2lcm

NMR structure of S3-4 peptide

Method: SOLUTION NMR Dmax: 42.4 Å Quality: REASONABLE

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

Voltage-dependent N-type calcium channel subunit alpha-1B

OrganismNot specified

UniProt Q00975

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 1242–1269 Fragment:S4 of repeat III residues 1242-1269 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 4;300 K;Pressure ambient NMR sample composition:10 mM D2O, 90 mM H2O, trifluoroethanol/water | trifluoroethanol/water 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAC1B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–28; UniProt 1242–1269

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 2lcm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2lcm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2lcm
Deposition date deposition_date2011-05-02
Structure title titleNMR structure of S3-4 peptide
Keywords keywordsvoltage sensor peptide, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.23
Radius of gyration Rg (electron density) rg_electron11.93
Forward intensity I(0) i047109700.00
Molecular weight molecular_weight67006.0 kDa
Excluded volume excluded_volume89074 ų
Envelope volume envelope_volume10951 ų
Hydration-shell volume shell_volume7717 ų
Envelope diameter envelope_diameter49.0
Shell Rg shell_rg17.75
Envelope Rg envelope_rg14.07
Shape Rg shape_rg11.89
Total Rg total_rg12.38
Total atoms total_atoms10540
Residues n_residues560
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 dmax42.4
Rg (real space) rg_real11.50
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real4.7110e+07
I(0) uncertainty (real space) i0_real_error5.7500e+05
Rg (reciprocal space) rg_reciprocal11.49
I(0) (reciprocal space) i0_reciprocal47110000.0000
Solution quality estimate total_estimate0.5879
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary6.4
Skewness Skewness skewness0.510
Kurtosis Kurtosis kurtosis-0.618
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3438.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.208; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.017; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)