1bha

THREE-DIMENSIONAL STRUCTURE OF (1-71) BACTERIOOPSIN SOLUBILIZED IN METHANOL-CHLOROFORM AND SDS MICELLES DETERMINED BY 15N-1H HETERONUCLEAR NMR SPECTROSCOPY

Method: SOLUTION NMR Dmax: 51.8 Å Quality: REASONABLE

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

BACTERIORHODOPSIN

Halobacterium salinarum

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 14–84 Not recorded No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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 1–71; UniProt 14–84

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 1bha

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1bha
Deposition date deposition_date1993-10-11
Structure title titleTHREE-DIMENSIONAL STRUCTURE OF (1-71) BACTERIOOPSIN SOLUBILIZED IN METHANOL-CHLOROFORM AND SDS MICELLES DETERMINED BY 15N-1H HETERONUCLEAR NMR SPECTROSCOPY
Keywords keywordsPHOTORECEPTOR; PHOTORECEPTOR
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.24
Radius of gyration Rg (electron density) rg_electron14.58
Forward intensity I(0) i077968400.00
Molecular weight molecular_weight87234.0 kDa
Excluded volume excluded_volume114540 ų
Envelope volume envelope_volume17610 ų
Hydration-shell volume shell_volume9776 ų
Envelope diameter envelope_diameter55.3
Shell Rg shell_rg20.70
Envelope Rg envelope_rg16.98
Shape Rg shape_rg14.56
Total Rg total_rg14.88
Total atoms total_atoms6131
Residues n_residues804
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 dmax51.8
Rg (real space) rg_real14.49
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real7.7970e+07
I(0) uncertainty (real space) i0_real_error8.8830e+05
Rg (reciprocal space) rg_reciprocal14.47
I(0) (reciprocal space) i0_reciprocal77970000.0000
Solution quality estimate total_estimate0.7015
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.4
Skewness Skewness skewness0.454
Kurtosis Kurtosis kurtosis-0.524
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17620.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.611; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.283; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1bhaa_
Class classj — Peptides
Fold Fold foldj.35 — Transmembrane helical fragments
Superfamily Superfamily superfamilyj.35.1 — Transmembrane helical fragments
Family Family familyj.35.1.1 — Transmembrane helical fragments

CATH v4.4 (1 domains)

Domain ID domain_id1bhaA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily170

8. Citations (4)

9. Files and Curves (10)