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Database: PDB
Entry: 3IRT
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Original site: 3IRT 
HEADER    HYDROLASE, LIGASE                       24-AUG-09   3IRT              
TITLE     CRYSTAL STRUCTURE OF THE I93M MUTANT OF UBIQUITIN CARBOXY-TERMINAL    
TITLE    2 HYDROLASE L1                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L1;          
COMPND   3 CHAIN: A, B;                                                         
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                                                        
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                                 
KEYWDS    UBIQUITIN HYDROLASE, PARKINSON'S DISEASE MUTANT, CYTOPLASM, DISEASE   
KEYWDS   2 MUTATION, GLYCOPROTEIN, HYDROLASE, LIGASE, OXIDATION, POLYMORPHISM,  
KEYWDS   3 PROTEASE, THIOL PROTEASE, UBL CONJUGATION PATHWAY                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.W.DAVIES,T.K.MAITI,C.DAS                                            
REVDAT   1   09-JUN-10 3IRT    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.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.75                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 11957                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.870                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 582                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 41.7526 -  4.4423    1.00     3101   151  0.1868 0.2189        
REMARK   3     2  4.4423 -  3.5265    1.00     2936   147  0.1912 0.2211        
REMARK   3     3  3.5265 -  3.0809    0.99     2865   153  0.2455 0.3329        
REMARK   3     4  3.0809 -  2.7993    0.85     2473   131  0.3058 0.3634        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.36                                          
REMARK   3   B_SOL              : 63.02                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 1.090            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.780           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 67.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 9.94330                                              
REMARK   3    B22 (A**2) : 9.94330                                              
REMARK   3    B33 (A**2) : -20.21160                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           3544                                  
REMARK   3   ANGLE     :  0.641           4772                                  
REMARK   3   CHIRALITY :  0.042            520                                  
REMARK   3   PLANARITY :  0.002            638                                  
REMARK   3   DIHEDRAL  : 14.325           1336                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 1:71 or resseq 74:223   
REMARK   3                          )                                           
REMARK   3     SELECTION          : chain B and (resseq 1:71 or resseq 74:223   
REMARK   3                          )                                           
REMARK   3     ATOM PAIRS NUMBER  : 1728                                        
REMARK   3     RMSD               : 0.035                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3IRT COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-AUG-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB054785.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.0                                
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-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0331                             
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   : 11988                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.750                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.780                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 12.800                             
REMARK 200  R MERGE                    (I) : 0.11100                            
REMARK 200  R SYM                      (I) : 0.11100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.9800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 70.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.54000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.780                              
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: ONE SUBUNIT OF THE ASYMMETRIC UNIT OF 2ETL           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M AMMONIUM SULFATE, 0.1 M TRIS       
REMARK 280  HYDROCHLORIDE, 0.1 M SODIUM SODIUM MALONATE, PH 7.0, VAPOR          
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z                                          
REMARK 290       4555   Y+1/2,-X+1/2,Z                                          
REMARK 290       5555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       6555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       54.96900            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       54.96900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       54.96900            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       54.96900            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       54.96900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       54.96900            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       54.96900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       54.96900            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 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 B 228  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 225  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 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 465     GLY B    -4                                                      
REMARK 465     PRO B    -3                                                      
REMARK 465     LEU B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
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 153   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG A 153   NE  -  CZ  -  NH2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG B 153   NE  -  CZ  -  NH1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG B 153   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 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    LEU A  34       76.22   -110.57                                   
REMARK 500    GLU A  36      -70.73    -38.43                                   
REMARK 500    SER A  38      -25.98     71.00                                   
REMARK 500    PRO A  43      157.81    -48.23                                   
REMARK 500    ASN A  88       -2.73     69.62                                   
REMARK 500    ASN A 102       30.29   -148.40                                   
REMARK 500    LYS A 123       70.84   -111.14                                   
REMARK 500    CYS A 152     -160.13   -109.56                                   
REMARK 500    ARG A 153     -100.11   -146.52                                   
REMARK 500    VAL A 154      113.21     65.62                                   
REMARK 500    ASP A 155       75.78   -163.33                                   
REMARK 500    GLU A 190       28.06    -75.88                                   
REMARK 500    ASP A 191      -27.50   -142.69                                   
REMARK 500    GLU A 208       67.35   -116.88                                   
REMARK 500    GLN A 209       36.67    -69.86                                   
REMARK 500    LEU B  34       76.52   -110.97                                   
REMARK 500    GLU B  36      -70.39    -38.21                                   
REMARK 500    SER B  38      -26.09     71.16                                   
REMARK 500    PRO B  43      157.61    -48.62                                   
REMARK 500    LYS B  71     -127.89    -66.11                                   
REMARK 500    GLN B  73      -68.47   -146.98                                   
REMARK 500    GLU B  74      -17.84   -159.76                                   
REMARK 500    ASN B  88       -2.82     69.77                                   
REMARK 500    ASN B 102       30.44   -148.70                                   
REMARK 500    LYS B 123       70.68   -111.38                                   
REMARK 500    CYS B 152     -160.39   -110.14                                   
REMARK 500    ARG B 153      -99.19   -146.24                                   
REMARK 500    VAL B 154      113.64     65.80                                   
REMARK 500    ASP B 155       75.63   -163.52                                   
REMARK 500    GLU B 190       28.46    -75.83                                   
REMARK 500    ASP B 191      -27.68   -143.04                                   
REMARK 500    GLU B 208       66.89   -117.10                                   
REMARK 500    GLN B 209       36.49    -69.13                                   
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 CL A 224                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 224                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ETL   RELATED DB: PDB                                   
REMARK 900 ISOLEUCINE 93 TO METHIONINE MUTANT                                   
DBREF  3IRT A    1   223  UNP    P09936   UCHL1_HUMAN      1    223             
DBREF  3IRT B    1   223  UNP    P09936   UCHL1_HUMAN      1    223             
SEQADV 3IRT GLY A   -4  UNP  P09936              EXPRESSION TAG                 
SEQADV 3IRT PRO A   -3  UNP  P09936              EXPRESSION TAG                 
SEQADV 3IRT LEU A   -2  UNP  P09936              EXPRESSION TAG                 
SEQADV 3IRT GLY A   -1  UNP  P09936              EXPRESSION TAG                 
SEQADV 3IRT SER A    0  UNP  P09936              EXPRESSION TAG                 
SEQADV 3IRT MET A   93  UNP  P09936    ILE    93 ENGINEERED                     
SEQADV 3IRT GLY B   -4  UNP  P09936              EXPRESSION TAG                 
SEQADV 3IRT PRO B   -3  UNP  P09936              EXPRESSION TAG                 
SEQADV 3IRT LEU B   -2  UNP  P09936              EXPRESSION TAG                 
SEQADV 3IRT GLY B   -1  UNP  P09936              EXPRESSION TAG                 
SEQADV 3IRT SER B    0  UNP  P09936              EXPRESSION TAG                 
SEQADV 3IRT MET B   93  UNP  P09936    ILE    93 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 SER 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 MET 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  228  GLY PRO LEU GLY SER MET GLN LEU LYS PRO MET GLU ILE          
SEQRES   2 B  228  ASN PRO GLU MET LEU ASN LYS VAL LEU SER ARG LEU GLY          
SEQRES   3 B  228  VAL ALA GLY GLN TRP ARG PHE VAL ASP VAL LEU GLY LEU          
SEQRES   4 B  228  GLU GLU GLU SER LEU GLY SER VAL PRO ALA PRO ALA CYS          
SEQRES   5 B  228  ALA LEU LEU LEU LEU PHE PRO LEU THR ALA GLN HIS GLU          
SEQRES   6 B  228  ASN PHE ARG LYS LYS GLN ILE GLU GLU LEU LYS GLY GLN          
SEQRES   7 B  228  GLU VAL SER PRO LYS VAL TYR PHE MET LYS GLN THR ILE          
SEQRES   8 B  228  GLY ASN SER CYS GLY THR MET GLY LEU ILE HIS ALA VAL          
SEQRES   9 B  228  ALA ASN ASN GLN ASP LYS LEU GLY PHE GLU ASP GLY SER          
SEQRES  10 B  228  VAL LEU LYS GLN PHE LEU SER GLU THR GLU LYS MET SER          
SEQRES  11 B  228  PRO GLU ASP ARG ALA LYS CYS PHE GLU LYS ASN GLU ALA          
SEQRES  12 B  228  ILE GLN ALA ALA HIS ASP ALA VAL ALA GLN GLU GLY GLN          
SEQRES  13 B  228  CYS ARG VAL ASP ASP LYS VAL ASN PHE HIS PHE ILE LEU          
SEQRES  14 B  228  PHE ASN ASN VAL ASP GLY HIS LEU TYR GLU LEU ASP GLY          
SEQRES  15 B  228  ARG MET PRO PHE PRO VAL ASN HIS GLY ALA SER SER GLU          
SEQRES  16 B  228  ASP THR LEU LEU LYS ASP ALA ALA LYS VAL CYS ARG GLU          
SEQRES  17 B  228  PHE THR GLU ARG GLU GLN GLY GLU VAL ARG PHE SER ALA          
SEQRES  18 B  228  VAL ALA LEU CYS LYS ALA ALA                                  
HET     CL  A 224       1                                                       
HET     CL  B 224       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   5  HOH   *35(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  LEU A   70  1                                  15    
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  ASN A  136  1                                  12    
HELIX    7   7 ASN A  136  GLN A  148  1                                  13    
HELIX    8   8 THR A  192  GLU A  206  1                                  15    
HELIX    9   9 ASN B    9  LEU B   20  1                                  12    
HELIX   10  10 GLU B   35  GLY B   40  1                                   6    
HELIX   11  11 THR B   56  LEU B   70  1                                  15    
HELIX   12  12 SER B   89  ASN B  101  1                                  13    
HELIX   13  13 SER B  112  THR B  121  1                                  10    
HELIX   14  14 SER B  125  ASN B  136  1                                  12    
HELIX   15  15 ASN B  136  GLN B  148  1                                  13    
HELIX   16  16 THR B  192  GLU B  206  1                                  15    
SHEET    1   A 6 TRP A  26  VAL A  31  0                                        
SHEET    2   A 6 SER A 215  LYS A 221 -1  O  ALA A 218   N  VAL A  29           
SHEET    3   A 6 ALA A  46  PRO A  54 -1  N  LEU A  52   O  SER A 215           
SHEET    4   A 6 PHE A 160  ASN A 167 -1  O  ILE A 163   N  LEU A  51           
SHEET    5   A 6 HIS A 171  LEU A 175 -1  O  LEU A 175   N  LEU A 164           
SHEET    6   A 6 VAL A 183  ALA A 187 -1  O  HIS A 185   N  LEU A 172           
SHEET    1   B 6 TRP B  26  VAL B  31  0                                        
SHEET    2   B 6 SER B 215  LYS B 221 -1  O  ALA B 218   N  VAL B  29           
SHEET    3   B 6 ALA B  46  PRO B  54 -1  N  LEU B  52   O  SER B 215           
SHEET    4   B 6 PHE B 160  ASN B 167 -1  O  ILE B 163   N  LEU B  51           
SHEET    5   B 6 HIS B 171  LEU B 175 -1  O  LEU B 175   N  LEU B 164           
SHEET    6   B 6 VAL B 183  ALA B 187 -1  O  HIS B 185   N  LEU B 172           
CISPEP   1 ALA A   44    PRO A   45          0        -2.72                     
CISPEP   2 ALA B   44    PRO B   45          0        -2.48                     
SITE     1 AC1  2 GLN A  84  CYS A  90                                          
SITE     1 AC2  3 GLN B  84  ASN B  88  CYS B  90                               
CRYST1  109.938  109.938   79.040  90.00  90.00  90.00 P 4 21 2     16          
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      0.009096  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009096  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012652        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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