1cek

THREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-LINING SEGMENT FROM THE NICOTINIC ACETYLCHOLINE RECEPTOR BY SOLID-STATE NMR SPECTROSCOPY

Method: SOLID-STATE NMR D_max: 22.0 Å Quality: REASONABLE

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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (ACETYLCHOLINE RECEPTOR M2)

Rattus norvegicus

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 274–298	Fragment：M2 DOMAIN	No other associated polymer	SOLID-STATE NMR NMR measurement conditions：pH 6；295 K NMR sample composition：DMPC	Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1CEK	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A11 NMR STRUCTURE OF MEMBRANE SPANNING SEGMENT 2 OF THE ACETYLCHOLINE RECEPTOR IN DPC MICELLES, 10 STRUCTURES Deposited 1997-12-19	Different construct Different experimental method Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 276–298（23 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；313 K	Resolution not provided

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ACHD_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–25； UniProt 274–298

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1cek
Deposition date deposition_date	1999-03-09
Structure title title	THREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-LINING SEGMENT FROM THE NICOTINIC ACETYLCHOLINE RECEPTOR BY SOLID-STATE NMR SPECTROSCOPY
Keywords keywords	ACETYLCHOLINE RECEPTOR, M2, LIPID BILAYERS, ION-CHANNEL; ACETYLCHOLINE RECEPTOR
Experimental Method method	SOLID-STATE NMR

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	7.79 Å
Radius of gyration Rg (electron density) rg_electron	7.33 Å
Forward intensity I(0) i0	56836.50
Molecular weight molecular_weight	886.7 kDa
Excluded volume excluded_volume	890 Å³
Envelope volume envelope_volume	1070 Å³
Hydration-shell volume shell_volume	1929 Å³
Envelope diameter envelope_diameter	24.4 Å
Shell Rg shell_rg	9.95 Å
Envelope Rg envelope_rg	7.36 Å
Shape Rg shape_rg	6.66 Å
Total Rg total_rg	8.85 Å
Total atoms total_atoms	70
Residues n_residues	14
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	22.0 Å
Rg (real space) rg_real	7.48 Å
Rg uncertainty (real space) rg_real_error	0.04 Å
I(0) (real space) i0_real	5.5010e+04
I(0) uncertainty (real space) i0_real_error	3.2580e+02
Rg (reciprocal space) rg_reciprocal	7.96 Å
I(0) (reciprocal space) i0_reciprocal	56840.0000
Solution quality estimate total_estimate	0.6436
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	7.0 Å
Skewness Skewness skewness	0.393
Kurtosis Kurtosis kurtosis	-0.657
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	5.8080
Highest regularization parameter α highest_alpha	932.8000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.983; Stabil: 0.939; Sysdev: 0.000; Positv: 1.000; Valcen: 0.603; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1ceka_
Class class	j — Peptides
Fold Fold fold	j.35 — Transmembrane helical fragments
Superfamily Superfamily superfamily	j.35.1 — Transmembrane helical fragments
Family Family family	j.35.1.1 — Transmembrane helical fragments

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8. Citations (2)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	PROTEIN (ACETYLCHOLINE RECEPTOR M2)
Molecular weight formula_weight	2666.1 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	71

来源生物 organism	Rattus norvegicus
通用名 common_name	Norway rat
NCBI Class编号 ncbi_taxonomy_id	10116
宿主生物 host_organism	Escherichia coli BL21

THREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-LINING SEGMENT FROM THE NICOTINIC ACETYLCHOLINE RECEPTOR BY SOLID-STATE NMR SPECTROSCOPY

1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (ACETYLCHOLINE RECEPTOR M2)

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/ce/1cek/1cek.fit
pddf	/app/data/pr_computation/ce/1cek/1cek.pr.out
profile	/app/data/saxs_computation/ce/1cek/1cek.dat