SAXSdb — 1gh1

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

NONSPECIFIC LIPID TRANSFER PROTEIN

OrganismNot specified

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 24–113	Not recorded	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 5.3；308 K；Ionic strength (raw mmCIF value) 50mM acetate buffer；Pressure ambient NMR sample composition：4mM lipid transfer protein, 50mM acetate buffer; 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 1GH1	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BWO THE CRYSTAL STRUCTURE OF WHEAT NON-SPECIFIC TRANSFER PROTEIN COMPLEXED WITH TWO MOLECULES OF PHOSPHOLIPID AT 2.1 A RESOLUTION Deposited 1998-09-25	Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 24–113（90 aa）	Not recorded	LPC [1-MYRISTOYL-GLYCEROL-3-YL]PHOSPHONYLCHOLINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；pH 5.6	Resolution 2.10 Å R-free 0.213
1BWO THE CRYSTAL STRUCTURE OF WHEAT NON-SPECIFIC TRANSFER PROTEIN COMPLEXED WITH TWO MOLECULES OF PHOSPHOLIPID AT 2.1 A RESOLUTION Deposited 1998-09-25	Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 24–113（90 aa）	Not recorded	LPC [1-MYRISTOYL-GLYCEROL-3-YL]PHOSPHONYLCHOLINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；pH 5.6	Resolution 2.10 Å R-free 0.213
1CZ2 SOLUTION STRUCTURE OF WHEAT NS-LTP COMPLEXED WITH PROSTAGLANDIN B2. Deposited 1999-09-01	Different construct Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–90（90 aa）	Not recorded	E2P PROSTAGLANDIN B2 × 1	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	NLTP1_WHEAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–90； UniProt 24–113

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1gh1
Deposition date deposition_date	2000-10-29
Structure title title	NMR STRUCTURES OF WHEAT NONSPECIFIC LIPID TRANSFER PROTEIN
Keywords keywords	4-HELIX WINDING, LIPID BINDING PROTEIN; LIPID BINDING PROTEIN
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	12.64 Å
Radius of gyration Rg (electron density) rg_electron	12.08 Å
Forward intensity I(0) i0	364821000.00
Molecular weight molecular_weight	144130.0 kDa
Excluded volume excluded_volume	174000 Å³
Envelope volume envelope_volume	19192 Å³
Hydration-shell volume shell_volume	11987 Å³
Envelope diameter envelope_diameter	47.3 Å
Shell Rg shell_rg	19.47 Å
Envelope Rg envelope_rg	13.95 Å
Shape Rg shape_rg	12.11 Å
Total Rg total_rg	12.17 Å
Total atoms total_atoms	19695
Residues n_residues	1350
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	40.4 Å
Rg (real space) rg_real	12.55 Å
Rg uncertainty (real space) rg_real_error	0.29 Å
I(0) (real space) i0_real	3.6480e+08
I(0) uncertainty (real space) i0_real_error	3.5430e+06
Rg (reciprocal space) rg_reciprocal	12.56 Å
I(0) (reciprocal space) i0_reciprocal	364800000.0000
Solution quality estimate total_estimate	0.7995
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	17.4 Å
Skewness Skewness skewness	0.058
Kurtosis Kurtosis kurtosis	-0.316
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	167500.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.800; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; 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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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1gh1a_
Class class	a — All alpha proteins
Fold Fold fold	a.52 — Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin
Superfamily Superfamily superfamily	a.52.1 — Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin
Family Family family	a.52.1.1 — Plant lipid-transfer and hydrophobic proteins

CATH v4.4 (1 domains)

Domain ID domain_id	1gh1A00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	110 — Hydrophobic Seed Protein
Homologous superfamily homologous superfamily	10 — Plant lipid-transfer and hydrophobic proteins

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8. Citations (2)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	NONSPECIFIC LIPID TRANSFER PROTEIN
Molecular weight formula_weight	9618.9 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	19695

fit	/app/data/saxs_computation/gh/1gh1/1gh1.fit
pddf	/app/data/pr_computation/gh/1gh1/1gh1.pr.out
profile	/app/data/saxs_computation/gh/1gh1/1gh1.dat

NMR STRUCTURES OF WHEAT NONSPECIFIC LIPID TRANSFER PROTEIN

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

NONSPECIFIC LIPID TRANSFER PROTEIN

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)