BMRB Entry 15486

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15486

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Title:
Complete Chemical Shift Assignments and XPLOR restraints for YmoA
Deposition date:
2007-09-24
Original release date:
2008-03-12
Authors:
McFeeters, Robert; Byrd, R. Andrew
Citation:

Citation: McFeeters, Robert; Altieri, Amanda; Cherry, Scott; Tropea, Joseph; Waugh, David; Byrd, R. Andrew. "The high-precision solution structure of Yersinia modulating protein YmoA provides insight into interaction with H-NS"  Biochemistry 46, 13975-13982 (2007).
PubMed: 18001134

Assembly members:

Assembly members:
YmoA, polymer, 73 residues, 8833.160 Da.

Natural source:

Natural source:   Common Name: Yersinia pestis   Taxonomy ID: 632   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Yersinia pestis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: derivative of pMal-C2 (Invitrogen)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
YmoA: GTKTDYLMRLRKCTTIDTLE RVIEKNKYELSDDELELFYS AADHRLAELTMNKLYDKIPP TVWQHVKHHHHHH

Data sets:
Data typeCount
13C chemical shifts319
15N chemical shifts67
1H chemical shifts498
T1 relaxation values62
T2 relaxation values62

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ymoa_11

Entities:

Entity 1, ymoa_1 73 residues - 8833.160 Da.

1   GLYTHRLYSTHRASPTYRLEUMETARGLEU
2   ARGLYSCYSTHRTHRILEASPTHRLEUGLU
3   ARGVALILEGLULYSASNLYSTYRGLULEU
4   SERASPASPGLULEUGLULEUPHETYRSER
5   ALAALAASPHISARGLEUALAGLULEUTHR
6   METASNLYSLEUTYRASPLYSILEPROPRO
7   THRVALTRPGLNHISVALLYSHISHISHIS
8   HISHISHIS

Samples:

sample_1: YmoA, [U-99% 13C; U-99% 15N], 1 mM; Sodium Phosphate 50 mM; NaCl 150 mM; DTT 5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 150 mM; pH: 6; 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 HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
Jmod-NHsample_1anisotropicsample_conditions_1
Jmod-HaCasample_1anisotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
15N T1sample_1isotropicsample_conditions_1
15N T2sample_1isotropicsample_conditions_1
Jmod-CoCasample_1anisotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

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

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
DBJ GAE11657
EMBL CAA41091 CAH20218 CAL13150 CAL21733 CBX70721
GB AAM84627 AAQ90017 AAS61058 AAY16112 AAY16113
REF WP_002208622 WP_016257260 WP_016261370 WP_016582302 WP_016590523
SP P0A3X0 P0A3X1
AlphaFold P0A3X0 P0A3X1

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