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Database: PDB
Entry: 3VHT
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Original site: 3VHT 
HEADER    FLUORESCENT PROTEIN/PROTEIN BINDING     06-SEP-11   3VHT              
TITLE     CRYSTAL STRUCTURE OF GFP-WRNIP1 UBZ DOMAIN FUSION PROTEIN IN COMPLEX  
TITLE    2 WITH UBIQUITIN                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GREEN FLUORESCENT PROTEIN;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: GFP DOMAIN;                                                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: GREEN FLUORESCENT PROTEIN,ATPASE WRNIP1;                   
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: GFP,WRNIP1 UBZ DOMAIN (UNP RESIDUES 9-46);                 
COMPND  10 SYNONYM: WERNER HELICASE-INTERACTING PROTEIN 1;                      
COMPND  11 EC: 3.6.1.3;                                                         
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 OTHER_DETAILS: THE FUSION PROTEIN OF YEAST ENHANCED GREEN FLUORESCENT
COMPND  14 PROTEIN, LINKER (GLY-SER) AND HUMAN WRNIP1 UBZ;                      
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: UBIQUITIN;                                                 
COMPND  17 CHAIN: C                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AEQUOREA VICTORIA;                              
SOURCE   3 ORGANISM_COMMON: JELLYFISH;                                          
SOURCE   4 ORGANISM_TAXID: 6100;                                                
SOURCE   5 GENE: GFP;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: AEQUOREA VICTORIA, HOMO SAPIENS;                
SOURCE  13 ORGANISM_COMMON: JELLYFISH, HUMAN;                                   
SOURCE  14 ORGANISM_TAXID: 6100, 9606;                                          
SOURCE  15 GENE: GFP, WRNIP1, WHIP;                                             
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET28;                                    
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  23 ORGANISM_COMMON: MOUSE;                                              
SOURCE  24 ORGANISM_TAXID: 10090                                                
KEYWDS    GREEN FLUORESCENT PROTEIN, FUSION PROTEIN, ZINC FINGER, UBIQUITIN-    
KEYWDS   2 BINDING DOMAIN, FLUORESCENT PROTEIN-PROTEIN BINDING COMPLEX          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.SUZUKI,S.WAKATSUKI,M.KAWASAKI                                       
REVDAT   3   28-JUN-17 3VHT    1       COMPND SOURCE DBREF                      
REVDAT   2   01-JUN-16 3VHT    1       JRNL                                     
REVDAT   1   10-OCT-12 3VHT    0                                                
JRNL        AUTH   N.SUZUKI,A.ROHAIM,R.KATO,I.DIKIC,S.WAKATSUKI,M.KAWASAKI      
JRNL        TITL   A NOVEL MODE OF UBIQUITIN RECOGNITION BY THE                 
JRNL        TITL 2 UBIQUITIN-BINDING ZINC FINGER DOMAIN OF WRNIP1.              
JRNL        REF    FEBS J.                                    2016              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   27062441                                                     
JRNL        DOI    10.1111/FEBS.13734                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 25484                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1347                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1809                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 83                           
REMARK   3   BIN FREE R VALUE                    : 0.3630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4497                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 133                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.58                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.13000                                              
REMARK   3    B22 (A**2) : -1.24000                                             
REMARK   3    B33 (A**2) : 0.11000                                              
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.248         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.178         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.892        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.914                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4597 ; 0.019 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6202 ; 1.820 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   557 ; 7.134 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   221 ;36.195 ;25.204       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   804 ;18.834 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;15.778 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   677 ; 0.114 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7737 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2792 ; 0.912 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4507 ; 1.785 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1805 ; 2.901 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1695 ; 4.722 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   231                          
REMARK   3    RESIDUE RANGE :   B     2        B   229                          
REMARK   3    RESIDUE RANGE :   B   237        B   270                          
REMARK   3    RESIDUE RANGE :   C     1        C    76                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.8285 -56.4302 -10.6721              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0483 T22:   0.0450                                     
REMARK   3      T33:   0.0328 T12:   0.0127                                     
REMARK   3      T13:  -0.0297 T23:   0.0084                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6759 L22:   1.0357                                     
REMARK   3      L33:   0.9658 L12:   0.2402                                     
REMARK   3      L13:  -0.0375 L23:   0.5445                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0052 S12:   0.0982 S13:   0.0860                       
REMARK   3      S21:  -0.0756 S22:  -0.0649 S23:   0.0931                       
REMARK   3      S31:  -0.0623 S32:   0.0438 S33:   0.0701                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3VHT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-SEP-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000095061.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26943                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 75.630                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.10500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.9000                            
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) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3AI5                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M DL-MALIC ACID, 20% PEG 3350, PH     
REMARK 280  7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.0K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.43200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.43200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       44.47500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       71.84600            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       44.47500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       71.84600            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       53.43200            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       44.47500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       71.84600            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       53.43200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       44.47500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       71.84600            
REMARK 290   SMTRY3   8  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: 3270 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     SER A   232                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B   230                                                      
REMARK 465     GLY B   231                                                      
REMARK 465     SER B   232                                                      
REMARK 465     ASP B   233                                                      
REMARK 465     PRO B   234                                                      
REMARK 465     PHE B   235                                                      
REMARK 465     LEU B   236                                                      
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   OE1  GLU A   111     O    HOH A   550              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR B 106   CD1   TYR B 106   CE1     0.101                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B 215   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  23       47.36     36.74                                   
REMARK 500    GLU A 172      -38.37    -32.10                                   
REMARK 500    ASP B 103     -163.93   -163.84                                   
REMARK 500    TYR B 143       74.29   -101.27                                   
REMARK 500    ASN B 212       30.17    -96.71                                   
REMARK 500    GLN B 248       -2.88     74.37                                   
REMARK 500    THR C   9       31.07    -91.67                                   
REMARK 500    ALA C  46       59.25     31.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ARG B   96     THR B   97                  149.64                    
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 B 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 259   NE2                                                    
REMARK 620 2 CYS B 263   SG  108.4                                              
REMARK 620 3 CYS B 244   SG  100.4 120.0                                        
REMARK 620 4 CYS B 247   SG  113.5 105.0 109.9                                  
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 B 401                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3VHS   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 (1) THE SEQUENCE OF YEAST ENHANCED GREEN FLUORESCENT PROTEIN NOT     
REMARK 999 CURRENTLY EXIST IN UNIPROT. THIS SEQUENCE IS FOUND IN GENBANK WITH   
REMARK 999 ACCESSION CODE: ABI82055. (2) IN THE CHAIN A, RESIDUES -2, -1, 0,    
REMARK 999 231, 232 ARE EXPRESSION TAGS. (3) THE CHAIN B IS FUSION PROTEIN OF   
REMARK 999 YEAST ENHANCED GREEN FLUORESCENT PROTEIN (RESIDUES 1-230), LINKER    
REMARK 999 (GLY-SER) AND HUMAN WRNIP1 (RESIDUES 9-46). RESIDUES -2, -1, 0 ARE   
REMARK 999 EXPRESSION TAGS.                                                     
DBREF  3VHT A   -2   232  PDB    3VHT     3VHT            -2    232             
DBREF  3VHT B   -2   230  PDB    3VHT     3VHT            -2    230             
DBREF  3VHT B  233   270  UNP    Q96S55   WRIP1_HUMAN      9     46             
DBREF  3VHT C    1    76  UNP    P62983   RS27A_MOUSE      1     76             
SEQADV 3VHT GLY B  231  UNP  Q96S55              LINKER                         
SEQADV 3VHT SER B  232  UNP  Q96S55              LINKER                         
SEQRES   1 A  233  GLY SER HIS MET SER LYS GLY GLU GLU LEU PHE THR GLY          
SEQRES   2 A  233  VAL VAL PRO ILE LEU VAL GLU LEU ASP GLY ASP VAL ASN          
SEQRES   3 A  233  GLY HIS LYS PHE SER VAL SER GLY GLU GLY GLU GLY ASP          
SEQRES   4 A  233  ALA THR TYR GLY LYS LEU THR LEU LYS PHE ILE CYS THR          
SEQRES   5 A  233  THR GLY LYS LEU PRO VAL PRO TRP PRO THR LEU VAL THR          
SEQRES   6 A  233  THR PHE CR2 VAL GLN CYS PHE ALA ARG TYR PRO ASP HIS          
SEQRES   7 A  233  MET LYS GLN HIS ASP PHE PHE LYS SER ALA MET PRO GLU          
SEQRES   8 A  233  GLY TYR VAL GLN GLU ARG THR ILE PHE PHE LYS ASP ASP          
SEQRES   9 A  233  GLY ASN TYR LYS THR ARG ALA GLU VAL LYS PHE GLU GLY          
SEQRES  10 A  233  ASP THR LEU VAL ASN ARG ILE GLU LEU LYS GLY ILE ASP          
SEQRES  11 A  233  PHE LYS GLU ASP GLY ASN ILE LEU GLY HIS LYS LEU GLU          
SEQRES  12 A  233  TYR ASN TYR ASN SER HIS ASN VAL TYR ILE MET ALA ASP          
SEQRES  13 A  233  LYS GLN LYS ASN GLY ILE LYS VAL ASN PHE LYS ILE ARG          
SEQRES  14 A  233  HIS ASN ILE GLU ASP GLY SER VAL GLN LEU ALA ASP HIS          
SEQRES  15 A  233  TYR GLN GLN ASN THR PRO ILE GLY ASP GLY PRO VAL LEU          
SEQRES  16 A  233  LEU PRO ASP ASN HIS TYR LEU SER THR GLN SER ALA LEU          
SEQRES  17 A  233  SER LYS ASP PRO ASN GLU LYS ARG ASP HIS MET VAL LEU          
SEQRES  18 A  233  LEU GLU PHE VAL THR ALA ALA GLY ILE THR GLY SER              
SEQRES   1 B  271  GLY SER HIS MET SER LYS GLY GLU GLU LEU PHE THR GLY          
SEQRES   2 B  271  VAL VAL PRO ILE LEU VAL GLU LEU ASP GLY ASP VAL ASN          
SEQRES   3 B  271  GLY HIS LYS PHE SER VAL SER GLY GLU GLY GLU GLY ASP          
SEQRES   4 B  271  ALA THR TYR GLY LYS LEU THR LEU LYS PHE ILE CYS THR          
SEQRES   5 B  271  THR GLY LYS LEU PRO VAL PRO TRP PRO THR LEU VAL THR          
SEQRES   6 B  271  THR PHE CR2 VAL GLN CYS PHE ALA ARG TYR PRO ASP HIS          
SEQRES   7 B  271  MET LYS GLN HIS ASP PHE PHE LYS SER ALA MET PRO GLU          
SEQRES   8 B  271  GLY TYR VAL GLN GLU ARG THR ILE PHE PHE LYS ASP ASP          
SEQRES   9 B  271  GLY ASN TYR LYS THR ARG ALA GLU VAL LYS PHE GLU GLY          
SEQRES  10 B  271  ASP THR LEU VAL ASN ARG ILE GLU LEU LYS GLY ILE ASP          
SEQRES  11 B  271  PHE LYS GLU ASP GLY ASN ILE LEU GLY HIS LYS LEU GLU          
SEQRES  12 B  271  TYR ASN TYR ASN SER HIS ASN VAL TYR ILE MET ALA ASP          
SEQRES  13 B  271  LYS GLN LYS ASN GLY ILE LYS VAL ASN PHE LYS ILE ARG          
SEQRES  14 B  271  HIS ASN ILE GLU ASP GLY SER VAL GLN LEU ALA ASP HIS          
SEQRES  15 B  271  TYR GLN GLN ASN THR PRO ILE GLY ASP GLY PRO VAL LEU          
SEQRES  16 B  271  LEU PRO ASP ASN HIS TYR LEU SER THR GLN SER ALA LEU          
SEQRES  17 B  271  SER LYS ASP PRO ASN GLU LYS ARG ASP HIS MET VAL LEU          
SEQRES  18 B  271  LEU GLU PHE VAL THR ALA ALA GLY ILE THR GLY SER ASP          
SEQRES  19 B  271  PRO PHE LEU SER GLN LEU HIS GLN VAL GLN CYS PRO VAL          
SEQRES  20 B  271  CYS GLN GLN MET MET PRO ALA ALA HIS ILE ASN SER HIS          
SEQRES  21 B  271  LEU ASP ARG CYS LEU LEU LEU HIS PRO ALA GLY                  
SEQRES   1 C   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 C   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 C   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 C   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 C   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 C   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
MODRES 3VHT CR2 A   66  GLY                                                     
MODRES 3VHT CR2 A   66  TYR                                                     
MODRES 3VHT CR2 A   66  GLY                                                     
MODRES 3VHT CR2 B   66  GLY                                                     
MODRES 3VHT CR2 B   66  TYR                                                     
MODRES 3VHT CR2 B   66  GLY                                                     
HET    CR2  A  66      19                                                       
HET    CR2  B  66      19                                                       
HET     ZN  B 401       1                                                       
HETNAM     CR2 {(4Z)-2-(AMINOMETHYL)-4-[(4-HYDROXYPHENYL)METHYLIDENE]-          
HETNAM   2 CR2  5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC ACID                  
HETNAM      ZN ZINC ION                                                         
HETSYN     CR2 CHROMOPHORE (GLY-TYR-GLY)                                        
FORMUL   1  CR2    2(C13 H13 N3 O4)                                             
FORMUL   4   ZN    ZN 2+                                                        
FORMUL   5  HOH   *133(H2 O)                                                    
HELIX    1   1 SER A    2  LEU A    7  1                                   6    
HELIX    2   2 PRO A   56  VAL A   61  5                                   6    
HELIX    3   3 VAL A   68  ALA A   72  5                                   5    
HELIX    4   4 PRO A   75  HIS A   81  5                                   7    
HELIX    5   5 ASP A   82  ALA A   87  1                                   6    
HELIX    6   6 LYS A  156  ASN A  159  5                                   4    
HELIX    7   7 LYS B    3  THR B    9  5                                   7    
HELIX    8   8 PRO B   56  VAL B   61  5                                   6    
HELIX    9   9 VAL B   68  ALA B   72  5                                   5    
HELIX   10  10 PRO B   75  HIS B   81  5                                   7    
HELIX   11  11 ASP B   82  ALA B   87  1                                   6    
HELIX   12  12 LYS B  156  ASN B  159  5                                   4    
HELIX   13  13 HIS B  255  HIS B  267  1                                  13    
HELIX   14  14 THR C   22  GLY C   35  1                                  14    
HELIX   15  15 PRO C   37  ASP C   39  5                                   3    
SHEET    1   A12 VAL A  11  VAL A  22  0                                        
SHEET    2   A12 HIS A  25  ASP A  36 -1  O  PHE A  27   N  GLY A  20           
SHEET    3   A12 LYS A  41  CYS A  48 -1  O  THR A  43   N  GLU A  34           
SHEET    4   A12 HIS A 217  ALA A 227 -1  O  LEU A 220   N  LEU A  44           
SHEET    5   A12 HIS A 199  SER A 208 -1  N  SER A 202   O  THR A 225           
SHEET    6   A12 HIS A 148  ASP A 155 -1  N  ILE A 152   O  HIS A 199           
SHEET    7   A12 GLY A 160  ASN A 170 -1  O  GLY A 160   N  ASP A 155           
SHEET    8   A12 VAL A 176  PRO A 187 -1  O  HIS A 181   N  PHE A 165           
SHEET    9   A12 TYR A  92  PHE A 100 -1  N  VAL A  93   O  THR A 186           
SHEET   10   A12 ASN A 105  GLU A 115 -1  O  ALA A 110   N  GLN A  94           
SHEET   11   A12 THR A 118  ILE A 128 -1  O  GLU A 124   N  ARG A 109           
SHEET   12   A12 VAL A  11  VAL A  22  1  N  ASP A  21   O  GLY A 127           
SHEET    1   B12 VAL B  12  VAL B  22  0                                        
SHEET    2   B12 HIS B  25  GLY B  35 -1  O  GLY B  33   N  ILE B  14           
SHEET    3   B12 LYS B  41  CYS B  48 -1  O  ILE B  47   N  SER B  30           
SHEET    4   B12 HIS B 217  ALA B 227 -1  O  LEU B 220   N  LEU B  44           
SHEET    5   B12 HIS B 199  SER B 208 -1  N  SER B 202   O  THR B 225           
SHEET    6   B12 HIS B 148  ASP B 155 -1  N  HIS B 148   O  THR B 203           
SHEET    7   B12 GLY B 160  ASN B 170 -1  O  LYS B 162   N  MET B 153           
SHEET    8   B12 VAL B 176  PRO B 187 -1  O  HIS B 181   N  PHE B 165           
SHEET    9   B12 TYR B  92  PHE B 100 -1  N  VAL B  93   O  THR B 186           
SHEET   10   B12 ASN B 105  GLU B 115 -1  O  TYR B 106   N  ILE B  98           
SHEET   11   B12 THR B 118  ILE B 128 -1  O  THR B 118   N  GLU B 115           
SHEET   12   B12 VAL B  12  VAL B  22  1  N  ASP B  21   O  GLY B 127           
SHEET    1   C 2 GLN B 241  GLN B 243  0                                        
SHEET    2   C 2 MET B 250  PRO B 252 -1  O  MET B 251   N  VAL B 242           
SHEET    1   D 5 THR C  12  GLU C  16  0                                        
SHEET    2   D 5 GLN C   2  THR C   7 -1  N  ILE C   3   O  LEU C  15           
SHEET    3   D 5 THR C  66  LEU C  71  1  O  LEU C  67   N  LYS C   6           
SHEET    4   D 5 GLN C  41  PHE C  45 -1  N  ILE C  44   O  HIS C  68           
SHEET    5   D 5 LYS C  48  GLN C  49 -1  O  LYS C  48   N  PHE C  45           
LINK         C   PHE A  64                 N1  CR2 A  66     1555   1555  1.32  
LINK         C3  CR2 A  66                 N   VAL A  68     1555   1555  1.27  
LINK         C   PHE B  64                 N1  CR2 B  66     1555   1555  1.29  
LINK         C3  CR2 B  66                 N   VAL B  68     1555   1555  1.27  
LINK         NE2 HIS B 259                ZN    ZN B 401     1555   1555  1.83  
LINK         SG  CYS B 263                ZN    ZN B 401     1555   1555  2.26  
LINK         SG  CYS B 244                ZN    ZN B 401     1555   1555  2.30  
LINK         SG  CYS B 247                ZN    ZN B 401     1555   1555  2.36  
CISPEP   1 MET A   88    PRO A   89          0         6.56                     
CISPEP   2 MET B   88    PRO B   89          0         5.42                     
SITE     1 AC1  4 CYS B 244  CYS B 247  HIS B 259  CYS B 263                    
CRYST1   88.950  143.692  106.864  90.00  90.00  90.00 C 2 2 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      0.011242  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006959  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009358        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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