9ia7

NMR solution structure of RPRD2 CTD-interacting domain and pT4 RNAPII CTD peptide.

Method: SOLUTION NMR Dmax: 45.0 Å Quality: GOOD

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

Regulation of nuclear pre-mRNA domain-containing protein 2

Homo sapiens

UniProt Q5VT52

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 16–155 Not recorded DNA-directed RNA polymerase II subunit RPB1 × 1 (P24928) SOLUTION NMR NMR measurement conditions:pH 8;293.15 K;Ionic strength (raw mmCIF value) 100;Pressure 1 NMR sample composition:0.5 mM [U-100% 13C; U-100% 15N] RPRD2 CID, 1.5 mM pT4 CTD, 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.

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

View Construct and Data Evidence
UniProt name RPRD2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–141; UniProt 16–155

DNA-directed RNA polymerase II subunit RPB1

OrganismNot specified

UniProt P24928

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 1612–1623 Non-standard monomer:Yes (specific site not provided by mmCIF) Regulation of nuclear pre-mRNA domain-containing protein 2 × 1 (Q5VT52) SOLUTION NMR NMR measurement conditions:pH 8;293.15 K;Ionic strength (raw mmCIF value) 100;Pressure 1 NMR sample composition:0.5 mM [U-100% 13C; U-100% 15N] RPRD2 CID, 1.5 mM pT4 CTD, 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.

33 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPB1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–12; UniProt 1612–1623

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 9ia7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ia7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ia7
Deposition date deposition_date2025-02-07
最后修订 last_revision2026-02-18
Structure title titleNMR solution structure of RPRD2 CTD-interacting domain and pT4 RNAPII CTD peptide.
Keywords keywordsRPRD2, CID, RNAPII CTD, Complex, PROTEIN BINDING, Threonine, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.88
Radius of gyration Rg (electron density) rg_electron14.49
Forward intensity I(0) i01481040000.00
Molecular weight molecular_weight325970.0 kDa
Excluded volume excluded_volume407300 ų
Envelope volume envelope_volume34343 ų
Hydration-shell volume shell_volume17230 ų
Envelope diameter envelope_diameter53.1
Shell Rg shell_rg22.91
Envelope Rg envelope_rg16.75
Shape Rg shape_rg14.44
Total Rg total_rg14.76
Total atoms total_atoms45560
Residues n_residues2800
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 dmax45.0
Rg (real space) rg_real14.75
Rg uncertainty (real space) rg_real_error0.21
I(0) (real space) i0_real1.4810e+09
I(0) uncertainty (real space) i0_real_error1.6160e+07
Rg (reciprocal space) rg_reciprocal14.76
I(0) (reciprocal space) i0_reciprocal1481000000.0000
Solution quality estimate total_estimate0.8186
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.5
Skewness Skewness skewness0.021
Kurtosis Kurtosis kurtosis-0.399
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha455800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.889; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)