HEADER TRANSMEMBRANE CHANNEL 22-APR-99 1QG9
TITLE SECOND REPEAT (IS2MIC) FROM VOLTAGE-GATED SODIUM CHANNEL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (SODIUM CHANNEL PROTEIN, BRAIN II ALPHA SUBUNIT);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: S2 OF REPEAT I;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SEQUENCE FROM MEMBRANES OF BRAIN CELLS OF RAT (RATTUS
SOURCE 4 NORVEGICUS)
KEYWDS TRANSMEMBRANE SODIUM CHANNEL, TRANSMEMBRANE CHANNEL
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR D.J.DOAK,D.MULVEY,K.KAWAGUCHI,J.VILLALAIN,I.D.CAMPBELL
REVDAT 5 27-DEC-23 1QG9 1 REMARK
REVDAT 4 02-MAR-22 1QG9 1 REMARK
REVDAT 3 24-FEB-09 1QG9 1 VERSN
REVDAT 2 01-APR-03 1QG9 1 JRNL
REVDAT 1 30-APR-99 1QG9 0
JRNL AUTH D.G.DOAK,D.MULVEY,K.KAWAGUCHI,J.VILLALAIN,I.D.CAMPBELL
JRNL TITL STRUCTURAL STUDIES OF SYNTHETIC PEPTIDES DISSECTED FROM THE
JRNL TITL 2 VOLTAGE-GATED SODIUM CHANNEL.
JRNL REF J.MOL.BIOL. V. 258 672 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8637001
JRNL DOI 10.1006/JMBI.1996.0278
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: STRUCTURES HAVE BEEN RECALCULATED USING
REMARK 3 PARAMETERS PARALLHDG5.1.PRO (MICHAEL NILGES)
REMARK 4
REMARK 4 1QG9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000911.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 3.3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : MICELLE MOLAR RATIO DPC/ IS2 =
REMARK 210 68
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; HOHAHA; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AM500; AM600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: SEE JOURNAL REFERENCE
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 VAL A 2 -70.24 -100.60
REMARK 500 1 THR A 5 -81.91 -90.14
REMARK 500 2 GLU A 3 -52.78 -148.60
REMARK 500 3 TYR A 4 -59.53 -151.34
REMARK 500 4 PHE A 6 -70.31 -47.52
REMARK 500 5 VAL A 2 -50.93 -144.46
REMARK 500 6 GLU A 3 -79.87 -56.39
REMARK 500 8 GLU A 3 48.28 -179.84
REMARK 500 12 THR A 5 -47.95 -160.68
REMARK 500 13 TYR A 4 -37.49 -179.31
REMARK 500 14 VAL A 2 -51.86 -121.09
REMARK 500 15 VAL A 2 -67.56 -129.69
REMARK 500 15 THR A 5 -77.78 -93.77
REMARK 500 15 ALA A 20 36.62 -93.24
REMARK 500 16 GLU A 3 74.89 -65.54
REMARK 500 17 TYR A 4 -42.83 -179.39
REMARK 500 17 PHE A 6 -70.06 -49.12
REMARK 500 18 VAL A 2 -67.08 -97.75
REMARK 500 18 TYR A 4 -44.09 -176.14
REMARK 500 19 GLU A 3 119.04 67.73
REMARK 500 19 TYR A 4 -42.08 -174.38
REMARK 500 20 ALA A 20 44.32 -93.87
REMARK 500 21 TYR A 4 -50.06 -133.92
REMARK 500 22 ALA A 20 46.32 -142.22
REMARK 500 23 VAL A 2 -44.99 -157.61
REMARK 500 24 GLU A 3 81.69 -65.54
REMARK 500 25 TYR A 4 -72.03 -96.94
REMARK 500 28 GLU A 3 44.57 -171.92
REMARK 500 30 VAL A 2 -51.41 -122.66
REMARK 500 30 GLU A 3 -71.53 -173.87
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1QG9 A 1 21 UNP P08104 SCN3A_RAT 157 177
SEQRES 1 A 21 ASN VAL GLU TYR THR PHE THR GLY ILE TYR THR PHE GLU
SEQRES 2 A 21 SER LEU ILE LYS ILE LEU ALA ARG
HELIX 1 1 PHE A 6 LEU A 19 1 14
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
(ATOM LINES ARE NOT SHOWN.)
END