Header list of 1dxz.pdb file
Complete list - 25 20 Bytes
HEADER TRANSMEMBRANE PROTEIN 20-JAN-00 1DXZ
TITLE M2 TRANSMEMBRANE SEGMENT OF ALPHA-SUBUNIT OF NICOTINIC
TITLE 2 ACETYLCHOLINE RECEPTOR FROM TORPEDO CALIFORNICA, NMR, 20
TITLE 3 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: M2 TRANSMEMBRANE SEGMENT;
COMPND 5 OTHER_DETAILS: THE C-TERMINAL RESIDUE OF THE PEPTIDE IS
COMPND 6 AMIDATED. THE COMPLETE RECEPTOR CONSISTS OF A PENTAMER OF
COMPND 7 TWO ALPHA CHAINS, AND ONE EACH OF THE BETA, DELTA, AND
COMPND 8 GAMMA CHAINS
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: THE C-TERMINAL CARBOXYL GROUP OF THR267 IS
SOURCE 3 AMIDATED;
SOURCE 4 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;
SOURCE 5 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 6 ORGANISM_TAXID: 7787;
SOURCE 7 ORGAN: ELECTRIC ORGAN;
SOURCE 8 TISSUE: ELECTRIC TISSUE
KEYWDS TRANSMEMBRANE PROTEIN, NICOTINIC ACETYLCHOLINE RECEPTOR,
KEYWDS 2 TRANSMEMBRANE SEGMENT, M2, ION-CHANNEL
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR V.S.PASHKOV,I.V.MASLENNIKOV,L.D.TCHIKIN,R.G.EFREMOV,
AUTHOR 2 V.T.IVANOV,A.S.ARSENIEV
REVDAT 2 24-FEB-09 1DXZ 1 VERSN
REVDAT 1 02-FEB-00 1DXZ 0
JRNL AUTH V.S.PASHKOV,I.V.MASLENNIKOV,L.D.TCHIKIN,
JRNL AUTH 2 R.G.EFREMOV,V.T.IVANOV,A.S.ARSENIEV
JRNL TITL SPATIAL STRUCTURE OF THE M2 TRANSMEMBRANE SEGMENT
JRNL TITL 2 OF THE NICOTINIC ACETYLCHOLINE RECEPTOR
JRNL TITL 3 ALPHA-SUBUNIT
JRNL REF FEBS LETT. V. 457 117 1999
JRNL REFN ISSN 0014-5793
JRNL PMID 10486576
JRNL DOI 10.1016/S0014-5793(99)01023-6
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FANTOM 4.0
REMARK 3 AUTHORS : R.FRACZKIEWICZ,C.MUMENTHALER,B. VON FREYBERG,
REMARK 3 T.SCHAUMANN,W.BRAUN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN
REMARK 3 THE JRNL CITATION ABOVE. THE NMR STUDY HAS BEEN CONDUCTED
REMARK 3 USING THE SYNTHETIC PEPTIDE WITH METHIONINE 243 REPLACED BY
REMARK 3 NORLEUCINE. SUCH AN ISOSTERIC REPLACEMENT USUALLY DOES NOT
REMARK 3 AFFECT THE PEPTIDE CONFORMATION, WHILE SYMPLIFYING THE
REMARK 3 SYNTHESIS. TO AVOID DIFFICULTIES WHICH MAY ARISE FROM THE
REMARK 3 PRESENCE OF A NONSTANDARD AMINO ACID RESIDUE AS WELL AS FOR
REMARK 3 THE PURPOSE OF AGREEMENT BETWEEN THE NATIVE M2 FRAGMENT AND
REMARK 3 THE CONFORMERS TO BE DEPOSITED, THE NORLEUCINE RESIDUE WAS
REMARK 3 REPLACED BY METHIONINE.
REMARK 4
REMARK 4 1DXZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-JAN-00.
REMARK 100 THE PDBE ID CODE IS EBI-4527.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : 0.1 M LICLO4
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : CDCL3/CD3OH=1/1 WITH
REMARK 210 0.1 M LICLO4
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY, TOCSY; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600
REMARK 210 SPECTROMETER MODEL : UNITY 600
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VARIAN VNMR, XEASY,
REMARK 210 DYANA, MARDIGRAS
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINTS
REMARK 210 VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 4
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 2D-1H-NMR
REMARK 210 SPECTROSCOPY IN THE MEDIUM WHICH SHOULD BE ADEQUATE FOR
REMARK 210 THE M2 SEGMENT WITH ITS NON-LIPID SURROUNDING IN THE
REMARK 210 INTACT NICOTINIC ACTYLCHOLINE RECEPTOR.
REMARK 210 THE PH GIVEN IN THE EXPERIMENTAL DETAILS IS AN APPROXIMATION
REMARK 210 ONLY FOR THE MIXTURE OF ORGANIC SOLVENTS USED.
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 400
REMARK 400 COMPOUND
REMARK 400 THE COMPLETE RECEPTOR CONSISTS OF A PENTAMER OF TWO ALPHA
REMARK 400 CHAINS, AND ONE EACH OF THE BETA, DELTA, AND GAMMA CHAINS.
REMARK 400 THE PEPTIDE STUDIED HERE REPRESENTS THE SECOND TRANS-MEMBRANE
REMARK 400 SEGMENT OF THE ALPHA CHAIN OF ACETYLCHOLINE RECEPTOR PROTEIN,
REMARK 400 ALPHA CHAIN (RESIDUES 267 TO 285)
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 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 2 GLU A 241 -67.07 71.32
REMARK 500 2 SER A 266 -47.85 -171.12
REMARK 500 3 ASP A 238 -46.85 171.04
REMARK 500 4 ASP A 238 126.23 163.95
REMARK 500 4 SER A 266 -64.74 179.28
REMARK 500 5 ASP A 238 -55.91 -162.51
REMARK 500 5 SER A 266 -44.59 179.24
REMARK 500 6 ASP A 238 -58.45 -159.20
REMARK 500 7 SER A 266 -51.88 178.73
REMARK 500 8 ASP A 238 -39.96 162.24
REMARK 500 8 GLU A 241 -123.23 68.47
REMARK 500 9 THR A 237 -168.54 47.50
REMARK 500 9 ASP A 238 -65.44 173.96
REMARK 500 9 GLU A 241 -79.99 64.22
REMARK 500 9 SER A 266 -53.14 179.21
REMARK 500 10 THR A 237 146.60 65.38
REMARK 500 10 ASP A 238 -86.37 -115.68
REMARK 500 10 SER A 266 -48.09 178.79
REMARK 500 11 THR A 237 102.16 62.71
REMARK 500 11 GLU A 241 -91.64 53.49
REMARK 500 11 SER A 266 -51.01 178.71
REMARK 500 12 GLU A 241 -115.47 64.96
REMARK 500 13 THR A 237 144.76 65.98
REMARK 500 13 ASP A 238 -53.99 178.14
REMARK 500 13 SER A 266 -54.34 -166.14
REMARK 500 14 GLU A 241 -78.75 63.26
REMARK 500 15 SER A 266 -49.81 -164.36
REMARK 500 16 GLU A 241 -126.73 65.24
REMARK 500 17 THR A 237 77.04 38.33
REMARK 500 17 ASP A 238 -53.25 -170.35
REMARK 500 17 GLU A 241 -60.58 82.04
REMARK 500 17 SER A 266 -50.78 -156.24
REMARK 500 18 THR A 237 -157.99 -153.65
REMARK 500 18 ASP A 238 34.61 -89.39
REMARK 500 18 GLU A 241 -88.19 60.23
REMARK 500 18 SER A 266 -53.12 179.11
REMARK 500 19 THR A 237 164.52 63.90
REMARK 500 19 ASP A 238 45.94 -85.20
REMARK 500 19 SER A 266 -51.79 179.70
REMARK 500 20 THR A 237 115.72 64.14
REMARK 500 20 ASP A 238 -73.08 -77.41
REMARK 500 20 GLU A 241 -126.33 69.15
REMARK 500 20 SER A 266 -52.79 -163.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ABT RELATED DB: PDB
REMARK 900 ALPHA-BUNGAROTOXIN COMPLEXED WITH THE 185 - 196 FRAGMENT OF
REMARK 900 THE ALPHA-SUBUNIT OF THE TORPEDO NICOTINIC ACETYLCHOLINE
REMARK 900 RECEPTOR (NMR, 4 STRUCTURES)
REMARK 900 RELATED ID: 1TOR RELATED DB: PDB
REMARK 900 ACETYLCHOLINE RECEPTOR, MAIN IMMUNOGENIC REGION
REMARK 900 (NMR, 5 STRUCTURES)
REMARK 900 RELATED ID: 1TOS RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACHR RECEPTOR [ALA76] ANALOGUE
REMARK 900 COMPLEXED WITH THE ANTI-ACETYLCHOLINE MAB6 MONOCLONAL
REMARK 900 ANTIBODY
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AMINO ACIDS NUMERATION IN THE ENTRY DOES NOT INCLUDE THE
REMARK 999 SIGNAL SEQUENCE. THE C-TERMINAL RESIDUE OF THIS ENTRY,
REMARK 999 THR267, IS AMIDATED.
DBREF 1DXZ A 236 267 UNP P02710 ACHA_TORCA 260 291
SEQRES 1 A 33 PRO THR ASP SER GLY GLU LYS MET THR LEU SER ILE SER
SEQRES 2 A 33 VAL LEU LEU SER LEU THR VAL PHE LEU LEU VAL ILE VAL
SEQRES 3 A 33 GLU LEU ILE PRO SER THR NH2
HET NH2 A 268 3
HETNAM NH2 AMINO GROUP
FORMUL 2 NH2 H2 N
HELIX 1 1 GLU A 241 LEU A 263 1 23
LINK C THR A 267 N NH2 A 268 1555 1555 1.33
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 - 25 20 Bytes