Header list of 1x6g.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 17-MAY-05 1X6G
TITLE SOLUTION STRUCTURES OF THE SH3 DOMAIN OF HUMAN MEGAKARYOCYTE-
TITLE 2 ASSOCIATED TYROSINE-PROTEIN KINASE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MEGAKARYOCYTE-ASSOCIATED TYROSINE-PROTEIN KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN;
COMPND 5 SYNONYM: TYROSINE-PROTEIN KINASE CTK, PROTEIN KINASE HYL,
COMPND 6 HEMATOPOIETIC CONSENSUS TYROSINE-LACKING KINASE;
COMPND 7 EC: 2.7.1.112;
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 GENE: MATK;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041101-07;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS MATK, CTK, HYL, SH3 DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 3 STRUCTURAL 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 1X6G 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X6G 1 VERSN
REVDAT 1 17-NOV-05 1X6G 0
JRNL AUTH M.SATO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURES OF THE SH3 DOMAIN OF HUMAN
JRNL TITL 2 MEGAKARYOCYTE-ASSOCIATED TYROSINE-PROTEIN KINASE.
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 1X6G 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_1000024438.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM SH3 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 H ARG A 37 OD2 ASP A 40 1.59
REMARK 500 H HIS A 26 O PHE A 36 1.59
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 6 -63.66 -97.07
REMARK 500 1 ARG A 12 -58.13 -145.04
REMARK 500 1 GLU A 49 34.71 -167.40
REMARK 500 1 ASN A 50 18.95 -144.42
REMARK 500 1 LYS A 51 93.98 65.90
REMARK 500 1 SER A 52 60.47 62.69
REMARK 500 1 SER A 61 -74.21 -59.69
REMARK 500 1 ALA A 71 18.32 -144.68
REMARK 500 1 ARG A 75 107.73 -42.70
REMARK 500 1 SER A 76 82.50 -171.91
REMARK 500 1 SER A 80 125.30 65.57
REMARK 500 2 SER A 3 102.47 -42.16
REMARK 500 2 SER A 6 -58.00 -167.21
REMARK 500 2 ARG A 8 89.70 45.45
REMARK 500 2 MET A 9 146.45 60.45
REMARK 500 2 ARG A 12 124.13 61.86
REMARK 500 2 ARG A 13 158.22 58.53
REMARK 500 2 CYS A 48 98.60 87.07
REMARK 500 2 ASN A 50 21.23 81.49
REMARK 500 2 LYS A 51 152.09 64.46
REMARK 500 2 HIS A 59 -70.14 -60.86
REMARK 500 2 ALA A 71 27.59 -157.37
REMARK 500 2 SER A 76 96.51 -56.05
REMARK 500 2 SER A 79 85.86 47.59
REMARK 500 3 ARG A 8 -55.92 -132.75
REMARK 500 3 CYS A 48 172.06 179.79
REMARK 500 3 GLU A 49 107.93 62.39
REMARK 500 3 ASN A 50 123.63 71.81
REMARK 500 3 LYS A 51 49.94 -85.05
REMARK 500 3 SER A 52 42.16 -174.78
REMARK 500 3 HIS A 59 -79.63 -58.26
REMARK 500 3 SER A 76 74.42 44.14
REMARK 500 4 SER A 5 108.61 -164.88
REMARK 500 4 THR A 11 64.86 -103.75
REMARK 500 4 ARG A 13 170.63 59.18
REMARK 500 4 ILE A 44 109.13 -59.51
REMARK 500 4 ASN A 50 -41.76 169.89
REMARK 500 4 SER A 52 24.85 -154.96
REMARK 500 4 SER A 76 133.55 -172.02
REMARK 500 4 SER A 79 162.49 -43.20
REMARK 500 5 SER A 5 163.91 64.15
REMARK 500 5 ASN A 50 -39.18 176.94
REMARK 500 5 SER A 52 22.36 -150.89
REMARK 500 5 HIS A 59 -70.07 -59.58
REMARK 500 5 ALA A 71 26.54 -154.27
REMARK 500 5 ARG A 75 136.20 -39.80
REMARK 500 6 SER A 5 -58.96 -120.40
REMARK 500 6 SER A 6 121.18 65.76
REMARK 500 6 ARG A 8 106.61 -59.95
REMARK 500 6 ARG A 12 -53.13 -144.48
REMARK 500
REMARK 500 THIS ENTRY HAS 181 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002004506.1 RELATED DB: TARGETDB
DBREF 1X6G A 8 75 UNP P42679 MATK_HUMAN 41 108
SEQADV 1X6G GLY A 1 UNP P42679 CLONING ARTIFACT
SEQADV 1X6G SER A 2 UNP P42679 CLONING ARTIFACT
SEQADV 1X6G SER A 3 UNP P42679 CLONING ARTIFACT
SEQADV 1X6G GLY A 4 UNP P42679 CLONING ARTIFACT
SEQADV 1X6G SER A 5 UNP P42679 CLONING ARTIFACT
SEQADV 1X6G SER A 6 UNP P42679 CLONING ARTIFACT
SEQADV 1X6G GLY A 7 UNP P42679 CLONING ARTIFACT
SEQADV 1X6G SER A 76 UNP P42679 CLONING ARTIFACT
SEQADV 1X6G GLY A 77 UNP P42679 CLONING ARTIFACT
SEQADV 1X6G PRO A 78 UNP P42679 CLONING ARTIFACT
SEQADV 1X6G SER A 79 UNP P42679 CLONING ARTIFACT
SEQADV 1X6G SER A 80 UNP P42679 CLONING ARTIFACT
SEQADV 1X6G GLY A 81 UNP P42679 CLONING ARTIFACT
SEQRES 1 A 81 GLY SER SER GLY SER SER GLY ARG MET PRO THR ARG ARG
SEQRES 2 A 81 TRP ALA PRO GLY THR GLN CYS ILE THR LYS CYS GLU HIS
SEQRES 3 A 81 THR ARG PRO LYS PRO GLY GLU LEU ALA PHE ARG LYS GLY
SEQRES 4 A 81 ASP VAL VAL THR ILE LEU GLU ALA CYS GLU ASN LYS SER
SEQRES 5 A 81 TRP TYR ARG VAL LYS HIS HIS THR SER GLY GLN GLU GLY
SEQRES 6 A 81 LEU LEU ALA ALA GLY ALA LEU ARG GLU ARG SER GLY PRO
SEQRES 7 A 81 SER SER GLY
SHEET 1 A 5 GLU A 64 ALA A 68 0
SHEET 2 A 5 TRP A 53 HIS A 58 -1 N TYR A 54 O LEU A 67
SHEET 3 A 5 VAL A 41 GLU A 46 -1 N LEU A 45 O ARG A 55
SHEET 4 A 5 GLN A 19 THR A 22 -1 N CYS A 20 O VAL A 42
SHEET 5 A 5 LEU A 72 GLU A 74 -1 O ARG A 73 N ILE A 21
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