5o1w

Structure of Nrd1 RNA binding domain

Method: X-RAY DIFFRACTION Dmax: 64.0 Å Quality: REASONABLE

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 301–489 Fragment:UNP residues 301-489 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;291 K;12% PEG 8000, 0.1 M Bicine pH 9 Resolution 2.30 Å R-free 0.233

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 3–191; UniProt 301–489

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 5o1w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5o1w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5o1w
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_guinier17.11
Radius of gyration Rg (electron density) rg_electron16.16
Forward intensity I(0) i06645500.00
Molecular weight molecular_weight18824.0 kDa
Excluded volume excluded_volume23586 ų
Envelope volume envelope_volume27405 ų
Hydration-shell volume shell_volume14507 ų
Envelope diameter envelope_diameter54.5
Shell Rg shell_rg21.70
Envelope Rg envelope_rg16.39
Shape Rg shape_rg16.13
Total Rg total_rg17.22
Total atoms total_atoms1331
Residues n_residues167
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 dmax64.0
Rg (real space) rg_real17.03
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real6.6460e+06
I(0) uncertainty (real space) i0_real_error7.3030e+04
Rg (reciprocal space) rg_reciprocal17.04
I(0) (reciprocal space) i0_reciprocal6646000.0000
Solution quality estimate total_estimate0.7499
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.2
Skewness Skewness skewness0.186
Kurtosis Kurtosis kurtosis-0.432
Angular range angular_range— – 0.4650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1324000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.603; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.934; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)