Header list of 1fu3.pdb file
Complete list - 23 20 Bytes
HEADER METAL TRANSPORT INHIBITOR 14-SEP-00 1FU3
TITLE THREE-DIMENSIONAL STRUCTURE IN SOLUTION OF THE SODIUM CHANNEL
TITLE 2 AGONIST/ANTAGONIST DELTA-CONOTOXIN TXVIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DELTA-CONOTOXIN TXVIA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TXIA, CONOTOXIN KING-KONG 0, KK-0;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN CONUS TEXTILE
KEYWDS DELTA-CONOTOXIN, CYSTINE KNOT MOTIF, TRIPLE-STRANDED, METAL TRANSPORT
KEYWDS 2 INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.KOHNO,T.SASAKI,M.FAINZILBER,K.SATO
REVDAT 3 23-FEB-22 1FU3 1 REMARK
REVDAT 2 24-FEB-09 1FU3 1 VERSN
REVDAT 1 20-SEP-02 1FU3 0
JRNL AUTH T.KOHNO,T.SASAKI,K.KOBAYASHI,M.FAINZILBER,K.SATO
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SODIUM CHANNEL
JRNL TITL 2 AGONIST/ANTAGONIST DELTA-CONOTOXIN TXVIA.
JRNL REF J.BIOL.CHEM. V. 277 36387 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 12145313
JRNL DOI 10.1074/JBC.M206833200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FU3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000011901.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288.0
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 5MM DELTA-CONOTOXIN TXVIA; 5MM
REMARK 210 DELTA-CONOTOXIN TXVIA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; PE-COSY;
REMARK 210 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 : 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 : 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 SER A 5 97.82 -62.15
REMARK 500 1 ASN A 15 49.94 -148.03
REMARK 500 1 ASP A 18 43.32 -160.95
REMARK 500 1 VAL A 23 -85.03 60.72
REMARK 500 1 LEU A 24 24.43 -152.67
REMARK 500 2 CYS A 2 170.24 49.76
REMARK 500 2 SER A 5 96.95 -66.60
REMARK 500 2 ASP A 13 71.45 -161.11
REMARK 500 2 ASN A 15 59.80 -111.98
REMARK 500 2 CYS A 16 172.36 -54.54
REMARK 500 2 ASP A 18 31.77 -160.26
REMARK 500 2 VAL A 23 -86.31 59.89
REMARK 500 2 LEU A 24 19.01 -149.41
REMARK 500 3 CYS A 2 166.45 52.56
REMARK 500 3 SER A 5 98.16 -61.83
REMARK 500 3 CYS A 9 -168.43 -120.61
REMARK 500 3 ASN A 10 -93.83 -118.76
REMARK 500 3 LEU A 11 -33.03 170.16
REMARK 500 3 ASP A 13 36.27 -146.06
REMARK 500 3 ASN A 15 43.40 -144.84
REMARK 500 3 ASP A 18 44.29 -160.28
REMARK 500 3 VAL A 23 -86.37 61.13
REMARK 500 3 LEU A 24 19.52 -156.17
REMARK 500 4 SER A 5 95.92 -47.78
REMARK 500 4 CYS A 9 -168.88 -122.17
REMARK 500 4 LEU A 12 -61.86 -96.04
REMARK 500 4 ASN A 15 44.78 -147.78
REMARK 500 4 CYS A 16 165.08 -46.79
REMARK 500 4 ASP A 18 45.23 -160.93
REMARK 500 4 VAL A 23 -79.68 70.90
REMARK 500 4 LEU A 24 22.23 -160.24
REMARK 500 5 CYS A 2 166.16 62.87
REMARK 500 5 SER A 5 98.89 -66.54
REMARK 500 5 ASP A 13 45.37 -93.43
REMARK 500 5 ASN A 15 42.86 -140.71
REMARK 500 5 ASP A 18 50.06 -160.76
REMARK 500 5 VAL A 23 -85.69 60.73
REMARK 500 5 LEU A 24 27.45 -154.78
REMARK 500 6 SER A 5 96.50 -66.83
REMARK 500 6 LEU A 12 -56.58 -124.50
REMARK 500 6 ASP A 13 54.01 -101.04
REMARK 500 6 ASN A 15 46.86 -143.84
REMARK 500 6 ASP A 18 43.14 -158.63
REMARK 500 6 VAL A 23 -86.12 60.03
REMARK 500 6 LEU A 24 24.05 -157.76
REMARK 500 7 SER A 5 96.82 -53.41
REMARK 500 7 ASP A 13 38.39 -92.93
REMARK 500 7 ASN A 15 40.67 -150.53
REMARK 500 7 CYS A 16 162.79 -45.12
REMARK 500 7 ASP A 18 46.52 -161.00
REMARK 500
REMARK 500 THIS ENTRY HAS 136 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FU3 A 1 27 UNP P18511 CXDA_CONTE 52 78
SEQRES 1 A 27 TRP CYS LYS GLN SER GLY GLU MET CYS ASN LEU LEU ASP
SEQRES 2 A 27 GLN ASN CYS CYS ASP GLY TYR CYS ILE VAL LEU VAL CYS
SEQRES 3 A 27 THR
SHEET 1 A 2 CYS A 21 ILE A 22 0
SHEET 2 A 2 VAL A 25 CYS A 26 -1 N VAL A 25 O ILE A 22
SSBOND 1 CYS A 2 CYS A 17 1555 1555 2.02
SSBOND 2 CYS A 9 CYS A 21 1555 1555 2.02
SSBOND 3 CYS A 16 CYS A 26 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 - 23 20 Bytes