Header list of 1wh0.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 28-MAY-04 1WH0
TITLE SOLUTION STRUCTURE OF THE CS DOMAIN OF HUMAN USP19
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 19;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CS DOMAIN;
COMPND 5 SYNONYM: UBIQUITIN SPECIFIC PROTEASE 19, UBIQUITIN THIOLESTERASE 19,
COMPND 6 UBIQUITIN-SPECIFIC PROCESSING PROTEASE 19, DEUBIQUITINATING ENZYME
COMPND 7 19, ZINC FINGER MYND DOMAIN CONTAINING PROTEIN 9;
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 GENE: KAZUSA CDNA HK08201;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040114-29;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS USP, CS DOMAIN, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.NAKANISHI,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WH0 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WH0 1 VERSN
REVDAT 1 28-NOV-04 1WH0 0
JRNL AUTH T.NAKANISHI,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE CS DOMAIN OF HUMAN USP19
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.0.17
REMARK 3 AUTHORS : GUNTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WH0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023570.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.15MM CS DOMAIN U-15N, 13C;
REMARK 210 20MM NAPI; 100MM NACL; 2MM D-DTT;
REMARK 210 0.02% NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, NMRPIPE 20030801,
REMARK 210 NMRVIEW 5.0.4, KUJIRA 0.8999,
REMARK 210 CYANA 2.0.17
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
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 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 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 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 1 PRO A 11 5.51 -69.70
REMARK 500 1 VAL A 38 146.37 -172.44
REMARK 500 1 ASP A 54 -178.73 -171.33
REMARK 500 1 PHE A 55 117.54 -164.31
REMARK 500 1 ALA A 100 -75.39 -39.62
REMARK 500 1 PRO A 121 -173.02 -69.71
REMARK 500 1 ALA A 123 138.09 -38.27
REMARK 500 1 SER A 132 100.20 -36.60
REMARK 500 2 SER A 6 -179.90 -69.20
REMARK 500 2 GLU A 10 155.80 -41.70
REMARK 500 2 PRO A 11 3.52 -69.67
REMARK 500 2 LYS A 21 104.21 -56.00
REMARK 500 2 ASP A 54 -178.05 -172.37
REMARK 500 2 PHE A 55 115.53 -164.97
REMARK 500 2 ALA A 100 -75.18 -39.97
REMARK 500 2 SER A 112 53.58 -90.54
REMARK 500 2 PRO A 121 -174.04 -69.83
REMARK 500 2 ALA A 128 173.53 -48.38
REMARK 500 2 PRO A 131 -179.66 -69.76
REMARK 500 3 SER A 3 96.80 -62.54
REMARK 500 3 GLU A 10 138.40 -34.54
REMARK 500 3 PRO A 11 5.40 -69.77
REMARK 500 3 VAL A 38 148.32 -173.65
REMARK 500 3 ASP A 54 -177.42 -171.49
REMARK 500 3 PHE A 55 115.88 -161.95
REMARK 500 3 ALA A 100 -76.56 -39.89
REMARK 500 3 PRO A 121 -173.05 -69.77
REMARK 500 3 ARG A 124 41.27 34.07
REMARK 500 4 GLU A 10 145.41 -37.74
REMARK 500 4 PRO A 11 3.72 -69.75
REMARK 500 4 LYS A 21 103.35 -58.36
REMARK 500 4 ASP A 54 -175.18 -175.84
REMARK 500 4 ALA A 100 -76.18 -40.58
REMARK 500 4 PRO A 121 -173.70 -69.75
REMARK 500 4 ALA A 122 48.29 73.76
REMARK 500 4 ALA A 123 122.67 -170.46
REMARK 500 4 PRO A 131 -176.45 -69.77
REMARK 500 5 ASP A 9 50.82 -98.11
REMARK 500 5 PRO A 11 2.47 -69.77
REMARK 500 5 VAL A 38 146.02 -170.19
REMARK 500 5 ASP A 54 -178.57 -172.57
REMARK 500 5 PHE A 55 114.82 -166.79
REMARK 500 5 ALA A 100 -75.10 -47.85
REMARK 500 5 LEU A 118 -73.37 -38.61
REMARK 500 5 PRO A 121 -176.73 -69.72
REMARK 500 6 SER A 2 40.86 -105.85
REMARK 500 6 SER A 6 50.51 39.96
REMARK 500 6 GLU A 10 145.20 -35.15
REMARK 500 6 PRO A 11 5.50 -69.82
REMARK 500 6 LYS A 21 106.39 -57.23
REMARK 500
REMARK 500 THIS ENTRY HAS 200 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 AUTHOR DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 AUTHOR DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002000870.1 RELATED DB: TARGETDB
DBREF 1WH0 A 8 128 UNP O94966 UBP19_HUMAN 326 446
SEQADV 1WH0 GLY A 1 UNP O94966 CLONING ARTIFACT
SEQADV 1WH0 SER A 2 UNP O94966 CLONING ARTIFACT
SEQADV 1WH0 SER A 3 UNP O94966 CLONING ARTIFACT
SEQADV 1WH0 GLY A 4 UNP O94966 CLONING ARTIFACT
SEQADV 1WH0 SER A 5 UNP O94966 CLONING ARTIFACT
SEQADV 1WH0 SER A 6 UNP O94966 CLONING ARTIFACT
SEQADV 1WH0 GLY A 7 UNP O94966 CLONING ARTIFACT
SEQADV 1WH0 SER A 129 UNP O94966 CLONING ARTIFACT
SEQADV 1WH0 GLY A 130 UNP O94966 CLONING ARTIFACT
SEQADV 1WH0 PRO A 131 UNP O94966 CLONING ARTIFACT
SEQADV 1WH0 SER A 132 UNP O94966 CLONING ARTIFACT
SEQADV 1WH0 SER A 133 UNP O94966 CLONING ARTIFACT
SEQADV 1WH0 GLY A 134 UNP O94966 CLONING ARTIFACT
SEQRES 1 A 134 GLY SER SER GLY SER SER GLY VAL ASP GLU PRO GLU SER
SEQRES 2 A 134 MET VAL ASN LEU ALA PHE VAL LYS ASN ASP SER TYR GLU
SEQRES 3 A 134 LYS GLY PRO ASP SER VAL VAL VAL HIS VAL TYR VAL LYS
SEQRES 4 A 134 GLU ILE CYS ARG ASP THR SER ARG VAL LEU PHE ARG GLU
SEQRES 5 A 134 GLN ASP PHE THR LEU ILE PHE GLN THR ARG ASP GLY ASN
SEQRES 6 A 134 PHE LEU ARG LEU HIS PRO GLY CYS GLY PRO HIS THR THR
SEQRES 7 A 134 PHE ARG TRP GLN VAL LYS LEU ARG ASN LEU ILE GLU PRO
SEQRES 8 A 134 GLU GLN CYS THR PHE CYS PHE THR ALA SER ARG ILE ASP
SEQRES 9 A 134 ILE CYS LEU ARG LYS ARG GLN SER GLN ARG TRP GLY GLY
SEQRES 10 A 134 LEU GLU ALA PRO ALA ALA ARG VAL GLY GLY ALA SER GLY
SEQRES 11 A 134 PRO SER SER GLY
HELIX 1 1 PRO A 11 SER A 13 5 3
HELIX 2 2 GLY A 64 LEU A 69 1 6
SHEET 1 A 8 VAL A 15 LEU A 17 0
SHEET 2 A 8 ASN A 22 LYS A 27 0
SHEET 3 A 8 SER A 31 TYR A 37 -1 O HIS A 35 N ASP A 23
SHEET 4 A 8 ARG A 47 PHE A 50 -1 N LEU A 49 O THR A 56
SHEET 5 A 8 ASP A 54 ILE A 58 -1 N LEU A 57 O TRP A 81
SHEET 6 A 8 PHE A 79 LYS A 84 1 O ARG A 80 N VAL A 15
SHEET 7 A 8 THR A 95 PHE A 98 -1 N CYS A 97 O ASP A 104
SHEET 8 A 8 ARG A 102 ARG A 108 -1 O LEU A 107 N VAL A 32
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 2 2 Bytes