2jp8

Angiotensin 1-7

Method: SOLUTION NMR Dmax: 17.6 Å Quality: REASONABLE

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

Angiotensin-(1-7)

OrganismNot specified

UniProt P01019

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 P; UniProt 34–40 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 2.9;278 K;Ionic strength (raw mmCIF value) 12;Pressure ambient NMR sample composition:12.0 mM angiotensin, 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.

13 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ANGT_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain P; PDBConstruct 1–7; UniProt 34–40

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 2jp8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2jp8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2jp8
Deposition date deposition_date2007-04-27
Structure title titleAngiotensin 1-7
Keywords keywordsbend, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier6.17
Radius of gyration Rg (electron density) rg_electron5.97
Forward intensity I(0) i01308480.00
Molecular weight molecular_weight8990.0 kDa
Excluded volume excluded_volume11245 ų
Envelope volume envelope_volume1758 ų
Hydration-shell volume shell_volume2777 ų
Envelope diameter envelope_diameter22.7
Shell Rg shell_rg10.46
Envelope Rg envelope_rg7.06
Shape Rg shape_rg5.96
Total Rg total_rg6.55
Total atoms total_atoms1200
Residues n_residues70
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 dmax17.6
Rg (real space) rg_real6.01
Rg uncertainty (real space) rg_real_error0.02
I(0) (real space) i0_real1.2680e+06
I(0) uncertainty (real space) i0_real_error6.9390e+03
Rg (reciprocal space) rg_reciprocal6.30
I(0) (reciprocal space) i0_reciprocal1308000.0000
Solution quality estimate total_estimate0.6376
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary5.1
Skewness Skewness skewness0.342
Kurtosis Kurtosis kurtosis-0.773
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha9.0970
Highest regularization parameter α highest_alpha319.1000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.973; Stabil: 0.962; Sysdev: 0.000; Positv: 1.000; Valcen: 0.482; 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)