Header list of 1mtq.pdb file
Complete list - 24 20 Bytes
HEADER TOXIN 22-SEP-02 1MTQ
TITLE THREE-DIMENSIONAL SOLUTION STRUCTURE OF ALPHA-CONOTOXIN GID BY NMR
TITLE 2 SPECTROSCOPY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-CONOTOXIN GID;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 4 ORGANISM_TAXID: 32630;
SOURCE 5 OTHER_DETAILS: THIS SEQUENCE OCCURS IN NATURALLY IN CONUS GEOGRAPHUS
SOURCE 6 VENOM.
KEYWDS ALPHA-HELIX, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.NICKE,M.L.LOUGHNAN,E.L.MILLARD,P.F.ALEWOOD,D.J.ADAMS,N.L.DALY,
AUTHOR 2 D.J.CRAIK,R.J.LEWIS
REVDAT 3 24-JUN-20 1MTQ 1 SOURCE REMARK DBREF LINK
REVDAT 3 2 1 ATOM
REVDAT 2 24-FEB-09 1MTQ 1 VERSN
REVDAT 1 11-FEB-03 1MTQ 0
JRNL AUTH A.NICKE,M.L.LOUGHNAN,E.L.MILLARD,P.F.ALEWOOD,D.J.ADAMS,
JRNL AUTH 2 N.L.DALY,D.J.CRAIK,R.J.LEWIS
JRNL TITL ISOLATION, STRUCTURE, AND ACTIVITY OF GID, A NOVEL ALPHA
JRNL TITL 2 4/7-CONOTOXIN WITH AN EXTENDED N-TERMINAL SEQUENCE
JRNL REF J.BIOL.CHEM. V. 278 3137 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12419800
JRNL DOI 10.1074/JBC.M210280200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 183 NOE DERIVED DISTANCE RESTRAINTS, 15 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS.
REMARK 4
REMARK 4 1MTQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-02.
REMARK 100 THE DEPOSITION ID IS D_1000017175.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 287
REMARK 210 PH : 2.8
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.5MM PEPTIDE; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY; E
REMARK 210 -COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.7, DYANA 1.5
REMARK 210 METHOD USED : INITIAL STRUCTURES WERE
REMARK 210 CALCULATED USING TORSION ANGLE
REMARK 210 DYNAMICS AND STRUCTURES WERE
REMARK 210 REFINED IN A WATER SHELL USING
REMARK 210 CARTESIAN DYNAMICS.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED, STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 16
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 2 CGU A 4 -63.79 67.57
REMARK 500 3 ARG A 2 34.82 -82.74
REMARK 500 3 ASP A 3 109.21 -57.95
REMARK 500 5 SER A 7 36.97 -83.90
REMARK 500 6 ARG A 2 -42.10 -170.65
REMARK 500 6 CGU A 4 99.43 56.97
REMARK 500 9 ARG A 2 -76.92 -90.42
REMARK 500 9 ASP A 3 38.57 -142.26
REMARK 500 9 SER A 7 39.08 -88.91
REMARK 500 10 SER A 7 30.23 -86.57
REMARK 500 11 SER A 7 44.93 -84.67
REMARK 500 14 ARG A 2 -36.14 77.91
REMARK 500 14 SER A 7 41.23 -80.22
REMARK 500 15 ARG A 2 -10.69 -161.81
REMARK 500 15 SER A 7 30.57 -95.57
REMARK 500 16 ASP A 3 42.17 -83.81
REMARK 500 17 ASP A 3 22.14 -154.05
REMARK 500 20 ASP A 3 121.58 67.80
REMARK 500 20 SER A 7 44.90 -87.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 AN APPROPRIATE SEQUENCE DATABASE MATCH WAS NOT
REMARK 999 FOUND USING BLAST.
DBREF 1MTQ A 1 19 PDB 1MTQ 1MTQ 1 19
SEQRES 1 A 19 ILE ARG ASP CGU CYS CYS SER ASN PRO ALA CYS ARG VAL
SEQRES 2 A 19 ASN ASN HYP HIS VAL CYS
MODRES 1MTQ CGU A 4 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1MTQ HYP A 16 PRO 4-HYDROXYPROLINE
HET CGU A 4 17
HET HYP A 16 15
HETNAM CGU GAMMA-CARBOXY-GLUTAMIC ACID
HETNAM HYP 4-HYDROXYPROLINE
HETSYN HYP HYDROXYPROLINE
FORMUL 1 CGU C6 H9 N O6
FORMUL 1 HYP C5 H9 N O3
HELIX 1 1 ASN A 8 ASN A 15 1 8
SSBOND 1 CYS A 5 CYS A 11 1555 1555 2.03
SSBOND 2 CYS A 6 CYS A 19 1555 1555 2.03
LINK C ASP A 3 N CGU A 4 1555 1555 1.32
LINK C CGU A 4 N CYS A 5 1555 1555 1.33
LINK C ASN A 15 N HYP A 16 1555 1555 1.34
LINK C HYP A 16 N HIS A 17 1555 1555 1.33
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