6lng

Rapid crystallization of streptavidin using charged peptides

Method: X-RAY DIFFRACTION Dmax: 107.5 Å Quality: GOOD

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

Streptavidin

Streptomyces avidinii

UniProt P22629

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 39–163 Chain B; UniProt 39–163 Chain C; UniProt 39–163 Chain D; UniProt 39–163 Not recorded GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:BATCH MODE;298 K;0.2 M ammonium sulfate, 0.1 M MES pH 6.5, 30% w/v polyethylene glycol monomethyl ether 5000 Resolution 1.80 Å R-free 0.219
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 39–163 Chain F; UniProt 39–163 Not recorded GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:BATCH MODE;298 K;0.2 M ammonium sulfate, 0.1 M MES pH 6.5, 30% w/v polyethylene glycol monomethyl ether 5000 Resolution 1.80 Å R-free 0.219

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.

312 other PDB entries and 367 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SAV_STRAV
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–125; UniProt 39–163 Author chain B; PDBConstruct 1–125; UniProt 39–163 Author chain C; PDBConstruct 1–125; UniProt 39–163 Author chain D; PDBConstruct 1–125; UniProt 39–163 Author chain E; PDBConstruct 1–125; UniProt 39–163 Author chain F; PDBConstruct 1–125; UniProt 39–163

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 6lng

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6lng
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6lng
Deposition date deposition_date2019-12-30
Structure title titleRapid crystallization of streptavidin using charged peptides
Keywords keywordsBIOTIN-BINDING PROTEIN, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.12
Radius of gyration Rg (electron density) rg_electron31.83
Forward intensity I(0) i0101731000.00
Molecular weight molecular_weight77154.0 kDa
Excluded volume excluded_volume95291 ų
Envelope volume envelope_volume126570 ų
Hydration-shell volume shell_volume34795 ų
Envelope diameter envelope_diameter114.1
Shell Rg shell_rg36.80
Envelope Rg envelope_rg31.83
Shape Rg shape_rg31.80
Total Rg total_rg32.34
Total atoms total_atoms5466
Residues n_residues732
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 dmax107.5
Rg (real space) rg_real32.33
Rg uncertainty (real space) rg_real_error0.78
I(0) (real space) i0_real1.0170e+08
I(0) uncertainty (real space) i0_real_error1.5660e+06
Rg (reciprocal space) rg_reciprocal32.24
I(0) (reciprocal space) i0_reciprocal101700000.0000
Solution quality estimate total_estimate0.8633
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary35.1
Skewness Skewness skewness0.486
Kurtosis Kurtosis kurtosis-0.301
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14250000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.839; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.929; Smooth: 0.773

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd6lnga_
Class classb — All beta proteins
Fold Fold foldb.61 — Streptavidin-like
Superfamily Superfamily superfamilyb.61.1 — Avidin/streptavidin
Family Family familyb.61.1.1 — Avidin/streptavidin
Domain ID domain_idd6lngb_
Class classb — All beta proteins
Fold Fold foldb.61 — Streptavidin-like
Superfamily Superfamily superfamilyb.61.1 — Avidin/streptavidin
Family Family familyb.61.1.1 — Avidin/streptavidin
Domain ID domain_idd6lngc_
Class classb — All beta proteins
Fold Fold foldb.61 — Streptavidin-like
Superfamily Superfamily superfamilyb.61.1 — Avidin/streptavidin
Family Family familyb.61.1.1 — Avidin/streptavidin
Domain ID domain_idd6lngd_
Class classb — All beta proteins
Fold Fold foldb.61 — Streptavidin-like
Superfamily Superfamily superfamilyb.61.1 — Avidin/streptavidin
Family Family familyb.61.1.1 — Avidin/streptavidin
Domain ID domain_idd6lnge_
Class classb — All beta proteins
Fold Fold foldb.61 — Streptavidin-like
Superfamily Superfamily superfamilyb.61.1 — Avidin/streptavidin
Family Family familyb.61.1.1 — Avidin/streptavidin
Domain ID domain_idd6lngf_
Class classb — All beta proteins
Fold Fold foldb.61 — Streptavidin-like
Superfamily Superfamily superfamilyb.61.1 — Avidin/streptavidin
Family Family familyb.61.1.1 — Avidin/streptavidin

CATH v4.4 (6 domains)

Domain ID domain_id6lngA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id6lngB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id6lngC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id6lngD00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id6lngE00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id6lngF00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like

8. Citations (1)

9. Files and Curves (10)