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2lnf

Neurotensin 40 structures in DMPC/CHAPS(q=0.25) bicelle pH 5.5 & 298K. NMR data & Structures

Method: SOLUTION NMR Dmax: 17.4 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Neurotensin

Homo sapiens

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 151–163 Fragment：UNP RESIDUES 151-163 No other associated polymer SOLUTION NMR NMR measurement conditions：pH 5.5；298 K；Ionic strength (raw mmCIF value) 4.5；Pressure ambient NMR sample composition：4.5 mM Neurotensin-1, 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.

Other PDB Difference from Current Entry 2LNF Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2LNE Neurotensin 40 structures in water pH 5.5 298 K. NMR data & structures Deposited 2011-12-27 Different construct Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 151–163（13 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.5；298 K；Ionic strength (raw mmCIF value) 4.5；Pressure ambient
NMR sample composition 4.5 mM Neurotensin-1, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2LNG Neurotensin 40 structures in DMPC:CHAPS:GM1(q= 0.25) bicelle pH 5.5 & 298K. NMR data & Structures Deposited 2011-12-27 Different construct Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 151–163（13 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.5；298 K；Ionic strength (raw mmCIF value) 4.5；Pressure ambient
NMR sample composition 4.5 mM Neurotensin-1, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2LYW Intermolecular interactions between neurotensin and the third extracellular loop of human neurotensin 1 receptor Deposited 2012-09-20 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 151–163（13 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule 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
3F6K Crystal structure of the Vps10p domain of human sortilin/NTS3 in complex with neurotensin Deposited 2008-11-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain N 151–163（13 aa） Fragment：UNP residues 151-163
Non-standard monomer：Yes (specific site not provided by mmCIF) PGE TRIETHYLENE GLYCOL × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.8；293 K；19% PEG 6000, 600 mM NaCl, 3% Glycerol, 100 mM HEPES, 93 mM Tris-HCl, pH 7.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.00 Å R-free 0.229
4PO7 Structure of the Sortilin:neurotensin complex at excess neurotensin concentration Deposited 2014-02-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric
Chain N 151–163（13 aa） Fragment：unp residues 151-163
Chain P 151–163（13 aa） Fragment：unp residues 151-163
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 PG4 TETRAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.9；292 K；20% PEG 6k, 300 mM sodium malonate, 3% glycerol and 100 mM TrisHCl, pH 7.9, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 2.66 Å R-free 0.212

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 1
Chains and sequence ranges Author chain A； 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 2lnf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2lnf
Deposition date deposition_date2011-12-27
Structure title titleNeurotensin 40 structures in DMPC/CHAPS(q=0.25) bicelle pH 5.5 & 298K. NMR data & Structures
Keywords keywordsNT, DMPC:CHAPS Bicelle, NEUROPEPTIDE; NEUROPEPTIDE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier6.44 Å
Radius of gyration Rg (electron density) rg_electron7.81 Å
Forward intensity I(0) i056761000.00
Molecular weight molecular_weight67679.0 kDa
Excluded volume excluded_volume86578 ų
Envelope volume envelope_volume5688 ų
Hydration-shell volume shell_volume5689 ų
Envelope diameter envelope_diameter31.5 Å
Shell Rg shell_rg14.02 Å
Envelope Rg envelope_rg9.68 Å
Shape Rg shape_rg7.78 Å
Total Rg total_rg8.13 Å
Total atoms total_atoms9760
Residues n_residues520
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax17.4 Å
Rg (real space) rg_real6.28 Å
Rg uncertainty (real space) rg_real_error0.02 Å
I(0) (real space) i0_real5.5130e+07
I(0) uncertainty (real space) i0_real_error2.9270e+05
Rg (reciprocal space) rg_reciprocal6.46 Å
I(0) (reciprocal space) i0_reciprocal56760000.0000
Solution quality estimate total_estimate0.6734
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary7.3 Å
Skewness Skewness skewness0.149
Kurtosis Kurtosis kurtosis-0.758
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha8.1290
Highest regularization parameter α highest_alpha671.5000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.987; Stabil: 0.966; Sysdev: 0.000; Positv: 1.000; Valcen: 0.901; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)