1q38

Anastellin

Method: SOLUTION NMR Dmax: 44.1 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 631–705 Fragment:Type 3 (FN3) domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 150;Pressure ambient NMR sample composition:1.5 mM anastellin U-15N, 10 mM Na2HPO4, 1.8 mM KH2PO4, 140 mM NaCl, 2.7 mM KCl, 2 mM CHAPS | 90% H2O/10% D2O NMR sample composition:1.5 mM anastellin U-15N,13C, 10 mM Na2HPO4, 1.8 mM KH2PO4, 140 mM NaCl, 2.7 mM KCl, 2 mM CHAPS | 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 5–79; UniProt 631–705

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 1q38

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1q38
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1q38
Deposition date deposition_date2003-07-28
Structure title titleAnastellin
Keywords keywords;amyloid fibril, anastellin, extracellular matrix, fibronectin type 3 (FN3) domain, dynamic fluctuations, conformational exchange, CHAPS, CELL ADHESION ;; CELL ADHESION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier17.17
Radius of gyration Rg (electron density) rg_electron16.24
Forward intensity I(0) i01919080000.00
Molecular weight molecular_weight355690.0 kDa
Excluded volume excluded_volume439460 ų
Envelope volume envelope_volume95255 ų
Hydration-shell volume shell_volume31718 ų
Envelope diameter envelope_diameter90.6
Shell Rg shell_rg32.46
Envelope Rg envelope_rg24.99
Shape Rg shape_rg16.21
Total Rg total_rg16.76
Total atoms total_atoms49665
Residues n_residues3115
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 dmax44.1
Rg (real space) rg_real16.10
Rg uncertainty (real space) rg_real_error0.06
I(0) (real space) i0_real1.8220e+09
I(0) uncertainty (real space) i0_real_error1.4880e+07
Rg (reciprocal space) rg_reciprocal17.28
I(0) (reciprocal space) i0_reciprocal1919000000.0000
Solution quality estimate total_estimate0.6875
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary18.6
Skewness Skewness skewness0.168
Kurtosis Kurtosis kurtosis-0.589
Angular range angular_range— – 0.4650 −1
Current regularization parameter α current_alpha3.9100
Highest regularization parameter α highest_alpha270600.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.009; Oscil: 0.998; Stabil: 0.982; Sysdev: 0.000; Positv: 1.000; Valcen: 0.997; 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 (3 domains)

Domain ID domain_idd1q38a1
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
Domain ID domain_idd1q38a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1q38a3
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_id1q38A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (4)

9. Files and Curves (10)