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PDB ID: 9ia7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34979
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Name: NMR solution structure of RPRD2 CTD-interacting domain and pT4 RNAPII CTD peptide.
Published: 2026-02-21

Title:

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

Deposition date:

2025-02-07

Original release date:

2026-02-21

Authors:

Linhartova, K.; Kubicek, K.; Stefl, R.

Citation:

Citation: Linhartova, K.; Macosek, J.; Kubicek, K.; Smirakova, E.; Stefl, R.. "Recognition of RNA Polymerase II C-terminal domain by RPRD2" .

Assembly members:

Assembly members:
entity_1, polymer, 148 residues, 17305.770 Da.
entity_2, polymer, 12 residues, 1339.258 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSASSAGALESSLDRKFQSV TNTMESIQGLSSWCIENKKH HSTIVYHWMKWLRRSAYPHR LNLFYLANDVIQNCKRKNAI IFRESFADVLPEAAALVKDP SVSKSVERIFKIWEDRNVYP EEMIVALREALSTTFKTQKQ LEHHHHHH
entity_2: SPSYSPXSPSYS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	340
15N chemical shifts	116
1H chemical shifts	705

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	2

Entities:

Entity 1, unit_1 148 residues - 17305.770 Da.

1

MET

SER

ALA

SER

ALA

GLY

ALA

LEU

GLU

2

SER

LEU

ASP

ARG

LYS

PHE

GLN

SER

VAL

3

THR

ASN

THR

MET

GLU

SER

ILE

GLN

GLY

LEU

4

SER

TRP

CYS

ILE

GLU

ASN

LYS

HIS

5

HIS

SER

THR

ILE

VAL

TYR

HIS

TRP

MET

LYS

6

TRP

LEU

ARG

SER

ALA

TYR

PRO

HIS

ARG

7

LEU

ASN

LEU

PHE

TYR

LEU

ALA

ASN

ASP

VAL

8

ILE

GLN

ASN

CYS

LYS

ARG

LYS

ASN

ALA

ILE

9

ILE

PHE

ARG

GLU

SER

PHE

ALA

ASP

VAL

LEU

10

PRO

GLU

ALA

LEU

VAL

LYS

ASP

PRO

11

SER

VAL

SER

LYS

SER

VAL

GLU

ARG

ILE

PHE

12

LYS

ILE

TRP

GLU

ASP

ARG

ASN

VAL

TYR

PRO

13

GLU

MET

ILE

VAL

ALA

LEU

ARG

GLU

ALA

14

LEU

SER

THR

PHE

LYS

THR

GLN

LYS

GLN

15

LEU

GLU

HIS

Entity 2, unit_2 12 residues - 1339.258 Da.

1

SER

PRO

SER

TYR

SER

PRO

TPO

SER

PRO

SER

2

TYR

SER

Samples:

sample_1: RPRD2 CID, [U-100% 13C; U-100% 15N], 0.5 mM; pT4 CTD, none, 1.5 mM

sample_conditions_1: ionic strength: 100 mM; pH: 8; pressure: 1 Pa; temperature: 293.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CC(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

NMRFAM-SPARKY, Lee W, Tonelli M, Markley JL - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Amber, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

Bruker AVANCE III HD 600 MHz
Bruker AVANCE III 850 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks

BMRB Entry 34979