3t13

Crystal structure of Staphylococcal nuclease variant Delta+PHS A69G at cryogenic temperature

Method: X-RAY DIFFRACTION Dmax: 70.7 Å Quality: GOOD

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

Thermonuclease

Staphylococcus aureus

UniProt P00644

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 83–231 Fragment:Nuclease A (UNP residues 83-231) Mutation:G50F/V51N/A69G/P117G/H124L/S128A/Del44-49 PO4 PHOSPHATE ION × 2 CA CALCIUM ION × 1 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;277 K;41% MPD, 25 mM potassium phosphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.80 Å R-free 0.199
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 83–231 Fragment:Nuclease A (UNP residues 83-231) Mutation:G50F/V51N/A69G/P117G/H124L/S128A/Del44-49 PO4 PHOSPHATE ION × 1 CA CALCIUM ION × 1 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;277 K;41% MPD, 25 mM potassium phosphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.80 Å R-free 0.199

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.

298 other PDB entries and 309 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NUC_STAAU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–143; UniProt 83–231 Author chain B; PDBConstruct 1–143; UniProt 83–231

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 3t13

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3t13
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3t13
Deposition date deposition_date2011-07-21
Structure title titleCrystal structure of Staphylococcal nuclease variant Delta+PHS A69G at cryogenic temperature
Keywords keywordsStaphylococcal nuclease, hyperstable variant, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.75
Radius of gyration Rg (electron density) rg_electron21.11
Forward intensity I(0) i015289300.00
Molecular weight molecular_weight30283.0 kDa
Excluded volume excluded_volume38322 ų
Envelope volume envelope_volume45265 ų
Hydration-shell volume shell_volume18583 ų
Envelope diameter envelope_diameter71.4
Shell Rg shell_rg26.74
Envelope Rg envelope_rg21.14
Shape Rg shape_rg21.11
Total Rg total_rg21.90
Total atoms total_atoms2122
Residues n_residues259
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 dmax70.7
Rg (real space) rg_real21.78
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real1.5290e+07
I(0) uncertainty (real space) i0_real_error2.0440e+05
Rg (reciprocal space) rg_reciprocal21.78
I(0) (reciprocal space) i0_reciprocal15290000.0000
Solution quality estimate total_estimate0.8861
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.1
Skewness Skewness skewness0.323
Kurtosis Kurtosis kurtosis-0.589
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3857000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.879; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.924; Smooth: 0.953

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3t13a_
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.1 — Staphylococcal nuclease
Family Family familyb.40.1.1 — Staphylococcal nuclease
Domain ID domain_idd3t13b_
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.1 — Staphylococcal nuclease
Family Family familyb.40.1.1 — Staphylococcal nuclease

CATH v4.4 (2 domains)

Domain ID domain_id3t13A00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily90
Domain ID domain_id3t13B00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily90

8. Citations (1)

9. Files and Curves (10)