Header list of 1qmw.pdb file
Complete list - 9 20 Bytes
HEADER CONOTOXIN 08-OCT-99 1QMW
TITLE SOLUTION STRUCTURE OF ALPHA-CONOTOXIN SI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-CONOTOXIN SI;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SI (2-7,3-13);
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: AMIDATED C-TERMINUS
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: CONUS STRIATUS;
SOURCE 4 ORGANISM_COMMON: STRIATED CONE;
SOURCE 5 ORGANISM_TAXID: 6493;
SOURCE 6 OTHER_DETAILS: SYNTHESISED BY SOLID PHASE PEPTIDE CHEMISTRY
KEYWDS CONOTOXIN, NICOTINIC ACETYLCHOLINE RECEPTOR, TOXIN, VENOM
EXPDTA SOLUTION NMR
NUMMDL 36
AUTHOR A.J.BENIE,D.WHITFORD,B.HARGITTAI,G.BARANY,R.W.JANES
REVDAT 5 14-JUN-23 1QMW 1 REMARK
REVDAT 4 15-JAN-20 1QMW 1 LINK
REVDAT 3 24-FEB-09 1QMW 1 VERSN
REVDAT 2 05-FEB-04 1QMW 1 SOURCE SEQRES
REVDAT 1 25-AUG-00 1QMW 0
JRNL AUTH A.J.BENIE,D.WHITFORD,B.HARGITTAI,G.BARANY,R.W.JANES
JRNL TITL SOLUTION STRUCTURE OF ALPHA-CONOTOXIN SI
JRNL REF FEBS LETT. V. 476 287 2000
JRNL REFN ISSN 0014-5793
JRNL PMID 10913630
JRNL DOI 10.1016/S0014-5793(00)01724-5
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA
REMARK 3 AUTHORS : GUNTERT,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1QMW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-OCT-99.
REMARK 100 THE DEPOSITION ID IS D_1290004180.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283
REMARK 210 PH : 4.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; TOCSY; NOESY; HSQC; 2D J
REMARK 210 RESOLVED
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS; AMX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 36
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY STRUCTURES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED FROM A 2D HOMONUCLEAR NOESY
REMARK 210 SPECTRUM WITH A MIXING TIME OF 250MS.
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 CYS A 2 111.71 -160.07
REMARK 500 2 CYS A 2 111.82 -161.15
REMARK 500 3 CYS A 2 111.14 -161.89
REMARK 500 4 CYS A 2 111.27 -162.39
REMARK 500 5 CYS A 2 111.73 -161.12
REMARK 500 6 CYS A 2 110.61 -160.43
REMARK 500 7 SER A 12 67.90 -152.55
REMARK 500 9 CYS A 2 111.39 -160.37
REMARK 500 10 CYS A 2 111.81 -161.18
REMARK 500 11 CYS A 2 111.63 -161.95
REMARK 500 12 SER A 12 64.90 -152.30
REMARK 500 17 SER A 12 67.57 -153.34
REMARK 500 19 SER A 12 64.21 -153.20
REMARK 500 20 CYS A 3 71.69 -107.65
REMARK 500 23 CYS A 3 72.27 -107.76
REMARK 500 23 SER A 12 66.83 -151.66
REMARK 500 24 CYS A 2 116.39 -161.35
REMARK 500 26 CYS A 2 105.81 -161.69
REMARK 500 33 CYS A 3 68.43 -151.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4503 RELATED DB: BMRB
DBREF 1QMW A 1 13 UNP P15471 CXA1_CONST 1 13
SEQRES 1 A 14 ILE CYS CYS ASN PRO ALA CYS GLY PRO LYS TYR SER CYS
SEQRES 2 A 14 NH2
HET NH2 A 14 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 ASN A 4 GLY A 8 5 5
HELIX 2 2 CYS A 7 TYR A 11 5 5
SSBOND 1 CYS A 2 CYS A 7 1555 1555 1.88
SSBOND 2 CYS A 3 CYS A 13 1555 1555 2.17
LINK C CYS A 13 N NH2 A 14 1555 1555 1.32
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 - 9 20 Bytes