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Database: PDB
Entry: 4A3P
LinkDB: 4A3P
Original site: 4A3P 
HEADER    HYDROLASE                               03-OCT-11   4A3P              
TITLE     STRUCTURE OF USP15 DUSP-UBL DELETION MUTANT                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 15;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: DUSP-UBL, RESIDUES 6-123,127-223;                          
COMPND   5 SYNONYM: DEUBIQUITINATING ENZYME 15, UBIQUITIN THIOLESTERASE 15,     
COMPND   6 UBIQUITIN-SPECIFIC-PROCESSING PROTEASE 15, UNPH-2, UNPH4, USP15;     
COMPND   7 EC: 3.4.19.12;                                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.R.ELLIOTT,H.LIU,M.W.PASTOK,G.J.GROSSMANN,D.J.RIGDEN,M.J.CLAGUE,     
AUTHOR   2 S.URBE,I.L.BARSUKOV                                                  
REVDAT   2   20-DEC-23 4A3P    1       REMARK                                   
REVDAT   1   16-NOV-11 4A3P    0                                                
JRNL        AUTH   P.R.ELLIOTT,H.LIU,M.W.PASTOK,G.J.GROSSMANN,D.J.RIGDEN,       
JRNL        AUTH 2 M.J.CLAGUE,S.URBE,I.L.BARSUKOV                               
JRNL        TITL   STRUCTURAL VARIABILITY OF THE UBIQUITIN SPECIFIC PROTEASE    
JRNL        TITL 2 DUSP-UBL DOUBLE DOMAINS.                                     
JRNL        REF    FEBS LETT.                    V. 585  3385 2011              
JRNL        REFN                   ISSN 0014-5793                               
JRNL        PMID   22001210                                                     
JRNL        DOI    10.1016/J.FEBSLET.2011.09.040                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 37168                          
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) : 0.157                           
REMARK   3   R VALUE            (WORKING SET) : 0.153                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1981                            
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) : 1.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.43                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2714                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.42                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2050                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 143                          
REMARK   3   BIN FREE R VALUE                    : 0.3170                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1713                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 223                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.03000                                              
REMARK   3    B22 (A**2) : 0.04000                                              
REMARK   3    B33 (A**2) : -0.14000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.13000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.071         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.075         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.047         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.624         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1788 ; 0.020 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  1218 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2427 ; 1.891 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2987 ; 1.212 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   219 ; 5.667 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    86 ;39.109 ;25.349       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   325 ;13.376 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;14.948 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   266 ; 0.124 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1958 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   354 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   625 ; 0.321 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1151 ; 0.236 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   851 ; 0.191 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):   897 ; 0.110 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    44 ; 0.264 ; 0.200       
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):    91 ; 0.441 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    62 ; 0.505 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.324 ; 0.200       
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):  1788 ;13.509 ; 1.922       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1218 ;13.868 ; 1.973       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2420 ;15.308 ; 2.841       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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):  3006 ;16.083 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    64 ;28.951 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  3128 ;13.999 ; 5.000       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4A3P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-OCT-11.                  
REMARK 100 THE DEPOSITION ID IS D_1290049885.                                   
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                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.980                              
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : DUAL SLITS                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4R                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39193                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.330                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 13.400                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.8                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : 0.03000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.47                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3PV1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.9 M (NH4)2SO4, 100 MM HEPES PH 7.0,    
REMARK 280  200 MM KI.                                                          
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       22.12500            
REMARK 290   SMTRY3   2  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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ASP A    75                                                      
REMARK 465     ALA A    76                                                      
REMARK 465     GLN A    77                                                      
REMARK 465     GLY A   218                                                      
REMARK 465     GLY A   223                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  36    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 108    CD   OE1  OE2                                       
REMARK 470     LYS A 167    CD   CE   NZ                                        
REMARK 470     LYS A 193    CD   CE   NZ                                        
REMARK 470     LYS A 214    CD   CE   NZ                                        
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   NZ   LYS A    42     O    HOH A  2065              1.56            
REMARK 500   OD2  ASP A   200     O    HOH A  2209              2.10            
REMARK 500   O    HOH A  2068     O    HOH A  2125              2.10            
REMARK 500   O    HOH A  2007     O    HOH A  2023              2.10            
REMARK 500   O    HOH A  2013     O    HOH A  2014              2.13            
REMARK 500   OE2  GLU A   162     OG1  THR A   177              2.16            
REMARK 500   CE   LYS A    42     O    HOH A  2065              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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   OE1  GLU A   119     OE2  GLU A   174     2645     1.64            
REMARK 500   O    HOH A  2039     O    HOH A  2194     2655     2.15            
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    PHE A 123   CD1   PHE A 123   CE1    -0.124                       
REMARK 500    PHE A 123   CE1   PHE A 123   CZ     -0.118                       
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 A  13   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ASP A  57   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 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    GLU A  86      -50.90     80.24                                   
REMARK 500    THR A 105      158.08     71.31                                   
REMARK 500    PHE A 123     -159.35   -106.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1223                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1W6V   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF THE DUSP DOMAIN OF HUSP15                      
REMARK 900 RELATED ID: 4A3O   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE USP15 DUSP-UBL MONOMER                      
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUES 124-126 (VKH) WERE SUB-CLONED OUT OF THE SEQUENCE           
REMARK 999 TO GENERATE A DELETION MUTANT. F123 IS PEPTIDE LINKED TO C127.       
DBREF  4A3P A    6   223  UNP    Q9Y4E8   UBP15_HUMAN      6    223             
SEQADV 4A3P     A       UNP  Q9Y4E8    VAL   124 DELETION                       
SEQADV 4A3P     A       UNP  Q9Y4E8    LYS   125 DELETION                       
SEQADV 4A3P     A       UNP  Q9Y4E8    HIS   126 DELETION                       
SEQADV 4A3P GLY A    4  UNP  Q9Y4E8              EXPRESSION TAG                 
SEQADV 4A3P ALA A    5  UNP  Q9Y4E8              EXPRESSION TAG                 
SEQRES   1 A  217  GLY ALA ALA ALA ASP LEU ASP THR GLN ARG SER ASP ILE          
SEQRES   2 A  217  ALA THR LEU LEU LYS THR SER LEU ARG LYS GLY ASP THR          
SEQRES   3 A  217  TRP TYR LEU VAL ASP SER ARG TRP PHE LYS GLN TRP LYS          
SEQRES   4 A  217  LYS TYR VAL GLY PHE ASP SER TRP ASP LYS TYR GLN MET          
SEQRES   5 A  217  GLY ASP GLN ASN VAL TYR PRO GLY PRO ILE ASP ASN SER          
SEQRES   6 A  217  GLY LEU LEU LYS ASP GLY ASP ALA GLN SER LEU LYS GLU          
SEQRES   7 A  217  HIS LEU ILE ASP GLU LEU ASP TYR ILE LEU LEU PRO THR          
SEQRES   8 A  217  GLU GLY TRP ASN LYS LEU VAL SER TRP TYR THR LEU MET          
SEQRES   9 A  217  GLU GLY GLN GLU PRO ILE ALA ARG LYS VAL VAL GLU GLN          
SEQRES  10 A  217  GLY MET PHE CYS LYS VAL GLU VAL TYR LEU THR GLU LEU          
SEQRES  11 A  217  LYS LEU CYS GLU ASN GLY ASN MET ASN ASN VAL VAL THR          
SEQRES  12 A  217  ARG ARG PHE SER LYS ALA ASP THR ILE ASP THR ILE GLU          
SEQRES  13 A  217  LYS GLU ILE ARG LYS ILE PHE SER ILE PRO ASP GLU LYS          
SEQRES  14 A  217  GLU THR ARG LEU TRP ASN LYS TYR MET SER ASN THR PHE          
SEQRES  15 A  217  GLU PRO LEU ASN LYS PRO ASP SER THR ILE GLN ASP ALA          
SEQRES  16 A  217  GLY LEU TYR GLN GLY GLN VAL LEU VAL ILE GLU GLN LYS          
SEQRES  17 A  217  ASN GLU ASP GLY THR TRP PRO ARG GLY                          
HET    ACT  A1223       4                                                       
HET    IOD  A1224       1                                                       
HETNAM     ACT ACETATE ION                                                      
HETNAM     IOD IODIDE ION                                                       
FORMUL   2  ACT    C2 H3 O2 1-                                                  
FORMUL   3  IOD    I 1-                                                         
FORMUL   4  HOH   *223(H2 O)                                                    
HELIX    1   1 ASP A    8  LEU A   20  1                                  13    
HELIX    2   2 SER A   35  GLY A   46  1                                  12    
HELIX    3   3 ASP A   57  TYR A   61  5                                   5    
HELIX    4   4 ASN A   67  LEU A   70  5                                   4    
HELIX    5   5 THR A   94  THR A  105  1                                  12    
HELIX    6   6 THR A  157  PHE A  169  1                                  13    
HELIX    7   7 THR A  197  GLY A  202  1                                   6    
SHEET    1  AA 4 TYR A  89  PRO A  93  0                                        
SHEET    2  AA 4 THR A  29  ASP A  34 -1  O  TYR A  31   N  LEU A  92           
SHEET    3  AA 4 ALA A 114  GLN A 120 -1  O  ARG A 115   N  TRP A  30           
SHEET    4  AA 4 PHE A 123  VAL A 129 -1  O  PHE A 123   N  GLN A 120           
SHEET    1  AB 5 ASN A 143  PHE A 152  0                                        
SHEET    2  AB 5 THR A 134  GLU A 140 -1  O  THR A 134   N  PHE A 152           
SHEET    3  AB 5 VAL A 208  GLN A 213  1  O  LEU A 209   N  CYS A 139           
SHEET    4  AB 5 THR A 177  MET A 184 -1  O  ARG A 178   N  GLU A 212           
SHEET    5  AB 5 THR A 187  PRO A 190 -1  O  THR A 187   N  TYR A 183           
SITE     1 AC1  4 ASP A  15  LEU A  19  GLU A  95  LYS A  99                    
CRYST1   44.950   44.250   56.150  90.00 104.33  90.00 P 1 21 1      2          
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      0.022247  0.000000  0.005683        0.00000                         
SCALE2      0.000000  0.022599  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018381        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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