Header list of 1niy.pdb file
Complete list - 29 20 Bytes
HEADER TOXIN 30-DEC-02 1NIY
TITLE THREE DIMENSIONAL SOLUTION STRUCTURE OF HAINANTOXIN-IV BY 2D 1H-NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HAINANTOXIN-IV;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HNTX-IV
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORNITHOCTONUS HAINANA;
SOURCE 3 ORGANISM_TAXID: 209901;
SOURCE 4 SECRETION: VENOM
KEYWDS NEUROTOXIN, INHIBITOR CYSTINE KNOT MOTIF, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.LI,S.LU,X.GU,S.LIANG
REVDAT 4 29-NOV-17 1NIY 1 REMARK HELIX
REVDAT 3 24-FEB-09 1NIY 1 VERSN
REVDAT 2 21-SEP-04 1NIY 1 JRNL
REVDAT 1 14-JAN-03 1NIY 0
JRNL AUTH D.LI,Y.XIAO,X.XU,X.XIONG,S.LU,Z.LIU,Q.ZHU,M.WANG,X.GU,
JRNL AUTH 2 S.LIANG
JRNL TITL STRUCTURE-ACTIVITY RELATIONSHIPS OF HAINANTOXIN-IV AND
JRNL TITL 2 STRUCTURE DETERMINATION OF ACTIVE AND INACTIVE SODIUM
JRNL TITL 3 CHANNEL BLOCKERS.
JRNL REF J.BIOL.CHEM. V. 279 37734 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15201273
JRNL DOI 10.1074/JBC.M405765200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Z.H.LIU,P.CHEN,S.P.LIANG
REMARK 1 TITL SYNTHESIS AND OXIDATIVE REFOLDING OF HAINANTOXIN-IV
REMARK 1 REF ACTA BIOCHIM.BIOPHYS.SINICA V. 34 516 2002
REMARK 1 REFN ISSN 0582-9879
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 566 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS, 14 DIHEDRAL ANGEL RESTRAINTS, 9
REMARK 3 FAKE DISTANCE RESTRAINTS FROM DISULFIDE BONDS AND 8 HYDROGEN-
REMARK 3 BOND CONSTRAINTS.
REMARK 4
REMARK 4 1NIY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-DEC-02.
REMARK 100 THE DEPOSITION ID IS D_1000017906.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288.00
REMARK 210 PH : 4.00
REMARK 210 IONIC STRENGTH : 20
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 5.5 MM HAINANTOXIN-IV MMOL/L
REMARK 210 DEUTERIUM ACETIC ACID BU 90%H2O ,
REMARK 210 10%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQF-COSY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
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 : 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: 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 91.92 -161.05
REMARK 500 1 ASP A 14 99.04 62.87
REMARK 500 3 ASP A 14 74.76 53.38
REMARK 500 3 ASN A 21 72.85 52.40
REMARK 500 6 CYS A 2 96.46 61.45
REMARK 500 6 ASP A 14 80.96 58.03
REMARK 500 7 ASP A 14 85.47 56.43
REMARK 500 8 CYS A 2 92.30 60.61
REMARK 500 8 ASN A 13 71.97 -116.42
REMARK 500 9 ASP A 14 87.64 55.33
REMARK 500 10 ASP A 14 89.44 58.18
REMARK 500 12 ASP A 14 81.71 58.52
REMARK 500 13 ASP A 14 87.44 59.35
REMARK 500 14 ASP A 14 74.91 54.07
REMARK 500 15 CYS A 2 84.11 58.37
REMARK 500 15 ASP A 14 80.31 57.33
REMARK 500 16 ASP A 14 93.58 62.29
REMARK 500 17 ASP A 14 80.15 53.18
REMARK 500 18 ASN A 13 69.34 -110.98
REMARK 500 19 ASP A 14 84.18 57.24
REMARK 500 20 ASP A 14 82.73 55.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 26 0.31 SIDE CHAIN
REMARK 500 1 ARG A 29 0.32 SIDE CHAIN
REMARK 500 2 ARG A 26 0.31 SIDE CHAIN
REMARK 500 2 ARG A 29 0.30 SIDE CHAIN
REMARK 500 3 ARG A 26 0.30 SIDE CHAIN
REMARK 500 3 ARG A 29 0.32 SIDE CHAIN
REMARK 500 4 ARG A 26 0.32 SIDE CHAIN
REMARK 500 4 ARG A 29 0.32 SIDE CHAIN
REMARK 500 5 ARG A 26 0.32 SIDE CHAIN
REMARK 500 5 ARG A 29 0.32 SIDE CHAIN
REMARK 500 6 ARG A 26 0.31 SIDE CHAIN
REMARK 500 6 ARG A 29 0.31 SIDE CHAIN
REMARK 500 7 ARG A 26 0.31 SIDE CHAIN
REMARK 500 7 ARG A 29 0.32 SIDE CHAIN
REMARK 500 8 ARG A 26 0.31 SIDE CHAIN
REMARK 500 8 ARG A 29 0.29 SIDE CHAIN
REMARK 500 9 ARG A 26 0.32 SIDE CHAIN
REMARK 500 9 ARG A 29 0.31 SIDE CHAIN
REMARK 500 10 ARG A 26 0.32 SIDE CHAIN
REMARK 500 10 ARG A 29 0.31 SIDE CHAIN
REMARK 500 11 ARG A 26 0.32 SIDE CHAIN
REMARK 500 11 ARG A 29 0.31 SIDE CHAIN
REMARK 500 12 ARG A 26 0.28 SIDE CHAIN
REMARK 500 12 ARG A 29 0.32 SIDE CHAIN
REMARK 500 13 ARG A 26 0.32 SIDE CHAIN
REMARK 500 13 ARG A 29 0.31 SIDE CHAIN
REMARK 500 14 ARG A 26 0.32 SIDE CHAIN
REMARK 500 14 ARG A 29 0.31 SIDE CHAIN
REMARK 500 15 ARG A 26 0.31 SIDE CHAIN
REMARK 500 15 ARG A 29 0.30 SIDE CHAIN
REMARK 500 16 ARG A 26 0.31 SIDE CHAIN
REMARK 500 16 ARG A 29 0.32 SIDE CHAIN
REMARK 500 17 ARG A 26 0.31 SIDE CHAIN
REMARK 500 17 ARG A 29 0.31 SIDE CHAIN
REMARK 500 18 ARG A 26 0.32 SIDE CHAIN
REMARK 500 18 ARG A 29 0.31 SIDE CHAIN
REMARK 500 19 ARG A 26 0.32 SIDE CHAIN
REMARK 500 19 ARG A 29 0.31 SIDE CHAIN
REMARK 500 20 ARG A 26 0.29 SIDE CHAIN
REMARK 500 20 ARG A 29 0.30 SIDE CHAIN
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 36
DBREF 1NIY A 1 35 UNP P83471 TXHA4_SELHA 1 35
SEQRES 1 A 36 GLU CYS LEU GLY PHE GLY LYS GLY CYS ASN PRO SER ASN
SEQRES 2 A 36 ASP GLN CYS CYS LYS SER SER ASN LEU VAL CYS SER ARG
SEQRES 3 A 36 LYS HIS ARG TRP CYS LYS TYR GLU ILE NH2
HET NH2 A 36 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
SHEET 1 A 3 LYS A 7 CYS A 9 0
SHEET 2 A 3 TRP A 30 TYR A 33 -1 N CYS A 31 O LYS A 7
SHEET 3 A 3 LEU A 22 SER A 25 1 O VAL A 23 N LYS A 32
SSBOND 1 CYS A 2 CYS A 17 1555 1555 2.02
SSBOND 2 CYS A 9 CYS A 24 1555 1555 2.02
SSBOND 3 CYS A 16 CYS A 31 1555 1555 2.02
LINK C ILE A 35 N NH2 A 36 1555 1555 1.31
SITE 1 AC1 2 GLU A 34 ILE A 35
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 - 29 20 Bytes