Header list of 2d9y.pdb file
Complete list - r 9 2 Bytes
HEADER SIGNALING PROTEIN 13-DEC-05 2D9Y TITLE SOLUTION STRUCTURE OF THE PH DOMAIN OF PEPP-3 FROM HUMAN COMPND MOL_ID: 1; COMPND 2 MOLECULE: PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING PROTEIN FAMILY A COMPND 3 MEMBER 6; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: PH DOMAIN; COMPND 6 SYNONYM: PHOSPHOINOSITOL 3-PHOSPHATE-BINDING PROTEIN 3, PEPP-3; COMPND 7 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: PLEKHA6; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050711-08; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS PH DOMAIN, PEPP-3, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR H.LI,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2D9Y 1 REMARK SEQADV REVDAT 2 24-FEB-09 2D9Y 1 VERSN REVDAT 1 13-JUN-06 2D9Y 0 JRNL AUTH H.LI,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE PH DOMAIN OF PEPP-3 FROM HUMAN 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 2D9Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-DEC-05. REMARK 100 THE DEPOSITION ID IS D_1000025169. 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 : 1.14MM PH DOMAIN U-15N,13C; 20MM REMARK 210 D-TRIS-HCL(PH 7.0); 100MM NACL; REMARK 210 1MM D-DTT; 0.02% NAN3; 90% H2O, REMARK 210 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 20030801, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.932, 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 20 145.22 -39.42 REMARK 500 1 ALA A 21 98.24 -64.80 REMARK 500 1 VAL A 25 74.05 -109.58 REMARK 500 1 LYS A 26 35.55 37.24 REMARK 500 1 LEU A 57 54.01 -117.27 REMARK 500 1 VAL A 65 172.52 -58.38 REMARK 500 1 SER A 72 58.67 -99.52 REMARK 500 1 ALA A 82 40.85 71.26 REMARK 500 1 VAL A 84 -74.92 -60.03 REMARK 500 1 ILE A 101 -35.52 -38.72 REMARK 500 1 PRO A 114 -179.62 -69.81 REMARK 500 2 SER A 23 113.18 -174.49 REMARK 500 2 VAL A 25 170.78 -49.50 REMARK 500 2 LYS A 47 -38.52 -34.62 REMARK 500 2 VAL A 65 176.00 -59.10 REMARK 500 2 ALA A 82 73.78 -66.20 REMARK 500 2 ILE A 101 -37.25 -39.83 REMARK 500 3 ASN A 8 107.80 -36.28 REMARK 500 3 ARG A 38 41.32 34.28 REMARK 500 3 LYS A 47 -36.03 -35.56 REMARK 500 3 LEU A 57 40.46 -106.03 REMARK 500 3 VAL A 65 174.92 -53.74 REMARK 500 3 ALA A 82 41.49 73.57 REMARK 500 3 VAL A 84 -71.66 -52.64 REMARK 500 4 GLN A 20 152.84 -38.57 REMARK 500 4 SER A 23 100.37 -37.39 REMARK 500 4 ARG A 38 38.63 39.81 REMARK 500 4 GLU A 48 47.59 34.89 REMARK 500 4 LEU A 57 57.05 -100.06 REMARK 500 4 PRO A 114 94.61 -69.81 REMARK 500 5 ARG A 38 32.35 34.62 REMARK 500 5 GLU A 48 26.53 43.07 REMARK 500 5 VAL A 65 176.34 -52.52 REMARK 500 5 SER A 72 45.81 -83.44 REMARK 500 5 HIS A 81 67.88 -112.22 REMARK 500 5 ARG A 85 141.19 -174.31 REMARK 500 5 ILE A 101 -35.59 -36.95 REMARK 500 5 PRO A 114 85.23 -69.76 REMARK 500 5 SER A 115 149.73 -39.81 REMARK 500 6 SER A 23 49.34 71.62 REMARK 500 6 VAL A 25 163.35 -49.91 REMARK 500 6 ARG A 38 36.26 32.64 REMARK 500 6 LYS A 47 -30.64 -36.86 REMARK 500 6 GLU A 48 46.53 31.05 REMARK 500 6 LEU A 57 46.04 -91.71 REMARK 500 6 ALA A 63 142.75 -173.99 REMARK 500 6 ALA A 64 132.05 -35.31 REMARK 500 6 VAL A 65 -177.00 -54.02 REMARK 500 6 SER A 72 43.74 -80.98 REMARK 500 6 VAL A 84 -71.80 -60.70 REMARK 500 REMARK 500 THIS ENTRY HAS 202 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSK002000946.1 RELATED DB: TARGETDB DBREF 2D9Y A 8 111 UNP Q9Y2H5 PLEA6_HUMAN 57 160 SEQADV 2D9Y GLY A 1 UNP Q9Y2H5 CLONING ARTIFACT SEQADV 2D9Y SER A 2 UNP Q9Y2H5 CLONING ARTIFACT SEQADV 2D9Y SER A 3 UNP Q9Y2H5 CLONING ARTIFACT SEQADV 2D9Y GLY A 4 UNP Q9Y2H5 CLONING ARTIFACT SEQADV 2D9Y SER A 5 UNP Q9Y2H5 CLONING ARTIFACT SEQADV 2D9Y SER A 6 UNP Q9Y2H5 CLONING ARTIFACT SEQADV 2D9Y GLY A 7 UNP Q9Y2H5 CLONING ARTIFACT SEQADV 2D9Y SER A 112 UNP Q9Y2H5 CLONING ARTIFACT SEQADV 2D9Y GLY A 113 UNP Q9Y2H5 CLONING ARTIFACT SEQADV 2D9Y PRO A 114 UNP Q9Y2H5 CLONING ARTIFACT SEQADV 2D9Y SER A 115 UNP Q9Y2H5 CLONING ARTIFACT SEQADV 2D9Y SER A 116 UNP Q9Y2H5 CLONING ARTIFACT SEQADV 2D9Y GLY A 117 UNP Q9Y2H5 CLONING ARTIFACT SEQRES 1 A 117 GLY SER SER GLY SER SER GLY ASN ALA PRO VAL THR LYS SEQRES 2 A 117 ALA GLY TRP LEU PHE LYS GLN ALA SER SER GLY VAL LYS SEQRES 3 A 117 GLN TRP ASN LYS ARG TRP PHE VAL LEU VAL ASP ARG CYS SEQRES 4 A 117 LEU PHE TYR TYR LYS ASP GLU LYS GLU GLU SER ILE LEU SEQRES 5 A 117 GLY SER ILE PRO LEU LEU SER PHE ARG VAL ALA ALA VAL SEQRES 6 A 117 GLN PRO SER ASP ASN ILE SER ARG LYS HIS THR PHE LYS SEQRES 7 A 117 ALA GLU HIS ALA GLY VAL ARG THR TYR PHE PHE SER ALA SEQRES 8 A 117 GLU SER PRO GLU GLU GLN GLU ALA TRP ILE GLN ALA MET SEQRES 9 A 117 GLY GLU ALA ALA ARG VAL GLN SER GLY PRO SER SER GLY HELIX 1 1 PRO A 94 ALA A 107 1 14 SHEET 1 A 7 GLY A 53 PRO A 56 0 SHEET 2 A 7 CYS A 39 TYR A 43 -1 N LEU A 40 O ILE A 55 SHEET 3 A 7 TRP A 28 VAL A 36 -1 N VAL A 36 O CYS A 39 SHEET 4 A 7 LYS A 13 GLN A 20 -1 N LEU A 17 O ARG A 31 SHEET 5 A 7 THR A 86 SER A 90 -1 O SER A 90 N PHE A 18 SHEET 6 A 7 THR A 76 GLU A 80 -1 N ALA A 79 O TYR A 87 SHEET 7 A 7 ARG A 61 ALA A 64 -1 N ALA A 63 O LYS A 78 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