Header list of 2ct3.pdb file
Complete list - r 9 2 Bytes
HEADER SIGNALING PROTEIN 23-MAY-05 2CT3 TITLE SOLUTION STRUCTURE OF THE SH3 DOMAIN OF THE VINEXIN PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: VINEXIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SH3 DOMAIN; COMPND 5 SYNONYM: SH3-CONTAINING ADAPTER MOLECULE-1, SCAM-1; COMPND 6 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: SCAM1; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041101-09; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEI SYNTHESIS KEYWDS VINEXIN, SCAM-1, SH3 DOMIAN, 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 K.MIYAMOTO,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2CT3 1 REMARK SEQADV REVDAT 2 24-FEB-09 2CT3 1 VERSN REVDAT 1 23-NOV-05 2CT3 0 JRNL AUTH K.MIYAMOTO,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE SH3 DOMAIN OF THE VINEXIN PROTEIN 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 2.0.17 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2CT3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000024592. 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 : 120 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.42MM SH3 DOMAIN U-13C, 15N; REMARK 210 20MM D-TRIS-HCL(PH7.0); 100MM REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 90% REMARK 210 H2O, 10% D2O 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 : 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 0.925, 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 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: 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 GLU A 28 106.55 -50.19 REMARK 500 1 PRO A 67 98.45 -69.69 REMARK 500 2 PRO A 67 97.16 -69.80 REMARK 500 4 GLU A 28 107.84 -56.48 REMARK 500 4 SER A 68 126.95 -38.89 REMARK 500 6 GLU A 28 107.70 -44.64 REMARK 500 6 PRO A 63 99.54 -69.79 REMARK 500 7 SER A 2 98.22 -45.04 REMARK 500 8 GLU A 28 105.52 -51.62 REMARK 500 8 PRO A 63 99.88 -69.70 REMARK 500 9 GLN A 51 26.36 42.63 REMARK 500 9 PRO A 67 92.17 -69.75 REMARK 500 10 SER A 2 155.78 -44.53 REMARK 500 10 ASP A 22 -37.20 -34.29 REMARK 500 10 MET A 35 -62.10 -100.12 REMARK 500 10 PRO A 63 97.51 -69.78 REMARK 500 11 GLU A 28 107.73 -49.48 REMARK 500 11 PRO A 63 96.72 -69.83 REMARK 500 12 SER A 6 115.93 -165.38 REMARK 500 12 GLU A 28 106.71 -51.34 REMARK 500 13 ASP A 22 -38.40 -38.63 REMARK 500 13 GLU A 28 113.32 -35.92 REMARK 500 13 PRO A 63 97.11 -69.73 REMARK 500 14 SER A 2 -61.56 -132.29 REMARK 500 14 ASP A 22 -35.77 -37.75 REMARK 500 14 PRO A 63 99.62 -69.75 REMARK 500 15 SER A 68 88.91 -61.84 REMARK 500 16 GLU A 28 109.09 -48.36 REMARK 500 16 PRO A 67 84.59 -69.76 REMARK 500 16 SER A 68 35.91 -91.80 REMARK 500 17 GLN A 51 27.58 40.39 REMARK 500 17 PRO A 67 -174.00 -69.74 REMARK 500 18 TRP A 42 -179.98 -59.48 REMARK 500 18 PRO A 67 85.25 -69.77 REMARK 500 19 SER A 3 40.92 -81.71 REMARK 500 19 ASN A 59 -19.60 -48.87 REMARK 500 20 GLU A 28 106.43 -49.42 REMARK 500 20 SER A 68 -62.07 -101.46 REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSI002012305.1 RELATED DB: TARGETDB DBREF 2CT3 A 8 64 UNP O60504 VINEX_HUMAN 615 671 SEQADV 2CT3 GLY A 1 UNP O60504 CLONING ARTIFACT SEQADV 2CT3 SER A 2 UNP O60504 CLONING ARTIFACT SEQADV 2CT3 SER A 3 UNP O60504 CLONING ARTIFACT SEQADV 2CT3 GLY A 4 UNP O60504 CLONING ARTIFACT SEQADV 2CT3 SER A 5 UNP O60504 CLONING ARTIFACT SEQADV 2CT3 SER A 6 UNP O60504 CLONING ARTIFACT SEQADV 2CT3 GLY A 7 UNP O60504 CLONING ARTIFACT SEQADV 2CT3 SER A 65 UNP O60504 CLONING ARTIFACT SEQADV 2CT3 GLY A 66 UNP O60504 CLONING ARTIFACT SEQADV 2CT3 PRO A 67 UNP O60504 CLONING ARTIFACT SEQADV 2CT3 SER A 68 UNP O60504 CLONING ARTIFACT SEQADV 2CT3 SER A 69 UNP O60504 CLONING ARTIFACT SEQADV 2CT3 GLY A 70 UNP O60504 CLONING ARTIFACT SEQRES 1 A 70 GLY SER SER GLY SER SER GLY THR PRO TYR ARG ALA MET SEQRES 2 A 70 TYR GLN TYR ARG PRO GLN ASN GLU ASP GLU LEU GLU LEU SEQRES 3 A 70 ARG GLU GLY ASP ARG VAL ASP VAL MET GLN GLN CYS ASP SEQRES 4 A 70 ASP GLY TRP PHE VAL GLY VAL SER ARG ARG THR GLN LYS SEQRES 5 A 70 PHE GLY THR PHE PRO GLY ASN TYR VAL ALA PRO VAL SER SEQRES 6 A 70 GLY PRO SER SER GLY HELIX 1 1 GLY A 58 TYR A 60 1 3 SHEET 1 A 5 PHE A 53 PRO A 57 0 SHEET 2 A 5 TRP A 42 SER A 47 -1 N PHE A 43 O PHE A 56 SHEET 3 A 5 ASP A 30 GLN A 37 -1 N ASP A 33 O VAL A 46 SHEET 4 A 5 THR A 8 ALA A 12 -1 N ALA A 12 O ASP A 30 SHEET 5 A 5 VAL A 61 PRO A 63 -1 O ALA A 62 N ARG A 11 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