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6xor

Structure of the Self-Association Domain of Swallow

Method: SOLUTION NMR Dmax: 96.6 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Protein swallow

Drosophila melanogaster

UniProt P40688

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 205–275 Chain B； UniProt 205–275 Mutation：R224E, K244I, C253D, C265A No other associated polymer SOLUTION NMR NMR measurement conditions：pH 5.6；313 K；Ionic strength (raw mmCIF value) 30；Pressure 1 NMR sample composition：0.5 mM [U-99% 13C; U-99% 15N] Residues 205-275 of Swallow, 10 mM sodium chloride, 20 mM MES, 1 mM sodium azide, 0.2 mM DSS, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition：0.4 mM [U-99% 13C; U-99% 15N] Residues 205-275 of Swallow, 10 mM sodium chloride, 20 mM MES, 1 mM sodium azide, 0.2 mM DSS, 0.4 mM unlabeled Residues 205-275 of Swallow, 95% H2O/5% D2O | 95% H2O/5% 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.

Other PDB Difference from Current Entry 6XOR Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3BRL Crystal Structure of LC8 S88E / Swa Deposited 2007-12-21 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 287–296（10 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；Calcium acetate 0.2M, sodium cacodylate 0.1M, 15% PEG8000, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.90 Å R-free 0.254
3E2B Crystal structure of Dynein Light chain LC8 in complex with a peptide derived from Swallow Deposited 2008-08-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 281–296（16 aa）
Not recorded ACT ACETATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；0.2M sodium potassium tartrate, 0.1M sodium citrate, 2.0M ammonium sulfate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.00 Å R-free 0.266

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SWA_DROME
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–71； UniProt 205–275 Author chain B； PDBConstruct 1–71； UniProt 205–275

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 6xor

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6xor
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6xor
Deposition date deposition_date2020-07-07
Structure title titleStructure of the Self-Association Domain of Swallow
Keywords keywordscoiled coil, self-association domain, RNA BINDING PROTEIN; RNA 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_guinier28.39 Å
Radius of gyration Rg (electron density) rg_electron28.99 Å
Forward intensity I(0) i01814410000.00
Molecular weight molecular_weight341780.0 kDa
Excluded volume excluded_volume419920 ų
Envelope volume envelope_volume43826 ų
Hydration-shell volume shell_volume14746 ų
Envelope diameter envelope_diameter106.4 Å
Shell Rg shell_rg30.82 Å
Envelope Rg envelope_rg32.27 Å
Shape Rg shape_rg28.98 Å
Total Rg total_rg29.06 Å
Total atoms total_atoms47680
Residues n_residues2840
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 dmax96.6 Å
Rg (real space) rg_real29.38 Å
Rg uncertainty (real space) rg_real_error1.09 Å
I(0) (real space) i0_real1.8140e+09
I(0) uncertainty (real space) i0_real_error2.8230e+07
Rg (reciprocal space) rg_reciprocal29.08 Å
I(0) (reciprocal space) i0_reciprocal1814000000.0000
Solution quality estimate total_estimate0.5719
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.5 Å
Skewness Skewness skewness0.628
Kurtosis Kurtosis kurtosis-0.562
Angular range angular_range— – 0.2800 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha179700.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.142; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.011; Smooth: 0.000
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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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8. Citations (1)

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9. Files and Curves (10)