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Database: PDB
Entry: 4UVK
LinkDB: 4UVK
Original site: 4UVK 
HEADER    CELL CYCLE                              06-AUG-14   4UVK              
TITLE     COHESIN SUBUNIT SCC3 FROM Z. ROUXII, 88-1035                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ZYRO0D15994P;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: SCC3 HIS-TAGGED, UNP RESIDUES 88-1035;                     
COMPND   5 SYNONYM: SCC3;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ZYGOSACCHAROMYCES ROUXII;                       
SOURCE   3 ORGANISM_TAXID: 4956;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_VARIANT: C41                                       
KEYWDS    CELL CYCLE, COHESIN, MITOSIS, HEAT REPEATS, SMC PROTEINS              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.B.ROIG,K.NASMYTH,J.LOWE                                             
REVDAT   3   08-OCT-14 4UVK    1       JRNL                                     
REVDAT   2   10-SEP-14 4UVK    1       JRNL                                     
REVDAT   1   20-AUG-14 4UVK    0                                                
JRNL        AUTH   M.B.ROIG,J.LOWE,K.L.CHAN,F.BECKOUET,J.METSON,K.NASMYTH       
JRNL        TITL   STRUCTURE AND FUNCTION OF COHESINS SCC3/SA REGULATORY        
JRNL        TITL 2 SUBUNIT                                                      
JRNL        REF    FEBS LETT.                    V. 588  3692 2014              
JRNL        REFN                   ISSN 0014-5793                               
JRNL        PMID   25171859                                                     
JRNL        DOI    10.1016/J.FEBSLET.2014.08.015                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.600                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.347                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.00                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.85                          
REMARK   3   NUMBER OF REFLECTIONS             : 37521                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1901                          
REMARK   3   R VALUE            (WORKING SET) : 0.1871                          
REMARK   3   FREE R VALUE                     : 0.2450                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3748                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.3556 -  7.7896    0.97     2604   135  0.1673 0.1949        
REMARK   3     2  7.7896 -  6.1870    0.98     2604   148  0.2078 0.2103        
REMARK   3     3  6.1870 -  5.4061    0.98     2633   131  0.2174 0.2697        
REMARK   3     4  5.4061 -  4.9123    0.99     2634   121  0.1716 0.2086        
REMARK   3     5  4.9123 -  4.5605    0.99     2630   161  0.1352 0.1838        
REMARK   3     6  4.5605 -  4.2918    0.99     2630   145  0.1345 0.1833        
REMARK   3     7  4.2918 -  4.0770    0.99     2605   154  0.1378 0.2076        
REMARK   3     8  4.0770 -  3.8996    0.99     2644   130  0.1605 0.2285        
REMARK   3     9  3.8996 -  3.7495    0.99     2671   124  0.1814 0.2131        
REMARK   3    10  3.7495 -  3.6202    0.99     2632   141  0.1830 0.2828        
REMARK   3    11  3.6202 -  3.5070    0.99     2637   148  0.1842 0.2734        
REMARK   3    12  3.5070 -  3.4068    0.99     2665   129  0.2068 0.2749        
REMARK   3    13  3.4068 -  3.3171    0.99     2625   133  0.1955 0.2993        
REMARK   3    14  3.3171 -  3.2362    0.99     2659   168  0.1852 0.2462        
REMARK   3    15  3.2362 -  3.1627    0.99     2642   137  0.1838 0.2445        
REMARK   3    16  3.1627 -  3.0954    0.99     2634   141  0.2064 0.2611        
REMARK   3    17  3.0954 -  3.0335    0.99     2666   111  0.2100 0.3262        
REMARK   3    18  3.0335 -  2.9762    0.99     2683   112  0.1977 0.2725        
REMARK   3    19  2.9762 -  2.9231    0.99     2576   155  0.2071 0.2423        
REMARK   3    20  2.9231 -  2.8735    0.99     2643   176  0.2242 0.3358        
REMARK   3    21  2.8735 -  2.8272    0.99     2652   137  0.2332 0.2866        
REMARK   3    22  2.8272 -  2.7837    0.99     2638   134  0.2347 0.2968        
REMARK   3    23  2.7837 -  2.7428    0.99     2642   139  0.2525 0.3297        
REMARK   3    24  2.7428 -  2.7041    0.99     2652   152  0.2418 0.3323        
REMARK   3    25  2.7041 -  2.6676    0.99     2668   140  0.2464 0.2929        
REMARK   3    26  2.6676 -  2.6329    0.99     2624   120  0.2565 0.3171        
REMARK   3    27  2.6329 -  2.6000    0.99     2701   126  0.2732 0.3379        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.98                                          
REMARK   3   K_SOL              : 0.348                                         
REMARK   3   B_SOL              : 34.010                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.35             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.13            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 52                             
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.0655                                              
REMARK   3    B22 (A**2) : 2.7290                                               
REMARK   3    B33 (A**2) : -2.6635                                              
REMARK   3    B12 (A**2) : 0.0000                                               
REMARK   3    B13 (A**2) : -0.0000                                              
REMARK   3    B23 (A**2) : -0.0000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.015           7235                                  
REMARK   3   ANGLE     :  1.549           9769                                  
REMARK   3   CHIRALITY :  0.078           1136                                  
REMARK   3   PLANARITY :  0.006           1221                                  
REMARK   3   DIHEDRAL  : 18.243           2684                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4UVK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-AUG-14.                  
REMARK 100 THE PDBE ID CODE IS EBI-61455.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS)                    
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39907                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.60                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.7                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.30                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.40                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.50                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       36.68600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       79.51450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.58800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       79.51450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.68600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.58800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A   226                                                      
REMARK 465     SER A   227                                                      
REMARK 465     ASP A   228                                                      
REMARK 465     GLU A   229                                                      
REMARK 465     ASP A   230                                                      
REMARK 465     GLU A   231                                                      
REMARK 465     SER A   232                                                      
REMARK 465     GLU A   233                                                      
REMARK 465     ILE A   234                                                      
REMARK 465     SER A   398                                                      
REMARK 465     GLN A   399                                                      
REMARK 465     HIS A   400                                                      
REMARK 465     HIS A   401                                                      
REMARK 465     ASN A   402                                                      
REMARK 465     ARG A   403                                                      
REMARK 465     ALA A   404                                                      
REMARK 465     VAL A   405                                                      
REMARK 465     ASP A   406                                                      
REMARK 465     ASN A   407                                                      
REMARK 465     LEU A   582                                                      
REMARK 465     GLU A   583                                                      
REMARK 465     THR A   584                                                      
REMARK 465     PRO A   585                                                      
REMARK 465     THR A   586                                                      
REMARK 465     TYR A   587                                                      
REMARK 465     THR A   588                                                      
REMARK 465     GLY A   589                                                      
REMARK 465     ASP A   590                                                      
REMARK 465     ASN A   591                                                      
REMARK 465     ASN A   592                                                      
REMARK 465     ASN A   593                                                      
REMARK 465     GLU A   594                                                      
REMARK 465     GLU A   595                                                      
REMARK 465     ASN A   596                                                      
REMARK 465     ASN A   597                                                      
REMARK 465     ASP A   598                                                      
REMARK 465     GLU A   599                                                      
REMARK 465     ASN A   600                                                      
REMARK 465     ASN A   601                                                      
REMARK 465     ARG A   602                                                      
REMARK 465     SER A   603                                                      
REMARK 465     ASN A   604                                                      
REMARK 465     PRO A   754                                                      
REMARK 465     ASP A   755                                                      
REMARK 465     VAL A   756                                                      
REMARK 465     GLN A   757                                                      
REMARK 465     ASP A   758                                                      
REMARK 465     THR A   759                                                      
REMARK 465     GLU A   760                                                      
REMARK 465     GLU A   839                                                      
REMARK 465     LYS A   840                                                      
REMARK 465     SER A   841                                                      
REMARK 465     SER A   842                                                      
REMARK 465     GLU A   843                                                      
REMARK 465     ASN A   844                                                      
REMARK 465     ASP A   845                                                      
REMARK 465     SER A   846                                                      
REMARK 465     PRO A   847                                                      
REMARK 465     SER A   848                                                      
REMARK 465     ASP A  1023                                                      
REMARK 465     THR A  1024                                                      
REMARK 465     ILE A  1025                                                      
REMARK 465     PHE A  1026                                                      
REMARK 465     ASP A  1027                                                      
REMARK 465     GLN A  1028                                                      
REMARK 465     ASP A  1029                                                      
REMARK 465     LYS A  1030                                                      
REMARK 465     LYS A  1031                                                      
REMARK 465     GLY A  1032                                                      
REMARK 465     ARG A  1033                                                      
REMARK 465     VAL A  1034                                                      
REMARK 465     PRO A  1035                                                      
REMARK 465     HIS A  1036                                                      
REMARK 465     HIS A  1037                                                      
REMARK 465     HIS A  1038                                                      
REMARK 465     HIS A  1039                                                      
REMARK 465     HIS A  1040                                                      
REMARK 465     HIS A  1041                                                      
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 128    CG   CD   OE1  OE2                                  
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   N    SER A    88     O    HOH A  2001              1.88            
REMARK 500   O    GLN A   103     NH1  ARG A   154              2.09            
REMARK 500   OD1  ASP A   133     O    HOH A  2017              2.17            
REMARK 500   NE   ARG A   154     O    HOH A  2019              1.98            
REMARK 500   NH2  ARG A   154     O    HOH A  2019              2.20            
REMARK 500   O    TYR A   224     O    GLY A   235              2.10            
REMARK 500   O    VAL A   225     O    HOH A  2040              2.05            
REMARK 500   N    GLY A   235     O    HOH A  2042              2.16            
REMARK 500   O    LYS A   298     N    ARG A   300              2.19            
REMARK 500   NH1  ARG A   434     O    HOH A  2083              2.09            
REMARK 500   OG1  THR A   572     O    HOH A  2102              2.10            
REMARK 500   NZ   LYS A   781     O    HOH A  2140              2.19            
REMARK 500   OG   SER A   895     O    HOH A  2165              2.14            
REMARK 500   OE2  GLU A   979     O    HOH A  2204              2.19            
REMARK 500   O    ILE A  1006     OH   TYR A  1017              2.13            
REMARK 500   O    GLU A  1022     O    HOH A  2209              2.19            
REMARK 500   O    HOH A  2025     O    HOH A  2045              2.05            
REMARK 500   O    HOH A  2034     O    HOH A  2065              2.02            
REMARK 500   O    HOH A  2040     O    HOH A  2041              2.06            
REMARK 500   O    HOH A  2055     O    HOH A  2123              2.06            
REMARK 500   O    HOH A  2085     O    HOH A  2197              1.93            
REMARK 500   O    HOH A  2152     O    HOH A  2153              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  2036     O    HOH A  2052     3556     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 396   CA  -  CB  -  CG  ANGL. DEV. =  14.9 DEGREES          
REMARK 500    LEU A 435   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    LEU A 435   CB  -  CG  -  CD1 ANGL. DEV. = -12.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 193       51.05   -141.35                                   
REMARK 500    ASP A 281      -70.87    -57.77                                   
REMARK 500    TYR A 284      -63.85   -130.99                                   
REMARK 500    GLU A 295       54.37    -93.70                                   
REMARK 500    LYS A 299       37.19     19.76                                   
REMARK 500    ARG A 300       39.84   -145.40                                   
REMARK 500    CYS A 334      -74.68   -122.97                                   
REMARK 500    PHE A 361       56.29   -150.19                                   
REMARK 500    ASP A 510        0.85     89.10                                   
REMARK 500    SER A 542      -36.67    -38.98                                   
REMARK 500    HIS A 579      174.01    168.75                                   
REMARK 500    GLU A 580       63.07    -60.77                                   
REMARK 500    PHE A 637       -1.15     76.03                                   
REMARK 500    GLN A 707       18.83     55.07                                   
REMARK 500    PHE A 799      -74.04   -114.17                                   
REMARK 500    ASP A 836       38.39    -77.54                                   
REMARK 500    ILE A 837      -72.05   -142.43                                   
REMARK 500    GLU A 852      -76.60    -74.25                                   
REMARK 500    SER A 913      -36.63    -33.13                                   
REMARK 500    GLU A 914       55.10    -93.81                                   
REMARK 500    ASP A 963      109.54    -51.57                                   
REMARK 500    TYR A 971      115.20   -162.00                                   
REMARK 500    ASP A 999       97.06    -63.92                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4UVJ   RELATED DB: PDB                                   
REMARK 900  COHESIN SUBUNIT SCC3 FROM YEAST, 674-1072                           
DBREF  4UVK A   88  1035  UNP    C5DWM3   C5DWM3_ZYGRC    88   1035             
SEQADV 4UVK HIS A 1036  UNP  C5DWM3              EXPRESSION TAG                 
SEQADV 4UVK HIS A 1037  UNP  C5DWM3              EXPRESSION TAG                 
SEQADV 4UVK HIS A 1038  UNP  C5DWM3              EXPRESSION TAG                 
SEQADV 4UVK HIS A 1039  UNP  C5DWM3              EXPRESSION TAG                 
SEQADV 4UVK HIS A 1040  UNP  C5DWM3              EXPRESSION TAG                 
SEQADV 4UVK HIS A 1041  UNP  C5DWM3              EXPRESSION TAG                 
SEQRES   1 A  954  SER LYS GLN ASP GLN GLU THR TYR LEU GLU THR ILE LYS          
SEQRES   2 A  954  ASP PHE GLN PRO THR GLU LEU PHE GLN VAL LEU ALA THR          
SEQRES   3 A  954  SER GLU ASP LEU SER ILE ASP GLU LEU LEU ARG ASP SER          
SEQRES   4 A  954  LEU GLU SER TYR SER GLN ASP ARG ASP ARG PHE LEU GLN          
SEQRES   5 A  954  GLU PHE ILE ASN LEU LEU LEU CYS CYS CYS GLY ALA ILE          
SEQRES   6 A  954  ALA ARG LEU GLU VAL HIS ASP VAL HIS SER ASN GLU SER          
SEQRES   7 A  954  SER ASN GLU THR VAL GLY GLU LEU GLN LEU LEU PHE GLN          
SEQRES   8 A  954  ARG GLN LYS VAL HIS GLU PHE HIS LEU LEU ILE SER LYS          
SEQRES   9 A  954  ASP SER LYS LYS LYS SER LYS TYR PRO PRO LEU TYR ALA          
SEQRES  10 A  954  ASN PHE VAL GLU PHE MET PHE ARG LEU MET ASP VAL ALA          
SEQRES  11 A  954  ASN ASP LEU GLN LEU LEU TYR VAL GLU SER ASP GLU ASP          
SEQRES  12 A  954  GLU SER GLU ILE GLY THR GLY PRO LEU ILE ILE ASP LEU          
SEQRES  13 A  954  LEU THR TRP LEU SER PRO LEU SER VAL CYS LYS ILE ARG          
SEQRES  14 A  954  SER LEU ARG TYR ILE ALA THR LEU THR LEU TYR LEU PHE          
SEQRES  15 A  954  GLN ASP PHE LEU THR ASP HIS VAL VAL ASP LEU ASP LYS          
SEQRES  16 A  954  ASN TYR LEU SER LYS LEU SER LYS GLN LEU SER VAL GLU          
SEQRES  17 A  954  ASN LYS LYS LYS ARG PRO ASN GLY LYS THR VAL GLU LYS          
SEQRES  18 A  954  LEU GLU SER THR ILE ALA GLU ILE GLN SER SER LYS MET          
SEQRES  19 A  954  VAL THR GLN GLY ILE ILE ASP ASN ILE ILE LYS LEU CYS          
SEQRES  20 A  954  PHE VAL HIS ARG PHE LYS ASP VAL ASP GLU THR ILE ARG          
SEQRES  21 A  954  CYS GLU SER MET VAL HIS LEU ALA SER TRP THR LYS SER          
SEQRES  22 A  954  PHE PRO GLU TYR PHE LEU LYS VAL THR PHE LEU LYS TYR          
SEQRES  23 A  954  PHE GLY TRP LEU LEU SER ASP SER SER VAL THR VAL ARG          
SEQRES  24 A  954  LEU GLN VAL LEU LYS ILE LEU PRO GLN LEU ILE SER GLN          
SEQRES  25 A  954  HIS HIS ASN ARG ALA VAL ASP ASN SER ALA VAL ARG GLN          
SEQRES  26 A  954  PHE PHE GLU ARG PHE LYS GLU ARG ILE LEU GLU ILE ALA          
SEQRES  27 A  954  LEU LYS ASP SER ASN LEU GLU VAL ARG LEU SER ALA VAL          
SEQRES  28 A  954  GLN VAL LEU VAL GLU VAL ALA SER LEU GLY TYR LEU GLU          
SEQRES  29 A  954  ASP THR GLU ILE LEU SER ILE SER SER LEU ILE PHE GLU          
SEQRES  30 A  954  ASP ASN GLU ILE LYS VAL SER SER LEU GLY LYS ASN SER          
SEQRES  31 A  954  ARG TYR LEU ALA SER VAL ALA LYS PHE PHE ALA CYS ILE          
SEQRES  32 A  954  THR GLU GLU LYS PHE GLN GLU PHE THR ASN ASN ARG VAL          
SEQRES  33 A  954  LEU PRO LYS GLU LEU PHE ASP VAL LYS GLY SER SER ALA          
SEQRES  34 A  954  VAL ARG ILE GLY ILE PHE MET ASN LEU LEU ASN GLU SER          
SEQRES  35 A  954  LEU THR GLU TYR LEU GLN LYS VAL PRO GLN ILE GLY SER          
SEQRES  36 A  954  GLU LYS ARG ILE HIS ILE LEU PHE GLN ALA ALA GLU PHE          
SEQRES  37 A  954  LEU TYR PRO TYR PHE GLY SER LEU ILE LYS ASP ILE CYS          
SEQRES  38 A  954  LYS VAL LEU THR PHE GLU GLY GLU PHE THR HIS GLU SER          
SEQRES  39 A  954  LEU GLU THR PRO THR TYR THR GLY ASP ASN ASN ASN GLU          
SEQRES  40 A  954  GLU ASN ASN ASP GLU ASN ASN ARG SER ASN LEU LEU LEU          
SEQRES  41 A  954  PRO THR ASP SER ASN ASN ILE ILE LEU TYR VAL THR THR          
SEQRES  42 A  954  LEU HIS GLY LEU ALA TYR GLY GLY THR HIS MET ARG GLY          
SEQRES  43 A  954  GLN PRO LYS PHE LYS VAL ALA GLU ALA VAL LEU PRO HIS          
SEQRES  44 A  954  LEU ASP GLN LEU ILE LYS ARG LEU PRO ILE GLU SER SER          
SEQRES  45 A  954  ASN VAL LEU ALA SER ILE LEU GLY VAL PHE ASN LEU PHE          
SEQRES  46 A  954  ALA PHE GLU ASP TRP ILE HIS THR GLY TYR GLU LYS ASP          
SEQRES  47 A  954  ILE ARG LYS ILE LEU GLU LYS ILE ILE LYS ALA PHE ASN          
SEQRES  48 A  954  GLU SER THR LEU THR SER GLY ALA GLN ASP LEU LYS TYR          
SEQRES  49 A  954  LYS SER PHE SER GLU THR VAL SER GLN VAL ARG LYS LEU          
SEQRES  50 A  954  GLY PHE ASN GLU LEU ASP GLU LEU TRP LEU ASN HIS ILE          
SEQRES  51 A  954  SER GLN LEU LYS ILE HIS LEU GLY LYS PHE LEU GLU GLU          
SEQRES  52 A  954  LYS LEU HIS PRO ASP VAL GLN ASP THR GLU ASN ASP GLU          
SEQRES  53 A  954  ASN MET ASN THR LEU TYR GLY VAL PHE LEU ASN LYS LEU          
SEQRES  54 A  954  ALA LEU LEU GLY LYS VAL TYR PRO ILE GLU PHE GLN GLU          
SEQRES  55 A  954  ASN LEU LEU SER LEU PHE LEU ASN ARG PHE VAL GLN ARG          
SEQRES  56 A  954  LEU PRO GLN ILE GLY VAL HIS CYS GLN LEU GLU THR ILE          
SEQRES  57 A  954  GLN GLU ILE HIS LEU LYS LEU LEU ALA LEU LEU THR THR          
SEQRES  58 A  954  TRP GLN LEU GLN LYS TRP VAL ASP ILE LEU GLU LYS SER          
SEQRES  59 A  954  SER GLU ASN ASP SER PRO SER PRO VAL SER GLU PHE SER          
SEQRES  60 A  954  LEU ARG THR VAL SER SER ILE VAL LYS SER PHE LYS VAL          
SEQRES  61 A  954  ILE PHE ASP ALA LEU SER SER ASP THR ASN ASP ASN ASP          
SEQRES  62 A  954  GLY THR LEU GLY ASP PHE LEU LEU LYS TRP SER THR SER          
SEQRES  63 A  954  ASN SER PHE ILE ASP ILE ILE ILE SER LEU LYS VAL PHE          
SEQRES  64 A  954  GLU LEU GLY VAL ALA GLU SER GLU LYS SER TRP ARG HIS          
SEQRES  65 A  954  ALA LEU ARG GLU ASN PHE VAL PRO TYR VAL THR ASP SER          
SEQRES  66 A  954  ALA ASN GLN VAL LEU LEU LYS VAL PHE LEU TYR LEU GLU          
SEQRES  67 A  954  SER LEU PHE ALA ASN GLU SER SER GLU HIS LEU ASP ARG          
SEQRES  68 A  954  ASN PRO GLN GLU ASP VAL ASN LEU ASN ASP ILE LYS TYR          
SEQRES  69 A  954  ASP GLY PHE GLY ASP GLY CYS GLU LYS GLU LEU LEU LEU          
SEQRES  70 A  954  PHE THR ILE LYS LEU LYS GLY LEU MET LYS LEU GLY LEU          
SEQRES  71 A  954  LEU ASP GLU ALA LEU PHE SER ARG ILE ALA LEU ASN LYS          
SEQRES  72 A  954  GLU LYS LEU GLY PRO LEU TYR ALA LYS VAL ILE GLU ASP          
SEQRES  73 A  954  THR ILE PHE ASP GLN ASP LYS LYS GLY ARG VAL PRO HIS          
SEQRES  74 A  954  HIS HIS HIS HIS HIS                                          
FORMUL   2  HOH   *209(H2 O)                                                    
HELIX    1   1 SER A   88  LYS A  100  1                                  13    
HELIX    2   2 THR A  105  SER A  114  1                                  10    
HELIX    3   3 SER A  118  ASP A  133  1                                  16    
HELIX    4   4 ASP A  133  CYS A  149  1                                  17    
HELIX    5   5 GLU A  156  HIS A  161  5                                   6    
HELIX    6   6 SER A  162  GLU A  164  5                                   3    
HELIX    7   7 SER A  165  GLN A  180  1                                  16    
HELIX    8   8 PHE A  185  SER A  193  1                                   9    
HELIX    9   9 LYS A  194  SER A  197  5                                   4    
HELIX   10  10 PRO A  201  LEU A  220  1                                  20    
HELIX   11  11 GLY A  237  VAL A  252  1                                  16    
HELIX   12  12 ILE A  255  TYR A  284  1                                  30    
HELIX   13  13 TYR A  284  VAL A  294  1                                  11    
HELIX   14  14 LYS A  304  CYS A  334  1                                  31    
HELIX   15  15 CYS A  334  PHE A  339  1                                   6    
HELIX   16  16 ASP A  343  PHE A  361  1                                  19    
HELIX   17  17 PHE A  361  LEU A  366  1                                   6    
HELIX   18  18 LYS A  367  LEU A  378  1                                  12    
HELIX   19  19 SER A  382  ILE A  397  1                                  16    
HELIX   20  20 SER A  408  ASP A  428  1                                  21    
HELIX   21  21 ASN A  430  LEU A  447  1                                  18    
HELIX   22  22 GLU A  451  SER A  460  1                                  10    
HELIX   23  23 LEU A  461  PHE A  463  5                                   3    
HELIX   24  24 GLY A  474  ASN A  500  1                                  27    
HELIX   25  25 GLY A  513  LYS A  536  1                                  24    
HELIX   26  26 GLY A  541  GLY A  561  1                                  21    
HELIX   27  27 LEU A  563  PHE A  573  1                                  11    
HELIX   28  28 ASP A  610  MET A  631  1                                  22    
HELIX   29  29 PHE A  637  LEU A  654  1                                  18    
HELIX   30  30 SER A  658  ASN A  670  1                                  13    
HELIX   31  31 ALA A  673  THR A  680  1                                   8    
HELIX   32  32 TYR A  682  LYS A  684  5                                   3    
HELIX   33  33 ASP A  685  SER A  700  1                                  16    
HELIX   34  34 ASP A  708  GLY A  725  1                                  18    
HELIX   35  35 PHE A  726  LEU A  752  1                                  27    
HELIX   36  36 ASN A  761  PHE A  772  1                                  12    
HELIX   37  37 PHE A  772  LYS A  781  1                                  10    
HELIX   38  38 GLN A  788  PHE A  799  1                                  12    
HELIX   39  39 ARG A  802  HIS A  809  1                                   8    
HELIX   40  40 GLN A  811  GLU A  817  1                                   7    
HELIX   41  41 LEU A  820  ASP A  836  1                                  17    
HELIX   42  42 SER A  851  SER A  874  1                                  24    
HELIX   43  43 THR A  882  LEU A  908  1                                  27    
HELIX   44  44 SER A  916  VAL A  926  1                                  11    
HELIX   45  45 THR A  930  SER A  952  1                                  23    
HELIX   46  46 ASP A  963  ILE A  969  5                                   7    
HELIX   47  47 GLY A  977  LEU A  995  1                                  19    
HELIX   48  48 ASP A  999  SER A 1004  1                                   6    
HELIX   49  49 ARG A 1005  LEU A 1008  5                                   4    
HELIX   50  50 ASN A 1009  LEU A 1013  5                                   5    
HELIX   51  51 GLY A 1014  GLU A 1022  1                                   9    
SHEET    1  AA 2 GLU A 507  LEU A 508  0                                        
SHEET    2  AA 2 VAL A 511  LYS A 512 -1  O  VAL A 511   N  LEU A 508           
CISPEP   1 LYS A  297    LYS A  298          0         6.76                     
CISPEP   2 VAL A  926    PRO A  927          0        -9.29                     
CRYST1   73.372  109.176  159.029  90.00  90.00  90.00 P 21 21 21    4          
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      0.013629  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009160  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006288        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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