2maw

NMR structures of the alpha7 nAChR transmembrane domain.

Method: SOLUTION NMR Dmax: 70.3 Å Quality: REASONABLE

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

Neuronal acetylcholine receptor subunit alpha-7

Homo sapiens

UniProt P36544

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 228–326 Chain A; UniProt 467–496 Fragment:UNP residues 141-235, transmembrane domain Mutation:A195S, V200S, L202S No other associated polymer SOLUTION NMR NMR measurement conditions:pH 4.7;318 K;Ionic strength (raw mmCIF value) 0.01;Pressure ambient NMR sample composition:0.25 mM [U-100% 13C; U-100% 15N] protein, 95% H2O/5% D2O | 95% H2O/5% D2O 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.

44 other PDB entries and 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACHA7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–102; UniProt 228–326 Author chain A; PDBConstruct 108–137; UniProt 467–496

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

SAXS profile for 2maw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2maw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2maw
Deposition date deposition_date2013-07-19
Structure title titleNMR structures of the alpha7 nAChR transmembrane domain.
Keywords keywordstransmembrane domain, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.47
Radius of gyration Rg (electron density) rg_electron17.76
Forward intensity I(0) i0940534000.00
Molecular weight molecular_weight285520.0 kDa
Excluded volume excluded_volume367300 ų
Envelope volume envelope_volume43189 ų
Hydration-shell volume shell_volume18077 ų
Envelope diameter envelope_diameter74.4
Shell Rg shell_rg27.03
Envelope Rg envelope_rg21.84
Shape Rg shape_rg17.84
Total Rg total_rg17.65
Total atoms total_atoms40620
Residues n_residues2680
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax70.3
Rg (real space) rg_real18.71
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real9.4050e+08
I(0) uncertainty (real space) i0_real_error1.3270e+07
Rg (reciprocal space) rg_reciprocal18.68
I(0) (reciprocal space) i0_reciprocal940500000.0000
Solution quality estimate total_estimate0.6611
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.4
Skewness Skewness skewness0.604
Kurtosis Kurtosis kurtosis-0.213
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha752000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.103; Stabil: 0.992; Sysdev: 1.000; Positv: 1.000; Valcen: 0.316; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2mawA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily390 — Neurotransmitter-gated ion-channel transmembrane domain

8. Citations (1)

9. Files and Curves (10)