Header list of 1y29.pdb file
Complete list - 2 20 Bytes
HEADER TOXIN 22-NOV-04 1Y29
TITLE THREE DIMENSIONAL SOLUTION STRUCTURE OF HUWENTOXIN-X BY 2D 1H-NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HUWENTOXIN-X;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS ISOLATED FROM THE VENOM OF SPIDER
SOURCE 4 ORNITHOCTONUS HUWENA, SYNTHESIZED BY USING SOLID PHASE CHEMICAL
SOURCE 5 METHOD.
KEYWDS A DOUBLE-STRANDED BETA-SHEET, ICK, KNOTTIN, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Z.LIU,S.LIANG
REVDAT 4 02-MAR-22 1Y29 1 REMARK
REVDAT 3 24-FEB-09 1Y29 1 VERSN
REVDAT 2 14-AUG-07 1Y29 1 JRNL SOURCE AUTHOR
REVDAT 1 07-DEC-04 1Y29 0
JRNL AUTH Z.LIU,J.DAI,L.DAI,M.DENG,Z.HU,W.HU,S.LIANG
JRNL TITL FUNCTION AND SOLUTION STRUCTURE OF HUWENTOXIN-X, A SPECIFIC
JRNL TITL 2 BLOCKER OF N-TYPE CALCIUM CHANNELS, FROM THE CHINESE BIRD
JRNL TITL 3 SPIDER ORNITHOCTONUS HUWENA
JRNL REF J.BIOL.CHEM. V. 281 8628 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16439354
JRNL DOI 10.1074/JBC.M513542200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRVIEW 5.0, X-PLOR NIH-2.9.6
REMARK 3 AUTHORS : BRUCE A. JOHNSON (NMRVIEW), C.D. SCHWIETERS (X
REMARK 3 -PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 261 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS, 10 DIHEDRAL ANGEL RESTRAINTS AND
REMARK 3 9 FAKE DISTANCE RESTRAINTS FROM DISULFIDE BONDS.
REMARK 4
REMARK 4 1Y29 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000031024.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : 20
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 5MM HUWENTOXIN-X; PHOSPHATE
REMARK 210 BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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 : 6
REMARK 210
REMARK 210 REMARK: NULL
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 THR A 13 71.01 -106.44
REMARK 500 2 THR A 13 59.57 -177.49
REMARK 500 4 THR A 13 63.01 -170.88
REMARK 500 5 ALA A 12 49.48 -141.33
REMARK 500 5 THR A 13 91.95 56.09
REMARK 500 6 THR A 13 70.25 -154.86
REMARK 500 8 THR A 13 107.05 60.35
REMARK 500 10 THR A 13 66.17 -173.31
REMARK 500 11 THR A 13 69.84 -173.81
REMARK 500 11 SER A 23 -132.71 -88.89
REMARK 500 11 HIS A 24 74.42 -67.11
REMARK 500 12 THR A 13 59.50 -174.82
REMARK 500 12 SER A 23 -138.69 -95.41
REMARK 500 12 HIS A 24 76.88 -69.35
REMARK 500 14 GLN A 14 137.17 -172.00
REMARK 500 18 THR A 13 64.67 -150.27
REMARK 500 18 SER A 23 -139.57 -100.12
REMARK 500 19 GLN A 14 117.38 -163.48
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1Y29 A 1 28 UNP P68424 TXH10_ORNHU 1 28
SEQRES 1 A 28 LYS CYS LEU PRO PRO GLY LYS PRO CYS TYR GLY ALA THR
SEQRES 2 A 28 GLN LYS ILE PRO CYS CYS GLY VAL CYS SER HIS ASN LYS
SEQRES 3 A 28 CYS THR
SSBOND 1 CYS A 2 CYS A 19 1555 1555 2.02
SSBOND 2 CYS A 9 CYS A 22 1555 1555 2.02
SSBOND 3 CYS A 18 CYS A 27 1555 1555 2.02
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