1tsp

CRYSTAL STRUCTURE OF P22 TAILSPIKE PROTEIN: INTERDIGITATED SUBUNITS IN A THERMOSTABLE TRIMER

Method: X-RAY DIFFRACTION Dmax: 127.5 Å Quality: REASONABLE

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

TAILSPIKE-PROTEIN

OrganismNot specified

UniProt P12528

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 109–667 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 Å

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.

28 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TSPE_BPP22
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–559; UniProt 109–667

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 1tsp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1tsp
Deposition date deposition_date1994-06-16
Structure title titleCRYSTAL STRUCTURE OF P22 TAILSPIKE PROTEIN: INTERDIGITATED SUBUNITS IN A THERMOSTABLE TRIMER
Keywords keywordsLATE PROTEIN; LATE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.51
Radius of gyration Rg (electron density) rg_electron33.53
Forward intensity I(0) i055769100.00
Molecular weight molecular_weight58465.0 kDa
Excluded volume excluded_volume73032 ų
Envelope volume envelope_volume97688 ų
Hydration-shell volume shell_volume27957 ų
Envelope diameter envelope_diameter135.5
Shell Rg shell_rg34.37
Envelope Rg envelope_rg34.83
Shape Rg shape_rg33.52
Total Rg total_rg33.67
Total atoms total_atoms4121
Residues n_residues544
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 dmax127.5
Rg (real space) rg_real33.34
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real5.5770e+07
I(0) uncertainty (real space) i0_real_error1.0070e+06
Rg (reciprocal space) rg_reciprocal32.98
I(0) (reciprocal space) i0_reciprocal55750000.0000
Solution quality estimate total_estimate0.6919
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.6
Skewness Skewness skewness0.797
Kurtosis Kurtosis kurtosis0.128
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7042000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.299; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.203; Smooth: 0.891

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1tspa_
Class classb — All beta proteins
Fold Fold foldb.80 — Single-stranded right-handed beta-helix
Superfamily Superfamily superfamilyb.80.1 — Pectin lyase-like
Family Family familyb.80.1.6 — P22 tailspike protein

CATH v4.4 (1 domains)

Domain ID domain_id1tspA00
Class class2 — Mainly Beta
Architecture architecture160 — 3 Solenoid
Topology topology20 — Pectate Lyase C-like
Homologous superfamily homologous superfamily20

8. Citations (1)

9. Files and Curves (10)