2lo6

Structure of Nrd1 CID bound to phosphorylated RNAP II CTD

Method: SOLUTION NMR Dmax: 58.8 Å Quality: GOOD

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

Protein NRD1

Saccharomyces cerevisiae S288c

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–153 Fragment:CID domain residues 1-154 DNA-directed RNA polymerase II subunit RPB1 × 1 (P04050) SOLUTION NMR NMR measurement conditions:pH 8;293 K;Ionic strength (raw mmCIF value) 100;Pressure ambient NMR sample composition:2 mM [U-100% 13C; U-100% 15N] Nrd1 polypeptide, 2.3 mM phosphopeptide, 90% H2O/10% D2O | 90% H2O/10% 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.

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 1–153; UniProt 1–153

DNA-directed RNA polymerase II subunit RPB1

OrganismNot specified

UniProt P04050

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1556–1569 Fragment:UNP residues 1556-1569 Non-standard monomer:Yes (specific site not provided by mmCIF) Protein NRD1 × 1 (P53617) SOLUTION NMR NMR measurement conditions:pH 8;293 K;Ionic strength (raw mmCIF value) 100;Pressure ambient NMR sample composition:2 mM [U-100% 13C; U-100% 15N] Nrd1 polypeptide, 2.3 mM phosphopeptide, 90% H2O/10% D2O | 90% H2O/10% 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.

211 other PDB entries and 218 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPB1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–14; UniProt 1556–1569

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 2lo6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2lo6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2lo6
Deposition date deposition_date2012-01-17
Structure title titleStructure of Nrd1 CID bound to phosphorylated RNAP II CTD
Keywords keywords;CTD-interacting domain, CID, carboxy-terminal domain, CTD, RNA-processing, transciption termination, cis-trans isomerization of prolines, Ess1 isomerase, PEPTIDE BINDING PROTEIN, TRANSCRIPTION ;; TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier16.79
Radius of gyration Rg (electron density) rg_electron16.03
Forward intensity I(0) i02104650000.00
Molecular weight molecular_weight378700.0 kDa
Excluded volume excluded_volume469690 ų
Envelope volume envelope_volume50745 ų
Hydration-shell volume shell_volume21433 ų
Envelope diameter envelope_diameter68.3
Shell Rg shell_rg26.67
Envelope Rg envelope_rg20.24
Shape Rg shape_rg15.98
Total Rg total_rg16.35
Total atoms total_atoms52700
Residues n_residues3320
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 dmax58.8
Rg (real space) rg_real16.73
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real2.1050e+09
I(0) uncertainty (real space) i0_real_error2.9580e+07
Rg (reciprocal space) rg_reciprocal16.73
I(0) (reciprocal space) i0_reciprocal2105000000.0000
Solution quality estimate total_estimate0.7635
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary22.2
Skewness Skewness skewness0.249
Kurtosis Kurtosis kurtosis-0.096
Angular range angular_range— – 0.4750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha850100.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.642; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2lo6A00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily90

8. Citations (1)

9. Files and Curves (10)