1ssl

Solution structure of the PSI domain from the Met receptor

Method: SOLUTION NMR Dmax: 34.0 Å Quality: GOOD

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

Hepatocyte growth factor receptor

Homo sapiens

UniProt P08581

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 519–562 Fragment:PSI domain (residues 519-562) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6;283 K;Ionic strength (raw mmCIF value) 0.15M NaCl;Pressure ambient NMR sample composition:1mM PSI, 50mM phosphate buffer, 0.15M NaC, 90%H2O, 10%D2O | 90% H2O/10% D2O NMR sample composition:1mM PSI, 50mM phosphate buffer, 0.15M NaCl, 100%D2O | 100% 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.

128 other PDB entries and 166 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MET_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–48; UniProt 519–562

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 1ssl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ssl
Deposition date deposition_date2004-03-24
Structure title titleSolution structure of the PSI domain from the Met receptor
Keywords keywordscysteine knot, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier9.53
Radius of gyration Rg (electron density) rg_electron9.83
Forward intensity I(0) i0200942000.00
Molecular weight molecular_weight106200.0 kDa
Excluded volume excluded_volume127320 ų
Envelope volume envelope_volume12793 ų
Hydration-shell volume shell_volume9337 ų
Envelope diameter envelope_diameter39.1
Shell Rg shell_rg17.39
Envelope Rg envelope_rg12.23
Shape Rg shape_rg9.84
Total Rg total_rg10.00
Total atoms total_atoms13940
Residues n_residues960
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 dmax34.0
Rg (real space) rg_real9.50
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real2.0090e+08
I(0) uncertainty (real space) i0_real_error2.3980e+06
Rg (reciprocal space) rg_reciprocal9.50
I(0) (reciprocal space) i0_reciprocal200900000.0000
Solution quality estimate total_estimate0.8383
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary11.2
Skewness Skewness skewness0.234
Kurtosis Kurtosis kurtosis-0.267
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha95100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.660; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.947

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1ssla1
Class classg — Small proteins
Fold Fold foldg.16 — Trefoil/Plexin domain-like
Superfamily Superfamily superfamilyg.16.2 — Plexin repeat
Family Family familyg.16.2.1 — Plexin repeat
Domain ID domain_idd1ssla2
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_id1sslA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1680 — ligand-binding face of the semaphorins, domain 2
Homologous superfamily homologous superfamily10 — ligand-binding face of the semaphorins, domain 2

8. Citations (1)

9. Files and Curves (10)