BMRB Entry 34969

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34969
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title:
NMR solution structure of RPRD2 CTD-interacting domain and pS2,7 RNAPII CTD peptide.
Deposition date:
2024-12-07
Original release date:
2025-12-15
Authors:
Linhartova, K.; Macosek, J.; Kubicek, K.; Smirakova, E.; Stefl, R.
Citation:

Citation: Linhartova, K.; Macosek, J.; Kubicek, K.; Smirakova, E.; Steel, R.. "NMR solution structure of RPRD2 CTD-interacting domain and pS2,7 RNAPII CTD peptide."  .

Assembly members:

Assembly members:
entity_1, polymer, 148 residues, 17305.770 Da.
entity_2, polymer, 11 residues, 1412.137 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: SPXYXPTSPXY

Data sets:
Data typeCount
13C chemical shifts437
15N chemical shifts138
1H chemical shifts911

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

Entities:

Entity 1, unit_1 148 residues - 17305.770 Da.

1   METSERALASERSERALAGLYALALEUGLU
2   SERSERLEUASPARGLYSPHEGLNSERVAL
3   THRASNTHRMETGLUSERILEGLNGLYLEU
4   SERSERTRPCYSILEGLUASNLYSLYSHIS
5   HISSERTHRILEVALTYRHISTRPMETLYS
6   TRPLEUARGARGSERALATYRPROHISARG
7   LEUASNLEUPHETYRLEUALAASNASPVAL
8   ILEGLNASNCYSLYSARGLYSASNALAILE
9   ILEPHEARGGLUSERPHEALAASPVALLEU
10   PROGLUALAALAALALEUVALLYSASPPRO
11   SERVALSERLYSSERVALGLUARGILEPHE
12   LYSILETRPGLUASPARGASNVALTYRPRO
13   GLUGLUMETILEVALALALEUARGGLUALA
14   LEUSERTHRTHRPHELYSTHRGLNLYSGLN
15   LEUGLUHISHISHISHISHISHIS

Entity 2, unit_2 11 residues - 1412.137 Da.

1   SERPROSEPTYRSEPPROTHRSERPROSEP
2   TYR

Samples:

sample_1: RPRD2 CID, [U-100% 13C; U-100% 15N], 0.4 mM; pS2pS7 CTD 1 mM; Tris 50 mM; NaCl 100 mM; beta-mercaptoethanol 10 mM

sample_conditions_1: ionic strength: 100 mM; pH: 8.0; pressure: 1 Pa; temperature: 293.15 K

Experiments:

NameSampleSample stateSample conditions
3D (H)CC(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

Sparky, Goddard - 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 850 MHz
  • Bruker AVANCE III HD 700 MHz
  • Bruker AVANCE III HD 950 MHz

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