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7qjf

Llp mutant C1G, lytic conversion lipoprotein of phage T5

Method: SOLUTION NMR Dmax: 39.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Lytic conversion lipoprotein

Escherichia phage T5

UniProt Q38162

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 17–77 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6.5；303 K；Ionic strength (raw mmCIF value) 75；Pressure 1 NMR sample composition：25 mM no Tris, 75 mM no NaCl, 1.024 mM 13C 15N Sol-Llp, 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.

Other PDB Difference from Current Entry 7QJF Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8A60 Crystal structure of FhuA in complex with the superinfection exclusion lipoprotein Llp Deposited 2022-06-16 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–77（77 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；293 K；12-16% PEG 4000 0.4 M sodium isothiocyanate 0.1 M sodium acetate
Resolution 3.37 Å R-free 0.307

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LLP_BPT5
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–62； UniProt 17–77

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 7qjf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7qjf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7qjf
Deposition date deposition_date2021-12-16
Structure title titleLlp mutant C1G, lytic conversion lipoprotein of phage T5
Keywords keywordsPhage protein, Periplasmic protein, Soluble of acylated WT protein STRUCTURE FROM UNIO, UNIO VERSION 2.9.5, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier11.38 Å
Radius of gyration Rg (electron density) rg_electron11.27 Å
Forward intensity I(0) i0262888000.00
Molecular weight molecular_weight140560.0 kDa
Excluded volume excluded_volume176520 ų
Envelope volume envelope_volume19967 ų
Hydration-shell volume shell_volume12324 ų
Envelope diameter envelope_diameter43.4 Å
Shell Rg shell_rg19.68 Å
Envelope Rg envelope_rg14.01 Å
Shape Rg shape_rg11.25 Å
Total Rg total_rg11.58 Å
Total atoms total_atoms19120
Residues n_residues1240
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax39.1 Å
Rg (real space) rg_real11.33 Å
Rg uncertainty (real space) rg_real_error0.26 Å
I(0) (real space) i0_real2.6290e+08
I(0) uncertainty (real space) i0_real_error2.5740e+06
Rg (reciprocal space) rg_reciprocal11.33 Å
I(0) (reciprocal space) i0_reciprocal262900000.0000
Solution quality estimate total_estimate0.7969
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.3 Å
Skewness Skewness skewness0.182
Kurtosis Kurtosis kurtosis-0.284
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha85750.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.789; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)