2rpw

Structure of a peptide derived from H+-V-ATPase subunit a

Method: SOLUTION NMR Dmax: 30.4 Å Quality: REASONABLE

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

25 meric peptide from V-type proton ATPase subunit a, vacuolar isoform

OrganismNot specified

UniProt P32563

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 X; UniProt 728–748 Fragment:TM7, UNP residues 728-748 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 5;298 K;Pressure ambient NMR sample composition:1mM KMTM7, 250mM [U-100% 2H] SDS, 10mM sodium phosphate, 0.3mM DSS, 10% D2O, 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.

31 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPH1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain X; PDBConstruct 3–23; UniProt 728–748

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 2rpw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2rpw
Deposition date deposition_date2008-11-08
Structure title titleStructure of a peptide derived from H+-V-ATPase subunit a
Keywords keywords;V-ATPase subunit a, Acetylation, Coiled coil, Glycoprotein, Hydrogen ion transport, Ion transport, Membrane, Phosphoprotein, Transmembrane, Transport, Vacuole, TRANSPORT PROTEIN ;; TRANSPORT PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.17
Radius of gyration Rg (electron density) rg_electron11.38
Forward intensity I(0) i042334200.00
Molecular weight molecular_weight56607.0 kDa
Excluded volume excluded_volume72346 ų
Envelope volume envelope_volume13355 ų
Hydration-shell volume shell_volume8522 ų
Envelope diameter envelope_diameter47.8
Shell Rg shell_rg18.90
Envelope Rg envelope_rg14.98
Shape Rg shape_rg11.28
Total Rg total_rg12.14
Total atoms total_atoms8340
Residues n_residues500
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 dmax30.4
Rg (real space) rg_real10.47
Rg uncertainty (real space) rg_real_error0.06
I(0) (real space) i0_real4.0640e+07
I(0) uncertainty (real space) i0_real_error3.2340e+05
Rg (reciprocal space) rg_reciprocal11.46
I(0) (reciprocal space) i0_reciprocal42330000.0000
Solution quality estimate total_estimate0.5971
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary7.3
Skewness Skewness skewness0.381
Kurtosis Kurtosis kurtosis-0.849
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha3.7800
Highest regularization parameter α highest_alpha2749.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.875; Stabil: 0.969; Sysdev: 0.000; Positv: 1.000; Valcen: 0.243; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)