Header list of 1wfr.pdb file
Complete list - r 25 2 Bytes
HEADER LIPID BINDING PROTEIN 26-MAY-04 1WFR TITLE SOLUTION STRUCTURE OF THE CONSERVED HYPOTHETICAL PROTEIN TT1886, TITLE 2 POSSIBLY STEROL CARRIER PROTEIN, FROM THERMUS THERMOPHILUS HB8 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN TT1886; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS; SOURCE 3 ORGANISM_TAXID: 300852; SOURCE 4 STRAIN: HB8; SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 6 EXPRESSION_SYSTEM_PLASMID: P030826-87; SOURCE 7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS STEROL CARRIER PROTEIN, STRUCTURAL GENOMICS, LIPID BINDING, RIKEN KEYWDS 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, LIPID BINDING KEYWDS 3 PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.GORONCY,T.KIGAWA,S.KOSHIBA,T.TOMIZAWA,N.KOBAYASHI,N.TOCHIO,M.INOUE, AUTHOR 2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 13-JUL-11 1WFR 1 VERSN REVDAT 2 24-FEB-09 1WFR 1 VERSN REVDAT 1 26-NOV-04 1WFR 0 JRNL AUTH A.GORONCY,T.KIGAWA,S.KOSHIBA,T.TOMIZAWA,N.KOBAYASHI, JRNL AUTH 2 N.TOCHIO,M.INOUE,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE CONSERVED HYPOTHETICAL PROTEIN JRNL TITL 2 TT1886, POSSIBLY STEROL CARRIER PROTEIN, FROM THERMUS JRNL TITL 3 THERMOPHILUS HB8 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CYANA 2.0.26 REMARK 3 AUTHORS : GUENTERT, P. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WFR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUN-04. REMARK 100 THE RCSB ID CODE IS RCSB023530. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 318 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.09MM TT1886 U-15N, 13C; 20MM REMARK 210 PHOSPHATE BUFFER NA; 100MM NACL, REMARK 210 0.02% 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 : XWINNMR 2.6, NMRPIPE 20031121, REMARK 210 NMRVIEW 5.0.14, KUJIRA 0.899 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 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 5 178.11 51.27 REMARK 500 1 SER A 6 133.03 65.74 REMARK 500 1 MET A 8 -64.55 -92.40 REMARK 500 1 SER A 26 75.03 -67.66 REMARK 500 1 ALA A 33 33.85 -86.16 REMARK 500 1 LYS A 49 -26.06 -39.55 REMARK 500 1 ALA A 77 -162.37 -103.40 REMARK 500 1 GLU A 110 119.55 -161.07 REMARK 500 1 TYR A 122 52.75 -103.80 REMARK 500 1 SER A 138 -45.17 -163.84 REMARK 500 2 SER A 3 108.71 -39.89 REMARK 500 2 SER A 5 171.84 -47.83 REMARK 500 2 MET A 8 -65.07 -93.35 REMARK 500 2 GLU A 9 104.89 -59.94 REMARK 500 2 ALA A 33 32.49 -93.69 REMARK 500 2 THR A 35 -35.70 84.05 REMARK 500 2 LEU A 60 79.66 -153.47 REMARK 500 2 ARG A 68 -54.66 -160.23 REMARK 500 2 ALA A 125 -36.74 -36.22 REMARK 500 2 ALA A 137 109.16 -59.76 REMARK 500 2 SER A 138 -48.94 -131.75 REMARK 500 2 PRO A 140 1.25 -69.76 REMARK 500 3 SER A 2 -55.75 -178.85 REMARK 500 3 MET A 8 -58.12 -145.44 REMARK 500 3 ALA A 33 36.52 -98.09 REMARK 500 3 THR A 35 -5.11 76.69 REMARK 500 3 ASP A 47 139.15 179.93 REMARK 500 3 LYS A 49 -35.50 -39.27 REMARK 500 3 PHE A 52 81.81 -150.52 REMARK 500 3 ARG A 68 -48.09 -155.21 REMARK 500 3 ALA A 77 126.04 172.92 REMARK 500 3 ALA A 79 177.92 175.38 REMARK 500 3 GLU A 110 114.31 -165.43 REMARK 500 3 TYR A 122 51.23 -101.27 REMARK 500 3 ALA A 137 89.39 35.57 REMARK 500 3 SER A 138 -173.61 177.21 REMARK 500 4 SER A 6 126.57 -177.96 REMARK 500 4 ALA A 33 30.96 -88.14 REMARK 500 4 THR A 35 24.06 46.78 REMARK 500 4 GLU A 37 127.39 62.80 REMARK 500 4 ASP A 47 136.76 -173.12 REMARK 500 4 PHE A 52 79.07 -152.49 REMARK 500 4 LEU A 60 80.09 -154.44 REMARK 500 4 HIS A 64 16.87 54.51 REMARK 500 4 ALA A 77 143.01 178.66 REMARK 500 4 TYR A 122 48.23 -84.35 REMARK 500 4 ALA A 137 39.43 34.11 REMARK 500 4 PRO A 140 -175.94 -69.69 REMARK 500 4 SER A 141 154.98 -37.70 REMARK 500 5 SER A 3 149.16 -175.55 REMARK 500 REMARK 500 THIS ENTRY HAS 249 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: TTK003001886.1 RELATED DB: TARGETDB DBREF 1WFR A 8 137 UNP Q5SL92 Q5SL92_THET8 1 130 SEQRES 1 A 143 GLY SER SER GLY SER SER GLY MET GLU LEU PHE THR GLU SEQRES 2 A 143 ALA TRP ALA GLN ALA TYR CYS ARG LYS LEU ASN GLU SER SEQRES 3 A 143 GLU ALA TYR ARG LYS ALA ALA SER THR TRP GLU GLY SER SEQRES 4 A 143 LEU ALA LEU ALA VAL ARG PRO ASP PRO LYS ALA GLY PHE SEQRES 5 A 143 PRO LYS GLY VAL ALA VAL VAL LEU ASP LEU TRP HIS GLY SEQRES 6 A 143 ALA CYS ARG GLY ALA LYS ALA VAL GLU GLY GLU ALA GLU SEQRES 7 A 143 ALA ASP PHE VAL ILE GLU ALA ASP LEU ALA THR TRP GLN SEQRES 8 A 143 GLU VAL LEU GLU GLY ARG LEU GLU PRO LEU SER ALA LEU SEQRES 9 A 143 MET ARG GLY LEU LEU GLU LEU LYS LYS GLY THR ILE ALA SEQRES 10 A 143 ALA LEU ALA PRO TYR ALA GLN ALA ALA GLN GLU LEU VAL SEQRES 11 A 143 LYS VAL ALA ARG GLU VAL ALA SER GLY PRO SER SER GLY HELIX 1 1 THR A 12 SER A 26 1 15 HELIX 2 2 SER A 26 ALA A 33 1 8 HELIX 3 3 ASP A 47 GLY A 51 5 5 HELIX 4 4 ASP A 86 GLU A 95 1 10 HELIX 5 5 GLU A 99 GLY A 107 1 9 HELIX 6 6 THR A 115 LEU A 119 5 5 HELIX 7 7 GLN A 124 ALA A 137 1 14 SHEET 1 A 3 ALA A 66 GLY A 69 0 SHEET 2 A 3 VAL A 56 TRP A 63 -1 N ASP A 61 O ARG A 68 SHEET 3 A 3 ALA A 72 VAL A 73 -1 O VAL A 73 N ALA A 57 SHEET 1 B 4 ALA A 66 GLY A 69 0 SHEET 2 B 4 VAL A 56 TRP A 63 -1 N ASP A 61 O ARG A 68 SHEET 3 B 4 GLU A 37 VAL A 44 -1 N LEU A 42 O VAL A 58 SHEET 4 B 4 PHE A 81 ALA A 85 1 O PHE A 81 N ALA A 41 SSBOND 1 CYS A 20 CYS A 67 1555 1555 2.00 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 25 2 Bytes