2lyw

Intermolecular interactions between neurotensin and the third extracellular loop of human neurotensin 1 receptor

Method: SOLUTION NMR Dmax: 51.4 Å Quality: REASONABLE

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

Neurotensin receptor type 1

OrganismNot specified

UniProt P30989

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 321–344 Fragment:Extracellular domain residues 321-344 Mutation:C327S Neurotensin × 1 (P30990) SOLUTION NMR NMR measurement conditions:308 K;Pressure ambient NMR sample composition:0.7 mM neurotensin, 1.4 mM hNTS1(321-344), trifluoroethanol/water | trifluoroethanol/water 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.

47 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NTR1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–24; UniProt 321–344

Neurotensin

OrganismNot specified

UniProt P30990

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 151–163 Non-standard monomer:Yes (specific site not provided by mmCIF) Neurotensin receptor type 1 × 1 (P30989) SOLUTION NMR NMR measurement conditions:308 K;Pressure ambient NMR sample composition:0.7 mM neurotensin, 1.4 mM hNTS1(321-344), trifluoroethanol/water | trifluoroethanol/water 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NEUT_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–13; UniProt 151–163

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 2lyw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2lyw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2lyw
Deposition date deposition_date2012-09-20
Structure title titleIntermolecular interactions between neurotensin and the third extracellular loop of human neurotensin 1 receptor
Keywords keywordsInteraction ligand/receptor, NTS1, SIGNALING PROTEIN-NEUROPEPTIDE complex; SIGNALING PROTEIN/NEUROPEPTIDE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier12.18
Radius of gyration Rg (electron density) rg_electron12.18
Forward intensity I(0) i031205700.00
Molecular weight molecular_weight48516.0 kDa
Excluded volume excluded_volume61867 ų
Envelope volume envelope_volume24145 ų
Hydration-shell volume shell_volume13634 ų
Envelope diameter envelope_diameter52.9
Shell Rg shell_rg20.95
Envelope Rg envelope_rg15.55
Shape Rg shape_rg12.16
Total Rg total_rg13.05
Total atoms total_atoms6740
Residues n_residues360
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 dmax51.4
Rg (real space) rg_real12.25
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real3.1210e+07
I(0) uncertainty (real space) i0_real_error4.0440e+05
Rg (reciprocal space) rg_reciprocal12.25
I(0) (reciprocal space) i0_reciprocal31210000.0000
Solution quality estimate total_estimate0.6420
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.3
Skewness Skewness skewness0.592
Kurtosis Kurtosis kurtosis0.316
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha290000.0000
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: 0.362; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)