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Database: PDB
Entry: 2ETL
LinkDB: 2ETL
Original site: 2ETL 
HEADER    HYDROLASE, LIGASE                       27-OCT-05   2ETL              
TITLE     CRYSTAL STRUCTURE OF UBIQUITIN CARBOXY-TERMINAL HYDROLASE L1 (UCH-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 THIOLESTERASE 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                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: UCHL1;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P1                                  
KEYWDS    DEUBIQUITINATING THIOL HYDROLASE, HYDROLASE, LIGASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.DAS,Q.Q.HOANG,C.A.KREINBRING,S.J.LUCHANSKY,R.K.MERAY,S.S.RAY,       
AUTHOR   2 P.T.LANSBURY,D.RINGE,G.A.PETSKO                                      
REVDAT   3   13-JUL-11 2ETL    1       VERSN                                    
REVDAT   2   24-FEB-09 2ETL    1       VERSN                                    
REVDAT   1   28-MAR-06 2ETL    0                                                
JRNL        AUTH   C.DAS,Q.Q.HOANG,C.A.KREINBRING,S.J.LUCHANSKY,R.K.MERAY,      
JRNL        AUTH 2 S.S.RAY,P.T.LANSBURY,D.RINGE,G.A.PETSKO                      
JRNL        TITL   STRUCTURAL BASIS FOR CONFORMATIONAL PLASTICITY OF THE        
JRNL        TITL 2 PARKINSON'S DISEASE-ASSOCIATED UBIQUITIN HYDROLASE UCH-L1.   
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 103  4675 2006              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   16537382                                                     
JRNL        DOI    10.1073/PNAS.0510403103                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 34753                          
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 SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.274                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3369                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3482                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 107                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.28                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.03800                                             
REMARK   3    B22 (A**2) : -4.03800                                             
REMARK   3    B33 (A**2) : 8.07600                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 47.87                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:DNA-RNA_REP.PARAM                   
REMARK   3  PARAMETER FILE  3  : CNS_TOPPAR:WATER_REP.PARAM                     
REMARK   3  PARAMETER FILE  4  : CNS_TOPPAR:ION.PARAM                           
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : CNS_TOPPAR:PROTEIN.TOP                         
REMARK   3  TOPOLOGY FILE  2   : CNS_TOPPAR:DNA-RNA.TOP                         
REMARK   3  TOPOLOGY FILE  3   : CNS_TOPPAR:WATER.TOP                           
REMARK   3  TOPOLOGY FILE  4   : CNS_TOPPAR:ION.TOP                             
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2ETL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-NOV-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB035075.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-APR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 298.0                              
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98397                            
REMARK 200  MONOCHROMATOR                  : SI(311)                            
REMARK 200  OPTICS                         : FLAT MIRROR (VERTICAL FOCUSING)    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34753                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 14.100                             
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
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) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.30                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.77300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: HOMOLOGY MODEL BASED ON UCH-L3                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M AMMONIUM SULFATE, 0.1 M HEPES,     
REMARK 280  PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.0K           
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       55.04850            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       55.04850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       55.04850            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       55.04850            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       55.04850            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       55.04850            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       55.04850            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       55.04850            
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, 3, 4                                              
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 ASSEMBLY IS A MONOMER, A SUBUNIT OF THE       
REMARK 300 ASSYMETRIC UNIT WHICH CONTAINS TWO COPIES OF THE PROTEIN MOLECULE.   
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 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 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 11020 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 34070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -106.0 KCAL/MOL                       
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 350   BIOMT1   2 -1.000000  0.000000  0.000000      220.19400            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      110.09700            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      165.14550            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000      -55.04850            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000       55.04850            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000      165.14550            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
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   BIOMT1   2 -1.000000  0.000000  0.000000      110.09700            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000       55.04850            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000      -55.04850            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000       55.04850            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000       55.04850            
REMARK 350   BIOMT3   4  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     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: 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    PRO A  43      105.30    -59.91                                   
REMARK 500    ASN A 102       31.50   -146.28                                   
REMARK 500    ARG A 153      -96.64   -166.02                                   
REMARK 500    VAL A 154      132.80     61.37                                   
REMARK 500    ASN A 159       59.25    -68.83                                   
REMARK 500    GLN A 209       -6.93    -54.01                                   
REMARK 500    GLN B   2      145.03   -173.31                                   
REMARK 500    ALA B  23     -126.49     13.74                                   
REMARK 500    GLU B  35     -129.30    -77.66                                   
REMARK 500    PHE B  62      -52.72     77.19                                   
REMARK 500    ASN B 102       34.17   -144.08                                   
REMARK 500    PHE B 108      124.26     68.22                                   
REMARK 500    GLU B 109     -179.94    -59.76                                   
REMARK 500    ASP B 110      -85.39    -52.53                                   
REMARK 500    LYS B 123       45.51     36.79                                   
REMARK 500    ASP B 155      166.31    -14.43                                   
REMARK 500    ASP B 156     -103.98    -69.51                                   
REMARK 500    HIS B 185       42.30    -97.36                                   
REMARK 500    THR B 192       24.28    -73.63                                   
REMARK 500    ARG B 207       24.31    -62.75                                   
REMARK 500    ALA B 222       85.86     58.23                                   
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 B 3001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 3002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 3003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 3004                 
DBREF  2ETL A    1   223  UNP    P09936   UCHL1_HUMAN      1    223             
DBREF  2ETL B    1   223  UNP    P09936   UCHL1_HUMAN      1    223             
SEQADV 2ETL GLY A   -4  UNP  P09936              CLONING ARTIFACT               
SEQADV 2ETL PRO A   -3  UNP  P09936              CLONING ARTIFACT               
SEQADV 2ETL LEU A   -2  UNP  P09936              CLONING ARTIFACT               
SEQADV 2ETL GLY A   -1  UNP  P09936              CLONING ARTIFACT               
SEQADV 2ETL SER A    0  UNP  P09936              CLONING ARTIFACT               
SEQADV 2ETL GLY B   -4  UNP  P09936              CLONING ARTIFACT               
SEQADV 2ETL PRO B   -3  UNP  P09936              CLONING ARTIFACT               
SEQADV 2ETL LEU B   -2  UNP  P09936              CLONING ARTIFACT               
SEQADV 2ETL GLY B   -1  UNP  P09936              CLONING ARTIFACT               
SEQADV 2ETL SER B    0  UNP  P09936              CLONING ARTIFACT               
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 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  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 ILE 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  B3001       1                                                       
HET     CL  B3002       1                                                       
HET     CL  A3003       1                                                       
HET     CL  A3004       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3   CL    4(CL 1-)                                                     
FORMUL   7  HOH   *107(H2 O)                                                    
HELIX    1   1 ASN A    9  LEU A   20  1                                  12    
HELIX    2   2 THR A   56  LYS A   71  1                                  16    
HELIX    3   3 SER A   89  ASN A  101  1                                  13    
HELIX    4   4 SER A  112  THR A  121  1                                  10    
HELIX    5   5 SER A  125  ASN A  136  1                                  12    
HELIX    6   6 ASN A  136  GLN A  148  1                                  13    
HELIX    7   7 THR A  192  ARG A  207  1                                  16    
HELIX    8   8 ASN B    9  LEU B   20  1                                  12    
HELIX    9   9 THR B   56  GLU B   69  1                                  14    
HELIX   10  10 SER B   89  ASN B  101  1                                  13    
HELIX   11  11 SER B  112  GLU B  122  1                                  11    
HELIX   12  12 SER B  125  GLU B  134  1                                  10    
HELIX   13  13 ASN B  136  GLN B  148  1                                  13    
HELIX   14  14 THR B  192  ARG B  207  1                                  16    
SHEET    1   A 6 TRP A  26  ASP A  30  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  VAL A 168 -1  O  ILE A 163   N  LEU A  51           
SHEET    5   A 6 HIS A 171  LEU A 175 -1  O  TYR A 173   N  ASN A 166           
SHEET    6   A 6 VAL A 183  ALA A 187 -1  O  GLY A 186   N  LEU A 172           
SHEET    1   B 6 ARG B  27  VAL B  31  0                                        
SHEET    2   B 6 SER B 215  CYS B 220 -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  TYR B 173   N  ASN B 166           
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        -0.10                     
SITE     1 AC1  2 GLN B  84  ASN B  88                                          
SITE     1 AC2  1 ASP B 169                                                     
SITE     1 AC3  2 GLN A  84  ASN A  88                                          
SITE     1 AC4  1 ASP A 169                                                     
CRYST1  110.097  110.097   79.489  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      0.009083  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009083  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012580        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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