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PDBsum entry 3kw5

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Hydrolase/signaling protein PDB id
3kw5
Jmol
Contents
Protein chains
223 a.a.
75 a.a.
Ligands
GVE
HEADER    HYDROLASE/SIGNALING PROTEIN             30-NOV-09   3KW5
TITLE     CRYSTAL STRUCTURE OF UBIQUITIN CARBOXY TERMINAL HYDROLASE L1 BOUND TO
TITLE    2 UBIQUITIN VINYLMETHYLESTER
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L1;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: UCH-L1, UBIQUITIN THIOESTERASE L1, NEURON CYTOPLASMIC
COMPND   5 PROTEIN 9.5, PGP 9.5, PGP9.5;
COMPND   6 EC: 3.4.19.12, 6.-.-.-;
COMPND   7 ENGINEERED: YES;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: UBIQUITIN;
COMPND  10 CHAIN: B;
COMPND  11 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: PGP9.5, UCHL1;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1;
SOURCE  11 MOL_ID: 2;
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  13 ORGANISM_COMMON: HUMAN;
SOURCE  14 ORGANISM_TAXID: 9606;
SOURCE  15 GENE: RPS27A, UBA52, UBA80, UBB, UBC, UBCEP1, UBCEP2, UBIQ_HUMAN;
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PTYB1
KEYWDS    ENZYME-SUICIDE SUBSTRATE COMPLEX, HYDROLASE, LIGASE, PROTEASE, THIOL
KEYWDS   2 PROTEASE, UBL CONJUGATION PATHWAY, ISOPEPTIDE BOND, UBL CONJUGATION,
KEYWDS   3 HYDROLASE-HYDROLASE INHIBITOR COMPLEX, ACETYLATION, CYTOPLASM,
KEYWDS   4 DISEASE MUTATION, GLYCOPROTEIN, OXIDATION, POLYMORPHISM, NUCLEUS,
KEYWDS   5 PHOSPHOPROTEIN, HYDROLASE-SIGNALING PROTEIN COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    T.K.MAITI,D.A.BOUDREAUX,C.DAS
REVDAT   1   16-JUN-10 3KW5    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.    2.83 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.83
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.06
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3
REMARK   3   NUMBER OF REFLECTIONS             : 6387
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.235
REMARK   3   R VALUE            (WORKING SET) : 0.233
REMARK   3   FREE R VALUE                     : 0.286
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800
REMARK   3   FREE R VALUE TEST SET COUNT      : 321
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.83
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.91
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 383
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.63
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3560
REMARK   3   BIN FREE R VALUE SET COUNT          : 16
REMARK   3   BIN FREE R VALUE                    : 0.3420
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2338
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 8
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 122.88
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : 0.00000
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.505
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.542
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 70.674
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.908
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2384 ; 0.006 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3205 ; 0.837 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   296 ; 4.553 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   114 ;37.884 ;25.439
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   445 ;15.002 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;11.188 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   358 ; 0.050 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1786 ; 0.002 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1085 ; 0.162 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1616 ; 0.291 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    69 ; 0.107 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    56 ; 0.173 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.052 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1532 ; 0.128 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2382 ; 0.208 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   937 ; 0.425 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   823 ; 0.554 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3KW5 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-09.
REMARK 100 THE RCSB ID CODE IS RCSB056521.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 9.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 23-ID-D
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033
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   : 6726
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.830
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.100
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4
REMARK 200  DATA REDUNDANCY                : 10.000
REMARK 200  R MERGE                    (I) : 0.08100
REMARK 200  R SYM                      (I) : 0.08100
REMARK 200   FOR THE DATA SET  : 22.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.83
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.71000
REMARK 200  R SYM FOR SHELL            (I) : 0.71000
REMARK 200   FOR SHELL         : 2.300
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: 3IFW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BICINE, 2.4M AMMONIUM SULFATE, PH
REMARK 280  9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z
REMARK 290       3555   -X+Y,-X,Z
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z
REMARK 290       6555   -X,-X+Y,-Z
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       43.49450
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       25.11156
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       64.47800
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       43.49450
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       25.11156
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       64.47800
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       43.49450
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       25.11156
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       64.47800
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       43.49450
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       25.11156
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       64.47800
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       43.49450
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       25.11156
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       64.47800
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       43.49450
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       25.11156
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       64.47800
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       50.22312
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      128.95600
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       50.22312
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      128.95600
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       50.22312
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      128.95600
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       50.22312
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      128.95600
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       50.22312
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      128.95600
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       50.22312
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      128.95600
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A    -4
REMARK 465     PRO A    -3
REMARK 465     LEU A    -2
REMARK 465     GLY A    -1
REMARK 465     SER A     0
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    GLY B    75     N    GVE B    76              2.18
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    LYS A  71     -107.83     48.60
REMARK 500    ASN A 102       29.31   -145.11
REMARK 500    ASP A 156      -74.32     59.18
REMARK 500    VAL A 158      112.05    -37.61
REMARK 500    HIS A 185       52.63   -100.32
REMARK 500    GLU A 208       78.00   -117.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GVE B 76
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ETL   RELATED DB: PDB
REMARK 900 WILD TYPE UCHL1 BOUND TO UBIQUITIN VINYLMETHYLESTER
REMARK 900 RELATED ID: 3KVF   RELATED DB: PDB
DBREF  3KW5 A    1   223  UNP    P09936   UCHL1_HUMAN      1    223
DBREF  3KW5 B    1    75  UNP    P62988   UBIQ_HUMAN       1     75
SEQADV 3KW5 GLY A   -4  UNP  P09936              EXPRESSION TAG
SEQADV 3KW5 PRO A   -3  UNP  P09936              EXPRESSION TAG
SEQADV 3KW5 LEU A   -2  UNP  P09936              EXPRESSION TAG
SEQADV 3KW5 GLY A   -1  UNP  P09936              EXPRESSION TAG
SEQADV 3KW5 SER A    0  UNP  P09936              EXPRESSION TAG
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   75  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES   2 B   75  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES   3 B   75  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES   4 B   75  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES   5 B   75  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES   6 B   75  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY
HET    GVE  B  76       8
HETNAM     GVE METHYL 4-AMINOBUTANOATE
FORMUL   3  GVE    C5 H11 N O2
HELIX    1   1 ASN A    9  GLY A   21  1                                  13
HELIX    2   2 GLU A   35  GLY A   40  1                                   6
HELIX    3   3 THR A   56  LYS A   71  1                                  16
HELIX    4   4 SER A   89  ASN A  101  1                                  13
HELIX    5   5 SER A  112  GLU A  122  1                                  11
HELIX    6   6 SER A  125  LYS A  135  1                                  11
HELIX    7   7 ASN A  136  GLN A  148  1                                  13
HELIX    8   8 THR A  192  GLU A  208  1                                  17
HELIX    9   9 THR B   22  GLY B   35  1                                  14
HELIX   10  10 PRO B   37  ASP B   39  5                                   3
HELIX   11  11 LEU B   56  ASN B   60  5                                   5
SHEET    1   A 2 MET A   6  GLU A   7  0
SHEET    2   A 2 ARG B  74  GLY B  75 -1  O  GLY B  75   N  MET A   6
SHEET    1   B 2 VAL A  22  ALA A  23  0
SHEET    2   B 2 GLY A 107  PHE A 108 -1  O  GLY A 107   N  ALA A  23
SHEET    1   C 6 TRP A  26  ASP A  30  0
SHEET    2   C 6 SER A 215  LYS A 221 -1  O  ALA A 218   N  VAL A  29
SHEET    3   C 6 ALA A  46  PRO A  54 -1  N  LEU A  52   O  SER A 215
SHEET    4   C 6 PHE A 160  VAL A 168 -1  O  ILE A 163   N  LEU A  51
SHEET    5   C 6 HIS A 171  LEU A 175 -1  O  LEU A 175   N  LEU A 164
SHEET    6   C 6 VAL A 183  ALA A 187 -1  O  HIS A 185   N  LEU A 172
SHEET    1   D 5 THR B  12  GLU B  16  0
SHEET    2   D 5 GLN B   2  THR B   7 -1  N  ILE B   3   O  LEU B  15
SHEET    3   D 5 THR B  66  LEU B  71  1  O  LEU B  67   N  LYS B   6
SHEET    4   D 5 GLN B  41  PHE B  45 -1  N  ARG B  42   O  VAL B  70
SHEET    5   D 5 LYS B  48  GLN B  49 -1  O  LYS B  48   N  PHE B  45
LINK         C   GLY B  75                 N   GVE B  76     1555   1555  1.27
LINK         SG  CYS A  90                 CB  GVE B  76     1555   1555  1.81
CISPEP   1 ALA A   44    PRO A   45          0        -4.20
SITE     1 AC1  7 GLN A  84  ASN A  88  CYS A  90  ASN A 159
SITE     2 AC1  7 PHE A 160  HIS A 161  GLY B  75
CRYST1   86.989   86.989  193.434  90.00  90.00 120.00 H 3 2        18
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.011496  0.006637  0.000000        0.00000
SCALE2      0.000000  0.013274  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005170        0.00000
      
PROCHECK
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 References