6wl2

preTCRbeta-pMHC complex crystal structure

Method: X-RAY DIFFRACTION Dmax: 126.6 Å Quality: GOOD

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

H-2 class I histocompatibility antigen, K-B alpha chain

Mus musculus

UniProt P01901

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 22–206 Mutation:G56C, C121Q ARG-GLY-TYR-VAL-TYR-GLN-GLY-LEU × 1 N15 preTCR beta × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.100 M Bicine pH 9.0, 15% (w/v)PEG 20000 Resolution 3.30 Å R-free 0.270
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 22–206 Mutation:G56C, C121Q ARG-GLY-TYR-VAL-TYR-GLN-GLY-LEU × 1 N15 preTCR beta × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.100 M Bicine pH 9.0, 15% (w/v)PEG 20000 Resolution 3.30 Å R-free 0.270
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 22–206 Mutation:G56C, C121Q ARG-GLY-TYR-VAL-TYR-GLN-GLY-LEU × 1 N15 preTCR beta × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.100 M Bicine pH 9.0, 15% (w/v)PEG 20000 Resolution 3.30 Å R-free 0.270

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.

83 other PDB entries and 138 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HA1B_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–185; UniProt 22–206 Author chain D; PDBConstruct 1–185; UniProt 22–206 Author chain G; PDBConstruct 1–185; UniProt 22–206

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 6wl2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6wl2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6wl2
Deposition date deposition_date2020-04-18
Structure title titlepreTCRbeta-pMHC complex crystal structure
Keywords keywordspreTCR, H-2Kb, T cell development, beta selection, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.33
Radius of gyration Rg (electron density) rg_electron37.52
Forward intensity I(0) i0346652000.00
Molecular weight molecular_weight145580.0 kDa
Excluded volume excluded_volume179900 ų
Envelope volume envelope_volume253580 ų
Hydration-shell volume shell_volume56010 ų
Envelope diameter envelope_diameter135.7
Shell Rg shell_rg44.19
Envelope Rg envelope_rg36.51
Shape Rg shape_rg37.52
Total Rg total_rg37.96
Total atoms total_atoms10279
Residues n_residues1265
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 dmax126.6
Rg (real space) rg_real38.14
Rg uncertainty (real space) rg_real_error0.98
I(0) (real space) i0_real3.4670e+08
I(0) uncertainty (real space) i0_real_error5.9730e+06
Rg (reciprocal space) rg_reciprocal38.26
I(0) (reciprocal space) i0_reciprocal346700000.0000
Solution quality estimate total_estimate0.8779
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary52.5
Skewness Skewness skewness0.160
Kurtosis Kurtosis kurtosis-0.333
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha33830000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.825; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.940

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)