Header list of 1uht.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 10-JUL-03 1UHT TITLE SOLUTION STRUCTURE OF THE FHA DOMAIN OF ARABIDOPSIS THALIANA TITLE 2 HYPOTHETICAL PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: EXPRESSED PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FORKHEAD ASSOCIATED DOMAIN, FHA DOMAIN; COMPND 5 SYNONYM: HYPOTHETICAL PROTEIN; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA; SOURCE 3 ORGANISM_COMMON: THALE CRESS; SOURCE 4 ORGANISM_TAXID: 3702; SOURCE 5 GENE: RIKEN CDNA RAFL09-79-A12; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021218-71; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS FHA DOMAIN, BETA-SANDWICH, ANTIPARALLEL BETA-SHEETS, PHOSPHOPEPTIDE KEYWDS 2 BINDING MOTIF, STRUCTURAL GENOMICS, RIKEN STRUCTURAL KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.TOMIZAWA,M.INOUE,S.KOSHIBA,F.HAYASHI,M.SHIROUZU,T.TERADA,T.YABUKI, AUTHOR 2 M.AOKI,T.MATSUDA,E.SEKI,H.HIROTA,M.YOSHIDA,A.TANAKA,T.OSANAI, AUTHOR 3 K.SHINOZAKI,M.SEKI,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 4 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1UHT 1 REMARK SEQADV REVDAT 2 24-FEB-09 1UHT 1 VERSN REVDAT 1 10-JAN-04 1UHT 0 JRNL AUTH T.TOMIZAWA,M.INOUE,S.KOSHIBA,F.HAYASHI,M.SHIROUZU,T.TERADA, JRNL AUTH 2 T.YABUKI,M.AOKI,T.MATSUDA,E.SEKI,H.HIROTA,M.YOSHIDA, JRNL AUTH 3 A.TANAKA,T.OSANAI,K.SHINOZAKI,M.SEKI,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE FHA DOMAIN OF ARABIDOPSIS THALIANA JRNL TITL 2 HYPOTHETICAL PROTEIN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1C, CYANA 1.0.7 REMARK 3 AUTHORS : VARIAN (VNMR), GUENTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1UHT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUL-03. REMARK 100 THE DEPOSITION ID IS D_1000005843. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.5 REMARK 210 IONIC STRENGTH : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.09MM FHA DOMAIN U-15N, 13C; REMARK 210 20MM TRIS-HCL; 100MM NACL; 0.02% REMARK 210 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 : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.820, CYANA 1.0.7 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 RESTRAINTED MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES REMARK 210 WITH THE LOWEST ENERGY, TARGET REMARK 210 FUNCTION 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 O PRO A 11 HE1 TRP A 67 1.52 REMARK 500 H ILE A 99 O ILE A 107 1.55 REMARK 500 H PHE A 17 O ASP A 25 1.56 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 2 113.85 66.42 REMARK 500 1 SER A 5 -61.92 -122.97 REMARK 500 1 SER A 6 136.61 66.34 REMARK 500 1 GLU A 23 115.28 -39.33 REMARK 500 1 ALA A 51 -60.92 72.11 REMARK 500 1 LYS A 56 71.34 -111.10 REMARK 500 1 SER A 64 -81.23 66.12 REMARK 500 1 LEU A 72 60.92 -69.97 REMARK 500 1 ASN A 76 -54.92 162.90 REMARK 500 1 ASN A 81 -69.57 66.64 REMARK 500 1 SER A 82 47.67 -162.30 REMARK 500 1 GLU A 103 -63.49 -100.75 REMARK 500 2 SER A 3 130.20 -174.86 REMARK 500 2 MET A 8 92.22 66.64 REMARK 500 2 LYS A 49 65.71 -100.10 REMARK 500 2 ALA A 51 -51.96 83.44 REMARK 500 2 LYS A 56 71.73 -109.10 REMARK 500 2 SER A 64 61.21 39.56 REMARK 500 2 SER A 74 -88.89 -41.12 REMARK 500 2 SER A 75 -57.56 -174.76 REMARK 500 2 ASN A 81 -82.07 60.98 REMARK 500 2 ASN A 83 147.38 179.56 REMARK 500 2 THR A 105 131.08 -38.32 REMARK 500 3 SER A 3 86.03 48.95 REMARK 500 3 SER A 5 -62.93 -157.14 REMARK 500 3 SER A 6 104.05 54.35 REMARK 500 3 ALA A 51 -52.55 83.89 REMARK 500 3 LEU A 72 61.91 -69.91 REMARK 500 3 ASN A 76 -63.92 69.30 REMARK 500 3 ASN A 81 -81.60 62.23 REMARK 500 3 SER A 82 57.26 -151.53 REMARK 500 3 ASN A 83 141.64 -173.57 REMARK 500 3 GLU A 103 -66.17 -99.88 REMARK 500 3 SER A 117 88.45 51.31 REMARK 500 4 SER A 3 155.87 61.82 REMARK 500 4 SER A 5 158.12 61.20 REMARK 500 4 THR A 10 129.29 63.76 REMARK 500 4 LYS A 49 53.07 -98.74 REMARK 500 4 ALA A 51 -51.52 83.58 REMARK 500 4 LYS A 56 70.07 -115.34 REMARK 500 4 ASN A 76 -83.64 60.62 REMARK 500 4 ASN A 81 -68.43 67.31 REMARK 500 4 SER A 82 54.34 -164.61 REMARK 500 4 GLU A 103 -68.95 -105.53 REMARK 500 5 SER A 5 157.23 58.43 REMARK 500 5 VAL A 9 89.09 33.20 REMARK 500 5 THR A 10 120.38 67.18 REMARK 500 5 ALA A 51 -60.99 80.72 REMARK 500 5 LYS A 56 70.02 -107.13 REMARK 500 5 SER A 74 -83.67 -50.60 REMARK 500 REMARK 500 THIS ENTRY HAS 251 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: ATR001006273.1 RELATED DB: TARGETDB DBREF 1UHT A 8 112 UNP O23305 Y4449_ARATH 1 105 SEQADV 1UHT GLY A 1 UNP O23305 CLONING ARTIFACT SEQADV 1UHT SER A 2 UNP O23305 CLONING ARTIFACT SEQADV 1UHT SER A 3 UNP O23305 CLONING ARTIFACT SEQADV 1UHT GLY A 4 UNP O23305 CLONING ARTIFACT SEQADV 1UHT SER A 5 UNP O23305 CLONING ARTIFACT SEQADV 1UHT SER A 6 UNP O23305 CLONING ARTIFACT SEQADV 1UHT GLY A 7 UNP O23305 CLONING ARTIFACT SEQADV 1UHT SER A 113 UNP O23305 CLONING ARTIFACT SEQADV 1UHT GLY A 114 UNP O23305 CLONING ARTIFACT SEQADV 1UHT PRO A 115 UNP O23305 CLONING ARTIFACT SEQADV 1UHT SER A 116 UNP O23305 CLONING ARTIFACT SEQADV 1UHT SER A 117 UNP O23305 CLONING ARTIFACT SEQADV 1UHT GLY A 118 UNP O23305 CLONING ARTIFACT SEQRES 1 A 118 GLY SER SER GLY SER SER GLY MET VAL THR PRO SER LEU SEQRES 2 A 118 ARG LEU VAL PHE VAL LYS GLY PRO ARG GLU GLY ASP ALA SEQRES 3 A 118 LEU ASP TYR LYS PRO GLY SER THR ILE ARG VAL GLY ARG SEQRES 4 A 118 ILE VAL ARG GLY ASN GLU ILE ALA ILE LYS ASP ALA GLY SEQRES 5 A 118 ILE SER THR LYS HIS LEU ARG ILE GLU SER ASP SER GLY SEQRES 6 A 118 ASN TRP VAL ILE GLN ASP LEU GLY SER SER ASN GLY THR SEQRES 7 A 118 LEU LEU ASN SER ASN ALA LEU ASP PRO GLU THR SER VAL SEQRES 8 A 118 ASN LEU GLY ASP GLY ASP VAL ILE LYS LEU GLY GLU TYR SEQRES 9 A 118 THR SER ILE LEU VAL ASN PHE VAL SER GLY PRO SER SER SEQRES 10 A 118 GLY SHEET 1 A 9 SER A 12 PHE A 17 0 SHEET 2 A 9 ILE A 35 GLY A 38 1 SHEET 3 A 9 ILE A 46 ALA A 47 1 SHEET 4 A 9 LEU A 58 SER A 62 -1 SHEET 5 A 9 TRP A 67 GLN A 70 -1 SHEET 6 A 9 LEU A 79 LEU A 80 -1 SHEET 7 A 9 SER A 90 ASN A 92 1 SHEET 8 A 9 ASP A 97 LEU A 101 -1 SHEET 9 A 9 THR A 105 PHE A 111 -1 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