BMRB Entry 17161

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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/BMR17161
MolProbity Validation Chart

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Title:
Rna14p/Rna15p heterodimer
Deposition date:
2010-08-31
Original release date:
2010-10-26
Authors:
Mackereth, Cameron
Citation:

Citation: Mackereth, Cameron. "Chemical shift assignments of a minimal Rna14p/Rna15p heterodimer from the yeast cleavage factor IA complex."  Biomol. NMR Assignments 5, 93-95 (2011).
PubMed: 20967574

Assembly members:

Assembly members:
Rna14p, polymer, 53 residues, Formula weight is not available
Rna15p, polymer, 109 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: pCDF

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Rna14p: MKRDSELPTEVLDLLSVIPK RQYFNTNLLDAQKLVNFLND QVEIPTVESTKSG
Rna15p: GHMSNGPDFQNSGNANFLSQ KFPELPSGIDVNINMTTPAM MISSELAKKPKEVQLKFLQK FQEWTRAHPEDAASLLELCP QLSFVTAELLLTNGICKVDD LIPLASRPQ

Data sets:
Data typeCount
13C chemical shifts744
15N chemical shifts166
1H chemical shifts1167

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rna14p1
2Rna15p2

Entities:

Entity 1, Rna14p 53 residues - Formula weight is not available

Start methionine derives from the cloning site within the expression plasmid

1   METLYSARGASPSERGLULEUPROTHRGLU
2   VALLEUASPLEULEUSERVALILEPROLYS
3   ARGGLNTYRPHEASNTHRASNLEULEUASP
4   ALAGLNLYSLEUVALASNPHELEUASNASP
5   GLNVALGLUILEPROTHRVALGLUSERTHR
6   LYSSERGLY

Entity 2, Rna15p 109 residues - Formula weight is not available

The Gly-His-Met sequence derives from the cloning vector and is present at the N-terminus of the peptide following cleavage and removal of the His-tag by TEV protease

1   GLYHISMETSERASNGLYPROASPPHEGLN
2   ASNSERGLYASNALAASNPHELEUSERGLN
3   LYSPHEPROGLULEUPROSERGLYILEASP
4   VALASNILEASNMETTHRTHRPROALAMET
5   METILESERSERGLULEUALALYSLYSPRO
6   LYSGLUVALGLNLEULYSPHELEUGLNLYS
7   PHEGLNGLUTRPTHRARGALAHISPROGLU
8   ASPALAALASERLEULEUGLULEUCYSPRO
9   GLNLEUSERPHEVALTHRALAGLULEULEU
10   LEUTHRASNGLYILECYSLYSVALASPASP
11   LEUILEPROLEUALASERARGPROGLN

Samples:

sample_1: Rna14p, [U-100% 13C; U-100% 15N; U-70% 2H], 1.0 mM; Rna15p, [U-100% 13C; U-100% 15N; U-70% 2H], 1.0 mM; sodium phosphate 20 mM; Nacl 50 mM; DTT 25 mM; H2O 90%; D2O 10%

sample_2: Rna14p, [U-99% 15N], 0.2-1.0 mM; Rna15p, [U-99% 15N], 0.2-1.0 mM; sodium phosphate 20 mM; Nacl 50 mM; DTT 25 mM; H2O 90%; D2O 10%

sample_3: Rna14p, [U-99% 15N], 0.2 mM; Rna15p, [U-99% 15N], 0.2 mM; sodium phosphate 20 mM; Nacl 50 mM; DTT 25 mM; D2O 100%

sample_4: Rna14p, [U-99% 13C; U-99% 15N], 0.4 mM; Rna15p, [U-99% 13C; U-99% 15N], 0.4 mM; sodium phosphate 20 mM; Nacl 50 mM; DTT 25 mM; H2O 90%; D2O 10%

sample_5: Rna14p, [U-99% 13C; U-99% 15N], 0.4 mM; Rna15p, [U-99% 13C; U-99% 15N], 0.4 mM; sodium phosphate 20 mM; Nacl 50 mM; DTT 25 mM; D2O 100%

sample_6: Rna14p, [U-100% 13C; U-100% 15N; U-100% 2H, 1H-methyl Ile(delta 1),Leu,Val], 0.5 mM; Rna15p, [U-100% 13C; U-100% 15N; U-100% 2H, 1H-methyl Ile(delta 1),Leu,Val], 0.5 mM; sodium phosphate 20 mM; Nacl 50 mM; DTT 25 mM; H2O 90%; D2O 10%

sample_7: Rna14p, [U-100% 13C; U-100% 15N; U-100% 2H, 1H-methyl Ile(delta 1),Leu,Val], 0.5 mM; Rna15p, [U-100% 13C; U-100% 15N; U-100% 2H, 1H-methyl Ile(delta 1),Leu,Val], 0.5 mM; sodium phosphate 20 mM; Nacl 50 mM; DTT 25 mM; D2O 100%

sample_8: Rna14p, [U-99% 15N];[U-99% 13C]-Leu, 1.0 mM; Rna15p, [U-99% 15N];[U-99% 13C]-Leu, 1.0 mM; sodium phosphate 20 mM; Nacl 50 mM; DTT 25 mM; H2O 90%; D2O 10%

sample_9: Rna14p, [U-99% 15N];[U-99% 13C]-Leu, 1.0 mM; Rna15p, [U-99% 15N];[U-99% 13C]-Leu, 1.0 mM; sodium phosphate 20 mM; Nacl 50 mM; DTT 25 mM; D2O 100%

sample_10: Rna14p, [U-10% 13C; U-99% 15N], 1.0 mM; Rna15p, [U-10% 13C; U-99% 15N], 1.0 mM; sodium phosphate 20 mM; Nacl 50 mM; DTT 25 mM; D2O 100%

sample_conditions_1: ionic strength: 70 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N TROSYsample_2isotropicsample_conditions_1
2D 1H-15N HMBCsample_2isotropicsample_conditions_1
2D DQF-COSYsample_3isotropicsample_conditions_1
3D H(CCO)NHsample_4isotropicsample_conditions_1
2D 1H-13C HSQCsample_5isotropicsample_conditions_1
2D HBHDsample_5isotropicsample_conditions_1
2D HBHEsample_5isotropicsample_conditions_1
3D HCACOsample_5isotropicsample_conditions_1
3D HC(C)H-TOCSYsample_5isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_5isotropicsample_conditions_1
3D C(CO)NHsample_6isotropicsample_conditions_1
2D 1H-13C HSQCsample_7isotropicsample_conditions_1
3D HC(C)H-TOCSYsample_7isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_7isotropicsample_conditions_1
2D HNCOsample_8isotropicsample_conditions_1
3D HCACOsample_9isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_9isotropicsample_conditions_1
3D HC(C)H-TOCSYsample_9isotropicsample_conditions_1
2D 1H-13C HSQC-CTsample_10isotropicsample_conditions_1

Software:

TOPSPIN v2.0, Bruker Biospin - collection

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

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ GAA25502 GAA23344
EMBL CAA89771 CAY81879 CAA96746 CAY79715
GB AAA21300 AHY76517 AJP40760 AJS61929 AJS62366 AAA34984 AHY79328 EDN61560 EDV10275 EDZ72171
REF NP_013777 NP_011471
SP P25298 P25299
TPG DAA09959 DAA08056
AlphaFold P25298 P25299

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