1o9a

Solution structure of the complex of 1F12F1 from fibronectin with B3 from FnBB from S. dysgalactiae

Method: SOLUTION NMR Dmax: 74.7 Å Quality: REASONABLE

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

FIBRONECTIN

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 48–140 Fragment:N-TERMINAL F1 MODULE PAIR, RESIDUES 48-140 FIBRONECTIN BINDING PROTEIN × 1 (Q53971) SOLUTION NMR NMR measurement conditions:pH 5;298 K 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 1–93; UniProt 48–140

FIBRONECTIN BINDING PROTEIN

OrganismNot specified

UniProt Q53971

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 1031–1066 Fragment:B3 FIBRONECTIN-BINDING REPEAT, RESIDUES 1031-1066 FIBRONECTIN × 1 (P02751) SOLUTION NMR NMR measurement conditions:pH 5;298 K 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q53971
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–36; UniProt 1031–1066

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 1o9a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1o9a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1o9a
Deposition date deposition_date2002-12-11
Structure title titleSolution structure of the complex of 1F12F1 from fibronectin with B3 from FnBB from S. dysgalactiae
Keywords keywordsCELL ADHESION-COMPLEX, HOST-PATHOGEN PROTEIN COMPLEX, CELL ADHESION, FIBRONECTIN; CELL ADHESION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier20.48
Radius of gyration Rg (electron density) rg_electron20.41
Forward intensity I(0) i0675768000.00
Molecular weight molecular_weight200110.0 kDa
Excluded volume excluded_volume242410 ų
Envelope volume envelope_volume56987 ų
Hydration-shell volume shell_volume20880 ų
Envelope diameter envelope_diameter82.2
Shell Rg shell_rg29.95
Envelope Rg envelope_rg24.19
Shape Rg shape_rg20.40
Total Rg total_rg20.70
Total atoms total_atoms26775
Residues n_residues1755
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 dmax74.7
Rg (real space) rg_real20.74
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real6.7580e+08
I(0) uncertainty (real space) i0_real_error8.0980e+06
Rg (reciprocal space) rg_reciprocal20.70
I(0) (reciprocal space) i0_reciprocal675800000.0000
Solution quality estimate total_estimate0.6497
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary14.9
Skewness Skewness skewness0.505
Kurtosis Kurtosis kurtosis-0.513
Angular range angular_range— – 0.3900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1697000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.414; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.206; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1o9aa1
Class classg — Small proteins
Fold Fold foldg.27 — FnI-like domain
Superfamily Superfamily superfamilyg.27.1 — FnI-like domain
Family Family familyg.27.1.1 — Fibronectin type I module
Domain ID domain_idd1o9aa2
Class classg — Small proteins
Fold Fold foldg.27 — FnI-like domain
Superfamily Superfamily superfamilyg.27.1 — FnI-like domain
Family Family familyg.27.1.1 — Fibronectin type I module

CATH v4.4 (2 domains)

Domain ID domain_id1o9aA01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1
Domain ID domain_id1o9aA02
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1

8. Citations (1)

9. Files and Curves (10)