spacer
spacer

PDBsum entry 2etl

Go to PDB code: 
Top Page protein metals Protein-protein interface(s) links
Hydrolase, ligase PDB id
2etl
Jmol
Contents
Protein chain
223 a.a.
Metals
_CL ×4
Waters ×107
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   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   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
      
PROCHECK
Go to PROCHECK summary
 References

 

spacer

spacer