Header list of 2fq0.pdb file
Complete list - r 25 2 Bytes
HEADER LIPID TRANSPORT 17-JAN-06 2FQ0 TITLE SOLUTION STRUCTURE OF MAJOR CONFORMATION OF HOLO-ACYL CARRIER PROTEIN TITLE 2 FROM MALARIA PARASITE PLASMODIUM FALCIPARUM COMPND MOL_ID: 1; COMPND 2 MOLECULE: ACYL CARRIER PROTEIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM; SOURCE 3 ORGANISM_TAXID: 36329; SOURCE 4 STRAIN: 3D7; SOURCE 5 GENE: MALARIA PARASITE P. FALCIPARUM; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28A(+) KEYWDS HOLO-PFACP, 4'-PHOSPHOPANTETHEINE, LIPID TRANSPORT EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.K.SHARMA,S.K.SHARMA,A.SUROLIA,N.SUROLIA,S.P.SARMA REVDAT 3 13-JUL-11 2FQ0 1 VERSN REVDAT 2 24-FEB-09 2FQ0 1 VERSN REVDAT 1 08-AUG-06 2FQ0 0 JRNL AUTH A.K.SHARMA,S.K.SHARMA,A.SUROLIA,N.SUROLIA,S.P.SARMA JRNL TITL SOLUTION STRUCTURES OF CONFORMATIONALLY EQUILIBRIUM FORMS OF JRNL TITL 2 HOLO-ACYL CARRIER PROTEIN (PFACP) FROM PLASMODIUM FALCIPARUM JRNL TITL 3 PROVIDES INSIGHT INTO THE MECHANISM OF ACTIVATION OF ACPS JRNL REF BIOCHEMISTRY V. 45 6904 2006 JRNL REFN ISSN 0006-2960 JRNL PMID 16734426 JRNL DOI 10.1021/BI060368U REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CYANA 2.1 REMARK 3 AUTHORS : PETER GUNTERT REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2FQ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-JAN-06. REMARK 100 THE RCSB ID CODE IS RCSB036171. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE BUFFER IN 100MM REMARK 210 NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.2-1.4MM PFACP U-15N ,13C; 50MM REMARK 210 PHOSPHATE BUFFER, 100MM NACL; PH REMARK 210 6.5, 2MM DTT, 0.5% NAN3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C- REMARK 210 SEPARATED_NOESY; 2D NOESY; 2D REMARK 210 TOCSY; HNHA; HNCACB, CBCA(CO)NH, REMARK 210 H(CCO)NH, C(CCO)NH, HNCO, HCCH- REMARK 210 TOCSY, 1H-15N HSQC, 1H-13C HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 97.027.12.56, ANSIG REMARK 210 1.0.3, CYANA 2.1 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 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: STRUCTURES ARE BASED ON 1226 NOE DERIVED DISTANCE REMARK 210 CONSTRAINTS, 55 DIHEDRAL RESTRAINTS AND 26 DISTANCE RESTRAINTS REMARK 210 FROM HYDROGEN BONDS 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 LYS A 2 60.12 -115.27 REMARK 500 1 SER A 3 -175.30 63.93 REMARK 500 1 ASP A 6 -70.69 -51.35 REMARK 500 1 SER A 17 105.31 -45.56 REMARK 500 1 SER A 27 -75.77 -120.16 REMARK 500 1 ASP A 32 -69.28 -101.88 REMARK 500 1 ALA A 35 -75.74 -68.01 REMARK 500 1 ASP A 36 129.19 -178.91 REMARK 500 1 VAL A 53 -167.33 -115.76 REMARK 500 1 SER A 56 -63.87 -168.30 REMARK 500 1 LYS A 62 -60.02 -131.52 REMARK 500 1 ASN A 76 -76.46 -87.81 REMARK 500 2 LYS A 2 59.71 -101.17 REMARK 500 2 SER A 3 -174.67 61.49 REMARK 500 2 ASP A 6 -74.76 -58.44 REMARK 500 2 LEU A 16 -74.06 -109.41 REMARK 500 2 SER A 17 -75.95 -179.38 REMARK 500 2 VAL A 18 99.11 -162.66 REMARK 500 2 ASP A 21 43.39 -97.00 REMARK 500 2 LYS A 22 -32.96 179.84 REMARK 500 2 SER A 27 -71.25 -117.70 REMARK 500 2 ASP A 32 -76.11 -91.95 REMARK 500 2 ALA A 35 -78.38 -90.78 REMARK 500 2 ASP A 36 131.50 178.80 REMARK 500 2 SER A 56 -97.67 47.00 REMARK 500 2 LEU A 61 40.74 -97.23 REMARK 500 2 LYS A 62 -52.66 -153.32 REMARK 500 2 ASN A 76 -61.43 -93.55 REMARK 500 3 LYS A 2 53.78 -119.72 REMARK 500 3 SER A 3 -179.04 63.06 REMARK 500 3 ASP A 6 -73.75 -55.03 REMARK 500 3 LEU A 16 -68.84 -101.69 REMARK 500 3 SER A 17 -72.45 179.88 REMARK 500 3 LYS A 22 20.49 -162.65 REMARK 500 3 SER A 27 -76.53 -120.68 REMARK 500 3 ASP A 32 -66.72 -93.40 REMARK 500 3 ALA A 35 -77.06 -83.27 REMARK 500 3 ASP A 36 131.87 179.68 REMARK 500 3 ASN A 52 60.64 60.22 REMARK 500 3 SER A 56 -76.41 -176.68 REMARK 500 3 LYS A 62 -56.25 -139.80 REMARK 500 3 ASN A 76 -75.44 -83.29 REMARK 500 3 ASN A 77 90.66 -68.57 REMARK 500 3 LYS A 78 50.15 -99.63 REMARK 500 4 LYS A 2 51.24 -117.06 REMARK 500 4 ASP A 6 -73.25 -55.92 REMARK 500 4 LEU A 16 -67.44 -107.72 REMARK 500 4 SER A 17 -50.29 177.80 REMARK 500 4 VAL A 18 142.65 178.90 REMARK 500 4 GLU A 19 33.02 -160.60 REMARK 500 REMARK 500 THIS ENTRY HAS 294 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 1 PNS A 137 REMARK 610 2 PNS A 137 REMARK 610 3 PNS A 137 REMARK 610 4 PNS A 137 REMARK 610 5 PNS A 137 REMARK 610 6 PNS A 137 REMARK 610 7 PNS A 137 REMARK 610 8 PNS A 137 REMARK 610 9 PNS A 137 REMARK 610 10 PNS A 137 REMARK 610 11 PNS A 137 REMARK 610 12 PNS A 137 REMARK 610 13 PNS A 137 REMARK 610 14 PNS A 137 REMARK 610 15 PNS A 137 REMARK 610 16 PNS A 137 REMARK 610 17 PNS A 137 REMARK 610 18 PNS A 137 REMARK 610 19 PNS A 137 REMARK 610 20 PNS A 137 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PNS A 137 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2BAR RELATED DB: PDB REMARK 900 RELATED ID: 2FQ3 RELATED DB: PDB DBREF 2FQ0 A 1 79 UNP O77077 O77077_PLAFA 59 137 SEQRES 1 A 79 LEU LYS SER THR PHE ASP ASP ILE LYS LYS ILE ILE SER SEQRES 2 A 79 LYS GLN LEU SER VAL GLU GLU ASP LYS ILE GLN MET ASN SEQRES 3 A 79 SER ASN PHE THR LYS ASP LEU GLY ALA ASP SER LEU ASP SEQRES 4 A 79 LEU VAL GLU LEU ILE MET ALA LEU GLU GLU LYS PHE ASN SEQRES 5 A 79 VAL THR ILE SER ASP GLN ASP ALA LEU LYS ILE ASN THR SEQRES 6 A 79 VAL GLN ASP ALA ILE ASP TYR ILE GLU LYS ASN ASN LYS SEQRES 7 A 79 GLN HET PNS A 137 42 HETNAM PNS 4'-PHOSPHOPANTETHEINE FORMUL 2 PNS C11 H23 N2 O7 P S HELIX 1 1 THR A 4 SER A 17 1 14 HELIX 2 2 GLU A 19 ILE A 23 5 5 HELIX 3 3 ASP A 36 ASN A 52 1 17 HELIX 4 4 THR A 65 ASN A 77 1 13 LINK OG SER A 37 P24 PNS A 137 1555 1555 1.61 SITE 1 AC1 4 LYS A 31 ASP A 36 SER A 37 LEU A 38 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