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2mwn

Talin-F3 / RIAM N-terminal Peptide complex

Method: SOLUTION NMR Dmax: 43.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Amyloid beta A4 precursor protein-binding family B member 1-interacting protein

OrganismNot specified

UniProt Q7Z5R6

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 7–30 Not recorded Talin-1 × 1 （Q9Y490） SOLUTION NMR NMR measurement conditions：pH 6.8；298 K；Ionic strength (raw mmCIF value) 50；Pressure ambient NMR sample composition：0.5 mM [U-15N] Talin-F3, 50 mM sodium phosphate, 50 mM sodium chloride, 2 mM sodium azide, 1 mM DSS, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition：1.5 mM RIAM-N peptide, 0.5 mM [U-15N; U-2H] Talin-F3, 50 mM sodium phosphate, 50 mM sodium chloride, 2 mM sodium azide, 1 mM DSS, 95% H2O/5% D2O | 95% H2O/5% 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 2MWN Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3ZDL Vinculin head (1-258) in complex with a RIAM fragment Deposited 2012-11-28 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–32（32 aa） Fragment：N TERMINAL DOMAIN, RESIUDES 1-32
Mutation：YES No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions 1.2M AMMONIUM SULPHATE, 0.05M TRI-SODIUM CITRATE, 3% ISOPROPANOL
Resolution 2.30 Å R-free 0.230

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

View Construct and Data Evidence
UniProt name AB1IP_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–24； UniProt 7–30

Talin-1

Homo sapiens

UniProt Q9Y490

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain B； UniProt 308–400 Not recorded Amyloid beta A4 precursor protein-binding family B member 1-interacting protein × 1 （Q7Z5R6） SOLUTION NMR NMR measurement conditions：pH 6.8；298 K；Ionic strength (raw mmCIF value) 50；Pressure ambient NMR sample composition：0.5 mM [U-15N] Talin-F3, 50 mM sodium phosphate, 50 mM sodium chloride, 2 mM sodium azide, 1 mM DSS, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition：1.5 mM RIAM-N peptide, 0.5 mM [U-15N; U-2H] Talin-F3, 50 mM sodium phosphate, 50 mM sodium chloride, 2 mM sodium azide, 1 mM DSS, 95% H2O/5% D2O | 95% H2O/5% 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 2MWN Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1SYQ Human vinculin head domain VH1, residues 1-258, in complex with human talin's vinculin binding site 1, residues 607-636 Deposited 2004-04-01 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 607–631（25 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.42 Å R-free 0.236
1SYQ Human vinculin head domain VH1, residues 1-258, in complex with human talin's vinculin binding site 1, residues 607-636 Deposited 2004-04-01 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain B 607–631（25 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.42 Å R-free 0.236
1SYQ Human vinculin head domain VH1, residues 1-258, in complex with human talin's vinculin binding site 1, residues 607-636 Deposited 2004-04-01 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain B 607–631（25 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.42 Å R-free 0.236
4DJ9 Human vinculin head domain Vh1 (residues 1-258) in complex with the talin vinculin binding site 50 (VBS50, residues 2078-2099) Deposited 2012-02-01 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 2075–2103（29 aa） Fragment：unp residues 2075-2103
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；The human vinculin Vh1 domain (residues 1 - 258) was generated as described.9 Crystallization screens of Vh1 protein and VBS50 mixed in 1:5 molar ratio were performed at two temperatures. Co-crystals were obtained from Hampton crystal screen I with a reservoir of 0.1 M Hepes pH 7.5, 10% w/v polyethylene glycol 6,000, and 5% 2-Methyl-2,4-pentanediol. Crystals were transferred directly from the initial 96-well screening plate into Paratone-N oil and flash-frozen in liquid nitrogen. , VAPOR DIFFUSION
Resolution 2.25 Å R-free 0.247
6R9T Cryo-EM structure of autoinhibited human talin-1 Deposited 2019-04-04 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–2541（2541 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；Blotted 4 seconds before plunging, blot force 4
Resolution 6.20 Å

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TLN1_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B； PDBConstruct 1–93； UniProt 308–400

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 2mwn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2mwn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2mwn
Deposition date deposition_date2014-11-13
Structure title titleTalin-F3 / RIAM N-terminal Peptide complex
Keywords keywordsRIAM, Talin, Integrin, STRUCTURAL PROTEIN-SIGNALING PROTEIN complex; STRUCTURAL PROTEIN/SIGNALING 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_guinier13.82 Å
Radius of gyration Rg (electron density) rg_electron13.67 Å
Forward intensity I(0) i0895354000.00
Molecular weight molecular_weight266450.0 kDa
Excluded volume excluded_volume338330 ų
Envelope volume envelope_volume26675 ų
Hydration-shell volume shell_volume14556 ų
Envelope diameter envelope_diameter48.7 Å
Shell Rg shell_rg21.35 Å
Envelope Rg envelope_rg15.76 Å
Shape Rg shape_rg13.64 Å
Total Rg total_rg13.88 Å
Total atoms total_atoms37700
Residues n_residues2340
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 dmax43.1 Å
Rg (real space) rg_real13.73 Å
Rg uncertainty (real space) rg_real_error0.26 Å
I(0) (real space) i0_real8.9540e+08
I(0) uncertainty (real space) i0_real_error1.0050e+07
Rg (reciprocal space) rg_reciprocal13.73 Å
I(0) (reciprocal space) i0_reciprocal895400000.0000
Solution quality estimate total_estimate0.8025
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary19.1 Å
Skewness Skewness skewness0.090
Kurtosis Kurtosis kurtosis-0.250
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha246500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.816; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2mwnB00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
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8. Citations (1)

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9. Files and Curves (10)