HEADER HYDROLASE/SIGNALING PROTEIN 30-NOV-09 3KVF
TITLE CRYSTAL STRUCTURE OF THE I93M MUTANT OF UBIQUITIN CARBOXY TERMINAL
TITLE 2 HYDROLASE L1 BOUND TO UBIQUITIN VINYLMETHYLESTER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: UCH-L1, UBIQUITIN THIOESTERASE L1, NEURON CYTOPLASMIC
COMPND 5 PROTEIN 9.5, PGP 9.5, PGP9.5;
COMPND 6 EC: 3.4.19.12, 6.-.-.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: UBIQUITIN;
COMPND 11 CHAIN: B;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PGP9.5, UCHL1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: RPS27A, UBA52, UBA80, UBB, UBC, UBCEP1, UBCEP2, UBIQ_HUMAN;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PTYB1
KEYWDS ENZYME-SUICIDE SUBSTRATE COMPLEX, CYTOPLASM, DISEASE MUTATION,
KEYWDS 2 GLYCOPROTEIN, HYDROLASE, LIGASE, OXIDATION, POLYMORPHISM, PROTEASE,
KEYWDS 3 THIOL PROTEASE, UBL CONJUGATION PATHWAY, ISOPEPTIDE BOND, NUCLEUS,
KEYWDS 4 PHOSPHOPROTEIN, UBL CONJUGATION, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 5 COMPLEX, ACETYLATION, HYDROLASE-SIGNALING PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.W.DAVIES,T.K.MAITI,C.DAS
REVDAT 1 16-JUN-10 3KVF 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 : 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 6666
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) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 330
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 489
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.61
REMARK 3 BIN R VALUE (WORKING SET) : 0.3550
REMARK 3 BIN FREE R VALUE SET COUNT : 27
REMARK 3 BIN FREE R VALUE : 0.4000
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 : 3
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 109.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.91000
REMARK 3 B22 (A**2) : -1.91000
REMARK 3 B33 (A**2) : 2.86000
REMARK 3 B12 (A**2) : -0.95000
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): 0.485
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.476
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 57.287
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
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): 3204 ; 0.888 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 296 ; 4.594 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 114 ;38.310 ;25.439
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 446 ;15.289 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;14.994 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 357 ; 0.056 ; 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): 1073 ; 0.172 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1624 ; 0.290 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 86 ; 0.115 ; 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): 52 ; 0.211 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.114 ; 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): 1529 ; 0.137 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2381 ; 0.239 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 936 ; 0.419 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 823 ; 0.592 ; 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 3KVF COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-DEC-09.
REMARK 100 THE RCSB ID CODE IS RCSB056496.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-MAR-09
REMARK 200 TEMPERATURE (KELVIN) : 100.0
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 : 6996
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 70.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 10.500
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : 0.08900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.7000
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 8.40
REMARK 200 R MERGE FOR SHELL (I) : 0.85600
REMARK 200 R SYM FOR SHELL (I) : 0.85600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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 (%): 41.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
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 43.54450
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 25.14043
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 64.49200
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 43.54450
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 25.14043
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 64.49200
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 43.54450
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 25.14043
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 64.49200
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 43.54450
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 25.14043
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 64.49200
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 43.54450
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 25.14043
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 64.49200
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 43.54450
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 25.14043
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 64.49200
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 50.28086
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 128.98400
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 50.28086
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 128.98400
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 50.28086
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 128.98400
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 50.28086
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 128.98400
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 50.28086
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 128.98400
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 50.28086
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 128.98400
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: 2630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 CA GLY B 75 N GVE B 76 2.19
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 -125.50 48.19
REMARK 500 GLU A 149 10.72 -67.06
REMARK 500 ARG A 153 -165.19 -74.12
REMARK 500 ASP A 156 -116.70 66.49
REMARK 500 VAL A 158 76.09 -58.24
REMARK 500 GLU A 208 76.79 -101.26
REMARK 500 GLN A 209 -79.48 -43.11
REMARK 500 GLN B 62 -163.89 -106.37
REMARK 500 GLU B 64 -4.76 66.34
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 MUTANT OF THE WILD TYPE UCHL1 BOUND TO UBIQUITIN
REMARK 900 VINYLMETHYLESTER
REMARK 900 RELATED ID: 3KW5 RELATED DB: PDB
DBREF 3KVF A 1 223 UNP P09936 UCHL1_HUMAN 1 223
DBREF 3KVF B 1 75 UNP P62988 UBIQ_HUMAN 1 75
SEQADV 3KVF GLY A -4 UNP P09936 EXPRESSION TAG
SEQADV 3KVF PRO A -3 UNP P09936 EXPRESSION TAG
SEQADV 3KVF LEU A -2 UNP P09936 EXPRESSION TAG
SEQADV 3KVF GLY A -1 UNP P09936 EXPRESSION TAG
SEQADV 3KVF SER A 0 UNP P09936 EXPRESSION TAG
SEQADV 3KVF MET A 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 75 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 B 75 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 B 75 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 B 75 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 B 75 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 B 75 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY
HET GVE B 76 8
HETNAM GVE METHYL 4-AMINOBUTANOATE
FORMUL 3 GVE C5 H11 N O2
FORMUL 4 HOH *3(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 LYS A 71 1 16
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 GLU A 134 1 10
HELIX 7 7 ASN A 136 GLU A 149 1 14
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 CYS A 220 N ARG A 27
SHEET 3 C 6 ALA A 46 PRO A 54 -1 N ALA A 48 O LEU A 219
SHEET 4 C 6 PHE A 160 VAL A 168 -1 O PHE A 165 N LEU A 49
SHEET 5 C 6 HIS A 171 LEU A 175 -1 O TYR A 173 N ASN A 166
SHEET 6 C 6 VAL A 183 ALA A 187 -1 O HIS A 185 N LEU A 172
SHEET 1 D 5 THR B 12 GLU B 16 0
SHEET 2 D 5 GLN B 2 THR B 7 -1 N VAL B 5 O ILE B 13
SHEET 3 D 5 THR B 66 LEU B 71 1 O LEU B 69 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 1.26
LINK SG CYS A 90 CB GVE B 76 1555 1555 1.82
CISPEP 1 ALA A 44 PRO A 45 0 -5.43
SITE 1 AC1 6 GLN A 84 ASN A 88 CYS A 90 PHE A 160
SITE 2 AC1 6 HIS A 161 GLY B 75
CRYST1 87.089 87.089 193.476 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 0.011483 0.006629 0.000000 0.00000
SCALE2 0.000000 0.013259 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005169 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
