1oww

Solution structure of the first type III module of human fibronectin determined by 1H, 15N NMR spectroscopy

Method: SOLUTION NMR Dmax: 45.5 Å Quality: GOOD

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

Fibronectin first type III module

Homo sapiens

UniProt P02751

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 608–701 Fragment:Residues 608-701 of SWS P02751 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6;313 K;Ionic strength (raw mmCIF value) unbuffered;Pressure ambient NMR sample composition:1-2 mM [U-15N] protein, 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.

54 other PDB entries and 103 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FINC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–98; UniProt 608–701

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 1oww

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1oww
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1oww
Deposition date deposition_date2003-03-31
Structure title titleSolution structure of the first type III module of human fibronectin determined by 1H, 15N NMR spectroscopy
Keywords keywordsFibronectin type III module, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.71
Radius of gyration Rg (electron density) rg_electron13.38
Forward intensity I(0) i0862748000.00
Molecular weight molecular_weight253510.0 kDa
Excluded volume excluded_volume318520 ų
Envelope volume envelope_volume23571 ų
Hydration-shell volume shell_volume13349 ų
Envelope diameter envelope_diameter51.8
Shell Rg shell_rg20.69
Envelope Rg envelope_rg15.43
Shape Rg shape_rg13.35
Total Rg total_rg13.60
Total atoms total_atoms35688
Residues n_residues2232
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 dmax45.5
Rg (real space) rg_real13.69
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real8.6270e+08
I(0) uncertainty (real space) i0_real_error9.0540e+06
Rg (reciprocal space) rg_reciprocal13.69
I(0) (reciprocal space) i0_reciprocal862700000.0000
Solution quality estimate total_estimate0.8871
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.6
Skewness Skewness skewness0.271
Kurtosis Kurtosis kurtosis-0.397
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha208100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.854; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1owwa_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.2 — Fibronectin type III
Family Family familyb.1.2.1 — Fibronectin type III

CATH v4.4 (1 domains)

Domain ID domain_id1owwA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (2)

9. Files and Curves (10)