7z21

BAF A12T bound to the lamin A/C Ig-fold domain

Method: X-RAY DIFFRACTION Dmax: 93.3 Å Quality: REASONABLE

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

Barrier-to-autointegration factor, N-terminally processed

Homo sapiens

UniProt O75531

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 2–89 Chain C; UniProt 2–89 Mutation:A12T Lamin-A/C × 1 (P02545) CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;293 K;3 M ammonium sulfate 0.1 M bicine pH 9 Resolution 1.63 Å R-free 0.300
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 2–89 Chain D; UniProt 2–89 Mutation:A12T Lamin-A/C × 1 (P02545) CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;293 K;3 M ammonium sulfate 0.1 M bicine pH 9 Resolution 1.63 Å R-free 0.300

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.

27 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BAF_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–89; UniProt 2–89 Author chain B; PDBConstruct 2–89; UniProt 2–89 Author chain C; PDBConstruct 2–89; UniProt 2–89 Author chain D; PDBConstruct 2–89; UniProt 2–89

Lamin-A/C

Homo sapiens

UniProt P02545

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 F; UniProt 411–566 Non-standard monomer:Yes (specific site not provided by mmCIF) Barrier-to-autointegration factor, N-terminally processed × 2 (O75531) CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;293 K;3 M ammonium sulfate 0.1 M bicine pH 9 Resolution 1.63 Å R-free 0.300
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 411–566 Non-standard monomer:Yes (specific site not provided by mmCIF) Barrier-to-autointegration factor, N-terminally processed × 2 (O75531) CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;293 K;3 M ammonium sulfate 0.1 M bicine pH 9 Resolution 1.63 Å R-free 0.300

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.

24 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LMNA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–156; UniProt 411–566 Author chain F; PDBConstruct 1–156; UniProt 411–566

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 7z21

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7z21
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7z21
Deposition date deposition_date2022-02-25
Structure title titleBAF A12T bound to the lamin A/C Ig-fold domain
Keywords keywordsComplex, lamin A/C, BAF, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.85
Radius of gyration Rg (electron density) rg_electron27.13
Forward intensity I(0) i070709800.00
Molecular weight molecular_weight65262.0 kDa
Excluded volume excluded_volume81454 ų
Envelope volume envelope_volume98814 ų
Hydration-shell volume shell_volume30849 ų
Envelope diameter envelope_diameter95.2
Shell Rg shell_rg33.68
Envelope Rg envelope_rg27.21
Shape Rg shape_rg27.10
Total Rg total_rg27.87
Total atoms total_atoms9142
Residues n_residues583
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 dmax93.3
Rg (real space) rg_real27.87
Rg uncertainty (real space) rg_real_error0.78
I(0) (real space) i0_real7.0710e+07
I(0) uncertainty (real space) i0_real_error1.0750e+06
Rg (reciprocal space) rg_reciprocal27.87
I(0) (reciprocal space) i0_reciprocal70710000.0000
Solution quality estimate total_estimate0.6802
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.4
Skewness Skewness skewness0.405
Kurtosis Kurtosis kurtosis-0.144
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14690000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.840; Stabil: 0.999; Sysdev: 0.177; Positv: 1.000; Valcen: 0.987; Smooth: 0.804

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)