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Database: PDB
Entry: 5WHG
LinkDB: 5WHG
Original site: 5WHG 
HEADER    DNA BINDING PROTEIN                     17-JUL-17   5WHG              
TITLE     VMS1 MITOCHONDRIAL LOCALIZATION CORE                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN VMS1;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: VCP/CDC48-ASSOCIATED MITOCHONDRIAL STRESS-RESPONSIVE PROTEIN
COMPND   5 1;                                                                   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE   3 S288C);                                                              
SOURCE   4 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   5 ORGANISM_TAXID: 559292;                                              
SOURCE   6 STRAIN: ATCC 204508 / S288C;                                         
SOURCE   7 GENE: VMS1, YDR049W;                                                 
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ROS SIGNALLING, OXIDATIVE STRESS, MITOCHONDRIAL QUALITY CONTROL, DNA  
KEYWDS   2 BINDING PROTEIN                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.K.FREDRICKSON,H.L.SCHUBERT,J.RUTTER,C.P.HILL                        
REVDAT   3   01-JAN-20 5WHG    1       REMARK                                   
REVDAT   2   29-NOV-17 5WHG    1       JRNL                                     
REVDAT   1   15-NOV-17 5WHG    0                                                
JRNL        AUTH   J.R.NIELSON,E.K.FREDRICKSON,T.C.WALLER,O.Z.RENDON,           
JRNL        AUTH 2 H.L.SCHUBERT,Z.LIN,C.P.HILL,J.RUTTER                         
JRNL        TITL   STEROL OXIDATION MEDIATES STRESS-RESPONSIVE VMS1             
JRNL        TITL 2 TRANSLOCATION TO MITOCHONDRIA.                               
JRNL        REF    MOL. CELL                     V.  68   673 2017              
JRNL        REFN                   ISSN 1097-4164                               
JRNL        PMID   29149595                                                     
JRNL        DOI    10.1016/J.MOLCEL.2017.10.022                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1_2575                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.06                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 10237                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.250                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1041                            
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 24.0629 -  6.4641    0.99     1198   133  0.2151 0.2753        
REMARK   3     2  6.4641 -  5.1473    1.00     1188   140  0.2075 0.2758        
REMARK   3     3  5.1473 -  4.5014    1.00     1191   134  0.1479 0.2019        
REMARK   3     4  4.5014 -  4.0921    1.00     1238   140  0.1466 0.1911        
REMARK   3     5  4.0921 -  3.8000    1.00     1200   144  0.1585 0.2040        
REMARK   3     6  3.8000 -  3.5767    1.00     1202   144  0.1837 0.2439        
REMARK   3     7  3.5767 -  3.3981    1.00     1198   136  0.1849 0.2641        
REMARK   3     8  3.3981 -  3.2505    1.00     1212   138  0.2072 0.2807        
REMARK   3     9  3.2505 -  3.1257    1.00     1181   133  0.2012 0.2628        
REMARK   3    10  3.1257 -  3.0180    1.00     1188   140  0.1777 0.2257        
REMARK   3    11  3.0180 -  2.9238    1.00     1234   128  0.1879 0.2709        
REMARK   3    12  2.9238 -  2.8404    1.00     1207   132  0.2126 0.2690        
REMARK   3    13  2.8404 -  2.7657    1.00     1182   134  0.2708 0.3314        
REMARK   3    14  2.7657 -  2.6983    1.00     1200   144  0.3056 0.3589        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.360            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.710           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 88.91                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 106.4                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.008           1770                                  
REMARK   3   ANGLE     :  0.972           2378                                  
REMARK   3   CHIRALITY :  0.049            264                                  
REMARK   3   PLANARITY :  0.006            294                                  
REMARK   3   DIHEDRAL  : 13.175           1068                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  26.7007  17.3242  58.6358              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7968 T22:   0.5182                                     
REMARK   3      T33:   0.7214 T12:   0.1991                                     
REMARK   3      T13:   0.0109 T23:  -0.0998                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2558 L22:   5.6072                                     
REMARK   3      L33:   6.9590 L12:  -1.5529                                     
REMARK   3      L13:  -0.1731 L23:  -0.8464                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0352 S12:  -0.2923 S13:   0.1191                       
REMARK   3      S21:   0.6443 S22:   0.3049 S23:  -0.0146                       
REMARK   3      S31:  -0.6603 S32:  -0.0663 S33:  -0.2648                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: REFINED AGAINST I+,SIGI+, I-, SIGI-       
REMARK   4                                                                      
REMARK   4 5WHG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229005.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-AUG-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97862                            
REMARK 200  MONOCHROMATOR                  : SI(III)                            
REMARK 200  OPTICS                         : RH COATED FLAT                     
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10237                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 10.30                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 66.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.76300                            
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: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22-24% PEG MME 2000, 100 MM TRIS PH      
REMARK 280  8.5, AND 0.2 M TMAO, EVAPORATION, TEMPERATURE 286K                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      102.92200            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       51.46100            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       51.46100            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      102.92200            
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     GLY A    -3                                                      
REMARK 465     ALA A    -2                                                      
REMARK 465     MSE A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     MSE A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     LYS A     8                                                      
REMARK 465     MSE A     9                                                      
REMARK 465     THR A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     PHE A    68                                                      
REMARK 465     ASP A    69                                                      
REMARK 465     ASN A    70                                                      
REMARK 465     VAL A    71                                                      
REMARK 465     MSE A    72                                                      
REMARK 465     ARG A    73                                                      
REMARK 465     PHE A    81                                                      
REMARK 465     ASP A    82                                                      
REMARK 465     SER A    83                                                      
REMARK 465     ARG A    84                                                      
REMARK 465     ASN A    85                                                      
REMARK 465     GLU A    86                                                      
REMARK 465     GLN A    87                                                      
REMARK 465     LYS A    88                                                      
REMARK 465     ALA A    89                                                      
REMARK 465     LEU A   107                                                      
REMARK 465     ASP A   108                                                      
REMARK 465     ILE A   109                                                      
REMARK 465     LEU A   110                                                      
REMARK 465     SER A   111                                                      
REMARK 465     VAL A   112                                                      
REMARK 465     GLU A   113                                                      
REMARK 465     GLU A   114                                                      
REMARK 465     PHE A   115                                                      
REMARK 465     ASP A   116                                                      
REMARK 465     ALA A   117                                                      
REMARK 465     LEU A   118                                                      
REMARK 465     ILE A   119                                                      
REMARK 465     SER A   120                                                      
REMARK 465     LYS A   121                                                      
REMARK 465     GLU A   122                                                      
REMARK 465     HIS A   123                                                      
REMARK 465     GLY A   124                                                      
REMARK 465     ILE A   125                                                      
REMARK 465     LYS A   126                                                      
REMARK 465     SER A   127                                                      
REMARK 465     GLU A   128                                                      
REMARK 465     ASP A   129                                                      
REMARK 465     GLU A   130                                                      
REMARK 465     ASN A   131                                                      
REMARK 465     SER A   132                                                      
REMARK 465     GLY A   133                                                      
REMARK 465     GLY A   134                                                      
REMARK 465     GLU A   135                                                      
REMARK 465     GLN A   136                                                      
REMARK 465     THR A   137                                                      
REMARK 465     SER A   138                                                      
REMARK 465     SER A   139                                                      
REMARK 465     ASP A   140                                                      
REMARK 465     HIS A   141                                                      
REMARK 465     GLU A   142                                                      
REMARK 465     GLU A   143                                                      
REMARK 465     SER A   144                                                      
REMARK 465     GLU A   145                                                      
REMARK 465     GLU A   146                                                      
REMARK 465     ALA A   147                                                      
REMARK 465     SER A   148                                                      
REMARK 465     ASP A   149                                                      
REMARK 465     ARG A   150                                                      
REMARK 465     ASP A   151                                                      
REMARK 465     PRO A   152                                                      
REMARK 465     ASP A   153                                                      
REMARK 465     LEU A   154                                                      
REMARK 465     GLN A   155                                                      
REMARK 465     THR A   156                                                      
REMARK 465     ASN A   157                                                      
REMARK 465     ASN A   158                                                      
REMARK 465     TYR A   159                                                      
REMARK 465     MSE A   160                                                      
REMARK 465     GLU A   161                                                      
REMARK 465     THR A   162                                                      
REMARK 465     ILE A   163                                                      
REMARK 465     ILE A   164                                                      
REMARK 465     GLU A   165                                                      
REMARK 465     ASN A   166                                                      
REMARK 465     ASP A   167                                                      
REMARK 465     LEU A   168                                                      
REMARK 465     GLN A   169                                                      
REMARK 465     LYS A   170                                                      
REMARK 465     LEU A   171                                                      
REMARK 465     GLY A   172                                                      
REMARK 465     PHE A   173                                                      
REMARK 465     GLN A   174                                                      
REMARK 465     LYS A   175                                                      
REMARK 465     ASP A   176                                                      
REMARK 465     GLU A   177                                                      
REMARK 465     SER A   178                                                      
REMARK 465     ASP A   179                                                      
REMARK 465     ALA A   180                                                      
REMARK 465     ILE A   181                                                      
REMARK 465     SER A   182                                                      
REMARK 465     HIS A   183                                                      
REMARK 465     ILE A   184                                                      
REMARK 465     ASN A   185                                                      
REMARK 465     THR A   186                                                      
REMARK 465     GLN A   187                                                      
REMARK 465     LEU A   198                                                      
REMARK 465     GLN A   199                                                      
REMARK 465     LYS A   200                                                      
REMARK 465     ASN A   201                                                      
REMARK 465     GLU A   202                                                      
REMARK 465     VAL A   258                                                      
REMARK 465     LYS A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     ASN A   261                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     HIS A   263                                                      
REMARK 465     LYS A   264                                                      
REMARK 465     LYS A   265                                                      
REMARK 465     ASP A   266                                                      
REMARK 465     THR A   287                                                      
REMARK 465     ARG A   288                                                      
REMARK 465     ARG A   289                                                      
REMARK 465     LYS A   290                                                      
REMARK 465     GLN A   291                                                      
REMARK 465     GLY A   292                                                      
REMARK 465     GLY A   293                                                      
REMARK 465     SER A   294                                                      
REMARK 465     GLN A   295                                                      
REMARK 465     SER A   296                                                      
REMARK 465     ALA A   297                                                      
REMARK 465     MSE A   298                                                      
REMARK 465     ASP A   299                                                      
REMARK 465     ASN A   300                                                      
REMARK 465     ALA A   301                                                      
REMARK 465     LYS A   302                                                      
REMARK 465     GLY A   303                                                      
REMARK 465     LYS A   304                                                      
REMARK 465     ALA A   305                                                      
REMARK 465     ASN A   306                                                      
REMARK 465     SER A   307                                                      
REMARK 465     ALA A   308                                                      
REMARK 465     GLY A   309                                                      
REMARK 465     SER A   310                                                      
REMARK 465     ALA A   311                                                      
REMARK 465     LEU A   312                                                      
REMARK 465     ARG A   313                                                      
REMARK 465     ARG A   314                                                      
REMARK 465     TYR A   315                                                      
REMARK 465     ASN A   316                                                      
REMARK 465     GLU A   317                                                      
REMARK 465     PRO A   398                                                      
REMARK 465     GLU A   399                                                      
REMARK 465     PRO A   400                                                      
REMARK 465     LEU A   401                                                      
REMARK 465     ALA A   402                                                      
REMARK 465     VAL A   403                                                      
REMARK 465     LYS A   404                                                      
REMARK 465     GLU A   405                                                      
REMARK 465     THR A   406                                                      
REMARK 465     VAL A   407                                                      
REMARK 465     GLN A   408                                                      
REMARK 465     LYS A   409                                                      
REMARK 465     LEU A   410                                                      
REMARK 465     GLU A   411                                                      
REMARK 465     VAL A   412                                                      
REMARK 465     SER A   413                                                      
REMARK 465     ASN A   414                                                      
REMARK 465     LYS A   415                                                      
REMARK 465     LYS A   416                                                      
REMARK 465     ASP A   417                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  22       39.83   -157.80                                   
REMARK 500    TYR A  91      -18.45   -151.27                                   
REMARK 500    SER A 195      -85.48   -174.62                                   
REMARK 500    LEU A 256     -158.71   -130.05                                   
REMARK 500    ASP A 356       91.78    -69.66                                   
REMARK 500    THR A 358     -154.97   -119.64                                   
REMARK 500    PRO A 371       27.14    -76.08                                   
REMARK 500    ASN A 375     -133.54    -90.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  74   SG                                                     
REMARK 620 2 CYS A  77   SG   88.2                                              
REMARK 620 3 HIS A  90   NE2 108.3  88.0                                        
REMARK 620 4 HIS A  96   ND1 110.7 141.1 115.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 501                  
DBREF  5WHG A    1   417  UNP    Q04311   VMS1_YEAST       1    417             
SEQADV 5WHG GLY A   -3  UNP  Q04311              EXPRESSION TAG                 
SEQADV 5WHG ALA A   -2  UNP  Q04311              EXPRESSION TAG                 
SEQADV 5WHG MSE A   -1  UNP  Q04311              EXPRESSION TAG                 
SEQADV 5WHG GLY A    0  UNP  Q04311              EXPRESSION TAG                 
SEQADV 5WHG     A       UNP  Q04311    SER    38 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    THR    39 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    LEU    40 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    ARG    41 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    GLU    42 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    VAL    43 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    GLU    44 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    VAL    45 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    GLU    46 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    LYS    47 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    THR    48 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    SER    49 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    ASP    50 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    ASN    51 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    ASP    52 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    ARG    53 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    ASN    54 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    LYS    55 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    GLU    56 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    SER    57 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    GLY    58 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    ASP    59 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    LEU    60 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    GLN    61 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    ILE    62 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    ALA    63 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    ARG    64 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    LYS    65 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    LYS    66 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    VAL    67 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    THR    68 DELETION                       
SEQADV 5WHG     A       UNP  Q04311    SER    69 DELETION                       
SEQRES   1 A  389  GLY ALA MSE GLY MSE ASN SER GLN LYS ALA SER LYS MSE          
SEQRES   2 A  389  THR GLY SER LEU LYS LYS ASN ASP LEU TYR ILE PHE ASP          
SEQRES   3 A  389  LEU SER GLU GLN LEU LEU ASN SER LEU LYS LEU MSE SER          
SEQRES   4 A  389  PHE ASP ASN VAL MSE ARG CYS SER VAL CYS GLN MSE SER          
SEQRES   5 A  389  PHE ASP SER ARG ASN GLU GLN LYS ALA HIS TYR GLN THR          
SEQRES   6 A  389  ASP TYR HIS LEU MSE ASN VAL LYS ARG ASN LEU ARG GLY          
SEQRES   7 A  389  LEU ASP ILE LEU SER VAL GLU GLU PHE ASP ALA LEU ILE          
SEQRES   8 A  389  SER LYS GLU HIS GLY ILE LYS SER GLU ASP GLU ASN SER          
SEQRES   9 A  389  GLY GLY GLU GLN THR SER SER ASP HIS GLU GLU SER GLU          
SEQRES  10 A  389  GLU ALA SER ASP ARG ASP PRO ASP LEU GLN THR ASN ASN          
SEQRES  11 A  389  TYR MSE GLU THR ILE ILE GLU ASN ASP LEU GLN LYS LEU          
SEQRES  12 A  389  GLY PHE GLN LYS ASP GLU SER ASP ALA ILE SER HIS ILE          
SEQRES  13 A  389  ASN THR GLN SER PRO TYR ILE TYR PHE LYS SER LYS TYR          
SEQRES  14 A  389  LEU GLN LYS ASN GLU VAL LEU ALA ILE TYR LYS SER LEU          
SEQRES  15 A  389  PHE ASN LYS ARG SER LEU SER ASN PRO ASN GLU ALA LEU          
SEQRES  16 A  389  THR PHE TRP ASN SER GLN GLU ASN PRO MSE ALA ILE SER          
SEQRES  17 A  389  ALA LEU PHE MSE VAL GLY GLY GLY HIS PHE ALA GLY ALA          
SEQRES  18 A  389  ILE VAL SER HIS GLN ARG LEU ASN VAL LYS GLY ASN ALA          
SEQRES  19 A  389  HIS LYS LYS ASP GLU THR LEU ILE GLU GLN ALA VAL ASN          
SEQRES  20 A  389  PHE LEU GLU HIS LYS THR PHE HIS ARG TYR THR THR ARG          
SEQRES  21 A  389  ARG LYS GLN GLY GLY SER GLN SER ALA MSE ASP ASN ALA          
SEQRES  22 A  389  LYS GLY LYS ALA ASN SER ALA GLY SER ALA LEU ARG ARG          
SEQRES  23 A  389  TYR ASN GLU SER ALA LEU LYS THR ASP ILE GLN GLY VAL          
SEQRES  24 A  389  LEU LYS ASP TRP GLU PRO TYR LEU SER LYS CYS ASP ASN          
SEQRES  25 A  389  ILE PHE ILE ARG ALA ARG ASN VAL SER ASP LYS LYS ILE          
SEQRES  26 A  389  PHE THR ASP ASN THR VAL LEU ASN LYS GLY ASP GLU ARG          
SEQRES  27 A  389  ILE LYS SER PHE PRO PHE THR THR ASN ARG PRO THR VAL          
SEQRES  28 A  389  LEU GLU LEU LYS LYS ALA TRP CYS GLU LEU SER TYR LEU          
SEQRES  29 A  389  LYS ILE LEU PRO LYS PRO GLU PRO LEU ALA VAL LYS GLU          
SEQRES  30 A  389  THR VAL GLN LYS LEU GLU VAL SER ASN LYS LYS ASP              
MODRES 5WHG MSE A   34  MET  MODIFIED RESIDUE                                   
MODRES 5WHG MSE A   79  MET  MODIFIED RESIDUE                                   
MODRES 5WHG MSE A   98  MET  MODIFIED RESIDUE                                   
MODRES 5WHG MSE A  233  MET  MODIFIED RESIDUE                                   
MODRES 5WHG MSE A  240  MET  MODIFIED RESIDUE                                   
HET    MSE  A  34       8                                                       
HET    MSE  A  79       8                                                       
HET    MSE  A  98       8                                                       
HET    MSE  A 233       8                                                       
HET    MSE  A 240       8                                                       
HET     ZN  A 501       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      ZN ZINC ION                                                         
FORMUL   1  MSE    5(C5 H11 N O2 SE)                                            
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  HOH   *29(H2 O)                                                     
HELIX    1 AA1 LYS A   14  TYR A   19  5                                   6    
HELIX    2 AA2 SER A   24  LEU A   31  1                                   8    
HELIX    3 AA3 THR A   93  ARG A  105  1                                  13    
HELIX    4 AA4 SER A  209  PHE A  211  5                                   3    
HELIX    5 AA5 ASN A  218  ASN A  227  1                                  10    
HELIX    6 AA6 THR A  268  ALA A  273  1                                   6    
HELIX    7 AA7 ALA A  319  TRP A  331  1                                  13    
HELIX    8 AA8 TRP A  331  LYS A  337  1                                   7    
HELIX    9 AA9 ASN A  347  LYS A  352  1                                   6    
HELIX   10 AB1 ILE A  353  THR A  355  5                                   3    
HELIX   11 AB2 THR A  378  TYR A  391  1                                  14    
SHEET    1 AA1 4 LYS A  32  LEU A  33  0                                        
SHEET    2 AA1 4 TYR A 190  LYS A 194 -1  O  LYS A 194   N  LYS A  32           
SHEET    3 AA1 4 LEU A 204  TYR A 207 -1  O  LEU A 204   N  PHE A 193           
SHEET    4 AA1 4 LYS A 393  ILE A 394 -1  O  LYS A 393   N  ALA A 205           
SHEET    1 AA2 5 ASN A 275  HIS A 283  0                                        
SHEET    2 AA2 5 HIS A 245  SER A 252 -1  N  SER A 252   O  ASN A 275           
SHEET    3 AA2 5 ILE A 235  GLY A 242 -1  N  SER A 236   O  VAL A 251           
SHEET    4 AA2 5 ILE A 341  ARG A 344  1  O  PHE A 342   N  PHE A 239           
SHEET    5 AA2 5 ILE A 367  LYS A 368  1  O  LYS A 368   N  ILE A 341           
LINK         C   LEU A  33                 N   MSE A  34     1555   1555  1.33  
LINK         C   MSE A  34                 N   SER A  35     1555   1555  1.33  
LINK         SG  CYS A  74                ZN    ZN A 501     1555   1555  2.41  
LINK         SG  CYS A  77                ZN    ZN A 501     1555   1555  2.33  
LINK         C   GLN A  78                 N   MSE A  79     1555   1555  1.34  
LINK         C   MSE A  79                 N   SER A  80     1555   1555  1.33  
LINK         NE2 HIS A  90                ZN    ZN A 501     1555   1555  2.60  
LINK         ND1 HIS A  96                ZN    ZN A 501     1555   1555  1.89  
LINK         C   LEU A  97                 N   MSE A  98     1555   1555  1.33  
LINK         C   MSE A  98                 N   ASN A  99     1555   1555  1.33  
LINK         C   PRO A 232                 N   MSE A 233     1555   1555  1.33  
LINK         C   MSE A 233                 N   ALA A 234     1555   1555  1.33  
LINK         C   PHE A 239                 N   MSE A 240     1555   1555  1.33  
LINK         C   MSE A 240                 N   VAL A 241     1555   1555  1.33  
SITE     1 AC1  4 CYS A  74  CYS A  77  HIS A  90  HIS A  96                    
CRYST1   62.864   62.864  154.383  90.00  90.00 120.00 P 32 2 1      6          
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      0.015907  0.009184  0.000000        0.00000                         
SCALE2      0.000000  0.018368  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006477        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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