Header list of 1x5h.pdb file
Complete list - r 2 2 Bytes
HEADER CELL ADHESION 15-MAY-05 1X5H TITLE THE SOLUTION STRUCTURE OF THE THIRD FIBRONECTIN TYPE III DOMAIN OF TITLE 2 HUMAN NEOGENIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEOGENIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FN3 DOMAIN; COMPND 5 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: NEO1; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041213-04; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS RGM BINDING, FIBRONECTIN TYPE III DOMAIN, STRUCTURAL GENOMICS, KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, KEYWDS 4 CELL ADHESION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR N.TOCHIO,A.SASAGAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1X5H 1 REMARK SEQADV REVDAT 2 24-FEB-09 1X5H 1 VERSN REVDAT 1 15-NOV-05 1X5H 0 JRNL AUTH N.TOCHIO,A.SASAGAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA JRNL TITL THE SOLUTION STRUCTURE OF THE THIRD FIBRONECTIN TYPE III JRNL TITL 2 DOMAIN OF HUMAN NEOGENIN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1X5H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000024403. 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 : 1.5MM FN3 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_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 900 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 GLN A 47 103.93 -45.56 REMARK 500 1 ASN A 48 37.27 -86.79 REMARK 500 1 ASP A 107 168.51 -44.14 REMARK 500 1 PRO A 124 -171.63 -69.77 REMARK 500 1 PRO A 129 -174.94 -69.80 REMARK 500 2 VAL A 17 145.97 -35.24 REMARK 500 2 VAL A 29 92.89 -55.80 REMARK 500 2 GLN A 47 146.77 -38.52 REMARK 500 3 SER A 6 176.54 -55.82 REMARK 500 3 ASP A 8 175.64 -48.56 REMARK 500 3 ALA A 10 117.82 -173.90 REMARK 500 3 ARG A 12 39.09 38.04 REMARK 500 3 THR A 13 32.56 -85.94 REMARK 500 3 VAL A 17 154.25 -38.00 REMARK 500 3 VAL A 29 80.37 -58.41 REMARK 500 3 TRP A 108 106.33 -52.17 REMARK 500 3 ASP A 117 93.97 -51.78 REMARK 500 3 ASP A 119 93.24 -55.51 REMARK 500 3 PRO A 124 -177.32 -69.70 REMARK 500 3 PRO A 129 -176.14 -69.72 REMARK 500 4 SER A 3 151.86 -35.67 REMARK 500 4 VAL A 17 153.22 -37.94 REMARK 500 4 VAL A 29 84.75 -57.21 REMARK 500 4 GLN A 47 133.79 -36.74 REMARK 500 4 LYS A 64 42.94 -80.87 REMARK 500 4 SER A 65 -33.38 -130.74 REMARK 500 4 TRP A 108 109.45 -45.80 REMARK 500 4 VAL A 126 138.88 -33.86 REMARK 500 4 PRO A 129 -165.87 -69.77 REMARK 500 5 VAL A 17 153.34 -41.51 REMARK 500 5 VAL A 29 92.67 -45.61 REMARK 500 5 GLN A 47 -35.19 -33.15 REMARK 500 5 VAL A 72 -77.42 -130.32 REMARK 500 5 PRO A 124 -177.43 -69.77 REMARK 500 5 SER A 131 148.27 -35.91 REMARK 500 6 ALA A 10 114.34 -166.65 REMARK 500 6 ASP A 16 46.39 -82.53 REMARK 500 6 PRO A 18 84.13 -69.72 REMARK 500 6 ALA A 20 115.43 -169.69 REMARK 500 6 VAL A 29 108.57 -52.41 REMARK 500 6 GLN A 47 107.38 -48.96 REMARK 500 6 ASP A 107 142.69 -36.34 REMARK 500 6 TRP A 108 98.36 -56.65 REMARK 500 6 THR A 113 178.24 -58.32 REMARK 500 6 LEU A 118 98.85 -48.01 REMARK 500 6 ASP A 119 42.46 -100.81 REMARK 500 6 SER A 131 -58.66 -123.66 REMARK 500 7 SER A 2 175.70 -49.38 REMARK 500 7 VAL A 9 154.42 -39.66 REMARK 500 7 LEU A 14 99.83 -67.77 REMARK 500 REMARK 500 THIS ENTRY HAS 172 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSO002001179.4 RELATED DB: TARGETDB DBREF 1X5H A 8 126 UNP Q92859 NEO1_HUMAN 616 734 SEQADV 1X5H GLY A 1 UNP Q92859 CLONING ARTIFACT SEQADV 1X5H SER A 2 UNP Q92859 CLONING ARTIFACT SEQADV 1X5H SER A 3 UNP Q92859 CLONING ARTIFACT SEQADV 1X5H GLY A 4 UNP Q92859 CLONING ARTIFACT SEQADV 1X5H SER A 5 UNP Q92859 CLONING ARTIFACT SEQADV 1X5H SER A 6 UNP Q92859 CLONING ARTIFACT SEQADV 1X5H GLY A 7 UNP Q92859 CLONING ARTIFACT SEQADV 1X5H SER A 127 UNP Q92859 CLONING ARTIFACT SEQADV 1X5H GLY A 128 UNP Q92859 CLONING ARTIFACT SEQADV 1X5H PRO A 129 UNP Q92859 CLONING ARTIFACT SEQADV 1X5H SER A 130 UNP Q92859 CLONING ARTIFACT SEQADV 1X5H SER A 131 UNP Q92859 CLONING ARTIFACT SEQADV 1X5H GLY A 132 UNP Q92859 CLONING ARTIFACT SEQRES 1 A 132 GLY SER SER GLY SER SER GLY ASP VAL ALA VAL ARG THR SEQRES 2 A 132 LEU SER ASP VAL PRO SER ALA ALA PRO GLN ASN LEU SER SEQRES 3 A 132 LEU GLU VAL ARG ASN SER LYS SER ILE MET ILE HIS TRP SEQRES 4 A 132 GLN PRO PRO ALA PRO ALA THR GLN ASN GLY GLN ILE THR SEQRES 5 A 132 GLY TYR LYS ILE ARG TYR ARG LYS ALA SER ARG LYS SER SEQRES 6 A 132 ASP VAL THR GLU THR LEU VAL SER GLY THR GLN LEU SER SEQRES 7 A 132 GLN LEU ILE GLU GLY LEU ASP ARG GLY THR GLU TYR ASN SEQRES 8 A 132 PHE ARG VAL ALA ALA LEU THR ILE ASN GLY THR GLY PRO SEQRES 9 A 132 ALA THR ASP TRP LEU SER ALA GLU THR PHE GLU SER ASP SEQRES 10 A 132 LEU ASP GLU THR ARG VAL PRO GLU VAL SER GLY PRO SER SEQRES 11 A 132 SER GLY SHEET 1 A 3 GLN A 23 GLU A 28 0 SHEET 2 A 3 SER A 34 GLN A 40 -1 O HIS A 38 N SER A 26 SHEET 3 A 3 SER A 78 GLU A 82 -1 O GLN A 79 N ILE A 37 SHEET 1 B 3 ILE A 51 TYR A 54 0 SHEET 2 B 3 ALA A 95 THR A 98 -1 O LEU A 97 N THR A 52 SHEET 3 B 3 GLY A 101 ALA A 105 -1 O GLY A 101 N THR A 98 SHEET 1 C 4 ARG A 63 THR A 68 0 SHEET 2 C 4 ARG A 57 LYS A 60 -1 N TYR A 58 O THR A 68 SHEET 3 C 4 GLU A 89 ARG A 93 -1 O ASN A 91 N ARG A 59 SHEET 4 C 4 LEU A 109 GLU A 112 -1 O ALA A 111 N TYR A 90 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