Header list of 2fqc.pdb file
Complete list - 24 20 Bytes
HEADER TOXIN 18-JAN-06 2FQC
TITLE SOLUTION STRUCTURE OF CONOTOXIN PL14A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/KAPPA-CONOTOXIN PL14A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CONOTOXIN PL14A;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: CONUS PLANORBIS;
SOURCE 4 ORGANISM_COMMON: PLANORBIS CONE;
SOURCE 5 ORGANISM_TAXID: 97183;
SOURCE 6 OTHER_DETAILS: CHEMICALLY SYNTHESIZED. THIS SEQUENCE OCCURS
SOURCE 7 NATURALLY IN CONUS PLANORBIS
KEYWDS ALPHA-HELIX, DISULFIDE BONDS, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.J.CRAIK,N.L.DALY
REVDAT 3 24-JUN-20 2FQC 1 COMPND SOURCE REMARK DBREF
REVDAT 3 2 1 SEQADV LINK
REVDAT 2 24-FEB-09 2FQC 1 VERSN
REVDAT 1 18-JUL-06 2FQC 0
JRNL AUTH J.S.IMPERIAL,P.S.BANSAL,P.F.ALEWOOD,N.L.DALY,D.J.CRAIK,
JRNL AUTH 2 A.SPORNING,H.TERLAU,E.LOPEZ-VERA,P.K.BANDYOPADHYAY,
JRNL AUTH 3 B.M.OLIVERA
JRNL TITL A NOVEL CONOTOXIN INHIBITOR OF KV1.6 CHANNEL AND NACHR
JRNL TITL 2 SUBTYPES DEFINES A NEW SUPERFAMILY OF CONOTOXINS
JRNL REF BIOCHEMISTRY V. 45 8331 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16819832
JRNL DOI 10.1021/BI060263R
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER ET AL (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FQC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000036183.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 290
REMARK 210 PH : 3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM PL14A, PH 3; 95% H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY; E
REMARK 210 -COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.7, DYANA 1.5, CNS 1.1
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
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 : 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 HIS A 23 58.01 -65.89
REMARK 500 2 HIS A 23 56.37 -67.97
REMARK 500 2 CYS A 24 -168.99 -77.60
REMARK 500 3 CYS A 22 57.14 -148.41
REMARK 500 4 ARG A 5 33.79 -88.62
REMARK 500 4 CYS A 22 61.34 -150.06
REMARK 500 4 CYS A 24 -168.25 -76.86
REMARK 500 5 CYS A 22 57.64 -142.69
REMARK 500 6 CYS A 22 53.28 -140.04
REMARK 500 7 HIS A 23 55.62 -69.11
REMARK 500 8 ARG A 5 39.98 -77.11
REMARK 500 8 CYS A 22 51.46 -147.13
REMARK 500 8 HIS A 23 54.42 -68.66
REMARK 500 9 HIS A 23 53.07 -69.38
REMARK 500 10 CYS A 22 56.90 -147.34
REMARK 500 11 CYS A 22 55.72 -145.42
REMARK 500 12 CYS A 22 58.17 -147.21
REMARK 500 12 HIS A 23 54.17 -68.78
REMARK 500 12 CYS A 24 -169.55 -78.66
REMARK 500 13 CYS A 22 57.00 -146.55
REMARK 500 13 HIS A 23 53.83 -69.53
REMARK 500 15 CYS A 22 58.78 -150.00
REMARK 500 16 CYS A 22 57.91 -141.70
REMARK 500 16 HIS A 23 52.57 -69.83
REMARK 500 17 HIS A 23 54.72 -68.05
REMARK 500 18 CYS A 22 56.55 -147.61
REMARK 500 18 HIS A 23 52.63 -69.96
REMARK 500 19 CYS A 22 57.96 -146.89
REMARK 500 20 HIS A 23 55.77 -66.04
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 NH2 A 26
DBREF 2FQC A 1 25 UNP Q0N4U8 CJEA_CONPO 40 64
SEQADV 2FQC NH2 A 26 UNP Q0N4U8 AMIDATION
SEQRES 1 A 26 PHE PRO ARG PRO ARG ILE CYS ASN LEU ALA CYS ARG ALA
SEQRES 2 A 26 GLY ILE GLY HIS LYS TYR PRO PHE CYS HIS CYS ARG NH2
HET NH2 A 26 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 PRO A 4 GLY A 14 1 11
HELIX 2 2 ILE A 15 LYS A 18 5 4
HELIX 3 3 TYR A 19 HIS A 23 5 5
SSBOND 1 CYS A 7 CYS A 22 1555 1555 2.03
SSBOND 2 CYS A 11 CYS A 24 1555 1555 2.03
LINK C ARG A 25 N NH2 A 26 1555 1555 1.33
SITE 1 AC1 1 ARG A 25
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 - 24 20 Bytes