3fa0

Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant Arg96-->His

Method: X-RAY DIFFRACTION Dmax: 60.1 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 1–162 Not recorded HED 2-HYDROXYETHYL DISULFIDE × 1 BME BETA-MERCAPTOETHANOL × 1 PO4 PHOSPHATE ION × 2 CL CHLORIDE ION × 2 K POTASSIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.7;277 K;2 M Na/K phosphate, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.09 Å R-free 0.188

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 846 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 1–162; UniProt 1–162

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 3fa0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3fa0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3fa0
Deposition date deposition_date2008-11-14
Structure title titleEvaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant Arg96-->His
Keywords keywords;Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase, T4 lysozyme, bond angle strain, rotamer strain, temperature sensitive mutant ;; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.68
Radius of gyration Rg (electron density) rg_electron16.51
Forward intensity I(0) i07034620.00
Molecular weight molecular_weight18872.0 kDa
Excluded volume excluded_volume23432 ų
Envelope volume envelope_volume26933 ų
Hydration-shell volume shell_volume14164 ų
Envelope diameter envelope_diameter59.5
Shell Rg shell_rg21.91
Envelope Rg envelope_rg16.73
Shape Rg shape_rg16.47
Total Rg total_rg17.53
Total atoms total_atoms1313
Residues n_residues162
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 dmax60.1
Rg (real space) rg_real17.68
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real7.0350e+06
I(0) uncertainty (real space) i0_real_error8.8710e+04
Rg (reciprocal space) rg_reciprocal17.68
I(0) (reciprocal space) i0_reciprocal7035000.0000
Solution quality estimate total_estimate0.8608
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.8
Skewness Skewness skewness0.379
Kurtosis Kurtosis kurtosis-0.196
Angular range angular_range— – 0.4500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1499000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.774; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.960; Smooth: 0.906

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3fa0a_
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 (1 domains)

Domain ID domain_id3fa0A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily40

8. Citations (2)

9. Files and Curves (10)