1dip

THE SOLUTION STRUCTURE OF PORCINE DELTA-SLEEP-INDUCING PEPTIDE IMMUNOREACTIVE PEPTIDE, NMR, 10 STRUCTURES

Method: SOLUTION NMR Dmax: 86.8 Å Quality: REASONABLE

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

DELTA-SLEEP-INDUCING PEPTIDE IMMUNOREACTIVE PEPTIDE

Sus scrofa

UniProt P80220

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–77 Chain B; UniProt 1–77 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 3.5;298 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name T22D3_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–78; UniProt 1–77 Author chain B; PDBConstruct 2–78; UniProt 1–77

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 1dip

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1dip
Deposition date deposition_date1997-04-09
Structure title titleTHE SOLUTION STRUCTURE OF PORCINE DELTA-SLEEP-INDUCING PEPTIDE IMMUNOREACTIVE PEPTIDE, NMR, 10 STRUCTURES
Keywords keywordsDELTA-SLEEP-INDUCING PEPTIDE IMMUNOREACTIVE PEPTIDE, LEUCINE ZIPPER, PIG, ACETYLATION; ACETYLATION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier24.72
Radius of gyration Rg (electron density) rg_electron24.67
Forward intensity I(0) i0453520000.00
Molecular weight molecular_weight174980.0 kDa
Excluded volume excluded_volume218320 ų
Envelope volume envelope_volume88666 ų
Hydration-shell volume shell_volume26512 ų
Envelope diameter envelope_diameter98.3
Shell Rg shell_rg34.91
Envelope Rg envelope_rg29.09
Shape Rg shape_rg24.65
Total Rg total_rg25.15
Total atoms total_atoms24580
Residues n_residues1540
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 dmax86.8
Rg (real space) rg_real24.97
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real4.5350e+08
I(0) uncertainty (real space) i0_real_error6.3850e+06
Rg (reciprocal space) rg_reciprocal24.91
I(0) (reciprocal space) i0_reciprocal453500000.0000
Solution quality estimate total_estimate0.6621
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.8
Skewness Skewness skewness0.422
Kurtosis Kurtosis kurtosis-0.489
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha458400.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.839; Stabil: 1.000; Sysdev: 0.184; Positv: 1.000; Valcen: 0.568; Smooth: 0.967

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1dipa_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.12 — Delta-sleep-inducing peptide immunoreactive peptide
Family Family familyh.1.12.1 — Delta-sleep-inducing peptide immunoreactive peptide
Domain ID domain_idd1dipb_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.12 — Delta-sleep-inducing peptide immunoreactive peptide
Family Family familyh.1.12.1 — Delta-sleep-inducing peptide immunoreactive peptide

CATH v4.4 (2 domains)

Domain ID domain_id1dipA01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily490 — Single helix bin
Domain ID domain_id1dipB01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily490 — Single helix bin

8. Citations (2)

9. Files and Curves (10)