Header list of 1x6c.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 17-MAY-05 1X6C
TITLE SOLUTION STRUCTURES OF THE SH2 DOMAIN OF HUMAN PROTEIN-TYROSINE
TITLE 2 PHOSPHATASE SHP-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE, NON-RECEPTOR TYPE 6;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH2 DOMAIN;
COMPND 5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE 1C, PTP-1C, HEMATOPOIETIC CELL
COMPND 6 PROTEIN-TYROSINE PHOSPHATASE, SH-PTP1, PROTEIN-TYROSINE PHOSPHATASE
COMPND 7 SHP-1;
COMPND 8 EC: 3.1.3.48;
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: PTPN6;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040607-04;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS SH2 DOMAIN, HCP, PTP1C, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT
KEYWDS 2 ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.SATO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X6C 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X6C 1 VERSN
REVDAT 1 17-NOV-05 1X6C 0
JRNL AUTH M.SATO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURES OF THE SH2 DOMAIN OF HUMAN
JRNL TITL 2 PROTEIN-TYROSINE PHOSPHATASE SHP-1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 1.0.7
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X6C COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024434.
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 : 1MM SH2 DOMAIN U-15N, 13C; 20MM
REMARK 210 D-TRIS HCL; 100MM NACL; 1MM D-
REMARK 210 DTT; 0.02% NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9295, CYANA 1.0.7
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 LEAST RESTRAINT VIOLATIONS
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: CLOSE CONTACTS
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 O ILE A 97 H VAL A 105 1.51
REMARK 500 O LEU A 45 H ILE A 65 1.51
REMARK 500 O ALA A 18 H LEU A 22 1.51
REMARK 500 O LEU A 85 H VAL A 89 1.51
REMARK 500 O THR A 20 H ALA A 24 1.56
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 1 SER A 5 87.65 -158.32
REMARK 500 1 SER A 6 91.47 46.30
REMARK 500 1 TYR A 9 106.23 -54.92
REMARK 500 1 TRP A 29 52.16 74.80
REMARK 500 1 ARG A 61 167.25 -45.01
REMARK 500 1 SER A 113 167.65 58.55
REMARK 500 2 SER A 2 -60.12 -129.94
REMARK 500 2 SER A 5 86.99 40.14
REMARK 500 2 SER A 6 -61.32 71.50
REMARK 500 2 TYR A 9 101.77 -51.07
REMARK 500 2 GLU A 27 114.22 -38.42
REMARK 500 2 TRP A 29 52.92 74.10
REMARK 500 2 TYR A 112 -83.53 56.95
REMARK 500 2 SER A 113 140.72 74.59
REMARK 500 2 SER A 116 158.19 63.64
REMARK 500 3 SER A 5 125.62 -173.21
REMARK 500 3 SER A 6 70.51 -113.34
REMARK 500 3 TYR A 9 103.26 -54.93
REMARK 500 3 HIS A 12 91.95 -69.28
REMARK 500 3 TRP A 29 42.09 74.04
REMARK 500 3 ARG A 61 150.54 -40.87
REMARK 500 3 LYS A 94 -62.93 -120.98
REMARK 500 4 SER A 2 -62.07 -156.11
REMARK 500 4 SER A 3 103.83 65.14
REMARK 500 4 TYR A 9 101.45 -51.24
REMARK 500 4 GLU A 27 114.94 -38.49
REMARK 500 4 TRP A 29 46.89 73.70
REMARK 500 4 ARG A 61 160.40 -45.20
REMARK 500 4 LYS A 94 -62.75 -122.01
REMARK 500 4 SER A 113 -70.74 69.99
REMARK 500 4 SER A 116 156.21 -45.14
REMARK 500 5 SER A 2 119.69 -170.95
REMARK 500 5 SER A 3 -55.86 -157.83
REMARK 500 5 SER A 6 -175.10 -69.67
REMARK 500 5 TYR A 9 99.27 -57.14
REMARK 500 5 TRP A 29 45.50 76.30
REMARK 500 5 ARG A 61 168.56 -46.61
REMARK 500 5 LYS A 94 -63.17 -121.50
REMARK 500 5 SER A 113 165.20 60.62
REMARK 500 6 SER A 6 83.67 53.35
REMARK 500 6 TYR A 9 102.64 -57.06
REMARK 500 6 GLU A 27 113.80 -38.35
REMARK 500 6 TRP A 29 51.69 74.16
REMARK 500 6 ARG A 61 157.34 -47.28
REMARK 500 6 LYS A 94 -63.91 -120.37
REMARK 500 6 SER A 113 -46.09 -133.61
REMARK 500 6 SER A 116 82.20 46.19
REMARK 500 7 SER A 6 -171.45 51.08
REMARK 500 7 TYR A 9 103.78 -59.10
REMARK 500 7 TRP A 29 47.19 74.69
REMARK 500
REMARK 500 THIS ENTRY HAS 134 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001003119.1 RELATED DB: TARGETDB
DBREF 1X6C A 8 112 UNP P29350 PTN6_HUMAN 110 214
SEQADV 1X6C GLY A 1 UNP P29350 CLONING ARTIFACT
SEQADV 1X6C SER A 2 UNP P29350 CLONING ARTIFACT
SEQADV 1X6C SER A 3 UNP P29350 CLONING ARTIFACT
SEQADV 1X6C GLY A 4 UNP P29350 CLONING ARTIFACT
SEQADV 1X6C SER A 5 UNP P29350 CLONING ARTIFACT
SEQADV 1X6C SER A 6 UNP P29350 CLONING ARTIFACT
SEQADV 1X6C GLY A 7 UNP P29350 CLONING ARTIFACT
SEQADV 1X6C SER A 113 UNP P29350 CLONING ARTIFACT
SEQADV 1X6C GLY A 114 UNP P29350 CLONING ARTIFACT
SEQADV 1X6C PRO A 115 UNP P29350 CLONING ARTIFACT
SEQADV 1X6C SER A 116 UNP P29350 CLONING ARTIFACT
SEQADV 1X6C SER A 117 UNP P29350 CLONING ARTIFACT
SEQADV 1X6C GLY A 118 UNP P29350 CLONING ARTIFACT
SEQRES 1 A 118 GLY SER SER GLY SER SER GLY TRP TYR HIS GLY HIS MET
SEQRES 2 A 118 SER GLY GLY GLN ALA GLU THR LEU LEU GLN ALA LYS GLY
SEQRES 3 A 118 GLU PRO TRP THR PHE LEU VAL ARG GLU SER LEU SER GLN
SEQRES 4 A 118 PRO GLY ASP PHE VAL LEU SER VAL LEU SER ASP GLN PRO
SEQRES 5 A 118 LYS ALA GLY PRO GLY SER PRO LEU ARG VAL THR HIS ILE
SEQRES 6 A 118 LYS VAL MET CYS GLU GLY GLY ARG TYR THR VAL GLY GLY
SEQRES 7 A 118 LEU GLU THR PHE ASP SER LEU THR ASP LEU VAL GLU HIS
SEQRES 8 A 118 PHE LYS LYS THR GLY ILE GLU GLU ALA SER GLY ALA PHE
SEQRES 9 A 118 VAL TYR LEU ARG GLN PRO TYR TYR SER GLY PRO SER SER
SEQRES 10 A 118 GLY
HELIX 1 1 SER A 14 GLY A 26 1 13
HELIX 2 2 SER A 84 GLY A 96 1 13
SHEET 1 A 5 ARG A 73 THR A 75 0
SHEET 2 A 5 LEU A 60 GLU A 70 -1 N MET A 68 O THR A 75
SHEET 3 A 5 PHE A 43 PRO A 52 -1 N LEU A 45 O ILE A 65
SHEET 4 A 5 THR A 30 GLU A 35 -1 N THR A 30 O LEU A 48
SHEET 5 A 5 GLN A 109 PRO A 110 1 O GLN A 109 N PHE A 31
SHEET 1 B 2 ILE A 97 GLU A 98 0
SHEET 2 B 2 PHE A 104 VAL A 105 -1 O VAL A 105 N ILE A 97
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