1mux

SOLUTION NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES

Method: SOLUTION NMR Dmax: 96.6 Å Quality: GOOD

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

CALMODULIN

Xenopus laevis

UniProt P62155

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 1–148 Not recorded CA CALCIUM ION × 4 WW7 N-(6-AMINOHEXYL)-5-CHLORO-1-NAPHTHALENESULFONAMIDE × 2 SOLUTION NMR NMR measurement conditions:pH 6.8;308 K;Ionic strength (raw mmCIF value) KCL, 100mM;Pressure 1 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.

22 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM_XENLA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–148; UniProt 1–148

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 1mux

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1mux
Deposition date deposition_date1997-09-06
Structure title titleSOLUTION NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES
Keywords keywordsCOMPLEX (CALMODULIN-INHIBITOR), CALMODULIN, W-7, NAPHTHALENESULFONAMIDE, CALCIUM-BINDING; CALCIUM-BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier27.80
Radius of gyration Rg (electron density) rg_electron27.39
Forward intensity I(0) i04331480000.00
Molecular weight molecular_weight525730.0 kDa
Excluded volume excluded_volume643590 ų
Envelope volume envelope_volume284700 ų
Hydration-shell volume shell_volume63574 ų
Envelope diameter envelope_diameter113.2
Shell Rg shell_rg44.40
Envelope Rg envelope_rg35.45
Shape Rg shape_rg27.39
Total Rg total_rg27.81
Total atoms total_atoms70560
Residues n_residues4440
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 dmax96.6
Rg (real space) rg_real27.90
Rg uncertainty (real space) rg_real_error1.09
I(0) (real space) i0_real4.3310e+09
I(0) uncertainty (real space) i0_real_error6.6200e+07
Rg (reciprocal space) rg_reciprocal27.87
I(0) (reciprocal space) i0_reciprocal4331000000.0000
Solution quality estimate total_estimate0.7779
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary39.0
Skewness Skewness skewness0.272
Kurtosis Kurtosis kurtosis-0.496
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1530000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.783; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.760; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1muxa_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.5 — Calmodulin-like

CATH v4.4 (2 domains)

Domain ID domain_id1muxA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id1muxA02
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)