HEADER HYDROLASE 03-OCT-11 4A3P
TITLE STRUCTURE OF USP15 DUSP-UBL DELETION MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 15;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DUSP-UBL, RESIDUES 6-123,127-223;
COMPND 5 SYNONYM: DEUBIQUITINATING ENZYME 15, UBIQUITIN THIOLESTERASE 15,
COMPND 6 UBIQUITIN-SPECIFIC-PROCESSING PROTEASE 15, UNPH-2, UNPH4, USP15;
COMPND 7 EC: 3.4.19.12;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.R.ELLIOTT,H.LIU,M.W.PASTOK,G.J.GROSSMANN,D.J.RIGDEN,M.J.CLAGUE,
AUTHOR 2 S.URBE,I.L.BARSUKOV
REVDAT 2 20-DEC-23 4A3P 1 REMARK
REVDAT 1 16-NOV-11 4A3P 0
JRNL AUTH P.R.ELLIOTT,H.LIU,M.W.PASTOK,G.J.GROSSMANN,D.J.RIGDEN,
JRNL AUTH 2 M.J.CLAGUE,S.URBE,I.L.BARSUKOV
JRNL TITL STRUCTURAL VARIABILITY OF THE UBIQUITIN SPECIFIC PROTEASE
JRNL TITL 2 DUSP-UBL DOUBLE DOMAINS.
JRNL REF FEBS LETT. V. 585 3385 2011
JRNL REFN ISSN 0014-5793
JRNL PMID 22001210
JRNL DOI 10.1016/J.FEBSLET.2011.09.040
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 3 NUMBER OF REFLECTIONS : 37168
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) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1981
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.43
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2714
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.42
REMARK 3 BIN R VALUE (WORKING SET) : 0.2050
REMARK 3 BIN FREE R VALUE SET COUNT : 143
REMARK 3 BIN FREE R VALUE : 0.3170
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1713
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 223
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : 0.04000
REMARK 3 B33 (A**2) : -0.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.13000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.071
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.075
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.047
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.624
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1788 ; 0.020 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1218 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2427 ; 1.891 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2987 ; 1.212 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 219 ; 5.667 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 86 ;39.109 ;25.349
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 325 ;13.376 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;14.948 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 266 ; 0.124 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1958 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 354 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 625 ; 0.321 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1151 ; 0.236 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 851 ; 0.191 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 897 ; 0.110 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 44 ; 0.264 ; 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): 91 ; 0.441 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 62 ; 0.505 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.324 ; 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): 1788 ;13.509 ; 1.922
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1218 ;13.868 ; 1.973
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2420 ;15.308 ; 2.841
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 3006 ;16.083 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 64 ;28.951 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3128 ;13.999 ; 5.000
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 4A3P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1290049885.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : DUAL SLITS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39193
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 34.330
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 13.400
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 200 DATA REDUNDANCY : 2.200
REMARK 200 R MERGE (I) : 0.03000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.47
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.20000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3PV1
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.9 M (NH4)2SO4, 100 MM HEPES PH 7.0,
REMARK 280 200 MM KI.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-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 22.12500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ALA A 5
REMARK 465 ASP A 75
REMARK 465 ALA A 76
REMARK 465 GLN A 77
REMARK 465 GLY A 218
REMARK 465 GLY A 223
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 36 CD NE CZ NH1 NH2
REMARK 470 GLU A 108 CD OE1 OE2
REMARK 470 LYS A 167 CD CE NZ
REMARK 470 LYS A 193 CD CE NZ
REMARK 470 LYS A 214 CD CE NZ
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 NZ LYS A 42 O HOH A 2065 1.56
REMARK 500 OD2 ASP A 200 O HOH A 2209 2.10
REMARK 500 O HOH A 2068 O HOH A 2125 2.10
REMARK 500 O HOH A 2007 O HOH A 2023 2.10
REMARK 500 O HOH A 2013 O HOH A 2014 2.13
REMARK 500 OE2 GLU A 162 OG1 THR A 177 2.16
REMARK 500 CE LYS A 42 O HOH A 2065 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE1 GLU A 119 OE2 GLU A 174 2645 1.64
REMARK 500 O HOH A 2039 O HOH A 2194 2655 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PHE A 123 CD1 PHE A 123 CE1 -0.124
REMARK 500 PHE A 123 CE1 PHE A 123 CZ -0.118
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 13 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ASP A 57 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 86 -50.90 80.24
REMARK 500 THR A 105 158.08 71.31
REMARK 500 PHE A 123 -159.35 -106.22
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 ACT A 1223
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1W6V RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE DUSP DOMAIN OF HUSP15
REMARK 900 RELATED ID: 4A3O RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE USP15 DUSP-UBL MONOMER
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 124-126 (VKH) WERE SUB-CLONED OUT OF THE SEQUENCE
REMARK 999 TO GENERATE A DELETION MUTANT. F123 IS PEPTIDE LINKED TO C127.
DBREF 4A3P A 6 223 UNP Q9Y4E8 UBP15_HUMAN 6 223
SEQADV 4A3P A UNP Q9Y4E8 VAL 124 DELETION
SEQADV 4A3P A UNP Q9Y4E8 LYS 125 DELETION
SEQADV 4A3P A UNP Q9Y4E8 HIS 126 DELETION
SEQADV 4A3P GLY A 4 UNP Q9Y4E8 EXPRESSION TAG
SEQADV 4A3P ALA A 5 UNP Q9Y4E8 EXPRESSION TAG
SEQRES 1 A 217 GLY ALA ALA ALA ASP LEU ASP THR GLN ARG SER ASP ILE
SEQRES 2 A 217 ALA THR LEU LEU LYS THR SER LEU ARG LYS GLY ASP THR
SEQRES 3 A 217 TRP TYR LEU VAL ASP SER ARG TRP PHE LYS GLN TRP LYS
SEQRES 4 A 217 LYS TYR VAL GLY PHE ASP SER TRP ASP LYS TYR GLN MET
SEQRES 5 A 217 GLY ASP GLN ASN VAL TYR PRO GLY PRO ILE ASP ASN SER
SEQRES 6 A 217 GLY LEU LEU LYS ASP GLY ASP ALA GLN SER LEU LYS GLU
SEQRES 7 A 217 HIS LEU ILE ASP GLU LEU ASP TYR ILE LEU LEU PRO THR
SEQRES 8 A 217 GLU GLY TRP ASN LYS LEU VAL SER TRP TYR THR LEU MET
SEQRES 9 A 217 GLU GLY GLN GLU PRO ILE ALA ARG LYS VAL VAL GLU GLN
SEQRES 10 A 217 GLY MET PHE CYS LYS VAL GLU VAL TYR LEU THR GLU LEU
SEQRES 11 A 217 LYS LEU CYS GLU ASN GLY ASN MET ASN ASN VAL VAL THR
SEQRES 12 A 217 ARG ARG PHE SER LYS ALA ASP THR ILE ASP THR ILE GLU
SEQRES 13 A 217 LYS GLU ILE ARG LYS ILE PHE SER ILE PRO ASP GLU LYS
SEQRES 14 A 217 GLU THR ARG LEU TRP ASN LYS TYR MET SER ASN THR PHE
SEQRES 15 A 217 GLU PRO LEU ASN LYS PRO ASP SER THR ILE GLN ASP ALA
SEQRES 16 A 217 GLY LEU TYR GLN GLY GLN VAL LEU VAL ILE GLU GLN LYS
SEQRES 17 A 217 ASN GLU ASP GLY THR TRP PRO ARG GLY
HET ACT A1223 4
HET IOD A1224 1
HETNAM ACT ACETATE ION
HETNAM IOD IODIDE ION
FORMUL 2 ACT C2 H3 O2 1-
FORMUL 3 IOD I 1-
FORMUL 4 HOH *223(H2 O)
HELIX 1 1 ASP A 8 LEU A 20 1 13
HELIX 2 2 SER A 35 GLY A 46 1 12
HELIX 3 3 ASP A 57 TYR A 61 5 5
HELIX 4 4 ASN A 67 LEU A 70 5 4
HELIX 5 5 THR A 94 THR A 105 1 12
HELIX 6 6 THR A 157 PHE A 169 1 13
HELIX 7 7 THR A 197 GLY A 202 1 6
SHEET 1 AA 4 TYR A 89 PRO A 93 0
SHEET 2 AA 4 THR A 29 ASP A 34 -1 O TYR A 31 N LEU A 92
SHEET 3 AA 4 ALA A 114 GLN A 120 -1 O ARG A 115 N TRP A 30
SHEET 4 AA 4 PHE A 123 VAL A 129 -1 O PHE A 123 N GLN A 120
SHEET 1 AB 5 ASN A 143 PHE A 152 0
SHEET 2 AB 5 THR A 134 GLU A 140 -1 O THR A 134 N PHE A 152
SHEET 3 AB 5 VAL A 208 GLN A 213 1 O LEU A 209 N CYS A 139
SHEET 4 AB 5 THR A 177 MET A 184 -1 O ARG A 178 N GLU A 212
SHEET 5 AB 5 THR A 187 PRO A 190 -1 O THR A 187 N TYR A 183
SITE 1 AC1 4 ASP A 15 LEU A 19 GLU A 95 LYS A 99
CRYST1 44.950 44.250 56.150 90.00 104.33 90.00 P 1 21 1 2
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 0.022247 0.000000 0.005683 0.00000
SCALE2 0.000000 0.022599 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018381 0.00000
(ATOM LINES ARE NOT SHOWN.)
END