1ksm

AVERAGE NMR SOLUTION STRUCTURE OF CA LN CALBINDIN D9K

Method: SOLUTION NMR Dmax: 40.4 Å Quality: REASONABLE

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

VITAMIN D-DEPENDENT CALCIUM-BINDING PROTEIN

Bos taurus

UniProt P02633

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 0–78 Mutation:P43M LA LANTHANUM (III) ION × 1 SOLUTION NMR NMR measurement conditions:pH 6;300 K;Ionic strength (raw mmCIF value) WATER SOLUTION;Pressure AMBIENT NMR sample composition:1.5 MM [15N, 13C] - CA LN CALBINDIN, PH 6.0 | H20:D2O 90:10 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.

19 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name S100G_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–79; UniProt 0–78

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 1ksm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ksm
Deposition date deposition_date2002-01-14
Structure title titleAVERAGE NMR SOLUTION STRUCTURE OF CA LN CALBINDIN D9K
Keywords keywordsLANTHANIDE IONS, CALCIUM-BINDING PROTEIN, PARAMAGNETIC NMR, PSEUDOCONTACT SHIFTS, RESIDUAL DIPOLAR COUPLINGS, METAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.23
Radius of gyration Rg (electron density) rg_electron11.59
Forward intensity I(0) i01620140.00
Molecular weight molecular_weight8650.0 kDa
Excluded volume excluded_volume10859 ų
Envelope volume envelope_volume12234 ų
Hydration-shell volume shell_volume9122 ų
Envelope diameter envelope_diameter38.7
Shell Rg shell_rg17.08
Envelope Rg envelope_rg11.98
Shape Rg shape_rg11.52
Total Rg total_rg13.21
Total atoms total_atoms1203
Residues n_residues75
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 dmax40.4
Rg (real space) rg_real13.12
Rg uncertainty (real space) rg_real_error0.22
I(0) (real space) i0_real1.6200e+06
I(0) uncertainty (real space) i0_real_error1.8430e+04
Rg (reciprocal space) rg_reciprocal13.13
I(0) (reciprocal space) i0_reciprocal1620000.0000
Solution quality estimate total_estimate0.7496
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.4
Skewness Skewness skewness0.011
Kurtosis Kurtosis kurtosis-0.343
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha118000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 1.000; Sysdev: 0.368; Positv: 1.000; Valcen: 0.982; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ksma_
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_id1ksmA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand

8. Citations (1)

9. Files and Curves (10)