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Database: PDB
Entry: 3IFW
LinkDB: 3IFW
Original site: 3IFW 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           26-JUL-09   3IFW              
TITLE     CRYSTAL STRUCTURE OF THE S18Y VARIANT OF UBIQUITIN CARBOXY TERMINAL   
TITLE    2 HYDROLASE L1 BOUND TO UBIQUITIN VINYLMETHYLESTER.                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L1;          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: UCH-L1, UBIQUITIN THIOESTERASE L1, NEURON CYTOPLASMIC       
COMPND   5 PROTEIN 9.5, PGP 9.5, PGP9.5;                                        
COMPND   6 EC: 3.4.19.12, 6.-.-.-;                                              
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: UBIQUITIN;                                                 
COMPND  11 CHAIN: B;                                                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PGP9.5, UCHL1;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: RPS27A, UBA52, UBA80, UBB, UBC, UBCEP1, UBCEP2, UBIQ_HUMAN;    
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: ROSETTA;                                   
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PTYB1                                     
KEYWDS    ENZYME-SUICIDE SUBSTRATE COMPLEX, CYTOPLASM, DISEASE MUTATION,        
KEYWDS   2 GLYCOPROTEIN, HYDROLASE, LIGASE, OXIDATION, POLYMORPHISM, PROTEASE,  
KEYWDS   3 THIOL PROTEASE, UBL CONJUGATION PATHWAY, ISOPEPTIDE BOND, NUCLEUS,   
KEYWDS   4 PHOSPHOPROTEIN, UBL CONJUGATION, HYDROLASE-HYDROLASE INHIBITOR       
KEYWDS   5 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.DAS,D.BOUDREAUX,T.MAITI                                             
REVDAT   1   16-JUN-10 3IFW    0                                                
JRNL        AUTH   D.A.BOUDREAUX,T.K.MAITI,C.W.DAVIES,C.DAS                     
JRNL        TITL   UBIQUITIN VINYL METHYL ESTER BINDING ORIENTS THE MISALIGNED  
JRNL        TITL 2 ACTIVE SITE OF THE UBIQUITIN HYDROLASE UCHL1 INTO            
JRNL        TITL 3 PRODUCTIVE CONFORMATION.                                     
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 107  9117 2010              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   20439756                                                     
JRNL        DOI    10.1073/PNAS.0910870107                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 10699                          
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) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 539                             
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) : 749                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.46                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 42                           
REMARK   3   BIN FREE R VALUE                    : 0.3670                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2344                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 51                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 79.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.04000                                              
REMARK   3    B22 (A**2) : 0.04000                                              
REMARK   3    B33 (A**2) : -0.06000                                             
REMARK   3    B12 (A**2) : 0.02000                                              
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): 0.762         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.298         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.269         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.693        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2391 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3215 ; 0.896 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   296 ; 4.923 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   115 ;37.933 ;25.391       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   445 ;15.346 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;12.056 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   358 ; 0.054 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1794 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1016 ; 0.172 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1618 ; 0.291 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    95 ; 0.097 ; 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):    66 ; 0.186 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.087 ; 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):  1531 ; 0.162 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2382 ; 0.282 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   947 ; 0.507 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   833 ; 0.762 ; 4.500       
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  : 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 3IFW COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB054359.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-FEB-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0032                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11248                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 9.900                              
REMARK 200  R MERGE                    (I) : 0.09400                            
REMARK 200  R SYM                      (I) : 0.09400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.0000                            
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       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.60000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
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 2ETL    PDB ENTRY 1XD3, CHAIN B            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M AMMONIUM SULFATE, 0.1M BICINE,     
REMARK 280  PH 9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       43.65200            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       25.20249            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       64.51467            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       43.65200            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       25.20249            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       64.51467            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       43.65200            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       25.20249            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       64.51467            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       43.65200            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       25.20249            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       64.51467            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       43.65200            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       25.20249            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       64.51467            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       43.65200            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       25.20249            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       64.51467            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       50.40499            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      129.02933            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       50.40499            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      129.02933            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       50.40499            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      129.02933            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       50.40499            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      129.02933            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       50.40499            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      129.02933            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       50.40499            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      129.02933            
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 300 REMARK: THE BIOLOGICAL UNIT IS A HETERODIMER CONSIST OF CHAIN A AND  
REMARK 300 B IN THE ASYMMETRIC UNIT.                                            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 225  LIES ON A SPECIAL POSITION.                          
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     PRO A    -3                                                      
REMARK 465     LEU A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
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   SG   CYS A    90     CB   GVE B    76              1.80            
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    LEU A  70       39.27    -77.55                                   
REMARK 500    LYS A  71      -70.88    -36.35                                   
REMARK 500    ASP A 155      -60.36    -27.69                                   
REMARK 500    ASP A 156     -104.19     59.74                                   
REMARK 500    LYS A 157      -74.29    -65.01                                   
REMARK 500    VAL A 158      107.21    -43.21                                   
REMARK 500    GLU A 208       66.87   -104.88                                   
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 GVE B 76                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ETL   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF WILD TYPE UCHL1                                         
DBREF  3IFW A    1   223  UNP    P09936   UCHL1_HUMAN      1    223             
DBREF  3IFW B    1    75  UNP    P62988   UBIQ_HUMAN       1     75             
SEQADV 3IFW GLY A   -4  UNP  P09936              EXPRESSION TAG                 
SEQADV 3IFW PRO A   -3  UNP  P09936              EXPRESSION TAG                 
SEQADV 3IFW LEU A   -2  UNP  P09936              EXPRESSION TAG                 
SEQADV 3IFW GLY A   -1  UNP  P09936              EXPRESSION TAG                 
SEQADV 3IFW SER A    0  UNP  P09936              EXPRESSION TAG                 
SEQADV 3IFW TYR A   18  UNP  P09936    SER    18 ENGINEERED                     
SEQRES   1 A  228  GLY PRO LEU GLY SER MET GLN LEU LYS PRO MET GLU ILE          
SEQRES   2 A  228  ASN PRO GLU MET LEU ASN LYS VAL LEU TYR ARG LEU GLY          
SEQRES   3 A  228  VAL ALA GLY GLN TRP ARG PHE VAL ASP VAL LEU GLY LEU          
SEQRES   4 A  228  GLU GLU GLU SER LEU GLY SER VAL PRO ALA PRO ALA CYS          
SEQRES   5 A  228  ALA LEU LEU LEU LEU PHE PRO LEU THR ALA GLN HIS GLU          
SEQRES   6 A  228  ASN PHE ARG LYS LYS GLN ILE GLU GLU LEU LYS GLY GLN          
SEQRES   7 A  228  GLU VAL SER PRO LYS VAL TYR PHE MET LYS GLN THR ILE          
SEQRES   8 A  228  GLY ASN SER CYS GLY THR ILE GLY LEU ILE HIS ALA VAL          
SEQRES   9 A  228  ALA ASN ASN GLN ASP LYS LEU GLY PHE GLU ASP GLY SER          
SEQRES  10 A  228  VAL LEU LYS GLN PHE LEU SER GLU THR GLU LYS MET SER          
SEQRES  11 A  228  PRO GLU ASP ARG ALA LYS CYS PHE GLU LYS ASN GLU ALA          
SEQRES  12 A  228  ILE GLN ALA ALA HIS ASP ALA VAL ALA GLN GLU GLY GLN          
SEQRES  13 A  228  CYS ARG VAL ASP ASP LYS VAL ASN PHE HIS PHE ILE LEU          
SEQRES  14 A  228  PHE ASN ASN VAL ASP GLY HIS LEU TYR GLU LEU ASP GLY          
SEQRES  15 A  228  ARG MET PRO PHE PRO VAL ASN HIS GLY ALA SER SER GLU          
SEQRES  16 A  228  ASP THR LEU LEU LYS ASP ALA ALA LYS VAL CYS ARG GLU          
SEQRES  17 A  228  PHE THR GLU ARG GLU GLN GLY GLU VAL ARG PHE SER ALA          
SEQRES  18 A  228  VAL ALA LEU CYS LYS ALA ALA                                  
SEQRES   1 B   75  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 B   75  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 B   75  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 B   75  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 B   75  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 B   75  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY                      
HET    GVE  B  76       8                                                       
HETNAM     GVE METHYL 4-AMINOBUTANOATE                                          
FORMUL   3  GVE    C5 H11 N O2                                                  
FORMUL   4  HOH   *51(H2 O)                                                     
HELIX    1   1 ASN A    9  LEU A   20  1                                  12    
HELIX    2   2 GLU A   35  GLY A   40  1                                   6    
HELIX    3   3 THR A   56  GLU A   68  1                                  13    
HELIX    4   4 SER A   89  ASN A  101  1                                  13    
HELIX    5   5 SER A  112  THR A  121  1                                  10    
HELIX    6   6 SER A  125  LYS A  135  1                                  11    
HELIX    7   7 ASN A  136  GLN A  148  1                                  13    
HELIX    8   8 THR A  192  GLU A  208  1                                  17    
HELIX    9   9 THR B   22  GLY B   35  1                                  14    
HELIX   10  10 PRO B   37  ASP B   39  5                                   3    
HELIX   11  11 LEU B   56  ASN B   60  5                                   5    
SHEET    1   A 2 MET A   6  GLU A   7  0                                        
SHEET    2   A 2 ARG B  74  GLY B  75 -1  O  GLY B  75   N  MET A   6           
SHEET    1   B 2 VAL A  22  ALA A  23  0                                        
SHEET    2   B 2 GLY A 107  PHE A 108 -1  O  GLY A 107   N  ALA A  23           
SHEET    1   C 6 TRP A  26  ASP A  30  0                                        
SHEET    2   C 6 SER A 215  LYS A 221 -1  O  ALA A 218   N  VAL A  29           
SHEET    3   C 6 ALA A  46  PRO A  54 -1  N  LEU A  52   O  SER A 215           
SHEET    4   C 6 PHE A 160  VAL A 168 -1  O  PHE A 165   N  LEU A  49           
SHEET    5   C 6 HIS A 171  LEU A 175 -1  O  LEU A 175   N  LEU A 164           
SHEET    6   C 6 VAL A 183  ALA A 187 -1  O  HIS A 185   N  LEU A 172           
SHEET    1   D 5 THR B  12  GLU B  16  0                                        
SHEET    2   D 5 GLN B   2  THR B   7 -1  N  VAL B   5   O  ILE B  13           
SHEET    3   D 5 THR B  66  LEU B  71  1  O  LEU B  67   N  PHE B   4           
SHEET    4   D 5 GLN B  41  PHE B  45 -1  N  ILE B  44   O  HIS B  68           
SHEET    5   D 5 LYS B  48  GLN B  49 -1  O  LYS B  48   N  PHE B  45           
LINK         C   GLY B  75                 N   GVE B  76     1555   1555  1.33  
CISPEP   1 ALA A   44    PRO A   45          0         1.79                     
SITE     1 AC1  6 LEU A  55  GLN A  84  ASN A  88  CYS A  90                    
SITE     2 AC1  6 PHE A 160  GLY B  75                                          
CRYST1   87.304   87.304  193.544  90.00  90.00 120.00 H 3 2        18          
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      0.011454  0.006613  0.000000        0.00000                         
SCALE2      0.000000  0.013226  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005167        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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