1afh

LIPID TRANSFER PROTEIN FROM MAIZE SEEDLINGS, NMR, 15 STRUCTURES

Method: SOLUTION NMR Dmax: 37.9 Å Quality: GOOD

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

MAIZE NONSPECIFIC LIPID TRANSFER PROTEIN

OrganismNot specified

UniProt P19656

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 28–120 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 5.5;308 K 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NLTP_MAIZE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–93; UniProt 28–120

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 1afh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1afh
Deposition date deposition_date1997-03-07
Structure title titleLIPID TRANSFER PROTEIN FROM MAIZE SEEDLINGS, NMR, 15 STRUCTURES
Keywords keywordsLIPID-BINDING PROTEIN, LIPID TRANSFER PROTEIN, MAIZE, MOLECULAR MODELING, LIPID BINDING PROTEIN; LIPID BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.92
Radius of gyration Rg (electron density) rg_electron11.58
Forward intensity I(0) i0333759000.00
Molecular weight molecular_weight135900.0 kDa
Excluded volume excluded_volume163350 ų
Envelope volume envelope_volume16071 ų
Hydration-shell volume shell_volume10776 ų
Envelope diameter envelope_diameter43.4
Shell Rg shell_rg18.56
Envelope Rg envelope_rg13.10
Shape Rg shape_rg11.58
Total Rg total_rg11.73
Total atoms total_atoms18600
Residues n_residues1395
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 dmax37.9
Rg (real space) rg_real11.84
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real3.3380e+08
I(0) uncertainty (real space) i0_real_error3.5720e+06
Rg (reciprocal space) rg_reciprocal11.85
I(0) (reciprocal space) i0_reciprocal333800000.0000
Solution quality estimate total_estimate0.8086
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.3
Skewness Skewness skewness0.088
Kurtosis Kurtosis kurtosis-0.320
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha100000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

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_idd1afha_
Class classa — All alpha proteins
Fold Fold folda.52 — Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin
Superfamily Superfamily superfamilya.52.1 — Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin
Family Family familya.52.1.1 — Plant lipid-transfer and hydrophobic proteins

CATH v4.4 (1 domains)

Domain ID domain_id1afhA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology110 — Hydrophobic Seed Protein
Homologous superfamily homologous superfamily10 — Plant lipid-transfer and hydrophobic proteins

8. Citations (1)

9. Files and Curves (10)