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1c3z

THP12-CARRIER PROTEIN FROM YELLOW MEAL WORM

Method: SOLUTION NMR Dmax: 62.3 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

THP12 CARRIER PROTEIN

Tenebrio molitor

UniProt Q27011

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 19–126 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6.9；25 K；Ionic strength (raw mmCIF value) NO SALT；Pressure AMBIENT NMR measurement conditions：pH 6.9；25 K；Ionic strength (raw mmCIF value) NO SALT；Pressure AMBIENT NMR sample composition：1MM PROTEIN, N15- OR N15/C13-DOUBLE LABELED NMR sample composition：1MM PROTEIN, N15- OR N15/C13-DOUBLE LABELED 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 1C3Z Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1C3Y THP12-CARRIER PROTEIN FROM YELLOW MEAL WORM Deposited 1999-07-10 Parsed fields agree Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 19–126（108 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.9；25 K；Ionic strength (raw mmCIF value) NO SALT；Pressure AMBIENT
NMR measurement conditions pH 6.9；25 K；Ionic strength (raw mmCIF value) NO SALT；Pressure AMBIENT
NMR sample composition 1MM PROTEIN, N15- OR N15/C13-DOUBLE LABELED
NMR sample composition 1MM PROTEIN, N15- OR N15/C13-DOUBLE LABELED
Resolution not provided

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q27011_TENMO
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–108； UniProt 19–126

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 1c3z

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1c3z
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1c3z
Deposition date deposition_date1999-07-10
Structure title titleTHP12-CARRIER PROTEIN FROM YELLOW MEAL WORM
Keywords keywordsEF-HAND, ALL-ALPHA, antifreeze PROTEIN; ANTIFREEZE 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_guinier16.85 Å
Radius of gyration Rg (electron density) rg_electron15.64 Å
Forward intensity I(0) i03510800.00
Molecular weight molecular_weight12307.0 kDa
Excluded volume excluded_volume15113 ų
Envelope volume envelope_volume20422 ų
Hydration-shell volume shell_volume11671 ų
Envelope diameter envelope_diameter64.2 Å
Shell Rg shell_rg20.68 Å
Envelope Rg envelope_rg16.34 Å
Shape Rg shape_rg15.61 Å
Total Rg total_rg16.80 Å
Total atoms total_atoms1703
Residues n_residues108
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 dmax62.3 Å
Rg (real space) rg_real16.88 Å
Rg uncertainty (real space) rg_real_error0.57 Å
I(0) (real space) i0_real3.5110e+06
I(0) uncertainty (real space) i0_real_error4.4340e+04
Rg (reciprocal space) rg_reciprocal16.88 Å
I(0) (reciprocal space) i0_reciprocal3511000.0000
Solution quality estimate total_estimate0.7425
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary56.5 Å
Skewness Skewness skewness0.440
Kurtosis Kurtosis kurtosis0.141
Angular range angular_range— – 0.4700 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha587500.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.593; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.872; 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_idd1c3za_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.2 — Insect pheromone/odorant-binding proteins
Family Family familya.39.2.1 — Insect pheromone/odorant-binding proteins

CATH v4.4 (1 domains)

Domain ID domain_id1c3zA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily20 — Pheromone/general odorant binding protein domain
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8. Citations (2)

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9. Files and Curves (10)