2f52

Solution structure of cold shock protein CspB from Bacillus subtilis in complex with heptathymidine

Method: SOLUTION NMR Dmax: 37.0 Å Quality: GOOD

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

Cold shock protein cspB

Bacillus subtilis

UniProt P32081

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 1–67 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;288 K;Ionic strength (raw mmCIF value) 53mM buffer salt;Pressure ambient NMR sample composition:0.8mM CspB U-15N, 50mM Na-cacodylate, 3mM MgCl2, 1.2mM heptathymidine, 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:0.8mM CspB U-15N, 13C, 50mM Na-cacodylate, 3mM MgCl2, 1.2mM heptathymidine, 90% H2O, 10% D2O | 90% H2O/10% 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.

9 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CSPB_BACSU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–67; UniProt 1–67

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 2f52

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2f52
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2f52
Deposition date deposition_date2005-11-25
Structure title titleSolution structure of cold shock protein CspB from Bacillus subtilis in complex with heptathymidine
Keywords keywordsbeta barrel, OB-fold, DNA BINDING PROTEIN-TRANSCRIPTION COMPLEX; DNA BINDING PROTEIN/TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.30
Radius of gyration Rg (electron density) rg_electron10.87
Forward intensity I(0) i0248248000.00
Molecular weight molecular_weight132460.0 kDa
Excluded volume excluded_volume165050 ų
Envelope volume envelope_volume14255 ų
Hydration-shell volume shell_volume10004 ų
Envelope diameter envelope_diameter40.6
Shell Rg shell_rg17.86
Envelope Rg envelope_rg12.63
Shape Rg shape_rg10.84
Total Rg total_rg11.16
Total atoms total_atoms18252
Residues n_residues1206
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 dmax37.0
Rg (real space) rg_real11.23
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real2.4820e+08
I(0) uncertainty (real space) i0_real_error2.4940e+06
Rg (reciprocal space) rg_reciprocal11.24
I(0) (reciprocal space) i0_reciprocal248200000.0000
Solution quality estimate total_estimate0.7911
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary15.0
Skewness Skewness skewness0.099
Kurtosis Kurtosis kurtosis-0.246
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha114300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.764; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; 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_idd2f52a_
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.4 — Nucleic acid-binding proteins
Family Family familyb.40.4.5 — Cold shock DNA-binding domain-like

CATH v4.4 (1 domains)

Domain ID domain_id2f52A00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily140 — Nucleic acid-binding proteins

8. Citations (1)

9. Files and Curves (10)