1qgb

SOLUTION STRUCTURE OF THE N-TERMINAL F1 MODULE PAIR FROM HUMAN FIBRONECTIN

Method: SOLUTION NMR Dmax: 77.7 Å Quality: GOOD

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

PROTEIN (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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 48–140 Fragment:N-TERMINAL F1 MODULE PAIR No other associated polymer SOLUTION NMR NMR measurement conditions:pH 4;310 K NMR sample composition:2.2 mM [U-15N] 1F1-2F1, 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 1–93; UniProt 48–140

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 1qgb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1qgb
Deposition date deposition_date1999-04-21
Structure title titleSOLUTION STRUCTURE OF THE N-TERMINAL F1 MODULE PAIR FROM HUMAN FIBRONECTIN
Keywords keywordsFIBRONECTIN TYPE 1 MODULE PAIR, CELL ADHESION; CELL ADHESION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier21.58
Radius of gyration Rg (electron density) rg_electron21.41
Forward intensity I(0) i01108920000.00
Molecular weight molecular_weight252300.0 kDa
Excluded volume excluded_volume304580 ų
Envelope volume envelope_volume116590 ų
Hydration-shell volume shell_volume35070 ų
Envelope diameter envelope_diameter92.8
Shell Rg shell_rg35.21
Envelope Rg envelope_rg27.40
Shape Rg shape_rg21.37
Total Rg total_rg22.00
Total atoms total_atoms33768
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 dmax77.7
Rg (real space) rg_real21.64
Rg uncertainty (real space) rg_real_error0.92
I(0) (real space) i0_real1.1090e+09
I(0) uncertainty (real space) i0_real_error1.6420e+07
Rg (reciprocal space) rg_reciprocal21.63
I(0) (reciprocal space) i0_reciprocal1109000000.0000
Solution quality estimate total_estimate0.7634
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary29.7
Skewness Skewness skewness0.247
Kurtosis Kurtosis kurtosis-0.512
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha483000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.747; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.685; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1qgba1
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_idd1qgba2
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_id1qgbA01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1
Domain ID domain_id1qgbA02
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)