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2kc1

NMR structure of the F0 domain (residues 0-85) of the talin ferm domain

Method: SOLUTION NMR Dmax: 44.4 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

MKIAA1027 protein

Mus musculus

UniProt Q80TM2

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 23–108 Fragment：N-TERMINAL RESIDUES 0-85 No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6.5；298 K；Ionic strength (raw mmCIF value) 50；Pressure AMBIENT NMR sample composition：1 mM [U-100% 13C; U-100% 15N] F0-1, 10 % [U-100% 2H] D2O-2, 2 mM DTT-3, 50 mM sodium chloride-4, 20 mM sodium phosphate-5, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：1 mM [U-100% 15N] F0-6, 10 % [U-100% 2H] D2O-7, 2 mM DTT-8, 50 mM sodium chloride-9, 20 mM sodium phosphate-10, 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 2KC1 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2KGX HADDOCK structure of the talin F3 domain in complex with talin 1655-1822 Deposited 2009-03-23 Different construct Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 334–424（91 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 50；Pressure ambient
NMR sample composition 0.5 mM [U-100% 15N] 1655-1822, 2 mM F3, 50 mM sodium chloride, 20 mM sodium phosphate, 2 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM 1655-1822, 2 mM [U-100% 15N] F3, 50 mM sodium chloride, 20 mM sodium phosphate, 2 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided

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

View Construct and Data Evidence
UniProt name Q80TM2_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 6–91； UniProt 23–108

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 2kc1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2kc1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2kc1
Deposition date deposition_date2008-12-13
Structure title titleNMR structure of the F0 domain (residues 0-85) of the talin ferm domain
Keywords keywordsTALIN, FERM, F0, integrin, CYTOSKELETON, Rap1, STRUCTURAL PROTEIN; STRUCTURAL 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_guinier12.74 Å
Radius of gyration Rg (electron density) rg_electron12.57 Å
Forward intensity I(0) i0572101000.00
Molecular weight molecular_weight206400.0 kDa
Excluded volume excluded_volume259820 ų
Envelope volume envelope_volume25130 ų
Hydration-shell volume shell_volume14029 ų
Envelope diameter envelope_diameter52.7 Å
Shell Rg shell_rg21.13 Å
Envelope Rg envelope_rg15.66 Å
Shape Rg shape_rg12.54 Å
Total Rg total_rg12.86 Å
Total atoms total_atoms28960
Residues n_residues1820
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 dmax44.4 Å
Rg (real space) rg_real12.66 Å
Rg uncertainty (real space) rg_real_error0.33 Å
I(0) (real space) i0_real5.7210e+08
I(0) uncertainty (real space) i0_real_error6.0270e+06
Rg (reciprocal space) rg_reciprocal12.66 Å
I(0) (reciprocal space) i0_reciprocal572100000.0000
Solution quality estimate total_estimate0.7525
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary16.3 Å
Skewness Skewness skewness0.141
Kurtosis Kurtosis kurtosis-0.136
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha303300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.598; Stabil: 0.994; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000
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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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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2kc1A00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
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8. Citations (1)

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9. Files and Curves (10)