1kl3

an engineered streptavidin with improved affinity for the strep-tag II peptide : SAm1-StrepII

Method: X-RAY DIFFRACTION Dmax: 67.5 Å Quality: EXCELLENT

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 38–163 Chain B; UniProt 38–163 Chain C; UniProt 38–163 Chain D; UniProt 38–163 Mutation:E44V,S45T,V47R strep-tag II peptide × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.9;293 K;100 mM Na2HPO4, 1.3-M (NH4)2SO4, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.70 Å R-free 0.217

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 368 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 2–127; UniProt 38–163 Author chain B; PDBConstruct 2–127; UniProt 38–163 Author chain C; PDBConstruct 2–127; UniProt 38–163 Author chain D; PDBConstruct 2–127; UniProt 38–163

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 1kl3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1kl3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1kl3
Deposition date deposition_date2001-12-11
Structure title titlean engineered streptavidin with improved affinity for the strep-tag II peptide : SAm1-StrepII
Keywords keywordsBIOTIN, PROTEIN ENGINEERING, STREP-TAG, STREPTAVIDIN, 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_guinier23.11
Radius of gyration Rg (electron density) rg_electron22.00
Forward intensity I(0) i051160100.00
Molecular weight molecular_weight53807.0 kDa
Excluded volume excluded_volume66490 ų
Envelope volume envelope_volume78419 ų
Hydration-shell volume shell_volume28482 ų
Envelope diameter envelope_diameter69.2
Shell Rg shell_rg29.61
Envelope Rg envelope_rg22.19
Shape Rg shape_rg21.96
Total Rg total_rg22.98
Total atoms total_atoms3816
Residues n_residues504
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 dmax67.5
Rg (real space) rg_real22.93
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real5.1160e+07
I(0) uncertainty (real space) i0_real_error6.0810e+05
Rg (reciprocal space) rg_reciprocal22.98
I(0) (reciprocal space) i0_reciprocal51160000.0000
Solution quality estimate total_estimate0.9118
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.1
Skewness Skewness skewness0.069
Kurtosis Kurtosis kurtosis-0.553
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13220000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.964; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.980

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1kl3a_
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_idd1kl3b_
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_idd1kl3c_
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_idd1kl3d_
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 (4 domains)

Domain ID domain_id1kl3A00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id1kl3B00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id1kl3C00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id1kl3D00
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)