BMRB Entry 15100

Title:
NMR structure of E.coli YfgJ protein modelled with two Zn+2 bound. Northeast Structural Genomics Consortium Target ER317.
Deposition date:
2007-01-12
Original release date:
2007-10-03
Authors:
Ramelot, Theresa; Cort, John; Yee, Adelinda; Semesi, Anthony; Johnathan, Lukin; Arrowsmith, Cheryl; Kennedy, Michael
Citation:

Citation: Ramelot, Theresa; Cort, John; Yee, Adelinda; Arrowsmith, Cheryl; Kennedy, Michael. "NMR structure of E.coli YfgJ protein modelled with two Zn+2 bound. Northeast Structural Genomics Consortium Target ER317."  .

Assembly members:

Assembly members:
YfgJ protein, polymer, 101 residues, 8010.390 Da.
ZN, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts302
15N chemical shifts71
1H chemical shifts478

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YfgJ protein1
21st Zn+22
32nd Zn+22

Entities:

Entity 1, YfgJ protein 101 residues - 8010.390 Da.

30 NON-NATIVE N-TERMINAL RESIDUES (FCLTLRRRYTMGSSHHHHHHSSGLVPRGSH) WERE NOT INCLUDED IN THE STRUCTURE CALCULATION.

1   PHECYSLEUTHRLEUARGARGARGTYRTHR
2   METGLYSERSERHISHISHISHISHISHIS
3   SERSERGLYLEUVALPROARGGLYSERHIS
4   METGLULEUHISCYSPROGLNCYSGLNHIS
5   VALLEUASPGLNASPASNGLYHISALAARG
6   CYSARGSERCYSGLYGLUPHEILEGLUMET
7   LYSALALEUCYSPROASPCYSHISGLNPRO
8   LEUGLNVALLEULYSALACYSGLYALAVAL
9   ASPTYRPHECYSGLNHISGLYHISGLYLEU
10   ILESERLYSLYSARGVALGLUPHEVALLEU
11   ALA

Entity 2, 1st Zn+2 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: protein, [U-100% 13C], 1 ± 0.2 mM; TRIS 10 ± 1 mM; sodium chloride 250 ± 5 mM; ZINC ION 10 ± 1 uM; DTT 10 ± 1 mM; sodium azide 0.01 ± 0.001 %

sample_conditions_1: ionic strength: 250 mM; pH: 7.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

AutoStruct v2.1.1, Huang, Swapana, Rajan, Ke, Xia, Shukla, Inouye and Montelione - data analysis

X-PLOR NIH v2.15.0, Schwieters, Kuszewski, Tjandra and Clore - structure solution

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.1, Goddard - peak picking

NMRPipe vlinux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz
  • Varian INOVA 800 MHz

Related Database Links:

SWS P76575
PDB
DBJ BAE76728 BAI31784 BAJ44293 BAL39266
EMBL CAQ32881 CBJ02173 CCP95953 CCQ02273 CDJ72855
GB AAC75563 ABV17482 ACB03662 ACD09416 ACR64901
REF NP_417005 WP_001295478 WP_001297332 WP_001301158 WP_001341056
SP P76575
AlphaFold P76575

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