1n9v

Differences and Similarities in Solution Structures of Angiotensin I & II: Implication for Structure-Function Relationship.

Method: SOLUTION NMR Dmax: 24.8 Å Quality: REASONABLE

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

Angiotensin II

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 A; UniProt 34–41 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:298 K;Pressure ambient NMR sample composition:2.5 mM; DMSO-d6 | DMSO-d6 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 A; PDBConstruct 1–8; UniProt 34–41

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 1n9v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1n9v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1n9v
Deposition date deposition_date2002-11-26
Structure title titleDifferences and Similarities in Solution Structures of Angiotensin I & II: Implication for Structure-Function Relationship.
Keywords keywordsAngiotensin, Renin-Angiotensin System, Solid Phase Peptide Synthesis, NMR Solution Structure, Peptides, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier6.44
Radius of gyration Rg (electron density) rg_electron7.06
Forward intensity I(0) i06221280.00
Molecular weight molecular_weight21970.0 kDa
Excluded volume excluded_volume27952 ų
Envelope volume envelope_volume2232 ų
Hydration-shell volume shell_volume3017 ų
Envelope diameter envelope_diameter25.6
Shell Rg shell_rg11.41
Envelope Rg envelope_rg8.22
Shape Rg shape_rg7.05
Total Rg total_rg7.37
Total atoms total_atoms3066
Residues n_residues168
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 dmax24.8
Rg (real space) rg_real6.48
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real6.2210e+06
I(0) uncertainty (real space) i0_real_error7.2040e+04
Rg (reciprocal space) rg_reciprocal6.48
I(0) (reciprocal space) i0_reciprocal6221000.0000
Solution quality estimate total_estimate0.6281
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary2.5
Skewness Skewness skewness0.007
Kurtosis Kurtosis kurtosis-1.412
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha502.8000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.046; Stabil: 0.994; Sysdev: 1.000; Positv: 1.000; Valcen: 0.138; Smooth: 0.904

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1n9va_
Class classj — Peptides
Fold Fold foldj.102 — Angiotensin
Superfamily Superfamily superfamilyj.102.1 — Angiotensin
Family Family familyj.102.1.1 — Angiotensin

8. Citations (2)

9. Files and Curves (10)