1nyf

NMR STUDY OF THE SH3 DOMAIN FROM FYN PROTO-ONCOGENE TYROSINE KINASE, MINIMIZED AVERAGE (PROBMAP) STRUCTURE

Method: SOLUTION NMR Dmax: 38.2 Å Quality: GOOD

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

FYN

Homo sapiens

UniProt P06241

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 81–147 Fragment:SH3 DOMAIN, RESIDUES 82 - 148 Mutation:INS(GS-T82) No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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.

50 other PDB entries and 68 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FYN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–67; UniProt 81–147

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 1nyf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1nyf
Deposition date deposition_date1996-04-22
Structure title titleNMR STUDY OF THE SH3 DOMAIN FROM FYN PROTO-ONCOGENE TYROSINE KINASE, MINIMIZED AVERAGE (PROBMAP) STRUCTURE
Keywords keywordsSH3 DOMAIN, POLYPROLINE-BINDING, PHOSPHOTRANSFERASE; PHOSPHOTRANSFERASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier12.02
Radius of gyration Rg (electron density) rg_electron10.40
Forward intensity I(0) i01017920.00
Molecular weight molecular_weight6595.0 kDa
Excluded volume excluded_volume8242 ų
Envelope volume envelope_volume9228 ų
Hydration-shell volume shell_volume7730 ų
Envelope diameter envelope_diameter35.9
Shell Rg shell_rg15.76
Envelope Rg envelope_rg10.84
Shape Rg shape_rg10.35
Total Rg total_rg12.08
Total atoms total_atoms901
Residues n_residues58
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 dmax38.2
Rg (real space) rg_real11.93
Rg uncertainty (real space) rg_real_error0.21
I(0) (real space) i0_real1.0180e+06
I(0) uncertainty (real space) i0_real_error9.9520e+03
Rg (reciprocal space) rg_reciprocal11.94
I(0) (reciprocal space) i0_reciprocal1018000.0000
Solution quality estimate total_estimate0.8823
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.5
Skewness Skewness skewness0.117
Kurtosis Kurtosis kurtosis-0.265
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha302900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.835; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.969

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_idd1nyfa_
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.2 — SH3-domain
Family Family familyb.34.2.1 — SH3-domain

CATH v4.4 (1 domains)

Domain ID domain_id1nyfA00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily40 — SH3 Domains

8. Citations (2)

9. Files and Curves (10)