BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15327

Title: Chemical Shift Assignments for E. coli protein YqcC: Northeast Structural Genomics Consortium target ER225

Authors: Cort, John

Citation: Cort, John. "Solution NMR Structure of protein YqcC from E. coli"  Not known ., .-..

Assembly members:
YqcC, polymer, 117 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
YqcC: MTTHDRVRLQLQALEALLRE HQHWRNDEPQPHQFNSTQPF FMDTMEPLEWLQWVLIPRMH DLLDNKQPLPGAFAVAPYYE MALATDHPQRALILAELEKL DALFADDASLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts420
15N chemical shifts99
1H chemical shifts692

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YqcC1

Entities:

Entity 1, YqcC 117 residues - Formula weight is not available

1   METTHRTHRHISASPARGVALARGLEUGLN
2   LEUGLNALALEUGLUALALEULEUARGGLU
3   HISGLNHISTRPARGASNASPGLUPROGLN
4   PROHISGLNPHEASNSERTHRGLNPROPHE
5   PHEMETASPTHRMETGLUPROLEUGLUTRP
6   LEUGLNTRPVALLEUILEPROARGMETHIS
7   ASPLEULEUASPASNLYSGLNPROLEUPRO
8   GLYALAPHEALAVALALAPROTYRTYRGLU
9   METALALEUALATHRASPHISPROGLNARG
10   ALALEUILELEUALAGLULEUGLULYSLEU
11   ASPALALEUPHEALAASPASPALASERLEU
12   GLUHISHISHISHISHISHIS

Samples:

sample_1: YqcC, [biosynthetically-directed-5% 13C; U-100% 15N], 1.2 ± 0.25 mM; D2O, [U-100% 2H], 5%; sodium chloride 100 mM; MES 20 mM; calcium chloride 5 mM; sodium azide 0.02%

sample_2: YqcC, [U-100% 13C; U-100% 15N], 1.2 ± 0.25 mM; D2O, 100%, 100%; sodium chloride 100 mM; MES 20 mM; calcium chloride 5 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 115 mM; pH: 6.5; 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 HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
4D 1H-13C-13C-1H NOESYsample_2isotropicsample_conditions_1
2D HBCBCGCDHD-aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

VNMR, Varian - collection

FELIX, Accelrys Software Inc. - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
DBJ BAB37075 BAE76864 BAG78576 BAI27053 BAI32082
EMBL CAP77225 CAQ33116 CAQ99720 CAR04302 CAR09405
GB AAB40442 AAC75834 AAG57906 AAN44293 AAN81805
REF NP_311679 NP_417272 NP_708586 WP_000206975 WP_000206977
SP Q46919