Header list of 1eq8.pdb file
Complete list - 16 20 Bytes
HEADER SIGNALING PROTEIN 03-APR-00 1EQ8
TITLE THREE-DIMENSIONAL STRUCTURE OF THE PENTAMERIC HELICAL BUNDLE OF THE
TITLE 2 ACETYLCHOLINE RECEPTOR M2 TRANSMEMBRANE SEGMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINE RECEPTOR PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 FRAGMENT: M2 SEGMENT;
COMPND 5 SYNONYM: ACHR M2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 4 ORGANISM_TAXID: 7787;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 CELL: NEURON;
SOURCE 7 CELLULAR_LOCATION: POST-SYNAPTIC MEMBRANE;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMAL
KEYWDS NEUROTRANSMITTER RECEPTOR, M2, LIPID BILAYERS, ION-CHANNEL, HELICAL
KEYWDS 2 BUNDLE, PENTAMERIC BUNDLE, SIGNALING PROTEIN
EXPDTA SOLID-STATE NMR
AUTHOR F.M.MARASSI,J.J.GESELL,Y.KIM,A.P.VALENTE,M.OBLATT-MONTAL,M.MONTAL,
AUTHOR 2 S.J.OPELLA
REVDAT 3 16-FEB-22 1EQ8 1 REMARK LINK
REVDAT 2 24-FEB-09 1EQ8 1 VERSN
REVDAT 1 26-APR-00 1EQ8 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 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.M.MARASSI,J.J.GESELL,A.P.VALENTE,Y.KIM,M.OBLATT-MONTAL,
REMARK 1 AUTH 2 M.MONTAL,S.J.OPELLA
REMARK 1 TITL DILUTE SPIN-EXCHANGE ASSIGNMENT OF SOLID-STATE NMR SPECTRA
REMARK 1 TITL 2 OF ORIENTED PROTEINS: ACETYLCHOLINE M2 IN BILAYERS
REMARK 1 REF J.BIOMOL.NMR V. 14 141 1999
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1008391823293
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.01
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE BACKBONE COORDINATES OBTAINED FROM
REMARK 3 SOLUTION NMR WERE SUPERIMPOSED ON THE COORDINATES OBTAINED FROM
REMARK 3 SOLID-STATE NMR TO FIX THE HELIX ORIENTATION AND ROTATION IN THE
REMARK 3 MEMBRANE. THE PENTAMERIC ARRAY WAS THEN OPTIMIZED USING
REMARK 3 MOLECULAR DYNAMICS. PORE CONTOURS WERE CALCULATED WITH THE
REMARK 3 PROGRAM HOLE.
REMARK 4
REMARK 4 1EQ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010812.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 298
REMARK 210 PH : 5.5; 5.5
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM M2 U-15N; 350MM DPC; PH5.5;;
REMARK 210 20MG M2 U-15N; 40MG DMPC;
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HSQC; HNCA; HNCOCA; 3D 15N- AND
REMARK 210 13C-EDITED NOESY; 3D 15N- AND
REMARK 210 13C-EDITED TOCSY; 3D HNHA; 1D
REMARK 210 CPMOIST; 2D 1H/1H-15N PISEMA; 2D
REMARK 210 1H/15N HETCOR;
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ; 400 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; CMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; CHEMAGNETICS
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FISI 1.01, HOLE, FELIX 95
REMARK 210 METHOD USED : X-PLOR 3.1, DISTANCE GEOMETRY,
REMARK 210 SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS, FISI, FINGERPRINT, HOLE
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE ORIENTATION OF EACH MONOMER IN THE PENTAMERIC BUNDLE
REMARK 210 WAS OBTAINED FROM THE COMBINATION OF THE SOLUTION NMR (PDB FILE
REMARK 210 1A11) AND SOLID-STATE NMR (PDB FILE 1CEK) STRUCTURES
REMARK 217
REMARK 217 SOLID STATE NMR STUDY
REMARK 217 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLID
REMARK 217 STATE NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 217 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 217 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: PENTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG E 23 C ARG E 23 O 0.150
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 23 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG C 23 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG D 23 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG E 23 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OH E 24
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A11 RELATED DB: PDB
REMARK 900 SOLUTION NMR COORDINATES OF THE MONOMERIC ACHR M2 HELIX
REMARK 900 RELATED ID: 1CEK RELATED DB: PDB
REMARK 900 SOLID-STATE NMR COORDINATES OF THE MONOMERIC ACHR M2 HELIX IN THE
REMARK 900 MEMBRANE
DBREF 1EQ8 A 1 23 UNP P02718 ACHD_TORCA 276 298
DBREF 1EQ8 B 1 23 UNP P02718 ACHD_TORCA 276 298
DBREF 1EQ8 C 1 23 UNP P02718 ACHD_TORCA 276 298
DBREF 1EQ8 D 1 23 UNP P02718 ACHD_TORCA 276 298
DBREF 1EQ8 E 1 23 UNP P02718 ACHD_TORCA 276 298
SEQRES 1 A 23 GLU LYS MET SER THR ALA ILE SER VAL LEU LEU ALA GLN
SEQRES 2 A 23 ALA VAL PHE LEU LEU LEU THR SER GLN ARG
SEQRES 1 B 23 GLU LYS MET SER THR ALA ILE SER VAL LEU LEU ALA GLN
SEQRES 2 B 23 ALA VAL PHE LEU LEU LEU THR SER GLN ARG
SEQRES 1 C 23 GLU LYS MET SER THR ALA ILE SER VAL LEU LEU ALA GLN
SEQRES 2 C 23 ALA VAL PHE LEU LEU LEU THR SER GLN ARG
SEQRES 1 D 23 GLU LYS MET SER THR ALA ILE SER VAL LEU LEU ALA GLN
SEQRES 2 D 23 ALA VAL PHE LEU LEU LEU THR SER GLN ARG
SEQRES 1 E 23 GLU LYS MET SER THR ALA ILE SER VAL LEU LEU ALA GLN
SEQRES 2 E 23 ALA VAL PHE LEU LEU LEU THR SER GLN ARG
HET OH E 24 2
HETNAM OH HYDROXIDE ION
FORMUL 6 OH H O 1-
HELIX 1 1 GLU A 1 ARG A 23 1 23
HELIX 2 2 GLU B 1 ARG B 23 1 23
HELIX 3 3 GLU C 1 ARG C 23 1 23
HELIX 4 4 GLU D 1 ARG D 23 1 23
HELIX 5 5 GLU E 1 ARG E 23 1 23
LINK C ARG E 23 O OH E 24 1555 1555 1.23
SITE 1 AC1 3 LEU E 19 THR E 20 ARG E 23
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
Complete list - 16 20 Bytes