Header list of 1tuj.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSPORT PROTEIN 25-JUN-04 1TUJ TITLE SOLUTION STRUCTURE OF THE HONEY BEE GENERAL ODORANT BINDING PROTEIN TITLE 2 ASP2 IN COMPLEX WITH TRIMETHYLSILYL-D4 PROPIONATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: ODORANT BINDING PROTEIN ASP2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 1-123; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: APIS MELLIFERA; SOURCE 3 ORGANISM_COMMON: HONEY BEE; SOURCE 4 ORGANISM_TAXID: 7460; SOURCE 5 GENE: ASP2; SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: GS115; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PHIL-D2; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNATASP2 KEYWDS ALPHA HELIX, COMPLEX, TSP, ODORANT-BINDING PROTEIN, TRANSPORT PROTEIN EXPDTA SOLUTION NMR NUMMDL 17 AUTHOR E.LESCOP,L.BRIAND,J.-C.PERNOLLET,E.GUITTET REVDAT 3 02-MAR-22 1TUJ 1 REMARK REVDAT 2 24-FEB-09 1TUJ 1 VERSN REVDAT 1 20-SEP-05 1TUJ 0 JRNL AUTH E.LESCOP,L.BRIAND,J.-C.PERNOLLET,E.GUITTET JRNL TITL SOLUTION STRUCTURE OF THE HONEY BEE GENERAL ODORANT BINDING JRNL TITL 2 PROTEIN ASP2 IN COMPLEX WITH TRIMETHYLSILYL-D4 PROPIONATE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 TITL 1H, 13C AND 15N CHEMICAL SHIFT ASSIGNMENT OF THE HONEYBEE REMARK 1 TITL 2 ODORANT-BINDING PROTEIN ASP2 REMARK 1 REF J.BIOMOL.NMR V. 21 181 2001 REMARK 1 REFN ISSN 0925-2738 REMARK 1 PMID 11727984 REMARK 1 DOI 10.1023/A:1012428527813 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, ARIA 1.2 REMARK 3 AUTHORS : BRUKER (XWINNMR), LINGE, NILGES (ARIA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2471 RESTRAINTS, 2348 ARE REMARK 3 NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS, 86 DIHEDRAL ANGLE RESTRAINTS, 37 DISTANCE REMARK 3 RESTRAINTS REMARK 3 FROM HYDROGEN BONDS. REMARK 4 REMARK 4 1TUJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1000022915. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308; 308 REMARK 210 PH : 6; 8 REMARK 210 IONIC STRENGTH : NULL; NULL REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM ASP2 U-15N; 30MM TSP; 0.1MM REMARK 210 SODIUM AZIDE; 100MM SODIUM REMARK 210 PHOSPHATE BUFFER; 1MM ASP2 U-15N, REMARK 210 U-13C; 30MM TSP; 0.1MM SODIUM REMARK 210 AZIDE; 100MM SODIUM PHOSPHATE REMARK 210 BUFFER; 1MM ASP2 UNLABELLED; REMARK 210 30MM TSP; 0.1MM SODIUM AZIDE; REMARK 210 100MM SODIUM PHOSPHATE BUFFER REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 2D NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.1, NMRVIEW 5.0.4, CNS REMARK 210 1.1, ARIA 1.2 REMARK 210 METHOD USED : AUTOMATIC NOE ASSIGNMENT USING REMARK 210 ARIA COMBINED WITH CNS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 17 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING CLASSICAL TRIPLE REMARK 210 -RESONANCE NMR SPECTROSCOPY. 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 LEU A 14 39.05 -147.07 REMARK 500 1 HIS A 26 -65.17 176.67 REMARK 500 1 THR A 33 125.32 -179.00 REMARK 500 1 ASN A 34 -82.71 -37.45 REMARK 500 1 ILE A 35 55.76 -140.06 REMARK 500 1 ALA A 37 -76.43 -85.08 REMARK 500 1 ALA A 38 -81.11 175.93 REMARK 500 1 MET A 44 -59.84 -154.71 REMARK 500 1 CYS A 49 -61.92 -135.77 REMARK 500 1 LYS A 62 78.68 -104.53 REMARK 500 1 TYR A 67 -167.28 -109.53 REMARK 500 1 VAL A 68 -14.24 -163.10 REMARK 500 1 HIS A 79 54.35 -118.54 REMARK 500 1 LYS A 101 33.73 33.06 REMARK 500 1 PHE A 122 -19.29 73.36 REMARK 500 2 LEU A 14 50.91 -146.90 REMARK 500 2 HIS A 26 -62.69 177.84 REMARK 500 2 THR A 33 -89.02 -59.22 REMARK 500 2 ALA A 38 -93.13 66.65 REMARK 500 2 LYS A 39 -62.05 -104.03 REMARK 500 2 ALA A 42 -71.80 -87.72 REMARK 500 2 MET A 44 -41.56 -130.13 REMARK 500 2 CYS A 49 -71.49 -137.01 REMARK 500 2 LEU A 61 109.77 -164.57 REMARK 500 2 LYS A 62 77.55 -108.56 REMARK 500 2 THR A 64 -15.54 -175.54 REMARK 500 2 THR A 104 -30.89 -135.16 REMARK 500 2 PHE A 122 -9.23 67.21 REMARK 500 3 HIS A 26 -59.29 177.46 REMARK 500 3 THR A 33 101.54 -168.99 REMARK 500 3 ASN A 34 75.60 38.69 REMARK 500 3 ILE A 35 -87.89 55.17 REMARK 500 3 GLN A 36 151.83 65.98 REMARK 500 3 ALA A 37 -74.09 -85.70 REMARK 500 3 ALA A 38 -103.78 -156.42 REMARK 500 3 ASP A 43 77.14 64.93 REMARK 500 3 CYS A 49 -70.10 -135.34 REMARK 500 3 VAL A 78 -8.55 -58.71 REMARK 500 3 HIS A 79 52.11 -141.04 REMARK 500 3 GLU A 103 -178.47 -62.29 REMARK 500 3 PHE A 122 -24.12 73.74 REMARK 500 4 LEU A 14 45.11 -152.10 REMARK 500 4 LEU A 25 38.72 -86.17 REMARK 500 4 HIS A 26 75.42 -63.09 REMARK 500 4 ILE A 27 54.92 -160.97 REMARK 500 4 SER A 28 177.09 -57.68 REMARK 500 4 THR A 33 107.79 179.76 REMARK 500 4 ALA A 38 -94.35 61.98 REMARK 500 4 LYS A 39 -62.13 -104.02 REMARK 500 4 ALA A 42 -142.50 -86.85 REMARK 500 REMARK 500 THIS ENTRY HAS 232 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TSD A 124 DBREF 1TUJ A 1 123 UNP Q9U9J5 Q9U9J5_APIME 20 142 SEQRES 1 A 123 ILE ASP GLN ASP THR VAL VAL ALA LYS TYR MET GLU TYR SEQRES 2 A 123 LEU MET PRO ASP ILE MET PRO CYS ALA ASP GLU LEU HIS SEQRES 3 A 123 ILE SER GLU ASP ILE ALA THR ASN ILE GLN ALA ALA LYS SEQRES 4 A 123 ASN GLY ALA ASP MET SER GLN LEU GLY CYS LEU LYS ALA SEQRES 5 A 123 CYS VAL MET LYS ARG ILE GLU MET LEU LYS GLY THR GLU SEQRES 6 A 123 LEU TYR VAL GLU PRO VAL TYR LYS MET ILE GLU VAL VAL SEQRES 7 A 123 HIS ALA GLY ASN ALA ASP ASP ILE GLN LEU VAL LYS GLY SEQRES 8 A 123 ILE ALA ASN GLU CYS ILE GLU ASN ALA LYS GLY GLU THR SEQRES 9 A 123 ASP GLU CYS ASN ILE GLY ASN LYS TYR THR ASP CYS TYR SEQRES 10 A 123 ILE GLU LYS LEU PHE SER HET TSD A 124 22 HETNAM TSD 3-TRIMETHYLSILYL-PROPIONATE-2,2,3,3,-D4 FORMUL 2 TSD C6 H9 O2 SI 1- HELIX 1 1 ASP A 2 TYR A 13 1 12 HELIX 2 2 LEU A 14 HIS A 26 1 13 HELIX 3 3 GLN A 46 LYS A 51 1 6 HELIX 4 4 ALA A 52 ILE A 58 1 7 HELIX 5 5 VAL A 68 HIS A 79 1 12 HELIX 6 6 ALA A 83 LYS A 101 1 19 HELIX 7 7 ASP A 105 LEU A 121 1 17 SHEET 1 A 2 LEU A 61 LYS A 62 0 SHEET 2 A 2 GLU A 65 LEU A 66 -1 O GLU A 65 N LYS A 62 SSBOND 1 CYS A 21 CYS A 53 1555 1555 2.03 SSBOND 2 CYS A 49 CYS A 107 1555 1555 2.03 SSBOND 3 CYS A 96 CYS A 116 1555 1555 2.03 SITE 1 AC1 2 TYR A 10 LYS A 51 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