2n7q

Structure of the transmembrane domain of human nicastrin in SDS micelles

Method: SOLUTION NMR Dmax: 72.9 Å Quality: REASONABLE

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

Nicastrin

Homo sapiens

UniProt Q92542

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 664–709 Fragment:UNP residues 664-709 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;313 K;Ionic strength (raw mmCIF value) 20;Pressure ambient NMR sample composition:0.8 mM [U-100% 13C; U-100% 15N] transmembrane domain of human nicastrin-1, 20 mM sodium phosphate-2, 100 mM SDS-3, 1 mM DTT-4, 90% H2O/10% D2O | 90% H2O/10% 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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NICA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 9–54; UniProt 664–709

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 2n7q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2n7q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2n7q
Deposition date deposition_date2015-09-17
Structure title titleStructure of the transmembrane domain of human nicastrin in SDS micelles
Keywords keywordsDetergent micelles, gamma-secretase, nicastrin, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier17.79
Radius of gyration Rg (electron density) rg_electron18.24
Forward intensity I(0) i0104285000.00
Molecular weight molecular_weight99138.0 kDa
Excluded volume excluded_volume129670 ų
Envelope volume envelope_volume24993 ų
Hydration-shell volume shell_volume11070 ų
Envelope diameter envelope_diameter76.3
Shell Rg shell_rg25.44
Envelope Rg envelope_rg22.12
Shape Rg shape_rg18.21
Total Rg total_rg18.63
Total atoms total_atoms14380
Residues n_residues920
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 dmax72.9
Rg (real space) rg_real18.34
Rg uncertainty (real space) rg_real_error1.01
I(0) (real space) i0_real1.0430e+08
I(0) uncertainty (real space) i0_real_error1.5630e+06
Rg (reciprocal space) rg_reciprocal18.28
I(0) (reciprocal space) i0_reciprocal104300000.0000
Solution quality estimate total_estimate0.6177
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary4.9
Skewness Skewness skewness0.524
Kurtosis Kurtosis kurtosis-0.545
Angular range angular_range— – 0.4450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11360.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.001; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.024; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)