5o1x

Structure of Nrd1 RNA binding domain

Method: X-RAY DIFFRACTION Dmax: 56.8 Å Quality: GOOD

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

Protein NRD1

Saccharomyces cerevisiae

UniProt P53617

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 290–468 Fragment:UNP residues 290-468 EDO 1,2-ETHANEDIOL × 7 SCN THIOCYANATE ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;291 K;0.2 M Potassium Thiocyanate, 23% PEG 3350 Resolution 1.60 Å R-free 0.208

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.

13 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NRD1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–180; UniProt 290–468

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 5o1x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5o1x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5o1x
Deposition date deposition_date2017-05-19
Structure title titleStructure of Nrd1 RNA binding domain
Keywords keywordsNrd1, RRM, RNA-binding, transcription non-coding RNAs, Nrd1 complex, transcription; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.96
Radius of gyration Rg (electron density) rg_electron15.93
Forward intensity I(0) i07398500.00
Molecular weight molecular_weight19306.0 kDa
Excluded volume excluded_volume23893 ų
Envelope volume envelope_volume27220 ų
Hydration-shell volume shell_volume14572 ų
Envelope diameter envelope_diameter55.4
Shell Rg shell_rg21.57
Envelope Rg envelope_rg16.14
Shape Rg shape_rg15.88
Total Rg total_rg17.02
Total atoms total_atoms1355
Residues n_residues162
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 dmax56.8
Rg (real space) rg_real16.88
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real7.3990e+06
I(0) uncertainty (real space) i0_real_error7.4250e+04
Rg (reciprocal space) rg_reciprocal16.89
I(0) (reciprocal space) i0_reciprocal7399000.0000
Solution quality estimate total_estimate0.8796
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.2
Skewness Skewness skewness0.225
Kurtosis Kurtosis kurtosis-0.367
Angular range angular_range— – 0.4700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1490000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.811; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)