BMRB Entry 27063

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27063

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Title:
Degenerate heptads 27-52 of human RNA polymerase II C-terminal domain (DNA-directed RNA polymerase II subunit RPB1): assignments and backbone relaxation
Deposition date:
2017-04-04
Original release date:
2017-10-04
Authors:
Janke, Abigail; Burke, Kathleen; Fawzi, Nicolas
Citation:

Citation: Janke, Abigail; Seo, Dahee; Burke, Kathleen; Conicella, Alexander; Rahmanian, Vahid; Mittal, Jeetain; Fawzi, Nicolas. "Lysines in RNA polymerase II C-terminal domain contribute to TAF15 fibril recruitment"  Biochemistry 57, 2549-2563 (2018).
PubMed: 28945358

Assembly members:

Assembly members:
RNA_Pol_II_CTD27-52, polymer, 201 residues, Formula weight is not available

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   Vector: pJ411

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RNA_Pol_II_CTD27-52: GHMSPNYTPTSPNYSPTSPS YSPTSPSYSPTSPSYSPSSP RYTPQSPTYTPSSPSYSPSS PSYSPASPKYTPTSPSYSPS SPEYTPTSPKYSPTSPKYSP TSPKYSPTSPTYSPTTPKYS PTSPTYSPTSPVYTPTSPKY SPTSPTYSPTSPKYSPTSPT YSPTSPKGSTYSPTSPGYSP TSPTYSLTSPAISPDDSDEE N

Data sets:
Data typeCount
13C chemical shifts425
15N chemical shifts108
1H chemical shifts108
T1 relaxation values58
T2 relaxation values59
heteronuclear NOE values59

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CTD27-52 monomer1

Entities:

Entity 1, CTD27-52 monomer 201 residues - Formula weight is not available

Residue 1-3 are cleavage and cloning artifact. Residue 4 is residue 1773 and the last residue is residue 1970. Residue 1835 is alanine as in canonical sequence Uniprot P24928.

1   GLYHISMETSERPROASNTYRTHRPROTHR
2   SERPROASNTYRSERPROTHRSERPROSER
3   TYRSERPROTHRSERPROSERTYRSERPRO
4   THRSERPROSERTYRSERPROSERSERPRO
5   ARGTYRTHRPROGLNSERPROTHRTYRTHR
6   PROSERSERPROSERTYRSERPROSERSER
7   PROSERTYRSERPROALASERPROLYSTYR
8   THRPROTHRSERPROSERTYRSERPROSER
9   SERPROGLUTYRTHRPROTHRSERPROLYS
10   TYRSERPROTHRSERPROLYSTYRSERPRO
11   THRSERPROLYSTYRSERPROTHRSERPRO
12   THRTYRSERPROTHRTHRPROLYSTYRSER
13   PROTHRSERPROTHRTYRSERPROTHRSER
14   PROVALTYRTHRPROTHRSERPROLYSTYR
15   SERPROTHRSERPROTHRTYRSERPROTHR
16   SERPROLYSTYRSERPROTHRSERPROTHR
17   TYRSERPROTHRSERPROLYSGLYSERTHR
18   TYRSERPROTHRSERPROGLYTYRSERPRO
19   THRSERPROTHRTYRSERLEUTHRSERPRO
20   ALAILESERPROASPASPSERASPGLUGLU
21   ASN

Samples:

sample_1: RNA Pol II CTD27-52, [U-99% 13C; U-99% 15N], 500 ± 25 uM; TRIS 20 mM; sodium chloride 200 mM; EDTA 0.5 mM; beta-mercaptoethanol 20 mM

sample_2: RNA Pol II CTD27-52, [U-99% 15N], 250 ± 25 uM; TRIS 20 mM; sodium chloride 200 mM; EDTA 0.5 mM; beta-mercaptoethanol 20 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 277 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D (H)N(CA)NNHsample_1isotropicsample_conditions_1
15N R2sample_2isotropicsample_conditions_1
15N R1sample_2isotropicsample_conditions_1
1H 15N het NOEsample_2isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 850 MHz

Related Database Links:

UNP P24928
AlphaFold Q6NX41

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