1bwx

THE SOLUTION STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-39, NMR, 10 STRUCTURES

Method: SOLUTION NMR Dmax: 38.2 Å Quality: REASONABLE

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

PARATHYROID HORMONE

Homo sapiens

UniProt P01270

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 32–70 Fragment:RESIDUES 1-39 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 5.8;298 K;Ionic strength (raw mmCIF value) 320 mM;Pressure 1 NMR sample composition:10% D2O/90% H2O 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.

25 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PTHY_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–39; UniProt 32–70

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 1bwx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1bwx
Deposition date deposition_date1998-09-29
Structure title titleTHE SOLUTION STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-39, NMR, 10 STRUCTURES
Keywords keywordsPEPTIDE HORMONE, SOLUTION STRUCTURE, HUMAN PARATHYROID HORMONE; PEPTIDE HORMONE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.54
Radius of gyration Rg (electron density) rg_electron14.42
Forward intensity I(0) i032498900.00
Molecular weight molecular_weight45303.0 kDa
Excluded volume excluded_volume56662 ų
Envelope volume envelope_volume27574 ų
Hydration-shell volume shell_volume13304 ų
Envelope diameter envelope_diameter64.2
Shell Rg shell_rg23.35
Envelope Rg envelope_rg18.80
Shape Rg shape_rg14.38
Total Rg total_rg15.32
Total atoms total_atoms6430
Residues n_residues390
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 dmax38.2
Rg (real space) rg_real13.55
Rg uncertainty (real space) rg_real_error0.07
I(0) (real space) i0_real3.0940e+07
I(0) uncertainty (real space) i0_real_error2.6280e+05
Rg (reciprocal space) rg_reciprocal14.76
I(0) (reciprocal space) i0_reciprocal32500000.0000
Solution quality estimate total_estimate0.6733
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary12.6
Skewness Skewness skewness0.246
Kurtosis Kurtosis kurtosis-0.727
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha4.7690
Highest regularization parameter α highest_alpha33210.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.005; Oscil: 1.000; Stabil: 0.980; Sysdev: 0.000; Positv: 1.000; Valcen: 0.813; Smooth: 0.000

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_idd1bwxa_
Class classj — Peptides
Fold Fold foldj.15 — Parathyroid hormone fragments (residues between 1 and 39)
Superfamily Superfamily superfamilyj.15.1 — Parathyroid hormone fragments (residues between 1 and 39)
Family Family familyj.15.1.1 — Parathyroid hormone fragments (residues between 1 and 39)

8. Citations (1)

9. Files and Curves (10)