262l

STRUCTURAL CHARACTERISATION OF AN ENGINEERED TANDEM REPEAT CONTRASTS THE IMPORTANCE OF CONTEXT AND SEQUENCE IN PROTEIN FOLDING

Method: X-RAY DIFFRACTION Dmax: 94.2 Å Quality: GOOD

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

LYSOZYME

Enterobacteria phage T4

UniProt P00720

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 1–50 Chain A; UniProt 51–162 Mutation:L39I No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;CRYSTALS WERE GROWN FROM 20% POLYETHYLENE GLYCOL 6000, 20% ISOPROPANOL, 50MM TRIS-HCL PH 7.5 Resolution 2.50 Å
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–50 Chain B; UniProt 51–162 Mutation:L39I No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;CRYSTALS WERE GROWN FROM 20% POLYETHYLENE GLYCOL 6000, 20% ISOPROPANOL, 50MM TRIS-HCL PH 7.5 Resolution 2.50 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.

721 other PDB entries and 845 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LYS_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–50; UniProt 1–50 Author chain A; PDBConstruct 62–173; UniProt 51–162 Author chain B; PDBConstruct 1–50; UniProt 1–50 Author chain B; PDBConstruct 62–173; UniProt 51–162

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 262l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 262l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id262l
Deposition date deposition_date1999-05-11
Structure title titleSTRUCTURAL CHARACTERISATION OF AN ENGINEERED TANDEM REPEAT CONTRASTS THE IMPORTANCE OF CONTEXT AND SEQUENCE IN PROTEIN FOLDING
Keywords keywordsHYDROLASE (O-GLYCOSYL), T4 LYSOZYME, ENGINEERED TANDEM REPEAT, PROTEIN ENGINEERING, PROTEIN DESIGN, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.64
Radius of gyration Rg (electron density) rg_electron30.98
Forward intensity I(0) i024711800.00
Molecular weight molecular_weight39013.0 kDa
Excluded volume excluded_volume48943 ų
Envelope volume envelope_volume69090 ų
Hydration-shell volume shell_volume18653 ų
Envelope diameter envelope_diameter91.1
Shell Rg shell_rg38.29
Envelope Rg envelope_rg29.59
Shape Rg shape_rg30.96
Total Rg total_rg31.77
Total atoms total_atoms2744
Residues n_residues346
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 dmax94.2
Rg (real space) rg_real31.74
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real2.4710e+07
I(0) uncertainty (real space) i0_real_error3.7910e+05
Rg (reciprocal space) rg_reciprocal31.71
I(0) (reciprocal space) i0_reciprocal24710000.0000
Solution quality estimate total_estimate0.7889
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary20.7
Skewness Skewness skewness0.093
Kurtosis Kurtosis kurtosis-1.169
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1946000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.593; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.534; Smooth: 0.939

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd262la_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.2 — Lysozyme-like
Superfamily Superfamily superfamilyd.2.1 — Lysozyme-like
Family Family familyd.2.1.3 — Phage lysozyme
Domain ID domain_idd262lb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.2 — Lysozyme-like
Superfamily Superfamily superfamilyd.2.1 — Lysozyme-like
Family Family familyd.2.1.3 — Phage lysozyme

CATH v4.4 (2 domains)

Domain ID domain_id262lA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily40
Domain ID domain_id262lB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily40

8. Citations (3)

9. Files and Curves (10)