1d1e

SOLUTION STRUCTURE OF LACTAM-BRIDGED C-TERMINAL ANALOGUE-II OF NEUROPEPTIDE Y

Method: SOLUTION NMR Dmax: 32.7 Å Quality: REASONABLE

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

No usable UniProt protein identity is available for this entry.

七张关系表仍保留该条目的 assembly 与组成信息,但缺少统一蛋白身份时,不能可靠建立跨 PDB 的同蛋白Chain接。

Assembly Composition of the Current Entry

Assembly Oligomeric State 实体与Construct证据 Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer 蛋白 1 / DNA 0 / RNA 0 / 其他Polymer 0 PDB declaration: monomeric Entity 1:C-TERMINAL ANALOGUE OF NEUROPEPTIDE Y, A POTENT Y2 RECEPTOR AGONIST × 1 缺少 UniProt 身份时不显示参考序列区间 Entity 1Fragment:C-TERMINAL ANALOGUE Entity 1Mutation:I28K, T32E Non-standard monomer:Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR NMR measurement conditions:pH 5;308 K;Pressure 1NMR sample composition:3.5 MG IN 0.6 ML H2O CONTAINING 30% TFE-D3 (BY VOLUME) Resolution not provided

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 1d1e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1d1e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1d1e
Deposition date deposition_date1999-09-15
Structure title titleSOLUTION STRUCTURE OF LACTAM-BRIDGED C-TERMINAL ANALOGUE-II OF NEUROPEPTIDE Y
Keywords keywordsLACTAM-BRIDGE, HELIX, NEUROPEPTIDE; NEUROPEPTIDE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier8.36
Radius of gyration Rg (electron density) rg_electron8.12
Forward intensity I(0) i018488200.00
Molecular weight molecular_weight34100.0 kDa
Excluded volume excluded_volume42496 ų
Envelope volume envelope_volume7831 ų
Hydration-shell volume shell_volume6729 ų
Envelope diameter envelope_diameter34.8
Shell Rg shell_rg15.48
Envelope Rg envelope_rg11.11
Shape Rg shape_rg8.09
Total Rg total_rg8.75
Total atoms total_atoms4860
Residues n_residues240
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 dmax32.7
Rg (real space) rg_real8.49
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real1.8490e+07
I(0) uncertainty (real space) i0_real_error2.1120e+05
Rg (reciprocal space) rg_reciprocal8.49
I(0) (reciprocal space) i0_reciprocal18490000.0000
Solution quality estimate total_estimate0.7417
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary8.3
Skewness Skewness skewness0.573
Kurtosis Kurtosis kurtosis-0.133
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2592.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.536; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.196; Smooth: 0.845

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1d1ea_
Class classj — Peptides
Fold Fold foldj.6 — Peptide hormones
Superfamily Superfamily superfamilyj.6.1 — Peptide hormones
Family Family familyj.6.1.1 — Peptide hormones

8. Citations (3)

9. Files and Curves (10)