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1bzb

GLYCOSYLATED EEL CALCITONIN

Method: SOLUTION NMR Dmax: 71.5 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (CALCITONIN)

OrganismNot specified

UniProt P01262

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–32 Non-standard monomer：Yes (specific site not provided by mmCIF) ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 SOLUTION NMR NMR measurement conditions：pH 4.5；308 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.

Other PDB Difference from Current Entry 1BZB Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BKU EFFECTS OF GLYCOSYLATION ON THE STRUCTURE AND DYNAMICS OF EEL CALCITONIN, NMR, 10 STRUCTURES Deposited 1998-07-13 Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–32（32 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4；308 K
Resolution not provided
1BYV GLYCOSYLATED EEL CALCITONIN Deposited 1998-10-16 Different oligomeric state Different ligand/ion Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–32（32 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SOLUTION NMR
NMR measurement conditions pH 4.5；308 K
Resolution not provided

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

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

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 1bzb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1bzb
Deposition date deposition_date1998-10-27
Structure title titleGLYCOSYLATED EEL CALCITONIN
Keywords keywordsHORMONE, CALCIUM-REGULATOR, OSTEOPOROSIS, HORMONE-GROWTH FACTOR COMPLEX; HORMONE/GROWTH FACTOR
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier15.92 Å
Radius of gyration Rg (electron density) rg_electron15.55 Å
Forward intensity I(0) i039025000.00
Molecular weight molecular_weight48036.0 kDa
Excluded volume excluded_volume59412 ų
Envelope volume envelope_volume30823 ų
Hydration-shell volume shell_volume14571 ų
Envelope diameter envelope_diameter73.6 Å
Shell Rg shell_rg23.90 Å
Envelope Rg envelope_rg19.18 Å
Shape Rg shape_rg15.52 Å
Total Rg total_rg16.31 Å
Total atoms total_atoms6609
Residues n_residues320
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 dmax71.5 Å
Rg (real space) rg_real16.16 Å
Rg uncertainty (real space) rg_real_error1.01 Å
I(0) (real space) i0_real3.9030e+07
I(0) uncertainty (real space) i0_real_error5.7780e+05
Rg (reciprocal space) rg_reciprocal16.13 Å
I(0) (reciprocal space) i0_reciprocal39020000.0000
Solution quality estimate total_estimate0.6048
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary19.0 Å
Skewness Skewness skewness0.579
Kurtosis Kurtosis kurtosis0.218
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha51690.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.253; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.100; 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) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1bzba_
Class classj — Peptides
Fold Fold foldj.6 — Peptide hormones
Superfamily Superfamily superfamilyj.6.1 — Peptide hormones
Family Family familyj.6.1.1 — Peptide hormones
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8. Citations (1)

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9. Files and Curves (10)