Header list of 1x2k.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 25-APR-05 1X2K TITLE SOLUTION STRUCTURE OF THE SH3 DOMAIN OF HUMAN OSTEOCLAST STIMULATING TITLE 2 FACTOR 1 (OSTF1) COMPND MOL_ID: 1; COMPND 2 MOLECULE: OSTEOCLAST STIMULATING FACTOR 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SH3 DOMAIN; COMPND 5 SYNONYM: OSTF1; 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: OSTF1; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040329-95; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS SH3 DOMAIN, HUMAN OSTEOCLAST STIMULATING FACTOR 1, OSTF1, STRUCTURAL KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS KEYWDS 4 INITIATIVE, RSGI, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR Y.O.KAMATARI,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1X2K 1 REMARK SEQADV REVDAT 2 24-FEB-09 1X2K 1 VERSN REVDAT 1 25-OCT-05 1X2K 0 JRNL AUTH Y.O.KAMATARI,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA, JRNL AUTH 2 S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE SH3 DOMAIN OF HUMAN OSTEOCLAST JRNL TITL 2 STIMULATING FACTOR 1 (OSTF1) 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 1X2K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-APR-05. REMARK 100 THE DEPOSITION ID IS D_1000024298. 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 : 1.24MM SH3 DOMAIN U-13C, 15N; REMARK 210 20MM D-TRIS-HCL BUFFER (PH7.0); REMARK 210 100MM NACL; 1MM D-DTT; 0.02% REMARK 210 NAN3; 90% 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 0.9295, 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 SER A 2 107.28 -165.45 REMARK 500 1 PRO A 21 1.09 -69.76 REMARK 500 1 SER A 47 -76.50 -118.17 REMARK 500 1 GLU A 61 105.67 -49.51 REMARK 500 1 PRO A 65 92.34 -69.74 REMARK 500 1 SER A 67 -51.62 -123.36 REMARK 500 2 GLU A 28 128.32 -39.56 REMARK 500 2 SER A 47 -76.64 -112.76 REMARK 500 2 SER A 67 146.55 -34.62 REMARK 500 3 SER A 5 133.78 -172.74 REMARK 500 3 SER A 6 163.64 -44.88 REMARK 500 3 SER A 47 -76.56 -116.86 REMARK 500 4 SER A 47 -76.64 -109.11 REMARK 500 5 SER A 47 -76.82 -111.10 REMARK 500 5 GLU A 61 109.61 -52.43 REMARK 500 6 SER A 47 -76.64 -112.21 REMARK 500 6 GLN A 62 98.46 -57.63 REMARK 500 6 SER A 66 84.61 -53.63 REMARK 500 7 SER A 47 -77.01 -106.07 REMARK 500 8 SER A 5 101.26 -55.15 REMARK 500 8 SER A 47 -76.64 -114.52 REMARK 500 8 SER A 67 -62.06 -122.89 REMARK 500 9 PRO A 21 1.20 -69.71 REMARK 500 9 SER A 47 -76.55 -121.20 REMARK 500 9 GLU A 61 108.51 -49.06 REMARK 500 10 SER A 3 137.84 -39.34 REMARK 500 10 PRO A 21 0.12 -69.77 REMARK 500 10 SER A 47 -76.56 -115.12 REMARK 500 10 SER A 66 102.41 -46.91 REMARK 500 11 SER A 47 -76.88 -117.03 REMARK 500 11 GLU A 61 105.81 -48.28 REMARK 500 11 SER A 66 159.06 -42.15 REMARK 500 12 SER A 47 -76.95 -106.83 REMARK 500 12 GLU A 61 103.91 -56.59 REMARK 500 13 SER A 3 101.27 -34.54 REMARK 500 13 SER A 5 130.07 -172.64 REMARK 500 13 SER A 47 -76.54 -111.23 REMARK 500 14 THR A 40 -32.75 -39.91 REMARK 500 14 SER A 47 -76.53 -113.02 REMARK 500 14 PRO A 65 85.39 -69.82 REMARK 500 14 SER A 67 -61.17 -129.15 REMARK 500 15 SER A 6 44.65 -82.29 REMARK 500 15 PRO A 21 0.56 -69.83 REMARK 500 15 SER A 47 -76.61 -112.41 REMARK 500 16 SER A 2 106.79 -46.18 REMARK 500 16 SER A 47 -76.64 -110.72 REMARK 500 16 GLU A 61 105.98 -51.41 REMARK 500 17 SER A 47 -76.79 -111.34 REMARK 500 17 GLU A 61 109.45 -56.91 REMARK 500 17 SER A 67 -61.51 -107.50 REMARK 500 REMARK 500 THIS ENTRY HAS 62 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSS001000445.1 RELATED DB: TARGETDB DBREF 1X2K A 8 62 UNP Q92882 OSTF1_HUMAN 15 69 SEQADV 1X2K GLY A 1 UNP Q92882 CLONING ARTIFACT SEQADV 1X2K SER A 2 UNP Q92882 CLONING ARTIFACT SEQADV 1X2K SER A 3 UNP Q92882 CLONING ARTIFACT SEQADV 1X2K GLY A 4 UNP Q92882 CLONING ARTIFACT SEQADV 1X2K SER A 5 UNP Q92882 CLONING ARTIFACT SEQADV 1X2K SER A 6 UNP Q92882 CLONING ARTIFACT SEQADV 1X2K GLY A 7 UNP Q92882 CLONING ARTIFACT SEQADV 1X2K SER A 63 UNP Q92882 CLONING ARTIFACT SEQADV 1X2K GLY A 64 UNP Q92882 CLONING ARTIFACT SEQADV 1X2K PRO A 65 UNP Q92882 CLONING ARTIFACT SEQADV 1X2K SER A 66 UNP Q92882 CLONING ARTIFACT SEQADV 1X2K SER A 67 UNP Q92882 CLONING ARTIFACT SEQADV 1X2K GLY A 68 UNP Q92882 CLONING ARTIFACT SEQRES 1 A 68 GLY SER SER GLY SER SER GLY LYS VAL PHE ARG ALA LEU SEQRES 2 A 68 TYR THR PHE GLU PRO ARG THR PRO ASP GLU LEU TYR PHE SEQRES 3 A 68 GLU GLU GLY ASP ILE ILE TYR ILE THR ASP MET SER ASP SEQRES 4 A 68 THR ASN TRP TRP LYS GLY THR SER LYS GLY ARG THR GLY SEQRES 5 A 68 LEU ILE PRO SER ASN TYR VAL ALA GLU GLN SER GLY PRO SEQRES 6 A 68 SER SER GLY SHEET 1 A 5 THR A 51 PRO A 55 0 SHEET 2 A 5 TRP A 42 THR A 46 -1 N TRP A 43 O ILE A 54 SHEET 3 A 5 ILE A 31 ASP A 36 -1 N ASP A 36 O LYS A 44 SHEET 4 A 5 LYS A 8 ALA A 12 -1 N PHE A 10 O ILE A 32 SHEET 5 A 5 VAL A 59 GLU A 61 -1 O ALA A 60 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 2 2 Bytes