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1cb1

THREE-DIMENSIONAL SOLUTION STRUCTURE OF CA2+-LOADED PORCINE CALBINDIN D9K DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY

Method: SOLUTION NMR Dmax: 42.0 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CALBINDIN D9K

Sus scrofa

UniProt P02632

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 1–78 Not recorded No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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 1CB1 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1RSW 12-mer from site II calbindin D9K (DKNGDGEVSFEE) coordination Pb(II) Deposited 2003-12-10 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 57–68（12 aa） Fragment：residues 57-68
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.4；288 K；Ionic strength (raw mmCIF value) aprox 0；Pressure ambient
NMR sample composition 3mM Peptide and Pb(NO3)2. NaOH and HNO3 added for pH fixing to 5.4; 80% H2O, 20% D2O. | 80% H2O, 20% D2O
Resolution not provided
1RSX 12-mer from site II calbindin D9K (DKNGDGEVSFEE) coordinating Cd(II) Deposited 2003-12-10 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 57–68（12 aa） Fragment：residues 57-68 (SWS P02632)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.6；288 K；Ionic strength (raw mmCIF value) aprox 0；Pressure ambient
NMR sample composition 3mM Peptide and Cd(NO3)2. NaOH and HNO3 added for pH fixing to 6.6; 80% H2O, 20% D2O | 80% H2O, 20% D2O
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 S100G_PIG
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–78； UniProt 1–78

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 1cb1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cb1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1cb1
Deposition date deposition_date1991-12-13
Structure title titleTHREE-DIMENSIONAL SOLUTION STRUCTURE OF CA2+-LOADED PORCINE CALBINDIN D9K DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
Keywords keywordsCALCIUM-BINDING PROTEIN; CALCIUM-BINDING 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_guinier12.26 Å
Radius of gyration Rg (electron density) rg_electron11.74 Å
Forward intensity I(0) i0176275000.00
Molecular weight molecular_weight114320.0 kDa
Excluded volume excluded_volume144310 ų
Envelope volume envelope_volume20204 ų
Hydration-shell volume shell_volume12410 ų
Envelope diameter envelope_diameter45.5 Å
Shell Rg shell_rg19.77 Å
Envelope Rg envelope_rg14.17 Å
Shape Rg shape_rg11.70 Å
Total Rg total_rg12.16 Å
Total atoms total_atoms16185
Residues n_residues1014
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 dmax42.0 Å
Rg (real space) rg_real12.18 Å
Rg uncertainty (real space) rg_real_error0.34 Å
I(0) (real space) i0_real1.7630e+08
I(0) uncertainty (real space) i0_real_error1.8480e+06
Rg (reciprocal space) rg_reciprocal12.19 Å
I(0) (reciprocal space) i0_reciprocal176300000.0000
Solution quality estimate total_estimate0.8506
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.4 Å
Skewness Skewness skewness0.099
Kurtosis Kurtosis kurtosis-0.236
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha95100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.692; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.978
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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_idd1cb1a_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.1 — Calbindin D9K

CATH v4.4 (1 domains)

Domain ID domain_id1cb1A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
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8. Citations (2)

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9. Files and Curves (10)