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1cz2

SOLUTION STRUCTURE OF WHEAT NS-LTP COMPLEXED WITH PROSTAGLANDIN B2.

Method: SOLUTION NMR Dmax: 39.5 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

NONSPECIFIC LIPID TRANSFER PROTEIN

OrganismNot specified

UniProt P24296

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 1–90 Not recorded E2P PROSTAGLANDIN B2 × 1 SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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 1CZ2 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 construct 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 construct 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
1GH1 NMR STRUCTURES OF WHEAT NONSPECIFIC LIPID TRANSFER PROTEIN Deposited 2000-10-29 Different construct Different ligand/ion Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 24–113（90 aa）
Not recorded No recorded non-water small molecule 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

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 1–90

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 1cz2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cz2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1cz2
Deposition date deposition_date1999-09-01
Structure title titleSOLUTION STRUCTURE OF WHEAT NS-LTP COMPLEXED WITH PROSTAGLANDIN B2.
Keywords keywordsPROTEIN COMPLEX ALPHA HELIX, LIPID BINDING PROTEIN; LIPID BINDING PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier12.53 Å
Radius of gyration Rg (electron density) rg_electron11.83 Å
Forward intensity I(0) i0240313000.00
Molecular weight molecular_weight119320.0 kDa
Excluded volume excluded_volume145420 ų
Envelope volume envelope_volume25062 ų
Hydration-shell volume shell_volume14496 ų
Envelope diameter envelope_diameter42.5 Å
Shell Rg shell_rg20.67 Å
Envelope Rg envelope_rg14.30 Å
Shape Rg shape_rg11.84 Å
Total Rg total_rg12.12 Å
Total atoms total_atoms16440
Residues n_residues1080
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 dmax39.5 Å
Rg (real space) rg_real12.40 Å
Rg uncertainty (real space) rg_real_error0.21 Å
I(0) (real space) i0_real2.4030e+08
I(0) uncertainty (real space) i0_real_error2.5940e+06
Rg (reciprocal space) rg_reciprocal12.41 Å
I(0) (reciprocal space) i0_reciprocal240300000.0000
Solution quality estimate total_estimate0.7806
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.0 Å
Skewness Skewness skewness-0.050
Kurtosis Kurtosis kurtosis-0.387
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2392000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.719; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1cz2a_
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_id1cz2A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology110 — Hydrophobic Seed Protein
Homologous superfamily homologous superfamily10 — Plant lipid-transfer and hydrophobic proteins
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8. Citations (1)

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9. Files and Curves (10)