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6mf8

TCR alpha transmembrane domain

Method: SOLUTION NMR Dmax: 53.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

T-cell receptor alpha chain C region

Mus musculus

UniProt P01849

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 93–138 Fragment：Transmembrane domain, residues 93-138 No other associated polymer SOLUTION NMR NMR measurement conditions：pH 7；310 K；Ionic strength (raw mmCIF value) 30；Pressure 1 NMR sample composition：2 mM U-15N; U-2H; Ile, Leu, Val selective labeling TCRa, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：1 mM [U-99% 13C; U-99% 15N] TCRa, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：0.5 mM [U-99% 15N] TCRa, 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 6MF8 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
5M01 Crystal structure of murine P14 TCR/ H-2Db complex with PA, modified gp33 peptide from LCMV Deposited 2016-10-03 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric
Chain G 3–88（86 aa）
Not recorded GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；280 K；19% PEG 6000, 0.1M Tris HCl pH 8.0
Resolution 1.95 Å R-free 0.229
5M02 Crystal structure of murine P14 TCR / H-2Db with PF, modified gp33 peptide from LCMV Deposited 2016-10-03 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric
Chain G 3–88（86 aa）
Not recorded GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；19% PEG 6000, 0.1M Tris HCl pH 8.0
Resolution 1.75 Å R-free 0.214
6G9Q Ternary complex of P14 TCR with murine MHC class I H-2 Db in complex with self-antigen derived from dopamine monooxygenase. Deposited 2018-04-11 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric
Chain G 1–88（88 aa） Fragment：UNP residues 22-120,UNP residues 1-88
Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；Tris HCl pH 8.0 PEG 6000
Resolution 1.89 Å R-free 0.248

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TCA_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–46； UniProt 93–138

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 6mf8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6mf8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6mf8
Deposition date deposition_date2018-09-10
Structure title titleTCR alpha transmembrane domain
Keywords keywordsmechanoreceptor, transmembrane, TCR, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier15.16 Å
Radius of gyration Rg (electron density) rg_electron14.69 Å
Forward intensity I(0) i037182500.00
Molecular weight molecular_weight52292.0 kDa
Excluded volume excluded_volume66805 ų
Envelope volume envelope_volume26085 ų
Hydration-shell volume shell_volume13486 ų
Envelope diameter envelope_diameter53.4 Å
Shell Rg shell_rg22.20 Å
Envelope Rg envelope_rg17.08 Å
Shape Rg shape_rg14.71 Å
Total Rg total_rg15.21 Å
Total atoms total_atoms7480
Residues n_residues460
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 dmax53.2 Å
Rg (real space) rg_real15.22 Å
Rg uncertainty (real space) rg_real_error0.52 Å
I(0) (real space) i0_real3.7180e+07
I(0) uncertainty (real space) i0_real_error4.5740e+05
Rg (reciprocal space) rg_reciprocal15.22 Å
I(0) (reciprocal space) i0_reciprocal37180000.0000
Solution quality estimate total_estimate0.8687
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.2 Å
Skewness Skewness skewness0.219
Kurtosis Kurtosis kurtosis-0.638
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha38970.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.853; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.734; Smooth: 0.996
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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)