Header list of 2gcz.pdb file
Complete list - 24 20 Bytes
HEADER TOXIN 15-MAR-06 2GCZ
TITLE SOLUTION STRUCTURE OF ALPHA-CONOTOXIN OMIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-CONOTOXIN OMIA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-17;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: CONUS OMARIA;
SOURCE 4 ORGANISM_COMMON: OMARIA CONE;
SOURCE 5 ORGANISM_TAXID: 89429;
SOURCE 6 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN CONUS OMARIA.
KEYWDS ALPHA-HELIX, BETA-TURN, TWO DISULFIDE BONDS, C-TERMINAL AMIDATION,
KEYWDS 2 TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.-W.CHI,D.-H.KIM,B.M.OLIVERA,J.M.MCINTOSH,K.-H.HAN
REVDAT 3 24-JUN-20 2GCZ 1 COMPND SOURCE REMARK DBREF
REVDAT 3 2 1 SEQADV LINK
REVDAT 2 24-FEB-09 2GCZ 1 VERSN
REVDAT 1 25-JUL-06 2GCZ 0
JRNL AUTH S.-W.CHI,D.-H.KIM,B.M.OLIVERA,J.M.MCINTOSH,K.-H.HAN
JRNL TITL SOLUTION CONFORMATION OF A NEURONAL NICOTINIC ACETYLCHOLINE
JRNL TITL 2 RECEPTOR ANTAGONIST ALPHA-CONOTOXIN OMIA THAT DISCRIMINATES
JRNL TITL 3 ALPHA3 VS. ALPHA6 NACHR SUBTYPES
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 345 248 2006
JRNL REFN ISSN 0006-291X
JRNL PMID 16678128
JRNL DOI 10.1016/J.BBRC.2006.04.099
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, CNS 1.1
REMARK 3 AUTHORS : VARIAN (VNMR),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GCZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000036968.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 288
REMARK 210 PH : 4.1; 4.1
REMARK 210 IONIC STRENGTH : 0; 0
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 4.8MM ALPHA-CONOTOXIN OMIA; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 5.0.4
REMARK 210 METHOD USED : SIMULATED ANNEALING
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: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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
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 ASN A 12 78.93 -119.68
REMARK 500 2 ASN A 12 77.29 -119.40
REMARK 500 5 CYS A 16 -67.98 -143.83
REMARK 500 6 CYS A 2 50.41 -115.57
REMARK 500 7 CYS A 2 53.13 39.75
REMARK 500 7 ASN A 12 77.72 -118.09
REMARK 500 8 ASN A 12 77.50 -119.56
REMARK 500 8 CYS A 16 -74.58 -116.02
REMARK 500 11 ASN A 12 78.70 -115.01
REMARK 500 11 CYS A 16 -36.09 -140.69
REMARK 500 12 CYS A 2 40.08 -147.73
REMARK 500 12 CYS A 3 5.15 -67.77
REMARK 500 14 CYS A 2 50.94 39.26
REMARK 500 18 CYS A 2 33.41 -140.81
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 18
DBREF 2GCZ A 1 17 UNP P0C1R7 CA1A_CONOM 1 17
SEQADV 2GCZ NH2 A 18 UNP P0C1R7 AMIDATION
SEQRES 1 A 18 GLY CYS CYS SER HIS PRO ALA CYS ASN VAL ASN ASN PRO
SEQRES 2 A 18 HIS ILE CYS GLY NH2
HET NH2 A 18 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 ALA A 7 ASN A 12 1 6
SSBOND 1 CYS A 2 CYS A 8 1555 1555 2.03
SSBOND 2 CYS A 3 CYS A 16 1555 1555 2.03
LINK C GLY A 17 N NH2 A 18 1555 1555 1.32
SITE 1 AC1 2 PRO A 13 GLY A 17
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