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Database: PDB
Entry: 2WX0
LinkDB: 2WX0
Original site: 2WX0 
HEADER    PROTEIN BINDING                         30-OCT-09   2WX0              
TITLE     TAB2 NZF DOMAIN IN COMPLEX WITH LYS63-LINKED DI-UBIQUITIN,            
TITLE    2 P21                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN;                                                 
COMPND   3 CHAIN: A, B, E, F;                                                   
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE             
COMPND   6  7-INTERACTING PROTEIN 2;                                            
COMPND   7 CHAIN: C, G;                                                         
COMPND   8 FRAGMENT: TAB2 NZF DOMAIN, RESIDUES 663-693;                         
COMPND   9 SYNONYM: TAK1-BINDING PROTEIN 2;                                     
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   4 ORGANISM_TAXID: 9913;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_TAXID: 9606;                                                
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN BINDING, ISOPEPTIDE BOND, NZF DOMAIN, ZINC-FINGER,            
KEYWDS   2 METAL-BINDING                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.KULATHU,M.AKUTSU,A.BREMM,K.HOFMANN,D.KOMANDER                       
REVDAT   4   11-MAY-11 2WX0    1       JRNL   REMARK SEQRES                     
REVDAT   3   02-FEB-10 2WX0    1       KEYWDS REMARK                            
REVDAT   2   08-DEC-09 2WX0    1       JRNL   ATOM                              
REVDAT   1   24-NOV-09 2WX0    0                                                
JRNL        AUTH   Y.KULATHU,M.AKUTSU,A.BREMM,K.HOFMANN,D.KOMANDER              
JRNL        TITL   TWO-SIDED UBIQUITIN BINDING EXPLAINS SPECIFICITY             
JRNL        TITL 2 OF THE TAB2 NZF DOMAIN                                       
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  16  1328 2009              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   19935683                                                     
JRNL        DOI    10.1038/NSMB.1731                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 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) : 2.400                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.799                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.02                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.46                          
REMARK   3   NUMBER OF REFLECTIONS             : 16855                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1769                          
REMARK   3   R VALUE            (WORKING SET) : 0.1736                          
REMARK   3   FREE R VALUE                     : 0.2359                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 857                             
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 38.8039 -  4.3594    0.99     2859   175  0.1428 0.1872        
REMARK   3     2  4.3594 -  3.4609    0.99     2822   151  0.1433 0.2008        
REMARK   3     3  3.4609 -  3.0236    0.97     2788   126  0.1825 0.2405        
REMARK   3     4  3.0236 -  2.7472    0.93     2645   137  0.2039 0.3160        
REMARK   3     5  2.7472 -  2.5504    0.90     2529   136  0.2091 0.3068        
REMARK   3     6  2.5504 -  2.4000    0.83     2355   132  0.2332 0.3188        
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              : 0.374                                         
REMARK   3   B_SOL              : 53.740                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.34             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.30            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 9.4250                                               
REMARK   3    B22 (A**2) : -7.4187                                              
REMARK   3    B33 (A**2) : -2.0063                                              
REMARK   3    B12 (A**2) : -0.0000                                              
REMARK   3    B13 (A**2) : -2.6818                                              
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      :  0.007           2832                                  
REMARK   3   ANGLE     :  1.099           3821                                  
REMARK   3   CHIRALITY :  0.071            448                                  
REMARK   3   PLANARITY :  0.004            494                                  
REMARK   3   DIHEDRAL  : 18.200           1092                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  16.0963  12.8195   8.6830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1280 T22:   0.1000                                     
REMARK   3      T33:   0.0215 T12:   0.0511                                     
REMARK   3      T13:  -0.0229 T23:   0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1213 L22:   2.1313                                     
REMARK   3      L33:   1.9330 L12:  -0.3432                                     
REMARK   3      L13:  -0.1543 L23:   0.1744                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0489 S12:   0.2542 S13:  -0.0701                       
REMARK   3      S21:  -0.5081 S22:  -0.0398 S23:   0.0010                       
REMARK   3      S31:   0.1571 S32:  -0.0723 S33:  -0.0038                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  14.2603  -6.6852  30.7969              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1725 T22:   0.1884                                     
REMARK   3      T33:   0.2467 T12:  -0.1364                                     
REMARK   3      T13:  -0.1116 T23:   0.1392                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7063 L22:   2.9118                                     
REMARK   3      L33:   3.3923 L12:  -0.3849                                     
REMARK   3      L13:   0.5596 L23:  -3.0685                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2749 S12:  -0.1069 S13:  -0.1488                       
REMARK   3      S21:  -0.7891 S22:   0.5437 S23:   0.7190                       
REMARK   3      S31:   0.8100 S32:  -0.6666 S33:  -0.5410                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  25.0581   8.1746  26.4847              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1712 T22:   0.1036                                     
REMARK   3      T33:   0.1569 T12:  -0.0364                                     
REMARK   3      T13:  -0.0351 T23:   0.0273                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1153 L22:   0.4530                                     
REMARK   3      L33:   1.0688 L12:  -0.8129                                     
REMARK   3      L13:  -1.1671 L23:   0.2749                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1264 S12:   0.3536 S13:  -0.0099                       
REMARK   3      S21:  -0.0138 S22:  -0.2279 S23:  -0.0974                       
REMARK   3      S31:  -0.2057 S32:  -0.0266 S33:   0.0627                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN E                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -12.7104  -2.0520   8.8730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2831 T22:   0.2359                                     
REMARK   3      T33:   0.1222 T12:   0.1616                                     
REMARK   3      T13:   0.0478 T23:   0.0155                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8344 L22:   1.6597                                     
REMARK   3      L33:   1.0576 L12:  -1.4183                                     
REMARK   3      L13:   0.4551 L23:  -0.2404                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4312 S12:   0.5803 S13:   0.3048                       
REMARK   3      S21:  -0.7218 S22:  -0.4586 S23:  -0.1682                       
REMARK   3      S31:   0.1752 S32:   0.0660 S33:   0.0851                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN F                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.1623  17.0427  28.8386              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0648 T22:   0.1033                                     
REMARK   3      T33:   0.2404 T12:  -0.0384                                     
REMARK   3      T13:  -0.0155 T23:  -0.0400                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1662 L22:   1.9802                                     
REMARK   3      L33:   1.5077 L12:  -0.1756                                     
REMARK   3      L13:   0.3252 L23:   0.9593                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0310 S12:  -0.0938 S13:  -0.0267                       
REMARK   3      S21:  -0.0132 S22:   0.1888 S23:  -0.2867                       
REMARK   3      S31:  -0.0797 S32:   0.1403 S33:  -0.1425                       
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 2WX0 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-NOV-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-41587.                                       
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               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18032                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.40                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.90                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.4                                
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.90                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.58                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.00                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.7                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       36.81000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -0.2 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.3 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G                               
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     LEU A    73                                                      
REMARK 465     ARG A    74                                                      
REMARK 465     GLY A    75                                                      
REMARK 465     GLY A    76                                                      
REMARK 465     ARG B    74                                                      
REMARK 465     GLY B    75                                                      
REMARK 465     GLY B    76                                                      
REMARK 465     LEU E    73                                                      
REMARK 465     ARG E    74                                                      
REMARK 465     GLY E    75                                                      
REMARK 465     GLY E    76                                                      
REMARK 465     ARG F    74                                                      
REMARK 465     GLY F    75                                                      
REMARK 465     GLY F    76                                                      
REMARK 465     ASP G   663                                                      
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     LEU B  73    CG   CD1  CD2                                       
REMARK 470     ASP C 663    CG   OD1  OD2                                       
REMARK 470     ARG E  72    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU F  73    CG   CD1  CD2                                       
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   OE2  GLU A    16     OE2  GLU E    16     2555     2.14            
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    LYS A  63      130.53    -37.61                                   
REMARK 500    GLU B  64        1.89     85.81                                   
REMARK 500    THR C 674      -10.34     79.19                                   
REMARK 500    SER F  20        2.39    -68.05                                   
REMARK 500    LYS F  63      120.46    -34.39                                   
REMARK 500    THR G 674       -1.38     75.94                                   
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 C1694  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 673   SG                                                     
REMARK 620 2 CYS C 687   SG  123.6                                              
REMARK 620 3 CYS C 670   SG  117.0  97.3                                        
REMARK 620 4 CYS C 684   SG  105.4 110.3 101.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G1694  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G 670   SG                                                     
REMARK 620 2 CYS G 673   SG  112.9                                              
REMARK 620 3 CYS G 684   SG   97.5  99.1                                        
REMARK 620 4 CYS G 687   SG   97.7 132.1 112.9                                  
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 C1694                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN G1694                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2C7M   RELATED DB: PDB                                   
REMARK 900  COMPLEX OF HUMAN RABEX-5 RESIDUES 1-74                              
REMARK 900  IN COMPLEX WITH UBIQUITIN                                           
REMARK 900 RELATED ID: 1YD8   RELATED DB: PDB                                   
REMARK 900  COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN                      
REMARK 900 RELATED ID: 1E0Q   RELATED DB: PDB                                   
REMARK 900  MUTANT PEPTIDE FROM THE FIRST N-TERMINAL                            
REMARK 900  17 AMINO-ACID OF UBIQUITIN                                          
REMARK 900 RELATED ID: 2C7N   RELATED DB: PDB                                   
REMARK 900  HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX                              
REMARK 900  WITH UBIQUITIN                                                      
REMARK 900 RELATED ID: 2FIF   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF A BOVINE RABEX-5                               
REMARK 900  FRAGMENT COMPLEXEDWITH UBIQUITIN                                    
REMARK 900 RELATED ID: 2D3G   RELATED DB: PDB                                   
REMARK 900  DOUBLE SIDED UBIQUITIN BINDING OF HRS-UIM                           
REMARK 900 RELATED ID: 1V80   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURES OF UBIQUITIN AT 30 BAR                          
REMARK 900  AND 3 KBAR                                                          
REMARK 900 RELATED ID: 1P3Q   RELATED DB: PDB                                   
REMARK 900  MECHANISM OF UBIQUITIN RECOGNITION BY THE                           
REMARK 900  CUE DOMAIN OF VPS9                                                  
REMARK 900 RELATED ID: 1WR6   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF GGA3 GAT DOMAIN IN                             
REMARK 900  COMPLEX WITHUBIQUITIN                                               
REMARK 900 RELATED ID: 2FID   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF A BOVINE RABEX-5                               
REMARK 900  FRAGMENT COMPLEXEDWITH UBIQUITIN                                    
REMARK 900 RELATED ID: 1V81   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURES OF UBIQUITIN AT 30 BAR                          
REMARK 900  AND 3 KBAR                                                          
REMARK 900 RELATED ID: 1AAR   RELATED DB: PDB                                   
REMARK 900  DI-UBIQUITIN                                                        
REMARK 900 RELATED ID: 1UZX   RELATED DB: PDB                                   
REMARK 900  A COMPLEX OF THE VPS23 UEV WITH UBIQUITIN                           
REMARK 900 RELATED ID: 1WRD   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF TOM1 GAT DOMAIN IN                             
REMARK 900  COMPLEX WITHUBIQUITIN                                               
REMARK 900 RELATED ID: 2WX1   RELATED DB: PDB                                   
REMARK 900  TAB2 NZF DOMAIN IN COMPLEX WITH LYS63-                              
REMARK 900  LINKED TRI-UBIQUITIN, P212121                                       
REMARK 900 RELATED ID: 2WWZ   RELATED DB: PDB                                   
REMARK 900  TAB2 NZF DOMAIN IN COMPLEX WITH LYS63-                              
REMARK 900  LINKED DI-UBIQUITIN, P212121                                        
DBREF  2WX0 A    1    76  UNP    P62990   UBIQ_BOVIN       1     76             
DBREF  2WX0 B    1    76  UNP    P62990   UBIQ_BOVIN       1     76             
DBREF  2WX0 C  663   693  UNP    Q9NYJ8   TAB2_HUMAN     663    693             
DBREF  2WX0 E    1    76  UNP    P62990   UBIQ_BOVIN       1     76             
DBREF  2WX0 F    1    76  UNP    P62990   UBIQ_BOVIN       1     76             
DBREF  2WX0 G  663   693  UNP    Q9NYJ8   TAB2_HUMAN     663    693             
SEQRES   1 A   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 A   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 A   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 A   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 A   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 A   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 B   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 B   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 B   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 B   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 B   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 B   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 C   31  ASP GLU GLY ALA GLN TRP ASN CYS THR ALA CYS THR PHE          
SEQRES   2 C   31  LEU ASN HIS PRO ALA LEU ILE ARG CYS GLU GLN CYS GLU          
SEQRES   3 C   31  MET PRO ARG HIS PHE                                          
SEQRES   1 E   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 E   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 E   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 E   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 E   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 E   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 F   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 F   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 F   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 F   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 F   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 F   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 G   31  ASP GLU GLY ALA GLN TRP ASN CYS THR ALA CYS THR PHE          
SEQRES   2 G   31  LEU ASN HIS PRO ALA LEU ILE ARG CYS GLU GLN CYS GLU          
SEQRES   3 G   31  MET PRO ARG HIS PHE                                          
HET     ZN  C1694       1                                                       
HET     ZN  G1694       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   7   ZN    2(ZN 2+)                                                     
FORMUL   8  HOH   *103(H2 O)                                                    
HELIX    1   1 THR A   22  GLY A   35  1                                  14    
HELIX    2   2 PRO A   37  ASP A   39  5                                   3    
HELIX    3   3 THR B   22  GLY B   35  1                                  14    
HELIX    4   4 PRO B   37  ASP B   39  5                                   3    
HELIX    5   5 LEU B   56  ASN B   60  5                                   5    
HELIX    6   6 THR E   22  GLY E   35  1                                  14    
HELIX    7   7 PRO E   37  ASP E   39  5                                   3    
HELIX    8   8 THR F   22  GLY F   35  1                                  14    
HELIX    9   9 PRO F   37  ASP F   39  5                                   3    
HELIX   10  10 LEU F   56  ASN F   60  5                                   5    
SHEET    1  AA 5 THR A  12  GLU A  16  0                                        
SHEET    2  AA 5 GLN A   2  THR A   7 -1  O  ILE A   3   N  LEU A  15           
SHEET    3  AA 5 THR A  66  LEU A  71  1  O  LEU A  67   N  LYS A   6           
SHEET    4  AA 5 GLN A  41  PHE A  45 -1  O  ARG A  42   N  VAL A  70           
SHEET    5  AA 5 LYS A  48  GLN A  49 -1  O  LYS A  48   N  PHE A  45           
SHEET    1  BA 5 THR B  12  GLU B  16  0                                        
SHEET    2  BA 5 GLN B   2  THR B   7 -1  O  ILE B   3   N  LEU B  15           
SHEET    3  BA 5 THR B  66  LEU B  71  1  O  LEU B  67   N  LYS B   6           
SHEET    4  BA 5 GLN B  41  PHE B  45 -1  O  ARG B  42   N  VAL B  70           
SHEET    5  BA 5 LYS B  48  GLN B  49 -1  O  LYS B  48   N  PHE B  45           
SHEET    1  CA 2 TRP C 668  ASN C 669  0                                        
SHEET    2  CA 2 LEU C 676  ASN C 677 -1  O  ASN C 677   N  TRP C 668           
SHEET    1  EA 5 THR E  12  GLU E  16  0                                        
SHEET    2  EA 5 GLN E   2  THR E   7 -1  O  ILE E   3   N  LEU E  15           
SHEET    3  EA 5 THR E  66  LEU E  71  1  O  LEU E  67   N  LYS E   6           
SHEET    4  EA 5 GLN E  41  PHE E  45 -1  O  ARG E  42   N  VAL E  70           
SHEET    5  EA 5 LYS E  48  GLN E  49 -1  O  LYS E  48   N  PHE E  45           
SHEET    1  FA 5 THR F  12  GLU F  16  0                                        
SHEET    2  FA 5 GLN F   2  LYS F   6 -1  O  ILE F   3   N  LEU F  15           
SHEET    3  FA 5 THR F  66  LEU F  71  1  O  LEU F  67   N  LYS F   6           
SHEET    4  FA 5 GLN F  41  PHE F  45 -1  O  ARG F  42   N  VAL F  70           
SHEET    5  FA 5 LYS F  48  GLN F  49 -1  O  LYS F  48   N  PHE F  45           
SHEET    1  GA 2 TRP G 668  ASN G 669  0                                        
SHEET    2  GA 2 LEU G 676  ASN G 677 -1  O  ASN G 677   N  TRP G 668           
LINK        ZN    ZN C1694                 SG  CYS C 673     1555   1555  2.31  
LINK        ZN    ZN C1694                 SG  CYS C 687     1555   1555  2.37  
LINK        ZN    ZN C1694                 SG  CYS C 670     1555   1555  2.38  
LINK        ZN    ZN C1694                 SG  CYS C 684     1555   1555  2.41  
LINK        ZN    ZN G1694                 SG  CYS G 673     1555   1555  2.17  
LINK        ZN    ZN G1694                 SG  CYS G 684     1555   1555  2.42  
LINK        ZN    ZN G1694                 SG  CYS G 687     1555   1555  2.32  
LINK        ZN    ZN G1694                 SG  CYS G 670     1555   1555  2.40  
SITE     1 AC1  4 CYS C 670  CYS C 673  CYS C 684  CYS C 687                    
SITE     1 AC2  4 CYS G 670  CYS G 673  CYS G 684  CYS G 687                    
CRYST1   55.390   73.620   59.250  90.00 105.91  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018054  0.000000  0.005146        0.00000                         
SCALE2      0.000000  0.013583  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017550        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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