BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19688

Title: 1H, 15N and 13C resonance assignments of the yeast Pih1 and Tah1 C-terminal domains complex   PubMed: 24493341

Authors: Clemence, Jacquemin; Charpentier, Bruno; Manival, Xavier; Quinternet, Marc

Citation: Manival, Xavier; Jacquemin, Clemence; Charpentier, Bruno; Quinternet, Marc. "1H, 15N and 13C resonance assignments of the yeast Pih1 and Tah1 C-terminal domains complex"  Biomol. NMR Assignments ., .-..

Assembly members:
Tah1(93-111), polymer, 23 residues, Formula weight is not available
Pih1(257-344), polymer, 88 residues, Formula weight is not available

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
Tah1(93-111): GPHMSVQIPVVEVDELPEGY DRS
Pih1(257-344): PHEQQEDVPEYEVKMKRFKG AAYKLRILIENKAPNSKPDR FSPSYNFAENILYINGKLSI PLPRDIVVNAADIKIFHIRK ERTLYIYI

Data sets:
Data typeCount
13C chemical shifts490
15N chemical shifts105
1H chemical shifts799

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Tah1, (93-111)1
2Pih1, (257-344)2

Entities:

Entity 1, Tah1, (93-111) 23 residues - Formula weight is not available

1   GLYPROHISMETSERVALGLNILEPROVAL
2   VALGLUVALASPGLULEUPROGLUGLYTYR
3   ASPARGSER

Entity 2, Pih1, (257-344) 88 residues - Formula weight is not available

1   PROHISGLUGLNGLNGLUASPVALPROGLU
2   TYRGLUVALLYSMETLYSARGPHELYSGLY
3   ALAALATYRLYSLEUARGILELEUILEGLU
4   ASNLYSALAPROASNSERLYSPROASPARG
5   PHESERPROSERTYRASNPHEALAGLUASN
6   ILELEUTYRILEASNGLYLYSLEUSERILE
7   PROLEUPROARGASPILEVALVALASNALA
8   ALAASPILELYSILEPHEHISILEARGLYS
9   GLUARGTHRLEUTYRILETYRILE

Samples:

sample_1: Tah1(93-111), [U-100% 13C; U-100% 15N], 1.5 mM; Pih1(257-344), [U-100% 13C; U-100% 15N], 1.5 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.4; pressure: 1 atm; temperature: 298 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 HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 17312 18445 18447
PDB
DBJ GAA21965 GAA23749
EMBL CAA42288 CAY78265 CAY80321
GB AAS56477 AHN96120 AHV79323 AHY79733 AJP37484 AAB68914 AHY77731 EDN62271 EDV09085 EEU05764
REF NP_009986 NP_011899
SP P25638 P38768
TPG DAA07534 DAA06725