BMRB Entry 18487

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18487
MolProbity Validation Chart

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Title:
Solution NMR Structure of NifU-like protein from Saccharomyces cerevisiae, Northeast Structural Genomics Consortium (NESG) Target YR313A
Deposition date:
2012-05-29
Original release date:
2012-07-02
Authors:
Liu, Gaohua; Xiao, Rong; Hamilton, Keith; Janjua, Haleema; Shastry, Ritu; Kohan, Eitan; Acton, Thomas; Everett, John; Lee, Hsiau-Wei; Huang, Yuangpeng; Montelione, Gaetano
Citation:

Citation: Liu, Gaohua; Xiao, Rong; Hamilton, Keith; Janjua, Haleema; Shastry, Ritu; Kohan, Eitan; Acton, Thomas; Everett, John; Lee, Hsiau-Wei; Huang, Yuangpeng; Montelione, Gaetano. "Solution NMR Structure of NifU-like protein from Saccharomyces cerevisiae, Northeast Structural Genomics Consortium (NESG) Target YR313A"  To be published ., .-..

Assembly members:

Assembly members:
YR313A, polymer, 119 residues, 13639.707 Da.

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: pET15_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
YR313A: MGHHHHHHSHMNSQRLIHIK TLTTPNENALKFLSTDGEML QTRGSKSIVIKNTDENLINH SKLAQQIFLQCPGVESLMIG DDFLTINKDRMVHWNSIKPE IIDLLTKQLAYGEDVISKE

Data sets:
Data typeCount
13C chemical shifts386
15N chemical shifts119
1H chemical shifts812

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YR313A1

Entities:

Entity 1, YR313A 119 residues - 13639.707 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METASNSERGLNARGLEUILEHISILELYS
3   THRLEUTHRTHRPROASNGLUASNALALEU
4   LYSPHELEUSERTHRASPGLYGLUMETLEU
5   GLNTHRARGGLYSERLYSSERILEVALILE
6   LYSASNTHRASPGLUASNLEUILEASNHIS
7   SERLYSLEUALAGLNGLNILEPHELEUGLN
8   CYSPROGLYVALGLUSERLEUMETILEGLY
9   ASPASPPHELEUTHRILEASNLYSASPARG
10   METVALHISTRPASNSERILELYSPROGLU
11   ILEILEASPLEULEUTHRLYSGLNLEUALA
12   TYRGLYGLUASPVALILESERLYSGLU

Samples:

sample_NC: YR313A.037, [U-100% 13C; U-100% 15N], 1.027 mM; NaCl 450 mM; Na2PO4 25 mM; DTT 10 mM; ZnSO4 20 uM; Proteinase inhibitors 1 X; NaN3 0.02%; D2O 10%; H2O 90%

sample_NC5: YR313A.040, [U-10% 13C; U-100% 15N], 0.52 mM; NaCl 450 mM; Na2PO4 25 mM; DTT 10 mM; ZnSO4 20 uM; Proteinase inhibitors 1 X; NaN3 0.02%; D2O 10%; H2O 90%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_NC5isotropicsample_conditions_1
3D HNCOsample_NCisotropicsample_conditions_1
3D CBCA(CO)NHsample_NCisotropicsample_conditions_1
3D HNCACBsample_NCisotropicsample_conditions_1
3D 1H-13C arom NOESYsample_NCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_NCisotropicsample_conditions_1
2D 1H-15N HSQCsample_NC5isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_NCisotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

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

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

REDCAT, Valafar, Prestegard - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ GAA24684
EMBL CAA49299 CAA81875 CAY81046
GB AAS56230 AHY76203 AJP39997 AJS30195 AJS30496
REF NP_012884
SP P32860
TPG DAA09116
AlphaFold P32860

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