Header list of 1mxn.pdb file
Complete list - 23 20 Bytes
HEADER TOXIN 02-OCT-02 1MXN
TITLE SOLUTION STRUCTURE OF ALPHA-CONOTOXIN AUIB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-CONOTOXIN AUIB;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS SYNTHESISED BY BOC CHEMISTRY BUT
SOURCE 4 OCCURS NATURALLY IN CONUS AULICUS.
KEYWDS ALPHA HELIX, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.L.DUTTON,P.S.BANSAL,R.C.HOGG,D.J.ADAMS,P.F.ALEWOOD,D.J.CRAIK
REVDAT 3 23-FEB-22 1MXN 1 REMARK LINK
REVDAT 2 24-FEB-09 1MXN 1 VERSN
REVDAT 1 30-DEC-02 1MXN 0
JRNL AUTH J.L.DUTTON,P.S.BANSAL,R.C.HOGG,D.J.ADAMS,P.F.ALEWOOD,
JRNL AUTH 2 D.J.CRAIK
JRNL TITL A NEW LEVEL OF CONOTOXIN DIVERSITY, A NON-NATIVE DISULFIDE
JRNL TITL 2 BOND CONNECTIVITY IN ALPHA -CONOTOXIN AUIB REDUCES
JRNL TITL 3 STRUCTURAL DEFINITION BUT INCREASES BIOLOGICAL ACTIVITY.
JRNL REF J.BIOL.CHEM. V. 277 48849 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 12376538
JRNL DOI 10.1074/JBC.M208842200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.851 THEN 3.1F
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 32 MEDIUM AND 18 LONG RANGE NOES WERE
REMARK 3 INCLUDED, 7 DIHEDRAL ANGLE RESTRAINTS WERE INCLUDED, 5 H-BOND
REMARK 3 RESTRAINTS WERE INCLUDED
REMARK 4
REMARK 4 1MXN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017284.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 290
REMARK 210 PH : 3.5
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : ATMOSPHERIC ATM
REMARK 210 SAMPLE CONTENTS : 2MM PEPTIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; E-COSY; DQF
REMARK 210 -COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; ARX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, X-PLOR 3.851 THEN
REMARK 210 3.1F
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS, ENERGY MINIMISATION IN
REMARK 210 A CHARM FORCEFIELD
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 8
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 2 CYS A 3 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 4 CYS A 2 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 4 CYS A 3 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 6 CYS A 2 CA - CB - SG ANGL. DEV. = 8.5 DEGREES
REMARK 500 7 CYS A 2 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 8 CYS A 2 CA - CB - SG ANGL. DEV. = 6.6 DEGREES
REMARK 500 10 CYS A 2 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 11 CYS A 2 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 12 CYS A 2 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500 12 CYS A 3 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 14 CYS A 3 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 18 CYS A 3 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 19 CYS A 2 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
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 20 PRO A 13 -9.22 -59.31
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 16
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MXP RELATED DB: PDB
REMARK 900 1MXP CONTAINS SOLUTION STRUCTURE OF THE RIBBON DISULFIDE BOND
REMARK 900 ISOMER OF THE SAME PROTEIN
DBREF 1MXN A 1 15 UNP P56640 CXA2_CONAL 1 15
SEQRES 1 A 16 GLY CYS CYS SER TYR PRO PRO CYS PHE ALA THR ASN PRO
SEQRES 2 A 16 ASP CYS NH2
HET NH2 A 16 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 GLY A 1 SER A 4 5 4
HELIX 2 2 TYR A 5 ASN A 12 1 8
SSBOND 1 CYS A 2 CYS A 8 1555 1555 2.02
SSBOND 2 CYS A 3 CYS A 15 1555 1555 2.02
LINK C CYS A 15 N NH2 A 16 1555 1555 1.31
SITE 1 AC1 3 PHE A 9 ASP A 14 CYS A 15
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 - 23 20 Bytes