2rq9

Solution structure of human acidic fibroblast growth factor (aFGF) in the presence of a protein stabilizer NDSB-new

Method: SOLUTION NMR Dmax: 63.9 Å Quality: REASONABLE

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

Heparin-binding growth factor 1

Homo sapiens

UniProt P05230

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 22–155 Fragment:residues in UNP, 22-155 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.6;298 K;Ionic strength (raw mmCIF value) 190;Pressure ambient NMR sample composition:1.0mM [U-99% 13C; U-99% 15N] aFGF-1, 500mM NDSB-new-2, 25mM sodium phosphate-3, 150mM NaCl-4, 1mM dioxane-5, 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.

96 other PDB entries and 217 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FGF1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–135; UniProt 22–155

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 2rq9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2rq9
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2rq9
Deposition date deposition_date2009-03-12
Structure title titleSolution structure of human acidic fibroblast growth factor (aFGF) in the presence of a protein stabilizer NDSB-new
Keywords keywords;beta-Trefoil, Acetylation, Alternative splicing, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, Polymorphism, PROTEIN BINDING ;; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier16.04
Radius of gyration Rg (electron density) rg_electron15.34
Forward intensity I(0) i01575690000.00
Molecular weight molecular_weight327790.0 kDa
Excluded volume excluded_volume406260 ų
Envelope volume envelope_volume49271 ų
Hydration-shell volume shell_volume20469 ų
Envelope diameter envelope_diameter70.0
Shell Rg shell_rg27.37
Envelope Rg envelope_rg22.03
Shape Rg shape_rg15.37
Total Rg total_rg15.45
Total atoms total_atoms45480
Residues n_residues2860
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 dmax63.9
Rg (real space) rg_real16.09
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real1.5760e+09
I(0) uncertainty (real space) i0_real_error1.7940e+07
Rg (reciprocal space) rg_reciprocal16.08
I(0) (reciprocal space) i0_reciprocal1576000000.0000
Solution quality estimate total_estimate0.7491
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.2
Skewness Skewness skewness0.578
Kurtosis Kurtosis kurtosis0.546
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha986900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.327; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.757; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2rq9a1
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.1 — Cytokine
Family Family familyb.42.1.1 — Fibroblast growth factors (FGF)
Domain ID domain_idd2rq9a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2rq9a3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2rq9A00
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50

8. Citations (1)

9. Files and Curves (10)