Header list of 1qwv.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSPORT PROTEIN 03-SEP-03 1QWV TITLE SOLUTION STRUCTURE OF ANTHERAEA POLYPHEMUS PHEROMONE BINDING PROTEIN TITLE 2 (APOLPBP) COMPND MOL_ID: 1; COMPND 2 MOLECULE: PHEROMONE-BINDING PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PBP; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ANTHERAEA POLYPHEMUS; SOURCE 3 ORGANISM_COMMON: POLYPHEMUS MOTH; SOURCE 4 ORGANISM_TAXID: 7120; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: XA-90; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHN1+ KEYWDS PHEROMONE BINDING PROTEIN, ANTHERAEA POLYPHEMUS, PBP, APOLPBP, KEYWDS 2 HEXAHELICAL FOLD, PBP FOLD, TRANSPORT PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR S.MOHANTY,S.ZUBKOV,A.M.GRONENBORN REVDAT 3 02-MAR-22 1QWV 1 REMARK REVDAT 2 24-FEB-09 1QWV 1 VERSN REVDAT 1 23-MAR-04 1QWV 0 JRNL AUTH S.MOHANTY,S.ZUBKOV,A.M.GRONENBORN JRNL TITL THE SOLUTION NMR STRUCTURE OF ANTHERAEA POLYPHEMUS PBP JRNL TITL 2 PROVIDES NEW INSIGHT INTO PHEROMONE RECOGNITION BY JRNL TITL 3 PHEROMONE-BINDING PROTEINS JRNL REF J.MOL.BIOL. V. 337 443 2004 JRNL REFN ISSN 0022-2836 JRNL PMID 15003458 JRNL DOI 10.1016/J.JMB.2004.01.009 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2.1, ARIA 1.2 REMARK 3 AUTHORS : DELAGLIO F., GRZESIEK S., VUISTER G.W., ZHU G., REMARK 3 PFIZER J., BAX A. (NMRPIPE), LINGE J.P., HABECK M., REMARK 3 RIEPING W., NILGES M. (ARIA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: 2501 NOE-DERIVED DISTANCE CONSTRAINTS, REMARK 3 243 DIHEDRAL ANGLE RESTRAINTS, 120 DISTANCE RESTRAINTS FROM REMARK 3 HYDROGEN BONDS REMARK 4 REMARK 4 1QWV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-03. REMARK 100 THE DEPOSITION ID IS D_1000020165. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 6.33 REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM APOLPBP U-15N,13C; 50MM REMARK 210 PHOSPHATE BUFFER; 1MM EDTA; 0.1% REMARK 210 NAN3; 95% H2O; 5% 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; 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX; DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW 5.0.4, CYANA 1.0.6 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS SIMULATED REMARK 210 ANNEALING, THIN LAYER WATER REMARK 210 REFINEMENT REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3 REMARK 210 REMARK 210 REMARK: MIXING TIME 110MS FOR 13C SEPARATED NOESY, 120MS FOR 15N REMARK 210 SEPARATED NOESY 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 HB2 ARG A 46 HB3 CYS A 108 1.35 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 PHE A 12 -78.01 -51.41 REMARK 500 1 ASP A 40 61.31 66.36 REMARK 500 1 ASP A 60 119.14 -176.28 REMARK 500 1 VAL A 61 31.18 -175.62 REMARK 500 1 PRO A 64 -143.77 -98.99 REMARK 500 1 PRO A 103 35.52 -73.37 REMARK 500 1 ASN A 126 -85.03 49.47 REMARK 500 1 ASP A 132 117.58 67.73 REMARK 500 2 PHE A 12 -73.02 -47.45 REMARK 500 2 TYR A 34 11.08 -66.95 REMARK 500 2 ASP A 40 70.92 59.41 REMARK 500 2 ASP A 60 123.21 -178.97 REMARK 500 2 VAL A 61 32.33 -177.42 REMARK 500 2 PRO A 64 -139.40 -104.62 REMARK 500 2 PRO A 103 33.34 -66.92 REMARK 500 2 LYS A 107 -77.26 -31.29 REMARK 500 3 PHE A 12 -86.50 -57.10 REMARK 500 3 TYR A 34 12.15 -68.51 REMARK 500 3 ASP A 39 12.10 -62.51 REMARK 500 3 ASP A 60 121.83 -176.76 REMARK 500 3 VAL A 61 50.84 -173.29 REMARK 500 3 PRO A 64 -139.52 -98.34 REMARK 500 3 PRO A 103 72.28 -66.55 REMARK 500 3 ALA A 140 -166.57 -122.23 REMARK 500 4 PHE A 12 -84.42 -57.21 REMARK 500 4 ASP A 39 12.58 -62.77 REMARK 500 4 ASP A 40 71.52 54.54 REMARK 500 4 ASP A 60 127.71 -178.10 REMARK 500 4 VAL A 61 32.95 -172.56 REMARK 500 4 PRO A 64 -140.86 -100.74 REMARK 500 4 PRO A 103 24.48 -68.68 REMARK 500 4 ASN A 126 -126.62 -135.00 REMARK 500 4 TRP A 127 99.71 -67.11 REMARK 500 5 PHE A 12 -74.95 -47.78 REMARK 500 5 TYR A 34 13.39 -64.92 REMARK 500 5 LYS A 38 54.28 -90.65 REMARK 500 5 ASP A 40 70.44 63.08 REMARK 500 5 ASP A 60 123.96 -177.40 REMARK 500 5 VAL A 61 34.57 -178.67 REMARK 500 5 PRO A 64 -138.98 -97.91 REMARK 500 5 PRO A 103 59.01 -69.20 REMARK 500 5 VAL A 128 109.12 -40.01 REMARK 500 5 LEU A 133 111.40 -160.09 REMARK 500 6 GLU A 3 -70.57 -49.06 REMARK 500 6 PHE A 12 -84.37 -55.23 REMARK 500 6 TYR A 34 9.80 -62.86 REMARK 500 6 ASP A 40 70.47 63.04 REMARK 500 6 ASP A 60 116.86 -176.02 REMARK 500 6 VAL A 61 31.37 -155.00 REMARK 500 6 PRO A 64 -138.18 -104.18 REMARK 500 REMARK 500 THIS ENTRY HAS 213 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1LS8 RELATED DB: PDB REMARK 900 NMR STRUCTURE OF THE UNLIGANDED BOMBYX MORI PHEROMONE-BINDING REMARK 900 PROTEIN AT PHYSIOLOGICAL PH DBREF 1QWV A 1 142 UNP P20797 PBP_ANTPO 22 163 SEQRES 1 A 142 SER PRO GLU ILE MET LYS ASN LEU SER ASN ASN PHE GLY SEQRES 2 A 142 LYS ALA MET ASP GLN CYS LYS ASP GLU LEU SER LEU PRO SEQRES 3 A 142 ASP SER VAL VAL ALA ASP LEU TYR ASN PHE TRP LYS ASP SEQRES 4 A 142 ASP TYR VAL MET THR ASP ARG LEU ALA GLY CYS ALA ILE SEQRES 5 A 142 ASN CYS LEU ALA THR LYS LEU ASP VAL VAL ASP PRO ASP SEQRES 6 A 142 GLY ASN LEU HIS HIS GLY ASN ALA LYS ASP PHE ALA MET SEQRES 7 A 142 LYS HIS GLY ALA ASP GLU THR MET ALA GLN GLN LEU VAL SEQRES 8 A 142 ASP ILE ILE HIS GLY CYS GLU LYS SER ALA PRO PRO ASN SEQRES 9 A 142 ASP ASP LYS CYS MET LYS THR ILE ASP VAL ALA MET CYS SEQRES 10 A 142 PHE LYS LYS GLU ILE HIS LYS LEU ASN TRP VAL PRO ASN SEQRES 11 A 142 MET ASP LEU VAL ILE GLY GLU VAL LEU ALA GLU VAL HELIX 1 1 SER A 1 LYS A 6 1 6 HELIX 2 2 ASN A 7 GLY A 13 1 7 HELIX 3 3 ALA A 15 SER A 24 1 10 HELIX 4 4 PRO A 26 TYR A 34 1 9 HELIX 5 5 ASP A 45 ASN A 53 1 9 HELIX 6 6 CYS A 54 ASP A 60 1 7 HELIX 7 7 HIS A 70 HIS A 80 1 11 HELIX 8 8 ASP A 83 SER A 100 1 18 HELIX 9 9 MET A 109 ASN A 126 1 18 SSBOND 1 CYS A 19 CYS A 54 1555 1555 2.03 SSBOND 2 CYS A 50 CYS A 108 1555 1555 2.03 SSBOND 3 CYS A 97 CYS A 117 1555 1555 2.04 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