0.500           
REMARK   3   MEDIUM THERMAL     3    C (A**2):     57 ; 0.030 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : C F                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C   1168       C    1174      2                      
REMARK   3           1     F   1168       F    1174      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   4    C    (A):     28 ; 0.110 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  4    C    (A):     25 ; 0.190 ; 0.500           
REMARK   3   TIGHT THERMAL      4    C (A**2):     28 ; 0.110 ; 0.500           
REMARK   3   MEDIUM THERMAL     4    C (A**2):     25 ; 0.110 ; 2.000           
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 3V62 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_1000069640.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0750                             
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   : 26583                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -1.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.63200                            
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: PHASER                                                
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   (%): 62.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.9 M AMMONIUM SULFATE 4% PEG 400 100    
REMARK 280  MM HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 279K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       98.40850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.12800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       98.40850            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       31.12800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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 COMPOSED OF 4 SUBUNITS THE     
REMARK 300 ASU HAS 2 AND THE UNIT CELL CONTAINS ONE TURN OF THIS HELICAL SCREW  
REMARK 300 WITH 4 PROTOMERS                                                     
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THERE IS AN ISOPEPTIDE LINKAGE BETWEEN RESIDUES A98 AND B164; D98    
REMARK 400 AND E164                                                             
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     ASP B   256                                                      
REMARK 465     GLU B   257                                                      
REMARK 465     GLU B   258                                                      
REMARK 465     SER C  1106                                                      
REMARK 465     HIS C  1107                                                      
REMARK 465     ASN C  1108                                                      
REMARK 465     PRO C  1109                                                      
REMARK 465     ASP C  1110                                                      
REMARK 465     ASP C  1111                                                      
REMARK 465     THR C  1112                                                      
REMARK 465     THR C  1113                                                      
REMARK 465     VAL C  1114                                                      
REMARK 465     ASP C  1115                                                      
REMARK 465     ASN C  1116                                                      
REMARK 465     ARG C  1117                                                      
REMARK 465     PRO C  1118                                                      
REMARK 465     ILE C  1119                                                      
REMARK 465     ILE C  1120                                                      
REMARK 465     SER C  1121                                                      
REMARK 465     ASN C  1122                                                      
REMARK 465     ALA C  1123                                                      
REMARK 465     LYS C  1124                                                      
REMARK 465     PHE C  1125                                                      
REMARK 465     LEU C  1126                                                      
REMARK 465     ALA C  1127                                                      
REMARK 465     ASP C  1128                                                      
REMARK 465     ALA C  1129                                                      
REMARK 465     ALA C  1130                                                      
REMARK 465     MET C  1131                                                      
REMARK 465     LYS C  1132                                                      
REMARK 465     LYS C  1133                                                      
REMARK 465     THR C  1134                                                      
REMARK 465     GLN C  1135                                                      
REMARK 465     LYS C  1136                                                      
REMARK 465     PHE C  1137                                                      
REMARK 465     SER C  1138                                                      
REMARK 465     LYS C  1139                                                      
REMARK 465     LYS C  1140                                                      
REMARK 465     VAL C  1141                                                      
REMARK 465     LYS C  1142                                                      
REMARK 465     ASN C  1143                                                      
REMARK 465     GLU C  1144                                                      
REMARK 465     PRO C  1145                                                      
REMARK 465     ALA C  1146                                                      
REMARK 465     SER C  1147                                                      
REMARK 465     LYS C  1162                                                      
REMARK 465     SER C  1163                                                      
REMARK 465     LYS C  1164                                                      
REMARK 465     LEU C  1165                                                      
REMARK 465     ASN C  1166                                                      
REMARK 465     ASN C  1167                                                      
REMARK 465     GLY D    15                                                      
REMARK 465     SER D    16                                                      
REMARK 465     HIS D    17                                                      
REMARK 465     MET D    18                                                      
REMARK 465     ARG D    19                                                      
REMARK 465     ASP E   256                                                      
REMARK 465     GLU E   257                                                      
REMARK 465     GLU E   258                                                      
REMARK 465     SER F  1106                                                      
REMARK 465     HIS F  1107                                                      
REMARK 465     ASN F  1108                                                      
REMARK 465     PRO F  1109                                                      
REMARK 465     ASP F  1110                                                      
REMARK 465     ASP F  1111                                                      
REMARK 465     THR F  1112                                                      
REMARK 465     THR F  1113                                                      
REMARK 465     VAL F  1114                                                      
REMARK 465     ASP F  1115                                                      
REMARK 465     ASN F  1116                                                      
REMARK 465     ARG F  1117                                                      
REMARK 465     PRO F  1118                                                      
REMARK 465     ILE F  1119                                                      
REMARK 465     ILE F  1120                                                      
REMARK 465     SER F  1121                                                      
REMARK 465     ASN F  1122                                                      
REMARK 465     ALA F  1123                                                      
REMARK 465     LYS F  1124                                                      
REMARK 465     PHE F  1125                                                      
REMARK 465     LEU F  1126                                                      
REMARK 465     ALA F  1127                                                      
REMARK 465     ASP F  1128                                                      
REMARK 465     ALA F  1129                                                      
REMARK 465     ALA F  1130                                                      
REMARK 465     MET F  1131                                                      
REMARK 465     LYS F  1132                                                      
REMARK 465     LYS F  1133                                                      
REMARK 465     THR F  1134                                                      
REMARK 465     GLN F  1135                                                      
REMARK 465     LYS F  1136                                                      
REMARK 465     PHE F  1137                                                      
REMARK 465     SER F  1138                                                      
REMARK 465     LYS F  1139                                                      
REMARK 465     LYS F  1140                                                      
REMARK 465     VAL F  1141                                                      
REMARK 465     LYS F  1142                                                      
REMARK 465     ASN F  1143                                                      
REMARK 465     GLU F  1144                                                      
REMARK 465     PRO F  1145                                                      
REMARK 465     ALA F  1146                                                      
REMARK 465     SER F  1147                                                      
REMARK 465     LYS F  1162                                                      
REMARK 465     SER F  1163                                                      
REMARK 465     LYS F  1164                                                      
REMARK 465     LEU F  1165                                                      
REMARK 465     ASN F  1166                                                      
REMARK 465     ASN F  1167                                                      
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     PRO A  20    CB   CG   CD                                        
REMARK 470     GLU A  21    CB   CG   CD   OE1  OE2                             
REMARK 470     PRO D  20    CB   CG   CD                                        
REMARK 470     GLU D  21    CB   CG   CD   OE1  OE2                             
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    THR A  22      -85.45    -32.04                                   
REMARK 500    HIS A  23     -150.98   -114.66                                   
REMARK 500    SER A  32      -61.34    -91.87                                   
REMARK 500    ASP A  68       23.06     48.92                                   
REMARK 500    ILE A  72      134.02    -27.50                                   
REMARK 500    GLN A  95     -159.99   -141.29                                   
REMARK 500    VAL B  45      -30.34   -138.22                                   
REMARK 500    HIS B  64      136.25   -173.58                                   
REMARK 500    THR B  73      -71.21    -61.44                                   
REMARK 500    CYS B  81       18.25    -59.25                                   
REMARK 500    ALA B 123       13.82    -69.54                                   
REMARK 500    LEU B 126       77.17   -115.86                                   
REMARK 500    GLU B 129       24.19    -79.97                                   
REMARK 500    GLU B 130      -13.98     55.40                                   
REMARK 500    LEU B 131     -155.75     65.96                                   
REMARK 500    GLU B 165       35.54   -144.40                                   
REMARK 500    ILE B 175       -0.15   -140.09                                   
REMARK 500    ILE B 215      -37.26    -34.52                                   
REMARK 500    SER B 243       55.89   -113.88                                   
REMARK 500    THR D  22      -84.29    -30.66                                   
REMARK 500    HIS D  23     -151.56   -115.24                                   
REMARK 500    SER D  32      -60.93    -91.27                                   
REMARK 500    ASP D  68       24.70     48.07                                   
REMARK 500    ILE D  72      133.70    -28.83                                   
REMARK 500    ILE D  96       67.49   -100.19                                   
REMARK 500    CYS E  81       29.85    -63.52                                   
REMARK 500    ASP E 109       31.17     73.74                                   
REMARK 500    ALA E 123       13.34    -64.29                                   
REMARK 500    GLU E 130       23.88     45.40                                   
REMARK 500    LEU E 131     -144.60     37.63                                   
REMARK 500    GLU E 165       36.05   -144.91                                   
REMARK 500    GLU E 232       62.99     39.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NEQ B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NEQ B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NEQ E 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NEQ E 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 304                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3V60   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3V61   RELATED DB: PDB                                   
DBREF  3V62 A   20    98  UNP    Q12306   SMT3_YEAST      20     98             
DBREF  3V62 B    1   258  UNP    P15873   PCNA_YEAST       1    258             
DBREF  3V62 C 1107  1174  UNP    P12954   SRS2_YEAST    1107   1174             
DBREF  3V62 D   20    98  UNP    Q12306   SMT3_YEAST      20     98             
DBREF  3V62 E    1   258  UNP    P15873   PCNA_YEAST       1    258             
DBREF  3V62 F 1107  1174  UNP    P12954   SRS2_YEAST    1107   1174             
SEQADV 3V62 GLY A   15  UNP  Q12306              EXPRESSION TAG                 
SEQADV 3V62 SER A   16  UNP  Q12306              EXPRESSION TAG                 
SEQADV 3V62 HIS A   17  UNP  Q12306              EXPRESSION TAG                 
SEQADV 3V62 MET A   18  UNP  Q12306              EXPRESSION TAG                 
SEQADV 3V62 ARG A   19  UNP  Q12306              EXPRESSION TAG                 
SEQADV 3V62 GLY B  127  UNP  P15873    LYS   127 ENGINEERED MUTATION            
SEQADV 3V62 SER C 1106  UNP  P12954              EXPRESSION TAG                 
SEQADV 3V62 GLY D   15  UNP  Q12306              EXPRESSION TAG                 
SEQADV 3V62 SER D   16  UNP  Q12306              EXPRESSION TAG                 
SEQADV 3V62 HIS D   17  UNP  Q12306              EXPRESSION TAG                 
SEQADV 3V62 MET D   18  UNP  Q12306              EXPRESSION TAG                 
SEQADV 3V62 ARG D   19  UNP  Q12306              EXPRESSION TAG                 
SEQADV 3V62 GLY E  127  UNP  P15873    LYS   127 ENGINEERED MUTATION            
SEQADV 3V62 SER F 1106  UNP  P12954              EXPRESSION TAG                 
SEQRES   1 A   84  GLY SER HIS MET ARG PRO GLU THR HIS ILE ASN LEU MLY          
SEQRES   2 A   84  VAL SER ASP GLY SER SER GLU ILE PHE PHE MLY ILE MLY          
SEQRES   3 A   84  MLY THR THR PRO LEU ARG ARG LEU MET GLU ALA PHE ALA          
SEQRES   4 A   84  MLY ARG GLN GLY MLY 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                  
SEQRES   1 C   69  SER HIS ASN PRO ASP ASP THR THR VAL ASP ASN ARG PRO          
SEQRES   2 C   69  ILE ILE SER ASN ALA LYS PHE LEU ALA ASP ALA ALA MET          
SEQRES   3 C   69  LYS LYS THR GLN LYS PHE SER LYS LYS VAL LYS ASN GLU          
SEQRES   4 C   69  PRO ALA SER SER GLN MET ASP ILE PHE SER GLN LEU SER          
SEQRES   5 C   69  ARG ALA LYS LYS LYS SER LYS LEU ASN ASN GLY GLU ILE          
SEQRES   6 C   69  ILE VAL ILE ASP                                              
SEQRES   1 D   84  GLY SER HIS MET ARG PRO GLU THR HIS ILE ASN LEU MLY          
SEQRES   2 D   84  VAL SER ASP GLY SER SER GLU ILE PHE PHE MLY ILE MLY          
SEQRES   3 D   84  MLY THR THR PRO LEU ARG ARG LEU MET GLU ALA PHE ALA          
SEQRES   4 D   84  MLY ARG GLN GLY MLY GLU MET ASP SER LEU ARG PHE LEU          
SEQRES   5 D   84  TYR ASP GLY ILE ARG ILE GLN ALA ASP GLN THR PRO GLU          
SEQRES   6 D   84  ASP LEU ASP MET GLU ASP ASN ASP ILE ILE GLU ALA HIS          
SEQRES   7 D   84  ARG GLU GLN ILE GLY GLY                                      
SEQRES   1 E  258  MET LEU GLU ALA LYS PHE GLU GLU ALA SER LEU PHE LYS          
SEQRES   2 E  258  ARG ILE ILE ASP GLY PHE LYS ASP CYS VAL GLN LEU VAL          
SEQRES   3 E  258  ASN PHE GLN CYS LYS GLU ASP GLY ILE ILE ALA GLN ALA          
SEQRES   4 E  258  VAL ASP ASP SER ARG VAL LEU LEU VAL SER LEU GLU ILE          
SEQRES   5 E  258  GLY VAL GLU ALA PHE GLN GLU TYR ARG CYS ASP HIS PRO          
SEQRES   6 E  258  VAL THR LEU GLY MET ASP LEU THR SER LEU SER LYS ILE          
SEQRES   7 E  258  LEU ARG CYS GLY ASN ASN THR ASP THR LEU THR LEU ILE          
SEQRES   8 E  258  ALA ASP ASN THR PRO ASP SER ILE ILE LEU LEU PHE GLU          
SEQRES   9 E  258  ASP THR LYS LYS ASP ARG ILE ALA GLU TYR SER LEU LYS          
SEQRES  10 E  258  LEU MET ASP ILE ASP ALA ASP PHE LEU GLY ILE GLU GLU          
SEQRES  11 E  258  LEU GLN TYR ASP SER THR LEU SER LEU PRO SER SER GLU          
SEQRES  12 E  258  PHE SER LYS ILE VAL ARG ASP LEU SER GLN LEU SER ASP          
SEQRES  13 E  258  SER ILE ASN ILE MET ILE THR LYS GLU THR ILE LYS PHE          
SEQRES  14 E  258  VAL ALA ASP GLY ASP ILE GLY SER GLY SER VAL ILE ILE          
SEQRES  15 E  258  LYS PRO PHE VAL ASP MET GLU HIS PRO GLU THR SER ILE          
SEQRES  16 E  258  LYS LEU GLU MET ASP GLN PRO VAL ASP LEU THR PHE GLY          
SEQRES  17 E  258  ALA LYS TYR LEU LEU ASP ILE ILE LYS GLY SER SER LEU          
SEQRES  18 E  258  SER ASP ARG VAL GLY ILE ARG LEU SER SER GLU ALA PRO          
SEQRES  19 E  258  ALA LEU PHE GLN PHE ASP LEU LYS SER GLY PHE LEU GLN          
SEQRES  20 E  258  PHE PHE LEU ALA PRO LYS PHE ASN ASP GLU GLU                  
SEQRES   1 F   69  SER HIS ASN PRO ASP ASP THR THR VAL ASP ASN ARG PRO          
SEQRES   2 F   69  ILE ILE SER ASN ALA LYS PHE LEU ALA ASP ALA ALA MET          
SEQRES   3 F   69  LYS LYS THR GLN LYS PHE SER LYS LYS VAL LYS ASN GLU          
SEQRES   4 F   69  PRO ALA SER SER GLN MET ASP ILE PHE SER GLN LEU SER          
SEQRES   5 F   69  ARG ALA LYS LYS LYS SER LYS LEU ASN ASN GLY GLU ILE          
SEQRES   6 F   69  ILE VAL ILE ASP                                              
MODRES 3V62 MLY A   27  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3V62 MLY A   38  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3V62 MLY A   40  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3V62 MLY A   41  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3V62 MLY A   54  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3V62 MLY A   58  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3V62 MLY D   27  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3V62 MLY D   38  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3V62 MLY D   40  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3V62 MLY D   41  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3V62 MLY D   54  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3V62 MLY D   58  LYS  N-DIMETHYL-LYSINE                                  
HET    MLY  A  27      11                                                       
HET    MLY  A  38      11                                                       
HET    MLY  A  40      11                                                       
HET    MLY  A  41      11                                                       
HET    MLY  A  54      11                                                       
HET    MLY  A  58      11                                                       
HET    MLY  D  27      11                                                       
HET    MLY  D  38      11                                                       
HET    MLY  D  40      11                                                       
HET    MLY  D  41      11                                                       
HET    MLY  D  54      11                                                       
HET    MLY  D  58      11                                                       
HET    NEQ  B 301       9                                                       
HET    NEQ  B 302       9                                                       
HET    SO4  B 303       5                                                       
HET    SO4  B 304       5                                                       
HET    NEQ  E 301       9                                                       
HET    NEQ  E 302       9                                                       
HET    SO4  E 303       5                                                       
HET    SO4  E 304       5                                                       
HETNAM     MLY N-DIMETHYL-LYSINE                                                
HETNAM     NEQ N-ETHYLMALEIMIDE                                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MLY    12(C8 H18 N2 O2)                                             
FORMUL   7  NEQ    4(C6 H7 N O2)                                                
FORMUL   9  SO4    4(O4 S 2-)                                                   
FORMUL  15  HOH   *51(H2 O)                                                     
HELIX    1   1 LEU A   45  GLY A   57  1                                  13    
HELIX    2   2 GLU A   59  ASP A   61  5                                   3    
HELIX    3   3 PRO A   78  ASP A   82  5                                   5    
HELIX    4   4 GLU B    8  ASP B   21  1                                  14    
HELIX    5   5 LEU B   72  CYS B   81  1                                  10    
HELIX    6   6 ILE B  121  PHE B  125  5                                   5    
HELIX    7   7 SER B  141  SER B  155  1                                  15    
HELIX    8   8 HIS B  190  SER B  194  5                                   5    
HELIX    9   9 ALA B  209  ILE B  216  1                                   8    
HELIX   10  10 LYS B  217  LEU B  221  5                                   5    
HELIX   11  11 ASP C 1151  LYS C 1161  1                                  11    
HELIX   12  12 LEU D   45  GLY D   57  1                                  13    
HELIX   13  13 GLU D   59  ASP D   61  5                                   3    
HELIX   14  14 PRO D   78  ASP D   82  5                                   5    
HELIX   15  15 GLU E    8  ASP E   21  1                                  14    
HELIX   16  16 GLU E   55  PHE E   57  5                                   3    
HELIX   17  17 LEU E   72  CYS E   81  1                                  10    
HELIX   18  18 ILE E  121  PHE E  125  5                                   5    
HELIX   19  19 SER E  141  SER E  155  1                                  15    
HELIX   20  20 HIS E  190  SER E  194  5                                   5    
HELIX   21  21 ALA E  209  ILE E  216  1                                   8    
HELIX   22  22 LYS E  217  LEU E  221  5                                   5    
HELIX   23  23 PHE F 1153  LYS F 1161  1                                   9    
SHEET    1   A 6 ILE A  70  ARG A  71  0                                        
SHEET    2   A 6 LEU A  63  TYR A  67 -1  N  TYR A  67   O  ILE A  70           
SHEET    3   A 6 ASP A  87  ARG A  93 -1  O  GLU A  90   N  LEU A  66           
SHEET    4   A 6 ASN A  25  SER A  29  1  N  MLY A  27   O  ILE A  89           
SHEET    5   A 6 GLU A  34  MLY A  38 -1  O  PHE A  37   N  LEU A  26           
SHEET    6   A 6 ILE C1170  VAL C1172  1  O  ILE C1171   N  PHE A  36           
SHEET    1   B 5 GLU B  59  CYS B  62  0                                        
SHEET    2   B 5 LEU B   2  PHE B   6 -1  N  LYS B   5   O  GLU B  59           
SHEET    3   B 5 LEU B  88  ALA B  92 -1  O  LEU B  90   N  ALA B   4           
SHEET    4   B 5 SER B  98  ASP B 105 -1  O  ILE B 100   N  ILE B  91           
SHEET    5   B 5 ARG B 110  LYS B 117 -1  O  LEU B 116   N  ILE B  99           
SHEET    1   C 9 VAL B  66  ASP B  71  0                                        
SHEET    2   C 9 LEU B  25  LYS B  31 -1  N  VAL B  26   O  MET B  70           
SHEET    3   C 9 GLY B  34  VAL B  40 -1  O  ILE B  36   N  GLN B  29           
SHEET    4   C 9 LEU B  46  GLY B  53 -1  O  VAL B  48   N  ALA B  39           
SHEET    5   C 9 GLY B 244  LEU B 250 -1  O  PHE B 249   N  LEU B  47           
SHEET    6   C 9 ALA B 233  LEU B 241 -1  N  PHE B 237   O  PHE B 248           
SHEET    7   C 9 ARG B 224  SER B 230 -1  N  ARG B 228   O  LEU B 236           
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 8 VAL B 203  GLY B 208  0                                        
SHEET    2   D 8 SER B 157  THR B 163 -1  N  ILE B 162   O  VAL B 203           
SHEET    3   D 8 THR B 166  GLY B 173 -1  O  VAL B 170   N  ASN B 159           
SHEET    4   D 8 GLY B 176  ILE B 182 -1  O  ILE B 182   N  ILE B 167           
SHEET    5   D 8 ARG E 110  LYS E 117 -1  O  ILE E 111   N  ILE B 181           
SHEET    6   D 8 SER E  98  ASP E 105 -1  N  ILE E  99   O  LEU E 116           
SHEET    7   D 8 THR E  87  ALA E  92 -1  N  THR E  89   O  LEU E 102           
SHEET    8   D 8 LEU E   2  PHE E   6 -1  N  ALA E   4   O  LEU E  90           
SHEET    1   E 6 ILE D  70  ARG D  71  0                                        
SHEET    2   E 6 LEU D  63  TYR D  67 -1  N  TYR D  67   O  ILE D  70           
SHEET    3   E 6 ASP D  87  ARG D  93 -1  O  GLU D  90   N  LEU D  66           
SHEET    4   E 6 ASN D  25  SER D  29  1  N  MLY D  27   O  ILE D  89           
SHEET    5   E 6 GLU D  34  ILE D  39 -1  O  PHE D  37   N  LEU D  26           
SHEET    6   E 6 ILE F1170  ILE F1173  1  O  ILE F1173   N  MLY D  38           
SHEET    1   F 9 VAL E  66  ASP E  71  0                                        
SHEET    2   F 9 LEU E  25  LYS E  31 -1  N  CYS E  30   O  VAL E  66           
SHEET    3   F 9 GLY E  34  VAL E  40 -1  O  GLN E  38   N  ASN E  27           
SHEET    4   F 9 LEU E  46  GLY E  53 -1  O  ILE E  52   N  ILE E  35           
SHEET    5   F 9 GLY E 244  LEU E 250 -1  O  GLN E 247   N  SER E  49           
SHEET    6   F 9 ALA E 233  LEU E 241 -1  N  PHE E 237   O  PHE E 248           
SHEET    7   F 9 ARG E 224  SER E 230 -1  N  ARG E 228   O  LEU E 236           
SHEET    8   F 9 SER E 135  PRO E 140 -1  N  LEU E 137   O  ILE E 227           
SHEET    9   F 9 LYS E 196  MET E 199 -1  O  LYS E 196   N  SER E 138           
SHEET    1   G 4 GLY E 176  ILE E 182  0                                        
SHEET    2   G 4 THR E 166  GLY E 173 -1  N  ILE E 167   O  ILE E 182           
SHEET    3   G 4 SER E 157  THR E 163 -1  N  ASN E 159   O  VAL E 170           
SHEET    4   G 4 VAL E 203  GLY E 208 -1  O  VAL E 203   N  ILE E 162           
LINK         C   LEU A  26                 N   MLY A  27     1555   1555  1.33  
LINK         C   MLY A  27                 N   VAL A  28     1555   1555  1.33  
LINK         C   PHE A  37                 N   MLY A  38     1555   1555  1.33  
LINK         C   MLY A  38                 N   ILE A  39     1555   1555  1.34  
LINK         C   ILE A  39                 N   MLY A  40     1555   1555  1.34  
LINK         C   MLY A  40                 N   MLY A  41     1555   1555  1.34  
LINK         C   MLY A  41                 N   THR A  42     1555   1555  1.33  
LINK         C   ALA A  53                 N   MLY A  54     1555   1555  1.34  
LINK         C   MLY A  54                 N   ARG A  55     1555   1555  1.33  
LINK         C   GLY A  57                 N   MLY A  58     1555   1555  1.33  
LINK         C   MLY A  58                 N   GLU A  59     1555   1555  1.33  
LINK         C   LEU D  26                 N   MLY D  27     1555   1555  1.33  
LINK         C   MLY D  27                 N   VAL D  28     1555   1555  1.33  
LINK         C   PHE D  37                 N   MLY D  38     1555   1555  1.33  
LINK         C   MLY D  38                 N   ILE D  39     1555   1555  1.34  
LINK         C   ILE D  39                 N   MLY D  40     1555   1555  1.34  
LINK         C   MLY D  40                 N   MLY D  41     1555   1555  1.34  
LINK         C   MLY D  41                 N   THR D  42     1555   1555  1.33  
LINK         C   ALA D  53                 N   MLY D  54     1555   1555  1.34  
LINK         C   MLY D  54                 N   ARG D  55     1555   1555  1.33  
LINK         C   GLY D  57                 N   MLY D  58     1555   1555  1.33  
LINK         C   MLY D  58                 N   GLU D  59     1555   1555  1.33  
LINK         SG  CYS B  81                 C3  NEQ B 302     1555   1555  1.66  
LINK         SG  CYS E  81                 C3  NEQ E 302     1555   1555  1.66  
LINK         SG  CYS B  22                 C3  NEQ B 301     1555   1555  1.67  
LINK         SG  CYS E  22                 C3  NEQ E 301     1555   1555  1.67  
LINK         C   GLY A  98                 NZ  LYS B 164     1555   1555  1.36  
LINK         C   GLY D  98                 NZ  LYS E 164     1555   1555  1.36  
SITE     1 AC1  4 GLY B  18  PHE B  19  CYS B  22  VAL B  48                    
SITE     1 AC2  5 LYS B  77  CYS B  81  TYR B 114  GLN E 153                    
SITE     2 AC2  5 LEU E 154                                                     
SITE     1 AC3  3 SER B 138  LYS B 196  ARG B 224                               
SITE     1 AC4  2 LYS B 146  ARG B 149                                          
SITE     1 AC5  3 GLY E  18  PHE E  19  CYS E  22                               
SITE     1 AC6  5 GLN B 153  LEU B 154  LYS E  77  CYS E  81                    
SITE     2 AC6  5 TYR E 114                                                     
SITE     1 AC7  4 SER E 138  LYS E 196  ARG E 224  HOH E 408                    
SITE     1 AC8  2 LYS E 146  ARG E 149                                          
CRYST1  196.817   62.256  139.247  90.00 135.04  90.00 C 1 2 1       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      0.005081  0.000000  0.005088        0.00000                         
SCALE2      0.000000  0.016063  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010163        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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