Header list of 1two.pdb file
Complete list - r 2 2 Bytes
HEADER PHEROMONE BINDING PROTEIN 01-JUL-04 1TWO
TITLE NMR STRUCTURE OF THE PHEROMONE BINDING PROTEIN FROM ANTHERAEA
TITLE 2 POLYPHEMUS AT ACIDIC PH
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 APOLPBP, PBP, PHEROMONE BINDING PROTEIN, CONFORMATIONAL TRANSITION,
KEYWDS 2 CONFORMATIONAL SWITCH
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.MOHANTY,S.ZUBKOV
REVDAT 5 02-MAR-22 1TWO 1 REMARK
REVDAT 4 24-FEB-09 1TWO 1 VERSN
REVDAT 3 13-DEC-05 1TWO 1 JRNL
REVDAT 2 01-NOV-05 1TWO 1 JRNL
REVDAT 1 25-OCT-05 1TWO 0
JRNL AUTH S.ZUBKOV,A.M.GRONENBORN,I.J.BYEON,S.MOHANTY
JRNL TITL STRUCTURAL CONSEQUENCES OF THE PH-INDUCED CONFORMATIONAL
JRNL TITL 2 SWITCH IN A.POLYPHEMUS PHEROMONE-BINDING PROTEIN: MECHANISMS
JRNL TITL 3 OF LIGAND RELEASE
JRNL REF J.MOL.BIOL. V. 354 1081 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 16289114
JRNL DOI 10.1016/J.JMB.2005.10.015
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.2, CYANA 1.0.6
REMARK 3 AUTHORS : GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1469 NOE-DERIVED DISTANCE CONSTRAINTS,
REMARK 3 272 DIHEDRAL ANGLE RESTRAINTS, 110 DISTANCE RESTRAINTS FROM
REMARK 3 HYDROGEN BONDS
REMARK 4
REMARK 4 1TWO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000022977.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 5.2
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
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
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,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 500
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: CARRIER FREQUENCIES IN 13C SEPARATED NOESY EXPERIMENTS:
REMARK 210 43PPM AND 125PPM
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 PHE A 12 H MET A 16 1.44
REMARK 500 O GLN A 89 H ASP A 92 1.44
REMARK 500 O LEU A 47 H ALA A 51 1.45
REMARK 500 O LEU A 59 H ASP A 63 1.49
REMARK 500 O LYS A 14 H GLN A 18 1.56
REMARK 500 O CYS A 54 H THR A 57 1.60
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 PRO A 2 -165.89 -75.04
REMARK 500 1 LEU A 8 -164.58 -70.26
REMARK 500 1 SER A 9 -103.42 -47.27
REMARK 500 1 ASN A 11 -29.79 -34.53
REMARK 500 1 SER A 24 18.10 50.19
REMARK 500 1 ASN A 35 -73.64 -67.98
REMARK 500 1 PHE A 36 29.08 159.88
REMARK 500 1 THR A 57 -59.99 -15.13
REMARK 500 1 LEU A 68 -174.66 -175.38
REMARK 500 1 HIS A 70 140.00 -39.99
REMARK 500 1 MET A 78 41.85 -77.77
REMARK 500 1 LYS A 79 -53.46 -153.52
REMARK 500 1 PRO A 103 44.67 -75.02
REMARK 500 1 LYS A 107 -30.19 -39.87
REMARK 500 1 LYS A 110 -79.40 -90.43
REMARK 500 1 LEU A 125 -102.97 -42.93
REMARK 500 1 LEU A 139 -57.19 -177.72
REMARK 500 2 PRO A 2 -165.94 -74.92
REMARK 500 2 SER A 9 -87.88 -49.38
REMARK 500 2 ASN A 11 -34.36 -35.78
REMARK 500 2 SER A 24 17.70 51.77
REMARK 500 2 PHE A 36 53.02 169.45
REMARK 500 2 VAL A 42 -30.62 -38.71
REMARK 500 2 THR A 57 -61.27 -12.94
REMARK 500 2 MET A 78 41.51 -76.55
REMARK 500 2 LYS A 79 -53.34 -149.59
REMARK 500 2 CYS A 97 -60.77 -90.16
REMARK 500 2 ALA A 101 79.68 -117.88
REMARK 500 2 PRO A 103 42.83 -74.92
REMARK 500 2 LYS A 110 -79.33 -90.14
REMARK 500 2 LEU A 125 -103.00 -44.43
REMARK 500 2 PRO A 129 49.83 -74.97
REMARK 500 2 LEU A 139 -56.31 175.18
REMARK 500 3 PRO A 2 -164.32 -75.04
REMARK 500 3 LEU A 8 -179.49 -63.53
REMARK 500 3 SER A 9 -92.98 -48.98
REMARK 500 3 ASN A 11 -37.83 -33.35
REMARK 500 3 SER A 24 17.79 49.85
REMARK 500 3 ASN A 35 -72.84 -78.63
REMARK 500 3 PHE A 36 46.88 172.87
REMARK 500 3 MET A 43 -27.85 -38.74
REMARK 500 3 THR A 57 -60.15 -14.92
REMARK 500 3 LEU A 68 -173.40 -174.05
REMARK 500 3 ALA A 77 -76.37 -68.16
REMARK 500 3 MET A 78 43.12 -74.39
REMARK 500 3 LYS A 79 -51.37 -143.56
REMARK 500 3 GLU A 84 -30.93 -38.72
REMARK 500 3 ASP A 92 -71.73 -79.71
REMARK 500 3 CYS A 97 -61.19 -90.62
REMARK 500 3 PRO A 103 43.57 -74.99
REMARK 500
REMARK 500 THIS ENTRY HAS 400 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QWV RELATED DB: PDB
REMARK 900 THE SAME PROTEIN AT PH 6.3
REMARK 900 RELATED ID: 1GM0 RELATED DB: PDB
REMARK 900 67% IDENTICAL PROTEIN UNDER SIMILAR CONDITIONS
DBREF 1TWO 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 PHE A 12 LEU A 23 1 12
HELIX 2 2 PRO A 26 TYR A 34 1 9
HELIX 3 3 ASP A 45 ALA A 56 1 12
HELIX 4 4 LYS A 58 ASP A 63 1 6
HELIX 5 5 PHE A 76 GLY A 81 1 6
HELIX 6 6 ASP A 83 GLU A 98 1 16
HELIX 7 7 LYS A 110 LYS A 124 1 15
SSBOND 1 CYS A 19 CYS A 54 1555 1555 1.78
SSBOND 2 CYS A 50 CYS A 108 1555 1555 1.99
SSBOND 3 CYS A 97 CYS A 117 1555 1555 2.11
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