GenomeNet

Database: PDB
Entry: 2WWZ
LinkDB: 2WWZ
Original site: 2WWZ 
HEADER    PROTEIN BINDING                         30-OCT-09   2WWZ              
TITLE     TAB2 NZF DOMAIN IN COMPLEX WITH LYS63-LINKED DI-UBIQUITIN, P212121    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN;                                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 7-          
COMPND   6 INTERACTING PROTEIN 2;                                               
COMPND   7 CHAIN: C;                                                            
COMPND   8 FRAGMENT: TAB2 NZF DOMAIN, RESIDUES 662-693;                         
COMPND   9 SYNONYM: TAK1-BINDING PROTEIN 2;                                     
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_TAXID: 9913;                                                
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   6 ORGANISM_COMMON: HUMAN;                                              
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, METAL-     
KEYWDS   2 BINDING                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.KULATHU,M.AKUTSU,A.BREMM,K.HOFMANN,D.KOMANDER                       
REVDAT   5   31-JUL-19 2WWZ    1       REMARK LINK                              
REVDAT   4   11-MAY-11 2WWZ    1       JRNL   REMARK                            
REVDAT   3   02-FEB-10 2WWZ    1       KEYWDS REMARK                            
REVDAT   2   08-DEC-09 2WWZ    1       JRNL                                     
REVDAT   1   24-NOV-09 2WWZ    0                                                
JRNL        AUTH   Y.KULATHU,M.AKUTSU,A.BREMM,K.HOFMANN,D.KOMANDER              
JRNL        TITL   TWO-SIDED UBIQUITIN BINDING EXPLAINS SPECIFICITY OF THE TAB2 
JRNL        TITL 2 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.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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 : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.19                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.030                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 28619                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1453                            
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 22.1960 -  3.0140    0.99     3096   194  0.1708 0.1813        
REMARK   3     2  3.0140 -  2.3932    1.00     2989   161  0.1759 0.2062        
REMARK   3     3  2.3932 -  2.0909    0.99     2957   149  0.1660 0.1980        
REMARK   3     4  2.0909 -  1.8999    0.98     2878   168  0.1630 0.2086        
REMARK   3     5  1.8999 -  1.7638    0.96     2871   128  0.1731 0.2157        
REMARK   3     6  1.7638 -  1.6598    0.95     2733   161  0.1742 0.1959        
REMARK   3     7  1.6598 -  1.5767    0.93     2766   144  0.1874 0.2376        
REMARK   3     8  1.5767 -  1.5081    0.90     2624   142  0.1993 0.2135        
REMARK   3     9  1.5081 -  1.4500    0.82     2382   110  0.2314 0.2546        
REMARK   3    10  1.4500 -  1.4000    0.64     1870    96  0.2659 0.2970        
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              : 0.40                                          
REMARK   3   B_SOL              : 44.08                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.420           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.23                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.18410                                             
REMARK   3    B22 (A**2) : 2.11490                                              
REMARK   3    B33 (A**2) : -0.93080                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           1546                                  
REMARK   3   ANGLE     :  1.082           2107                                  
REMARK   3   CHIRALITY :  0.071            245                                  
REMARK   3   PLANARITY :  0.005            277                                  
REMARK   3   DIHEDRAL  : 15.052            633                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  13.4743  15.6755  12.7194              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0652 T22:   0.1102                                     
REMARK   3      T33:   0.1162 T12:   0.0070                                     
REMARK   3      T13:   0.0003 T23:   0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4685 L22:   0.6717                                     
REMARK   3      L33:   0.8346 L12:   0.2858                                     
REMARK   3      L13:   0.6115 L23:  -0.0871                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0848 S12:   0.0667 S13:  -0.2285                       
REMARK   3      S21:  -0.0175 S22:  -0.0049 S23:  -0.0847                       
REMARK   3      S31:  -0.0219 S32:   0.0858 S33:  -0.0694                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  12.0061  38.6648  -4.2793              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1036 T22:   0.1100                                     
REMARK   3      T33:   0.0692 T12:   0.0111                                     
REMARK   3      T13:   0.0112 T23:  -0.0081                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7575 L22:   1.0789                                     
REMARK   3      L33:   0.9579 L12:  -0.0680                                     
REMARK   3      L13:  -0.5988 L23:  -0.1064                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0247 S12:   0.0940 S13:  -0.0424                       
REMARK   3      S21:   0.0016 S22:  -0.0703 S23:  -0.0052                       
REMARK   3      S31:  -0.0098 S32:  -0.0725 S33:   0.0397                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   1.5864  32.1806   9.8553              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0944 T22:   0.1151                                     
REMARK   3      T33:   0.0977 T12:   0.0035                                     
REMARK   3      T13:   0.0180 T23:   0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0967 L22:   1.0803                                     
REMARK   3      L33:   0.5459 L12:  -0.0037                                     
REMARK   3      L13:  -0.1835 L23:   0.1000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0065 S12:   0.0176 S13:   0.0260                       
REMARK   3      S21:   0.0284 S22:   0.0064 S23:   0.1857                       
REMARK   3      S31:   0.0233 S32:  -0.1041 S33:  -0.0104                       
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 2WWZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-OCT-09.                  
REMARK 100 THE DEPOSITION ID IS D_1290041584.                                   
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 CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30078                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 23.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.800                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 22.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       15.49000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.76000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.80500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       35.76000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       15.49000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.80500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 B    73                                                      
REMARK 465     ARG B    74                                                      
REMARK 465     GLY B    75                                                      
REMARK 465     GLY B    76                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP C 662    CG   OD1  OD2                                       
REMARK 470     ASP C 663    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   C    GLY A    76     NZ   LYS B    63              1.33            
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 B  63      122.96    -39.28                                   
REMARK 500    THR C 674       -2.33     78.48                                   
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 670   SG                                                     
REMARK 620 2 CYS C 673   SG  114.6                                              
REMARK 620 3 CYS C 684   SG  104.1 101.7                                        
REMARK 620 4 CYS C 687   SG   99.7 124.6 110.9                                  
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 C 1694                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1E0Q   RELATED DB: PDB                                   
REMARK 900 MUTANT PEPTIDE FROM THE FIRST N-TERMINAL 17 AMINO-ACID OF UBIQUITIN  
REMARK 900 RELATED ID: 1YD8   RELATED DB: PDB                                   
REMARK 900 COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN                       
REMARK 900 RELATED ID: 2C7M   RELATED DB: PDB                                   
REMARK 900 COMPLEX OF HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN     
REMARK 900 RELATED ID: 2C7N   RELATED DB: PDB                                   
REMARK 900 HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN                
REMARK 900 RELATED ID: 2FIF   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A BOVINE RABEX-5 FRAGMENT COMPLEXEDWITH         
REMARK 900 UBIQUITIN                                                            
REMARK 900 RELATED ID: 2D3G   RELATED DB: PDB                                   
REMARK 900 DOUBLE SIDED UBIQUITIN BINDING OF HRS-UIM                            
REMARK 900 RELATED ID: 1P3Q   RELATED DB: PDB                                   
REMARK 900 MECHANISM OF UBIQUITIN RECOGNITION BY THE CUE DOMAIN OF VPS9         
REMARK 900 RELATED ID: 1V80   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURES OF UBIQUITIN AT 30 BAR AND 3 KBAR                
REMARK 900 RELATED ID: 1WR6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF GGA3 GAT DOMAIN IN COMPLEX WITHUBIQUITIN        
REMARK 900 RELATED ID: 2FID   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A BOVINE RABEX-5 FRAGMENT COMPLEXEDWITH         
REMARK 900 UBIQUITIN                                                            
REMARK 900 RELATED ID: 1V81   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURES OF UBIQUITIN AT 30 BAR 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 COMPLEX WITHUBIQUITIN        
REMARK 900 RELATED ID: 2WX1   RELATED DB: PDB                                   
REMARK 900 TAB2 NZF DOMAIN IN COMPLEX WITH TRI- UBIQUITIN, P212121              
REMARK 900 RELATED ID: 2WX0   RELATED DB: PDB                                   
REMARK 900 TAB2 NZF DOMAIN IN COMPLEX WITH DI-UBIQUITIN, P21                    
DBREF  2WWZ A    1    76  UNP    P62990   UBIQ_BOVIN       1     76             
DBREF  2WWZ B    1    76  UNP    P62990   UBIQ_BOVIN       1     76             
DBREF  2WWZ C  662   693  UNP    Q9NYJ8   TAB2_HUMAN     662    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   32  ASP ASP GLU GLY ALA GLN TRP ASN CYS THR ALA CYS THR          
SEQRES   2 C   32  PHE LEU ASN HIS PRO ALA LEU ILE ARG CYS GLU GLN CYS          
SEQRES   3 C   32  GLU MET PRO ARG HIS PHE                                      
HET     ZN  C1694       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   4   ZN    ZN 2+                                                        
FORMUL   5  HOH   *214(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 LEU A   56  ASN A   60  5                                   5    
HELIX    4   4 THR B   22  GLY B   35  1                                  14    
HELIX    5   5 PRO B   37  ASP B   39  5                                   3    
HELIX    6   6 LEU B   56  ASN B   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           
LINK         SG  CYS C 670                ZN    ZN C1694     1555   1555  2.37  
LINK         SG  CYS C 673                ZN    ZN C1694     1555   1555  2.31  
LINK         SG  CYS C 684                ZN    ZN C1694     1555   1555  2.37  
LINK         SG  CYS C 687                ZN    ZN C1694     1555   1555  2.34  
SITE     1 AC1  4 CYS C 670  CYS C 673  CYS C 684  CYS C 687                    
CRYST1   30.980   69.610   71.520  90.00  90.00  90.00 P 21 21 21    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      0.032279  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014366  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013982        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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