Header list of 1a11.pdb file
Complete list - 16 20 Bytes
HEADER ACETYLCHOLINE RECEPTOR 19-DEC-97 1A11
TITLE NMR STRUCTURE OF MEMBRANE SPANNING SEGMENT 2 OF THE ACETYLCHOLINE
TITLE 2 RECEPTOR IN DPC MICELLES, 10 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINE RECEPTOR M2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACHR M2;
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 BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX FUSION
KEYWDS ACETYLCHOLINE RECEPTOR, M2, MICELLE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR J.J.GESELL,W.SUN,M.MONTAL,S.J.OPELLA
REVDAT 3 16-FEB-22 1A11 1 REMARK
REVDAT 2 24-FEB-09 1A11 1 VERSN
REVDAT 1 08-APR-98 1A11 0
JRNL AUTH S.J.OPELLA,F.M.MARASSI,J.J.GESELL,A.P.VALENTE,Y.KIM,
JRNL AUTH 2 M.OBLATT-MONTAL,M.MONTAL
JRNL TITL STRUCTURES OF THE M2 CHANNEL-LINING SEGMENTS FROM NICOTINIC
JRNL TITL 2 ACETYLCHOLINE AND NMDA RECEPTORS BY NMR SPECTROSCOPY.
JRNL REF NAT.STRUCT.BIOL. V. 6 374 1999
JRNL REFN ISSN 1072-8368
JRNL PMID 10201407
JRNL DOI 10.1038/7610
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: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1A11 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170259.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HMQC-NOESY; HMQC-TOCSY; HNCA;
REMARK 210 HNCOCA; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX600; DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 SER A 2 172.84 67.55
REMARK 500 2 SER A 2 158.49 65.25
REMARK 500 2 ALA A 16 -72.46 -72.79
REMARK 500 3 SER A 2 -164.36 67.47
REMARK 500 3 ALA A 14 -72.88 -50.20
REMARK 500 4 SER A 2 -148.23 58.46
REMARK 500 5 SER A 2 159.87 57.38
REMARK 500 7 SER A 2 -83.67 -75.82
REMARK 500 7 ALA A 14 -74.00 -59.47
REMARK 500 9 SER A 2 -176.53 70.90
REMARK 500 10 SER A 2 171.92 64.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 25 0.31 SIDE CHAIN
REMARK 500 3 ARG A 25 0.26 SIDE CHAIN
REMARK 500 4 ARG A 25 0.24 SIDE CHAIN
REMARK 500 5 ARG A 25 0.12 SIDE CHAIN
REMARK 500 6 ARG A 25 0.32 SIDE CHAIN
REMARK 500 7 ARG A 25 0.30 SIDE CHAIN
REMARK 500 8 ARG A 25 0.25 SIDE CHAIN
REMARK 500 9 ARG A 25 0.30 SIDE CHAIN
REMARK 500 10 ARG A 25 0.24 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1A11 A 3 25 UNP P25110 ACHD_RAT 276 298
SEQRES 1 A 25 GLY SER GLU LYS MET SER THR ALA ILE SER VAL LEU LEU
SEQRES 2 A 25 ALA GLN ALA VAL PHE LEU LEU LEU THR SER GLN ARG
HELIX 1 1 SER A 2 SER A 23 1 22
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