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2rrh

NMR structure of vasoactive intestinal peptide in Methanol

Method: SOLUTION NMR Dmax: 49.1 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

VIP peptides

Homo sapiens

UniProt P01282

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 125–153 Fragment：Vasoactive intestinal peptide, residues in UNP 125-153 No other associated polymer SOLUTION NMR NMR measurement conditions：pH 7.4；288 K；Pressure ambient NMR sample composition：0.5 mM [U-13C; U-15N] VIP-1, 20 mM TRIS-2, 50 % [U-2H] methanol-3, 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.

Other PDB Difference from Current Entry 2RRH Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2RRI NMR structure of vasoactive intestinal peptide in DPC Micelle Deposited 2010-12-21 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 125–153（29 aa） Fragment：UNP residues 125-153
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.2；298 K；Pressure ambient
NMR sample composition 0.5mM [U-13C; U-15N] entity; 1% DPC; 50mM potassium phosphate; 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
8E3Z Cryo-EM structure of the VPAC1R-VIP-Gs complex Deposited 2022-08-17 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain P 125–152（28 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.70 Å
9P92 Cryo-EM structure of the PAC1nR-VIP-Gs complex Deposited 2025-06-24 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain P 125–152（28 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.80 Å
9P93 Cryo-EM structure of the PAC1sR-VIP-Gs complex Deposited 2025-06-24 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain P 125–152（28 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VIP_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–29； UniProt 125–153

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 2rrh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2rrh
Deposition date deposition_date2010-11-12
Structure title titleNMR structure of vasoactive intestinal peptide in Methanol
Keywords keywordspeptide hormone, HORMONE; HORMONE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier12.65 Å
Radius of gyration Rg (electron density) rg_electron12.83 Å
Forward intensity I(0) i065399400.00
Molecular weight molecular_weight67398.0 kDa
Excluded volume excluded_volume84412 ų
Envelope volume envelope_volume9819 ų
Hydration-shell volume shell_volume6872 ų
Envelope diameter envelope_diameter53.0 Å
Shell Rg shell_rg17.74 Å
Envelope Rg envelope_rg15.61 Å
Shape Rg shape_rg12.89 Å
Total Rg total_rg12.78 Å
Total atoms total_atoms9580
Residues n_residues580
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax49.1 Å
Rg (real space) rg_real13.08 Å
Rg uncertainty (real space) rg_real_error0.68 Å
I(0) (real space) i0_real6.5400e+07
I(0) uncertainty (real space) i0_real_error8.3220e+05
Rg (reciprocal space) rg_reciprocal13.05 Å
I(0) (reciprocal space) i0_reciprocal65400000.0000
Solution quality estimate total_estimate0.5532
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary6.2 Å
Skewness Skewness skewness0.671
Kurtosis Kurtosis kurtosis-0.303
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4703.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.064; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.004; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)