Header list of 1w6v.pdb file
Complete list - r 25 2 Bytes
HEADER HYDROLASE 24-AUG-04 1W6V
TITLE SOLUTION STRUCTURE OF THE DUSP DOMAIN OF HUSP15
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 15;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DUSP DOMAIN, RESIDUES 1-120;
COMPND 5 SYNONYM: UBIQUITIN THIOLESTERASE 15, UBIQUITIN-SPECIFIC
COMPND 6 PROCESSING PROTEASE 15, UBIQUITINATING ENZYME 15, UNPH-2,
COMPND 7 UNPH4;
COMPND 8 EC: 3.1.2.15;
COMPND 9 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: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 9 OTHER_DETAILS: SELF MADE CDNA LIBRARY OF MULTIPLE HUMAN
SOURCE 10 CARCINOMA CELL LINES
KEYWDS HYDROLASE, UCH, USP, DUB, DEUBIQUITYLATION,
KEYWDS 2 DEUBIQUITINATING ENZYME, UBIQUITIN, UBIQUITIN SPECIFIC
KEYWDS 3 PROTEASE, UBIQUITIN CARBOXYTERMINAL HYDROLASE, CLEAVAGE,
KEYWDS 4 USP15, DUB15, UBP15, ENDOPEPTIDASE, THIOLESTERASE, DUSP,
KEYWDS 5 STRUCTURAL PROTEOMICS IN EUROPE, SPINE, STRUCTURAL
KEYWDS 6 GENOMICS
EXPDTA SOLUTION NMR
NUMMDL 13
AUTHOR R.D.DE JONG,E.AB,T.DIERCKS,V.TRUFFAULT,M.DANIELS,R.KAPTEIN,
AUTHOR 2 G.E.FOLKERS
REVDAT 3 24-FEB-09 1W6V 1 VERSN
REVDAT 2 22-FEB-06 1W6V 1 JRNL
REVDAT 1 12-JAN-06 1W6V 0
JRNL AUTH R.N.DE JONG,E.AB,T.DIERCKS,V.TRUFFAULT,M.DANIELS,
JRNL AUTH 2 R.KAPTEIN,G.E.FOLKERS
JRNL TITL SOLUTION STRUCTURE OF THE HUMAN UBIQUITIN-SPECIFIC
JRNL TITL 2 PROTEASE 15 DUSP DOMAIN.
JRNL REF J.BIOL.CHEM. V. 281 5026 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16298993
JRNL DOI 10.1074/JBC.M510993200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN
REMARK 3 THE JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1W6V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-AUG-04.
REMARK 100 THE PDBE ID CODE IS EBI-20880.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 150 MM
REMARK 210 PRESSURE : 1.0
REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCO,HNCACO,HNCACB,
REMARK 210 CBCACONH,HNCA,HBHACONH,
REMARK 210 HNCAHA,CCH-COSY,HCCH-TOCSY,
REMARK 210 HNH-NOESY,HCH-NOESY,CNH-
REMARK 210 NOESY,HH-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY
REMARK 210 METHOD USED : CANDID IN CYANA AND CNS
REMARK 210 FOR WATER REFINEMENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 13
REMARK 210 CONFORMERS, SELECTION CRITERIA : SMALLEST MAXIMUM RESTRAINT
REMARK 210 VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE
REMARK 210 NMR SPECTROSCOPY ON 15N- AND 13C, 15N-LABELED HIS-TAGGED
REMARK 210 HUSP15_1-120
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 CATALYTIC ACTIVITY: UBIQUITIN C-TERMINAL THIOLESTER + H(2)O =
REMARK 400 UBIQUITIN + A THIOL.
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 MET A -21
REMARK 465 GLY A -20
REMARK 465 SER A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 GLY A -9
REMARK 465 LEU A -8
REMARK 465 VAL A -7
REMARK 465 PRO A -6
REMARK 465 ARG A -5
REMARK 465 GLY A -4
REMARK 465 SER A -3
REMARK 465 HIS A -2
REMARK 465 MET A -1
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 13 LYS A 52 N - CA - CB ANGL. DEV. = -12.7 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 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 1 ALA A 6 -168.93 70.80
REMARK 500 1 ARG A 25 112.01 63.67
REMARK 500 1 ASP A 85 -151.81 -57.12
REMARK 500 1 GLU A 86 -17.81 -39.24
REMARK 500 1 THR A 105 -173.27 48.24
REMARK 500 2 LYS A 52 18.77 -142.33
REMARK 500 2 ALA A 76 13.59 58.22
REMARK 500 2 ASP A 85 -139.52 -59.64
REMARK 500 2 GLU A 86 -18.82 -41.44
REMARK 500 2 THR A 105 167.28 58.30
REMARK 500 3 ARG A 25 -157.45 -104.88
REMARK 500 3 LYS A 52 9.68 -162.39
REMARK 500 3 ASP A 85 -139.08 -62.87
REMARK 500 3 THR A 105 172.00 56.64
REMARK 500 3 VAL A 117 -172.11 -66.71
REMARK 500 4 ARG A 25 -145.52 -127.23
REMARK 500 4 THR A 29 110.20 49.55
REMARK 500 4 LYS A 52 21.41 -156.91
REMARK 500 4 ASP A 85 -139.98 -61.59
REMARK 500 4 GLU A 86 -18.86 -40.33
REMARK 500 4 THR A 105 -174.58 49.63
REMARK 500 5 ARG A 25 -159.55 -104.59
REMARK 500 5 LYS A 52 15.47 -157.50
REMARK 500 5 LYS A 72 -176.95 -64.22
REMARK 500 5 ASP A 85 -146.22 -62.55
REMARK 500 5 GLU A 86 -18.19 -40.74
REMARK 500 5 THR A 105 -174.11 50.62
REMARK 500 5 VAL A 117 -176.85 -60.40
REMARK 500 6 ASP A 51 78.62 -103.37
REMARK 500 6 LYS A 52 3.55 -169.92
REMARK 500 6 TYR A 61 100.47 -34.34
REMARK 500 6 ASP A 85 -130.53 -60.62
REMARK 500 6 GLU A 86 -17.39 -47.51
REMARK 500 6 THR A 105 174.63 56.33
REMARK 500 7 ALA A 6 -158.30 56.43
REMARK 500 7 ARG A 25 -144.68 -105.51
REMARK 500 7 LYS A 52 16.31 -145.93
REMARK 500 7 LYS A 72 -167.87 -74.64
REMARK 500 7 ASP A 85 -134.53 -71.54
REMARK 500 7 GLU A 86 -19.41 -45.53
REMARK 500 7 THR A 105 168.37 57.77
REMARK 500 8 LYS A 72 -169.32 -69.90
REMARK 500 8 ASP A 85 -141.15 -64.59
REMARK 500 8 GLU A 86 -19.90 -40.88
REMARK 500 8 THR A 105 -174.44 53.63
REMARK 500 9 ALA A 2 31.96 -149.61
REMARK 500 9 ASP A 51 -94.34 -129.26
REMARK 500 9 LYS A 52 29.11 42.80
REMARK 500 9 ASP A 85 -130.72 -64.87
REMARK 500 9 GLU A 86 -24.08 -38.43
REMARK 500 9 THR A 105 -170.05 47.28
REMARK 500 10 LYS A 52 13.05 -160.50
REMARK 500 10 TYR A 61 102.38 -33.73
REMARK 500 10 ASP A 85 -142.56 -56.24
REMARK 500 10 GLU A 86 -19.03 -39.09
REMARK 500 10 THR A 105 175.10 52.74
REMARK 500 11 ALA A 2 147.48 69.66
REMARK 500 11 ASP A 75 -49.49 72.16
REMARK 500 11 ASP A 85 -145.14 -63.83
REMARK 500 11 GLU A 86 -17.69 -40.63
REMARK 500 11 THR A 105 -173.46 50.02
REMARK 500 12 ALA A 6 64.42 66.24
REMARK 500 12 ALA A 7 155.34 73.52
REMARK 500 12 THR A 22 167.29 -46.31
REMARK 500 12 ARG A 25 -152.67 60.17
REMARK 500 12 ASP A 85 -110.87 -64.39
REMARK 500 12 THR A 105 -176.50 49.63
REMARK 500 13 ASP A 51 73.15 -150.18
REMARK 500 13 LYS A 52 13.89 -142.57
REMARK 500 13 ASP A 85 -142.03 -67.95
REMARK 500 13 GLU A 86 -18.62 -40.53
REMARK 500 13 THR A 105 174.87 54.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 5 ARG A 13 0.07 SIDE CHAIN
REMARK 500 6 ARG A 13 0.17 SIDE CHAIN
REMARK 500 9 ARG A 13 0.07 SIDE CHAIN
REMARK 500 9 ARG A 115 0.08 SIDE CHAIN
REMARK 500 10 ARG A 36 0.07 SIDE CHAIN
REMARK 500 11 ARG A 13 0.18 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 7 THR A 105 24.6 L L OUTSIDE RANGE
REMARK 500 10 LEU A 32 23.3 L L OUTSIDE RANGE
REMARK 500 10 THR A 105 24.6 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
DBREF 1W6V A -21 -1 PDB 1W6V 1W6V -21 -1
DBREF 1W6V A 1 120 UNP Q9Y4E8 UB15_HUMAN 1 120
SEQRES 1 A 141 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 141 LEU VAL PRO ARG GLY SER HIS MET MET ALA GLU GLY GLY
SEQRES 3 A 141 ALA ALA ASP LEU ASP THR GLN ARG SER ASP ILE ALA THR
SEQRES 4 A 141 LEU LEU LYS THR SER LEU ARG LYS GLY ASP THR TRP TYR
SEQRES 5 A 141 LEU VAL ASP SER ARG TRP PHE LYS GLN TRP LYS LYS TYR
SEQRES 6 A 141 VAL GLY PHE ASP SER TRP ASP LYS TYR GLN MET GLY ASP
SEQRES 7 A 141 GLN ASN VAL TYR PRO GLY PRO ILE ASP ASN SER GLY LEU
SEQRES 8 A 141 LEU LYS ASP GLY ASP ALA GLN SER LEU LYS GLU HIS LEU
SEQRES 9 A 141 ILE ASP GLU LEU ASP TYR ILE LEU LEU PRO THR GLU GLY
SEQRES 10 A 141 TRP ASN LYS LEU VAL SER TRP TYR THR LEU MET GLU GLY
SEQRES 11 A 141 GLN GLU PRO ILE ALA ARG LYS VAL VAL GLU GLN
HELIX 1 1 ASP A 8 LYS A 21 1 14
HELIX 2 2 SER A 35 GLY A 46 1 12
HELIX 3 3 PRO A 93 TYR A 104 1 12
SHEET 1 AA 3 TYR A 89 LEU A 92 0
SHEET 2 AA 3 THR A 29 ASP A 34 -1 O TYR A 31 N LEU A 92
SHEET 3 AA 3 ALA A 114 LYS A 116 -1 O ARG A 115 N TRP A 30
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 25 2 Bytes