Header list of 2cs5.pdb file
Complete list - r 9 2 Bytes
HEADER HYDROLASE 20-MAY-05 2CS5
TITLE SOLUTION STRUCTURE OF PDZ DOMAIN OF PROTEIN TYROSINE PHOSPHATASE, NON-
TITLE 2 RECEPTOR TYPE 4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE, NON-RECEPTOR TYPE 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ DOMAIN;
COMPND 5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE MEG1, PTPASE-MEG1, MEG;
COMPND 6 EC: 3.1.3.48;
COMPND 7 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: PTPN4;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041115-04;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PDZ DOMAIN, PTPASE, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CS5 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CS5 1 VERSN
REVDAT 1 20-NOV-05 2CS5 0
JRNL AUTH T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF PDZ DOMAIN OF PROTEIN TYROSINE
JRNL TITL 2 PHOSPHATASE, NON-RECEPTOR TYPE 4
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CS5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024562.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.83MM PDZ DOMAIN U-13C, 15N;
REMARK 210 20MM TRISHCL, 100MM NACL, 1MM
REMARK 210 DTT, 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.901, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION, STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY
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 ASP A 14 160.09 -43.01
REMARK 500 1 LYS A 40 36.18 32.80
REMARK 500 1 PRO A 50 -169.47 -69.77
REMARK 500 1 PRO A 53 2.83 -69.76
REMARK 500 1 ASP A 65 101.34 -52.92
REMARK 500 1 ASN A 71 30.25 38.35
REMARK 500 1 SER A 95 98.74 -52.24
REMARK 500 1 GLU A 113 107.60 -168.32
REMARK 500 1 PRO A 116 -176.81 -69.75
REMARK 500 2 HIS A 13 29.89 46.71
REMARK 500 2 ASN A 15 -53.31 -127.98
REMARK 500 2 LYS A 40 53.40 34.86
REMARK 500 2 VAL A 45 102.97 -50.66
REMARK 500 2 PRO A 53 0.42 -69.72
REMARK 500 2 GLU A 63 158.00 -45.66
REMARK 500 2 ASP A 65 85.99 -55.19
REMARK 500 2 ASN A 71 26.11 48.58
REMARK 500 2 ASN A 105 79.68 -116.02
REMARK 500 2 GLU A 113 114.61 -170.57
REMARK 500 2 PRO A 116 -170.48 -69.79
REMARK 500 3 PRO A 23 89.14 -69.71
REMARK 500 3 ASP A 24 -71.21 -122.30
REMARK 500 3 LYS A 40 39.58 39.40
REMARK 500 3 PRO A 53 2.72 -69.73
REMARK 500 3 LEU A 61 94.61 -69.58
REMARK 500 3 ASP A 65 105.07 -51.98
REMARK 500 3 GLU A 92 78.44 -100.95
REMARK 500 3 VAL A 110 149.76 -34.58
REMARK 500 3 GLU A 113 108.49 -165.46
REMARK 500 4 ASP A 14 106.59 -38.16
REMARK 500 4 ASP A 24 -176.92 -52.45
REMARK 500 4 ASP A 65 90.93 -53.31
REMARK 500 4 ARG A 93 88.03 -56.09
REMARK 500 4 GLU A 97 172.01 -46.92
REMARK 500 4 TYR A 108 132.86 -34.62
REMARK 500 4 ASP A 109 145.31 -170.69
REMARK 500 4 SER A 117 43.87 38.73
REMARK 500 5 ASN A 8 111.62 -161.39
REMARK 500 5 ASP A 24 179.37 -49.84
REMARK 500 5 LYS A 40 41.43 35.30
REMARK 500 5 ASP A 65 102.65 -48.33
REMARK 500 5 SER A 95 -55.69 -124.29
REMARK 500 5 ASN A 105 75.99 -103.58
REMARK 500 5 ALA A 106 99.23 -41.04
REMARK 500 5 SER A 117 -50.22 -132.84
REMARK 500 6 HIS A 13 -51.51 -120.73
REMARK 500 6 ASP A 24 177.61 -54.34
REMARK 500 6 LYS A 40 32.04 39.21
REMARK 500 6 PRO A 53 1.03 -69.79
REMARK 500 6 ASP A 55 -61.62 -99.07
REMARK 500
REMARK 500 THIS ENTRY HAS 167 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002021070.1 RELATED DB: TARGETDB
DBREF 2CS5 A 8 113 UNP P29074 PTN4_HUMAN 507 612
SEQADV 2CS5 GLY A 1 UNP P29074 CLONING ARTIFACT
SEQADV 2CS5 SER A 2 UNP P29074 CLONING ARTIFACT
SEQADV 2CS5 SER A 3 UNP P29074 CLONING ARTIFACT
SEQADV 2CS5 GLY A 4 UNP P29074 CLONING ARTIFACT
SEQADV 2CS5 SER A 5 UNP P29074 CLONING ARTIFACT
SEQADV 2CS5 SER A 6 UNP P29074 CLONING ARTIFACT
SEQADV 2CS5 GLY A 7 UNP P29074 CLONING ARTIFACT
SEQADV 2CS5 SER A 114 UNP P29074 CLONING ARTIFACT
SEQADV 2CS5 GLY A 115 UNP P29074 CLONING ARTIFACT
SEQADV 2CS5 PRO A 116 UNP P29074 CLONING ARTIFACT
SEQADV 2CS5 SER A 117 UNP P29074 CLONING ARTIFACT
SEQADV 2CS5 SER A 118 UNP P29074 CLONING ARTIFACT
SEQADV 2CS5 GLY A 119 UNP P29074 CLONING ARTIFACT
SEQRES 1 A 119 GLY SER SER GLY SER SER GLY ASN GLY GLY ILE PRO HIS
SEQRES 2 A 119 ASP ASN LEU VAL LEU ILE ARG MET LYS PRO ASP GLU ASN
SEQRES 3 A 119 GLY ARG PHE GLY PHE ASN VAL LYS GLY GLY TYR ASP GLN
SEQRES 4 A 119 LYS MET PRO VAL ILE VAL SER ARG VAL ALA PRO GLY THR
SEQRES 5 A 119 PRO ALA ASP LEU CYS VAL PRO ARG LEU ASN GLU GLY ASP
SEQRES 6 A 119 GLN VAL VAL LEU ILE ASN GLY ARG ASP ILE ALA GLU HIS
SEQRES 7 A 119 THR HIS ASP GLN VAL VAL LEU PHE ILE LYS ALA SER CYS
SEQRES 8 A 119 GLU ARG HIS SER GLY GLU LEU MET LEU LEU VAL ARG PRO
SEQRES 9 A 119 ASN ALA VAL TYR ASP VAL VAL GLU GLU SER GLY PRO SER
SEQRES 10 A 119 SER GLY
HELIX 1 1 TYR A 37 LYS A 40 5 4
HELIX 2 2 THR A 79 ARG A 93 1 15
SHEET 1 A 5 VAL A 17 MET A 21 0
SHEET 2 A 5 LEU A 98 ARG A 103 -1 O VAL A 102 N VAL A 17
SHEET 3 A 5 GLN A 66 ILE A 70 -1 N VAL A 68 O LEU A 101
SHEET 4 A 5 MET A 41 VAL A 48 -1 N VAL A 43 O VAL A 67
SHEET 5 A 5 PHE A 31 GLY A 36 -1 N ASN A 32 O SER A 46
CISPEP 1 VAL A 58 PRO A 59 1 0.01
CISPEP 2 VAL A 58 PRO A 59 2 0.05
CISPEP 3 VAL A 58 PRO A 59 3 -0.03
CISPEP 4 VAL A 58 PRO A 59 4 -0.04
CISPEP 5 VAL A 58 PRO A 59 5 -0.07
CISPEP 6 VAL A 58 PRO A 59 6 -0.03
CISPEP 7 VAL A 58 PRO A 59 7 -0.03
CISPEP 8 VAL A 58 PRO A 59 8 -0.02
CISPEP 9 VAL A 58 PRO A 59 9 0.00
CISPEP 10 VAL A 58 PRO A 59 10 -0.08
CISPEP 11 VAL A 58 PRO A 59 11 -0.05
CISPEP 12 VAL A 58 PRO A 59 12 0.00
CISPEP 13 VAL A 58 PRO A 59 13 -0.08
CISPEP 14 VAL A 58 PRO A 59 14 -0.06
CISPEP 15 VAL A 58 PRO A 59 15 -0.10
CISPEP 16 VAL A 58 PRO A 59 16 -0.07
CISPEP 17 VAL A 58 PRO A 59 17 0.01
CISPEP 18 VAL A 58 PRO A 59 18 -0.09
CISPEP 19 VAL A 58 PRO A 59 19 -0.02
CISPEP 20 VAL A 58 PRO A 59 20 -0.08
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 9 2 Bytes