1r2n

NMR structure of the all-trans retinal in dark-adapted Bacteriorhodopsin

Method: SOLUTION NMR Dmax: 60.0 Å Quality: GOOD

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

Bacteriorhodopsin

OrganismNot specified

UniProt P02945

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 14–262 Not recorded RET RETINAL × 1 SOLUTION NMR NMR measurement conditions:pH 6.5;308 K;Ionic strength (raw mmCIF value) 1;Pressure 1 NMR measurement conditions:pH 6.5;313 K;Ionic strength (raw mmCIF value) 1;Pressure 1 NMR measurement conditions:pH 6.5;318 K;Ionic strength (raw mmCIF value) 1;Pressure 1 NMR sample composition:residue specifically labeled purple membrane (12-20 mg Bacteriorhodopsin) suspended in 1% deuterated dodecal maltoside, 10 mM potassium phosphate buffer in D2O | 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.

173 other PDB entries and 201 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BACR_HALN1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–249; UniProt 14–262

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 1r2n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1r2n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1r2n
Deposition date deposition_date2003-09-29
Structure title titleNMR structure of the all-trans retinal in dark-adapted Bacteriorhodopsin
Keywords keywordsPROTON PUMP, MEMBRANE PROTEIN, RETINAL PROTEIN, PHOTOreceptor, HALOARCHAEA, proton transport; MEMBRANE PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.32
Radius of gyration Rg (electron density) rg_electron18.14
Forward intensity I(0) i0959785000.00
Molecular weight molecular_weight307320.0 kDa
Excluded volume excluded_volume401790 ų
Envelope volume envelope_volume36582 ų
Hydration-shell volume shell_volume17181 ų
Envelope diameter envelope_diameter67.7
Shell Rg shell_rg24.16
Envelope Rg envelope_rg18.54
Shape Rg shape_rg18.13
Total Rg total_rg18.30
Total atoms total_atoms44328
Residues n_residues2784
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 dmax60.0
Rg (real space) rg_real18.38
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real9.5980e+08
I(0) uncertainty (real space) i0_real_error1.2730e+07
Rg (reciprocal space) rg_reciprocal18.37
I(0) (reciprocal space) i0_reciprocal959800000.0000
Solution quality estimate total_estimate0.8818
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.6
Skewness Skewness skewness0.415
Kurtosis Kurtosis kurtosis-0.325
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha937700.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.843; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.969

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1r2na_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.13 — Class A G protein-coupled receptor (GPCR)-like
Superfamily Superfamily superfamilyf.13.1 — Class A G protein-coupled receptor (GPCR)-like
Family Family familyf.13.1.1 — Bacteriorhodopsin-like

CATH v4.4 (1 domains)

Domain ID domain_id1r2nA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1070 — Rhopdopsin 7-helix transmembrane proteins
Homologous superfamily homologous superfamily10 — Rhodopsin 7-helix transmembrane proteins

8. Citations (1)

9. Files and Curves (10)