Header list of 1byy.pdb file
Complete list - 16 20 Bytes
HEADER MEMBRANE PROTEIN 21-OCT-98 1BYY
TITLE SODIUM CHANNEL IIA INACTIVATION GATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (SODIUM CHANNEL ALPHA-SUBUNIT);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: INACTIVATION DOMAIN FRAGMENT;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL26;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX
KEYWDS SODIUM CHANNEL, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR C.A.ROHL,F.A.BOECKMAN,C.BAKER,T.SCHEUER,W.A.CATTERALL,R.E.KLEVIT
REVDAT 3 16-FEB-22 1BYY 1 REMARK
REVDAT 2 24-FEB-09 1BYY 1 VERSN
REVDAT 1 29-OCT-99 1BYY 0
JRNL AUTH C.A.ROHL,F.A.BOECKMAN,C.BAKER,T.SCHEUER,W.A.CATTERALL,
JRNL AUTH 2 R.E.KLEVIT
JRNL TITL SOLUTION STRUCTURE OF THE SODIUM CHANNEL INACTIVATION GATE.
JRNL REF BIOCHEMISTRY V. 38 855 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 9893979
JRNL DOI 10.1021/BI9823380
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BYY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-99.
REMARK 100 THE DEPOSITION ID IS D_1000007044.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 299
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : H2O/D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-EDITED NOESY; 13C-EDITED
REMARK 210 NOESY; HNHB; HMQC-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500; DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 25
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO VIOLATIONS >0.3 DEGREES OR 3
REMARK 210 ANGSTROMS; LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: STRUCTURE DETERMINATION USING TRIPLE-RESONANCE NMR ON 13C,
REMARK 210 15N-LABELED PROTEIN
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-10
REMARK 465 RES C SSSEQI
REMARK 465 ASP A 1474
REMARK 465 ASN A 1475
REMARK 465 PHE A 1476
REMARK 465 ASN A 1477
REMARK 465 GLN A 1478
REMARK 465 GLN A 1479
REMARK 465 LYS A 1480
REMARK 465 LYS A 1481
REMARK 465 LYS A 1482
REMARK 465 PHE A 1483
REMARK 465 GLY A 1484
REMARK 465 GLY A 1485
REMARK 465 LYS A 1507
REMARK 465 LYS A 1508
REMARK 465 PRO A 1509
REMARK 465 GLN A 1510
REMARK 465 LYS A 1511
REMARK 465 PRO A 1512
REMARK 465 ILE A 1513
REMARK 465 PRO A 1514
REMARK 465 ARG A 1515
REMARK 465 PRO A 1516
REMARK 465 ALA A 1517
REMARK 465 ASN A 1518
REMARK 465 LYS A 1519
REMARK 465 PHE A 1520
REMARK 465 GLN A 1521
REMARK 465 GLY A 1522
REMARK 465 MET A 1523
REMARK 465 VAL A 1524
REMARK 465 PHE A 1525
REMARK 465 ASP A 1526
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 ASP A1487 -168.12 -71.17
REMARK 500 1 ILE A1488 94.82 -65.66
REMARK 500 1 PHE A1489 -178.79 -53.48
REMARK 500 1 MET A1490 -164.79 -70.94
REMARK 500 1 LYS A1503 80.71 62.61
REMARK 500 1 LEU A1504 42.15 28.69
REMARK 500 2 ILE A1488 47.09 -93.82
REMARK 500 2 LYS A1503 75.74 58.27
REMARK 500 2 LEU A1504 34.85 35.53
REMARK 500 3 ILE A1488 90.94 -67.20
REMARK 500 3 PHE A1489 54.21 -175.18
REMARK 500 3 THR A1491 -165.51 -63.32
REMARK 500 3 LYS A1503 44.04 -95.79
REMARK 500 3 LEU A1504 32.98 -166.44
REMARK 500 4 PHE A1489 -175.55 174.66
REMARK 500 4 LYS A1503 37.19 -97.04
REMARK 500 5 ILE A1488 103.91 57.69
REMARK 500 5 PHE A1489 -173.32 -57.46
REMARK 500 5 LEU A1504 -35.75 91.66
REMARK 500 6 THR A1491 -165.92 -59.37
REMARK 500 6 LYS A1503 38.47 -95.73
REMARK 500 6 LEU A1504 34.60 -173.44
REMARK 500 7 ASP A1487 -163.66 -61.08
REMARK 500 7 PHE A1489 139.14 179.92
REMARK 500 7 LEU A1504 42.17 28.67
REMARK 500 8 ASP A1487 35.68 -98.86
REMARK 500 8 PHE A1489 -176.06 46.20
REMARK 500 8 LYS A1503 29.65 41.99
REMARK 500 8 LEU A1504 14.95 -153.26
REMARK 500 9 PHE A1489 -176.19 -179.82
REMARK 500 9 THR A1491 -167.83 -105.42
REMARK 500 9 LYS A1503 43.57 -92.71
REMARK 500 9 LEU A1504 35.93 -177.12
REMARK 500 10 ASP A1487 -166.11 -61.00
REMARK 500 10 PHE A1489 -176.00 44.72
REMARK 500 10 MET A1490 -156.53 -73.10
REMARK 500 10 LEU A1504 -35.89 -179.24
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BYY A 1474 1526 UNP P04775 SCN2A_RAT 1474 1526
SEQRES 1 A 53 ASP ASN PHE ASN GLN GLN LYS LYS LYS PHE GLY GLY GLN
SEQRES 2 A 53 ASP ILE PHE MET THR GLU GLU GLN LYS LYS TYR TYR ASN
SEQRES 3 A 53 ALA MET LYS LYS LEU GLY SER LYS LYS PRO GLN LYS PRO
SEQRES 4 A 53 ILE PRO ARG PRO ALA ASN LYS PHE GLN GLY MET VAL PHE
SEQRES 5 A 53 ASP
HELIX 1 1 GLU A 1492 LYS A 1502 1 11
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 - 16 20 Bytes