4yxc

Complex of FliM(SPOA)::FliN fusion protein and FliH(APAR)::T4lysozyme fusion protein

Method: X-RAY DIFFRACTION Dmax: 84.9 Å Quality: GOOD

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

Flagellar assembly protein H,Endolysin

Enterobacteria phage T4

UniProt L5WUL9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–18 Fragment:UNP Residues 1-18 Mutation:D20N, C54T, C97A Flagellar motor switch protein FliM,Flagellar motor switch protein FliN × 1 (P26418,P26419) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;FliM(245-334)::FliN(5-137) + FliH(1-18)::T4 lysozyme was concentrated to 17mg/mL and crystallized with 11% PEG400, 100mM sodium potassium phosphate pH=6.5. Crystals were cryoprotected with 40% PEG400, 200mM sodium potassium phosphate pH=6.5. Resolution 2.30 Å R-free 0.262

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name L5WUL9_SALEN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–22; UniProt 1–18

Flagellar assembly protein H,Endolysin

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 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–161 Fragment:UNP Residues 1-18 Mutation:D20N, C54T, C97A Flagellar motor switch protein FliM,Flagellar motor switch protein FliN × 1 (P26418,P26419) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;FliM(245-334)::FliN(5-137) + FliH(1-18)::T4 lysozyme was concentrated to 17mg/mL and crystallized with 11% PEG400, 100mM sodium potassium phosphate pH=6.5. Crystals were cryoprotected with 40% PEG400, 200mM sodium potassium phosphate pH=6.5. Resolution 2.30 Å R-free 0.262

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 ENLYS_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 23–182; UniProt 2–161

Flagellar motor switch protein FliM,Flagellar motor switch protein FliN

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

UniProt P26418

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 245–334 Fragment:UNP Residues 245-334,UNP Residues 5-137 Flagellar assembly protein H,Endolysin × 1 (L5WUL9,P00720) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;FliM(245-334)::FliN(5-137) + FliH(1-18)::T4 lysozyme was concentrated to 17mg/mL and crystallized with 11% PEG400, 100mM sodium potassium phosphate pH=6.5. Crystals were cryoprotected with 40% PEG400, 200mM sodium potassium phosphate pH=6.5. Resolution 2.30 Å R-free 0.262

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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLIM_SALTY
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–94; UniProt 245–334

Flagellar motor switch protein FliM,Flagellar motor switch protein FliN

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

UniProt P26419

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 5–137 Fragment:UNP Residues 245-334,UNP Residues 5-137 Flagellar assembly protein H,Endolysin × 1 (L5WUL9,P00720) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;FliM(245-334)::FliN(5-137) + FliH(1-18)::T4 lysozyme was concentrated to 17mg/mL and crystallized with 11% PEG400, 100mM sodium potassium phosphate pH=6.5. Crystals were cryoprotected with 40% PEG400, 200mM sodium potassium phosphate pH=6.5. Resolution 2.30 Å R-free 0.262

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.

16 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLIN_SALTY
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 95–227; UniProt 5–137

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 4yxc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4yxc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4yxc
Deposition date deposition_date2015-03-23
Structure title titleComplex of FliM(SPOA)::FliN fusion protein and FliH(APAR)::T4lysozyme fusion protein
Keywords keywordsType III Secretion System, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.33
Radius of gyration Rg (electron density) rg_electron24.45
Forward intensity I(0) i024069400.00
Molecular weight molecular_weight37857.0 kDa
Excluded volume excluded_volume47736 ų
Envelope volume envelope_volume62061 ų
Hydration-shell volume shell_volume22159 ų
Envelope diameter envelope_diameter88.2
Shell Rg shell_rg30.10
Envelope Rg envelope_rg24.89
Shape Rg shape_rg24.42
Total Rg total_rg25.32
Total atoms total_atoms2668
Residues n_residues349
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 dmax84.9
Rg (real space) rg_real25.36
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real2.4070e+07
I(0) uncertainty (real space) i0_real_error3.3550e+05
Rg (reciprocal space) rg_reciprocal25.35
I(0) (reciprocal space) i0_reciprocal24070000.0000
Solution quality estimate total_estimate0.8850
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.6
Skewness Skewness skewness0.322
Kurtosis Kurtosis kurtosis-0.491
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5018000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.885; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.883; Smooth: 0.963

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4yxcA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily40

8. Citations (1)

9. Files and Curves (10)