Header list of 1zlc.pdb file
Complete list - 2 20 Bytes
HEADER TOXIN 05-MAY-05 1ZLC
TITLE SOLUTION CONFORMATION OF ALPHA-CONOTOXIN PIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-CONOTOXIN PIA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FRAGMENT;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN CONUS PURPURASCENS.
KEYWDS ALPHA-HELIX, BETA-TURN, TWO DISULFIDE BONDS, C-TERMINAL AMIDATION,
KEYWDS 2 TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.-W.CHI,S.-H.LEE,D.-H.KIM,J.-S.KIM,B.M.OLIVERA,J.M.MCINTOSH,K.-H.HAN
REVDAT 3 02-MAR-22 1ZLC 1 REMARK LINK
REVDAT 2 24-FEB-09 1ZLC 1 VERSN
REVDAT 1 02-MAY-06 1ZLC 0
JRNL AUTH S.-W.CHI,S.-H.LEE,D.-H.KIM,J.-S.KIM,B.M.OLIVERA,
JRNL AUTH 2 J.M.MCINTOSH,K.-H.HAN
JRNL TITL SOLUTION STRUCTURE OF ALPHA-CONOTOXIN PIA, A NOVEL
JRNL TITL 2 ANTAGONIST OF ALPHA6 SUBUNIT CONTAINING NICOTINIC
JRNL TITL 3 ACETYLCHOLINE RECEPTORS
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 338 1990 2005
JRNL REFN ISSN 0006-291X
JRNL PMID 16289101
JRNL DOI 10.1016/J.BBRC.2005.10.176
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 1ZLC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000032852.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283; 293
REMARK 210 PH : 3.92; 3.92
REMARK 210 IONIC STRENGTH : 0; 0
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 10MM ALPHA-CONOTOXIN PIA
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 : FELIX 98.0
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 : 5
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: 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 15 30.33 -89.11
REMARK 500 2 PRO A 8 1.34 -59.57
REMARK 500 4 ASN A 14 58.29 -140.04
REMARK 500 9 ASN A 14 58.04 -140.13
REMARK 500 12 ASP A 2 174.16 -59.85
REMARK 500 15 PRO A 15 38.58 -87.89
REMARK 500 18 PRO A 15 33.53 -89.51
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 19
DBREF 1ZLC A 1 18 UNP P69658 CXA1_CONPU 22 39
SEQRES 1 A 19 ARG ASP PRO CYS CYS SER ASN PRO VAL CYS THR VAL HIS
SEQRES 2 A 19 ASN PRO GLN ILE CYS NH2
HET NH2 A 19 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 VAL A 9 ASN A 14 1 6
SSBOND 1 CYS A 4 CYS A 10 1555 1555 2.03
SSBOND 2 CYS A 5 CYS A 18 1555 1555 2.03
LINK C CYS A 18 N NH2 A 19 1555 1555 1.33
SITE 1 AC1 1 CYS A 18
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 - 2 20 Bytes