2lw9

NMR solution structure of Myo10 anti-CC

Method: SOLUTION NMR Dmax: 48.2 Å Quality: REASONABLE

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

Unconventionnal myosin-X

Homo sapiens

UniProt Q9HD67

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 883–933 Chain B; UniProt 883–933 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;303 K;Ionic strength (raw mmCIF value) 100 NMR sample composition:0.8 mM [U-100% 13C; U-100% 15N] entity-1, 100% D2O | 100% D2O 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 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYO10_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–51; UniProt 883–933 Author chain B; PDBConstruct 1–51; UniProt 883–933

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 2lw9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2lw9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2lw9
Deposition date deposition_date2012-07-25
Structure title titleNMR solution structure of Myo10 anti-CC
Keywords keywordsMyo10 anti-CC, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier19.10
Radius of gyration Rg (electron density) rg_electron18.73
Forward intensity I(0) i01032750000.00
Molecular weight molecular_weight252940.0 kDa
Excluded volume excluded_volume310250 ų
Envelope volume envelope_volume55188 ų
Hydration-shell volume shell_volume20249 ų
Envelope diameter envelope_diameter87.0
Shell Rg shell_rg30.10
Envelope Rg envelope_rg24.37
Shape Rg shape_rg18.74
Total Rg total_rg18.94
Total atoms total_atoms35540
Residues n_residues2040
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 dmax48.2
Rg (real space) rg_real17.99
Rg uncertainty (real space) rg_real_error0.09
I(0) (real space) i0_real9.8210e+08
I(0) uncertainty (real space) i0_real_error9.0520e+06
Rg (reciprocal space) rg_reciprocal19.24
I(0) (reciprocal space) i0_reciprocal1033000000.0000
Solution quality estimate total_estimate0.6770
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.183
Kurtosis Kurtosis kurtosis-0.866
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha4.0460
Highest regularization parameter α highest_alpha272900.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.003; Oscil: 1.000; Stabil: 0.985; Sysdev: 0.000; Positv: 1.000; Valcen: 0.852; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id2lw9A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily170
Domain ID domain_id2lw9B00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily170

8. Citations (1)

9. Files and Curves (10)