BMRB Entry 17173

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17173
MolProbity Validation Chart

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Title:
1H, 13C, and 15N chemical shift assignments of the Nrd1-CTD Interacting Domain
Deposition date:
2010-09-10
Original release date:
2011-03-30
Authors:
Kubicek, Karel; Pasulka, Josef; Cerna, Hana; Loehr, Frank; Stefl, Richard
Citation:

Citation: Kubiek, Karel; Pasulka, Josef; erna, Hana; Lohr, Frank; tefl, Richard. "1H, 13C, and 15N resonance assignments for the CTD-interacting domain of Nrd1 bound to Ser5-phosphorylated CTD of RNA polymerase II."  Biomol. NMR Assignments 5, 203-205 (2011).
PubMed: 21350922

Assembly members:

Assembly members:
Nrd1_CID, polymer, 161 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Nrd1_CID: MQQDDDFQNFVATLESFKDL KSGISGSRIKKLTTYALDHI DIESKIISLIIDYSRLCPDS HKLGSLYIIDSIGRAYLDET RSNSNSSSNKPGTCAHAINT LGEVIQELLSDAIAKSNQDH KEKIRMLLDIWDRSGLFQKS YLNAIRSKCFAMDLEHHHHH H

Data sets:
Data typeCount
13C chemical shifts348
15N chemical shifts116
1H chemical shifts703

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CTD Interacting domain1

Entities:

Entity 1, CTD Interacting domain 161 residues - Formula weight is not available

1   METGLNGLNASPASPASPPHEGLNASNPHE
2   VALALATHRLEUGLUSERPHELYSASPLEU
3   LYSSERGLYILESERGLYSERARGILELYS
4   LYSLEUTHRTHRTYRALALEUASPHISILE
5   ASPILEGLUSERLYSILEILESERLEUILE
6   ILEASPTYRSERARGLEUCYSPROASPSER
7   HISLYSLEUGLYSERLEUTYRILEILEASP
8   SERILEGLYARGALATYRLEUASPGLUTHR
9   ARGSERASNSERASNSERSERSERASNLYS
10   PROGLYTHRCYSALAHISALAILEASNTHR
11   LEUGLYGLUVALILEGLNGLULEULEUSER
12   ASPALAILEALALYSSERASNGLNASPHIS
13   LYSGLULYSILEARGMETLEULEUASPILE
14   TRPASPARGSERGLYLEUPHEGLNLYSSER
15   TYRLEUASNALAILEARGSERLYSCYSPHE
16   ALAMETASPLEUGLUHISHISHISHISHIS
17   HIS

Samples:

sample_1: Nrd1 CID, [U-100% 13C; U-100% 15N], 2 mM; Na2HPO4 50 mM; NaCl 100 mM; b-mercaptoethanol 10 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 8.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 19954
PDB
DBJ GAA25857
EMBL CAA65493 CAA96158 CAY82359
GB AAC49568 AHY76857 AJP41095 AJT01532 AJT02278
REF NP_014148
SP P53617
TPG DAA10308
AlphaFold P53617

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