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Database: PDB
Entry: 3OLM
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Original site: 3OLM 
HEADER    LIGASE                                  26-AUG-10   3OLM              
TITLE     STRUCTURE AND FUNCTION OF A UBIQUITIN BINDING SITE WITHIN THE         
TITLE    2 CATALYTIC DOMAIN OF A HECT UBIQUITIN LIGASE                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RSP5;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: WW3 AND HECT DOMAIN;                                       
COMPND   5 SYNONYM: REVERSES SPT-PHENOTYPE PROTEIN 5;                           
COMPND   6 EC: 6.3.2.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: UBIQUITIN;                                                 
COMPND  10 CHAIN: D;                                                            
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: YEAST;                                              
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: RSP5, MDP1, NPI1, YER125W, SYGP-ORF41;                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  10 ORGANISM_COMMON: YEAST;                                              
SOURCE  11 ORGANISM_TAXID: 4932;                                                
SOURCE  12 GENE: UBI4, SCD2, YLL039C;                                           
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    UBIQUITIN E3 LIGASE, LIGASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.C.KIM,A.STEFFEN,J.CHEN,J.M.HUIBREGTSE                               
REVDAT   3   25-SEP-13 3OLM    1       REMARK VERSN                             
REVDAT   2   13-APR-11 3OLM    1       JRNL                                     
REVDAT   1   23-MAR-11 3OLM    0                                                
JRNL        AUTH   H.C.KIM,A.M.STEFFEN,M.L.OLDHAM,J.CHEN,J.M.HUIBREGTSE         
JRNL        TITL   STRUCTURE AND FUNCTION OF A HECT DOMAIN UBIQUITIN-BINDING    
JRNL        TITL 2 SITE.                                                        
JRNL        REF    EMBO REP.                     V.  12   334 2011              
JRNL        REFN                   ISSN 1469-221X                               
JRNL        PMID   21399621                                                     
JRNL        DOI    10.1038/EMBOR.2011.23                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 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-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.09                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 71.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 14421                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 718                             
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 42.0907 -  4.2651    1.00     3922   218  0.1946 0.2393        
REMARK   3     2  4.2651 -  3.3858    0.99     3800   195  0.2080 0.2630        
REMARK   3     3  3.3858 -  2.9579    0.79     3036   146  0.2564 0.3353        
REMARK   3     4  2.9579 -  2.6875    0.51     1957    97  0.2885 0.3698        
REMARK   3     5  2.6875 -  2.4949    0.26      988    62  0.2990 0.3195        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.32                                          
REMARK   3   B_SOL              : 33.73                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.220           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.76                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.74640                                             
REMARK   3    B22 (A**2) : -1.65350                                             
REMARK   3    B33 (A**2) : 3.39990                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.61810                                              
REMARK   3    B23 (A**2) : -0.00000                                             
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      :  0.002           4112                                  
REMARK   3   ANGLE     :  0.488           5554                                  
REMARK   3   CHIRALITY :  0.038            595                                  
REMARK   3   PLANARITY :  0.001            725                                  
REMARK   3   DIHEDRAL  : 14.903           1539                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (chain A and resid 385:427)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -55.9213   7.2548 -37.5414              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0571 T22:  -0.4545                                     
REMARK   3      T33:   0.0156 T12:  -0.0518                                     
REMARK   3      T13:  -0.0447 T23:  -0.0372                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0002 L22:   0.0049                                     
REMARK   3      L33:  -0.0097 L12:  -0.0013                                     
REMARK   3      L13:   0.0107 L23:   0.0034                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0339 S12:   0.0368 S13:   0.0089                       
REMARK   3      S21:   0.0066 S22:  -0.0006 S23:   0.0127                       
REMARK   3      S31:   0.0410 S32:   0.1157 S33:  -0.0345                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (chain A and resid 428:469)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -36.6119   8.0638 -19.2273              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2820 T22:   0.5015                                     
REMARK   3      T33:   0.9746 T12:   0.0009                                     
REMARK   3      T13:   0.0662 T23:  -0.0707                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0982 L22:   0.0462                                     
REMARK   3      L33:   0.0596 L12:   0.0319                                     
REMARK   3      L13:   0.0135 L23:  -0.0281                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1457 S12:  -0.0446 S13:  -0.1411                       
REMARK   3      S21:  -0.1492 S22:  -0.0519 S23:   0.3423                       
REMARK   3      S31:   0.0445 S32:  -0.0509 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (chain A and resid 470:552)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -29.6839  16.8019  -9.0273              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1544 T22:   0.4347                                     
REMARK   3      T33:   0.1239 T12:   0.0428                                     
REMARK   3      T13:   0.1232 T23:   0.1986                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4029 L22:   0.4952                                     
REMARK   3      L33:   0.6013 L12:   0.1163                                     
REMARK   3      L13:   0.2131 L23:   0.1668                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0326 S12:  -0.4409 S13:  -0.0907                       
REMARK   3      S21:   0.1922 S22:   0.0147 S23:   0.1430                       
REMARK   3      S31:  -0.2087 S32:  -0.2030 S33:  -0.2042                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (chain A and resid 553:689)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -10.9867  12.3634 -18.2854              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.5792 T22:  -0.3282                                     
REMARK   3      T33:  -0.0943 T12:   0.2390                                     
REMARK   3      T13:  -0.0783 T23:   0.3056                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4014 L22:   0.2098                                     
REMARK   3      L33:   0.0514 L12:  -0.2681                                     
REMARK   3      L13:   0.1753 L23:  -0.0651                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1181 S12:  -0.2712 S13:  -0.1914                       
REMARK   3      S21:   0.0357 S22:   0.0736 S23:   0.1682                       
REMARK   3      S31:   0.0065 S32:  -0.0695 S33:   0.3555                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (chain A and resid 690:804)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -47.0555  28.4026 -28.3862              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0435 T22:  -0.5517                                     
REMARK   3      T33:   0.0643 T12:   0.1377                                     
REMARK   3      T13:  -0.1689 T23:  -0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1930 L22:   1.1960                                     
REMARK   3      L33:  -0.1043 L12:  -0.7401                                     
REMARK   3      L13:   0.0088 L23:  -0.4460                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1160 S12:  -0.0893 S13:   0.1299                       
REMARK   3      S21:   0.3370 S22:   0.1923 S23:  -0.2538                       
REMARK   3      S31:  -0.1506 S32:   0.0578 S33:   0.2093                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (chain D and resid 1:74)                               
REMARK   3    ORIGIN FOR THE GROUP (A): -16.4727  35.9852   2.8035              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3788 T22:   1.2990                                     
REMARK   3      T33:   0.7157 T12:  -0.0161                                     
REMARK   3      T13:   0.0440 T23:  -0.4546                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0295 L22:   0.1110                                     
REMARK   3      L33:   0.0381 L12:   0.0100                                     
REMARK   3      L13:   0.0060 L23:  -0.0197                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0464 S12:  -0.3172 S13:   0.2662                       
REMARK   3      S21:   0.5109 S22:  -0.0248 S23:  -0.3521                       
REMARK   3      S31:  -0.2548 S32:   0.1520 S33:  -0.0003                       
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 3OLM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061270.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03326                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED         
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14422                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 75.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 33.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: 1ND7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13.5% PEG 4000, 0.2M MAGNESIUM           
REMARK 280  CHLORIDE, 0.1M TRIS-HCL PH 9.0, VAPOR DIFFUSION, SITTING DROP,      
REMARK 280  TEMPERATURE 293K                                                    
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       80.78500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.16550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       80.78500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       25.16550            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A   381                                                      
REMARK 465     ASN A   382                                                      
REMARK 465     ALA A   383                                                      
REMARK 465     SER A   384                                                      
REMARK 465     GLY A   493                                                      
REMARK 465     LEU A   494                                                      
REMARK 465     ASP A   495                                                      
REMARK 465     TYR A   496                                                      
REMARK 465     GLY A   497                                                      
REMARK 465     GLY A   498                                                      
REMARK 465     VAL A   499                                                      
REMARK 465     SER A   500                                                      
REMARK 465     GLY A   805                                                      
REMARK 465     PHE A   806                                                      
REMARK 465     GLY A   807                                                      
REMARK 465     GLN A   808                                                      
REMARK 465     GLU A   809                                                      
REMARK 465     SER D    -2                                                      
REMARK 465     ASN D    -1                                                      
REMARK 465     ALA D     0                                                      
REMARK 465     GLY D    75                                                      
REMARK 465     GLY D    76                                                      
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     ARG D  74    CG   CD   NE   CZ   NH1  NH2                        
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    ASN A 463       40.11   -157.59                                   
REMARK 500    ARG A 483      130.88    -33.94                                   
REMARK 500    ALA A 523     -135.09     69.95                                   
REMARK 500    TYR A 524       74.36   -159.41                                   
REMARK 500    ASP A 525      -60.71    178.85                                   
REMARK 500    TYR A 527       48.09   -105.82                                   
REMARK 500    PRO A 539       -0.45    -57.66                                   
REMARK 500    ILE A 652      -65.95    -99.49                                   
REMARK 500    THR A 677        1.78    -66.99                                   
REMARK 500    HIS A 702       46.69   -107.77                                   
REMARK 500    SER D  19       31.35    -75.93                                   
REMARK 500    ASN D  60       47.30     35.82                                   
REMARK 500    LEU D  73      -86.08   -125.92                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3OLM A  384   809  UNP    P39940   RSP5_YEAST     384    809             
DBREF  3OLM D    1    76  UNP    P0CG63   UBI4P_YEAST      1     76             
SEQADV 3OLM SER A  381  UNP  P39940              EXPRESSION TAG                 
SEQADV 3OLM ASN A  382  UNP  P39940              EXPRESSION TAG                 
SEQADV 3OLM ALA A  383  UNP  P39940              EXPRESSION TAG                 
SEQADV 3OLM SER D   -2  UNP  P0CG63              EXPRESSION TAG                 
SEQADV 3OLM ASN D   -1  UNP  P0CG63              EXPRESSION TAG                 
SEQADV 3OLM ALA D    0  UNP  P0CG63              EXPRESSION TAG                 
SEQRES   1 A  429  SER ASN ALA SER GLN LEU GLY PRO LEU PRO SER GLY TRP          
SEQRES   2 A  429  GLU MET ARG LEU THR ASN THR ALA ARG VAL TYR PHE VAL          
SEQRES   3 A  429  ASP HIS ASN THR LYS THR THR THR TRP ASP ASP PRO ARG          
SEQRES   4 A  429  LEU PRO SER SER LEU ASP GLN ASN VAL PRO GLN TYR LYS          
SEQRES   5 A  429  ARG ASP PHE ARG ARG LYS VAL ILE TYR PHE ARG SER GLN          
SEQRES   6 A  429  PRO ALA LEU ARG ILE LEU PRO GLY GLN CYS HIS ILE LYS          
SEQRES   7 A  429  VAL ARG ARG LYS ASN ILE PHE GLU ASP ALA TYR GLN GLU          
SEQRES   8 A  429  ILE MET ARG GLN THR PRO GLU ASP LEU LYS LYS ARG LEU          
SEQRES   9 A  429  MET ILE LYS PHE ASP GLY GLU GLU GLY LEU ASP TYR GLY          
SEQRES  10 A  429  GLY VAL SER ARG GLU PHE PHE PHE LEU LEU SER HIS GLU          
SEQRES  11 A  429  MET PHE ASN PRO PHE TYR CYS LEU PHE GLU TYR SER ALA          
SEQRES  12 A  429  TYR ASP ASN TYR THR ILE GLN ILE ASN PRO ASN SER GLY          
SEQRES  13 A  429  ILE ASN PRO GLU HIS LEU ASN TYR PHE LYS PHE ILE GLY          
SEQRES  14 A  429  ARG VAL VAL GLY LEU GLY VAL PHE HIS ARG ARG PHE LEU          
SEQRES  15 A  429  ASP ALA PHE PHE VAL GLY ALA LEU TYR LYS MET MET LEU          
SEQRES  16 A  429  ARG LYS LYS VAL VAL LEU GLN ASP MET GLU GLY VAL ASP          
SEQRES  17 A  429  ALA GLU VAL TYR ASN SER LEU ASN TRP MET LEU GLU ASN          
SEQRES  18 A  429  SER ILE ASP GLY VAL LEU ASP LEU THR PHE SER ALA ASP          
SEQRES  19 A  429  ASP GLU ARG PHE GLY GLU VAL VAL THR VAL ASP LEU LYS          
SEQRES  20 A  429  PRO ASP GLY ARG ASN ILE GLU VAL THR ASP GLY ASN LYS          
SEQRES  21 A  429  LYS GLU TYR VAL GLU LEU TYR THR GLN TRP ARG ILE VAL          
SEQRES  22 A  429  ASP ARG VAL GLN GLU GLN PHE LYS ALA PHE MET ASP GLY          
SEQRES  23 A  429  PHE ASN GLU LEU ILE PRO GLU ASP LEU VAL THR VAL PHE          
SEQRES  24 A  429  ASP GLU ARG GLU LEU GLU LEU LEU ILE GLY GLY ILE ALA          
SEQRES  25 A  429  GLU ILE ASP ILE GLU ASP TRP LYS LYS HIS THR ASP TYR          
SEQRES  26 A  429  ARG GLY TYR GLN GLU SER ASP GLU VAL ILE GLN TRP PHE          
SEQRES  27 A  429  TRP LYS CYS VAL SER GLU TRP ASP ASN GLU GLN ARG ALA          
SEQRES  28 A  429  ARG LEU LEU GLN PHE THR THR GLY THR SER ARG ILE PRO          
SEQRES  29 A  429  VAL ASN GLY PHE LYS ASP LEU GLN GLY SER ASP GLY PRO          
SEQRES  30 A  429  ARG ARG PHE THR ILE GLU LYS ALA GLY GLU VAL GLN GLN          
SEQRES  31 A  429  LEU PRO LYS SER HIS THR CYS PHE ASN ARG VAL ASP LEU          
SEQRES  32 A  429  PRO GLN TYR VAL ASP TYR ASP SER MET LYS GLN LYS LEU          
SEQRES  33 A  429  THR LEU ALA VAL GLU GLU THR ILE GLY PHE GLY GLN GLU          
SEQRES   1 D   79  SER ASN ALA MET GLN ILE PHE VAL LYS THR LEU THR GLY          
SEQRES   2 D   79  LYS THR ILE THR LEU GLU VAL GLU SER SER ASP THR ILE          
SEQRES   3 D   79  ASP ASN VAL LYS SER LYS ILE GLN ASP LYS GLU GLY ILE          
SEQRES   4 D   79  PRO PRO ASP GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN          
SEQRES   5 D   79  LEU GLU ASP GLY ARG THR LEU SER ASP TYR ASN ILE GLN          
SEQRES   6 D   79  LYS GLU SER THR LEU HIS LEU VAL LEU ARG LEU ARG GLY          
SEQRES   7 D   79  GLY                                                          
FORMUL   3  HOH   *51(H2 O)                                                     
HELIX    1   1 PRO A  429  SER A  444  1                                  16    
HELIX    2   2 GLN A  445  ARG A  449  5                                   5    
HELIX    3   3 ASN A  463  GLN A  475  1                                  13    
HELIX    4   4 THR A  476  LYS A  481  1                                   6    
HELIX    5   5 ARG A  501  PHE A  512  1                                  12    
HELIX    6   6 ASN A  513  CYS A  517  5                                   5    
HELIX    7   7 PRO A  533  ASN A  538  5                                   6    
HELIX    8   8 GLU A  540  HIS A  558  1                                  19    
HELIX    9   9 VAL A  567  LEU A  575  1                                   9    
HELIX   10  10 VAL A  580  ASP A  588  1                                   9    
HELIX   11  11 ASP A  588  LEU A  599  1                                  12    
HELIX   12  12 ASP A  629  ILE A  633  5                                   5    
HELIX   13  13 ASN A  639  VAL A  653  1                                  15    
HELIX   14  14 VAL A  656  GLU A  669  1                                  14    
HELIX   15  15 PRO A  672  THR A  677  1                                   6    
HELIX   16  16 ASP A  680  GLY A  689  1                                  10    
HELIX   17  17 ASP A  695  HIS A  702  1                                   8    
HELIX   18  18 ASP A  712  TRP A  725  1                                  14    
HELIX   19  19 ASP A  726  GLY A  739  1                                  14    
HELIX   20  20 GLY A  747  ASP A  750  5                                   4    
HELIX   21  21 THR A  776  PHE A  778  5                                   3    
HELIX   22  22 ASP A  788  THR A  803  1                                  16    
HELIX   23  23 THR D   22  GLY D   35  1                                  14    
SHEET    1   A 2 PHE A 405  ASP A 407  0                                        
SHEET    2   A 2 THR A 412  THR A 414 -1  O  THR A 412   N  ASP A 407           
SHEET    1   B 2 CYS A 455  ARG A 460  0                                        
SHEET    2   B 2 LEU A 484  ASP A 489  1  O  LYS A 487   N  ILE A 457           
SHEET    1   C 2 PHE A 519  TYR A 521  0                                        
SHEET    2   C 2 ILE A 529  ILE A 531 -1  O  GLN A 530   N  GLU A 520           
SHEET    1   D 2 SER A 612  ARG A 617  0                                        
SHEET    2   D 2 GLU A 620  ASP A 625 -1  O  GLU A 620   N  ARG A 617           
SHEET    1   E 4 THR A 703  ARG A 706  0                                        
SHEET    2   E 4 PHE A 760  GLU A 763  1  O  PHE A 760   N  ASP A 704           
SHEET    3   E 4 ARG A 780  ASP A 782  1  O  VAL A 781   N  THR A 761           
SHEET    4   E 4 LYS A 773  HIS A 775 -1  N  LYS A 773   O  ASP A 782           
SHEET    1   F 2 GLN A 752  GLY A 753  0                                        
SHEET    2   F 2 GLY A 756  PRO A 757 -1  O  GLY A 756   N  GLY A 753           
SHEET    1   G 4 THR D  12  GLU D  16  0                                        
SHEET    2   G 4 GLN D   2  LYS D   6 -1  N  ILE D   3   O  LEU D  15           
SHEET    3   G 4 THR D  66  LEU D  71  1  O  LEU D  67   N  PHE D   4           
SHEET    4   G 4 GLN D  41  ILE D  44 -1  N  ILE D  44   O  HIS D  68           
CRYST1  161.570   50.331   79.684  90.00 116.72  90.00 C 1 2 1       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      0.006189  0.000000  0.003116        0.00000                         
SCALE2      0.000000  0.019868  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014050        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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