BMRB Entry 18489

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: LACS
BMRB Entry DOI: doi:10.13018/BMR18489
MolProbity Validation Chart

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Title:
Solution NMR Structure of NFU1 Iron-Sulfur Cluster Scaffold Homolog from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR2876B
Deposition date:
2012-05-29
Original release date:
2012-07-23
Authors:
Liu, Gaohua; Xiao, Rong; Janjua, Haleema; Hamilton, Keith; Shastry, Ritu; Kohan, Eitan; Acton, Thomas; Everett, John; Lee, Hsiau-Wei; Huang, Yuangpeng; Montelione, Gaetano; Northeast Structural Genomics Consortium, NESG
Citation:

Citation: Liu, Gaohua; Xiao, Rong; Janjua, Haleema; Hamilton, Keith; Shastry, Ritu; Kohan, Eitan; Acton, Thomas; Everett, John; Lee, Hsiau-Wei; Huang, Yuangpeng; Montelione, Gaetano. "Solution NMR Structure of NFU1 Iron-Sulfur Cluster Scaffold Homolog from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR2876B"  To be published ., .-..

Assembly members:

Assembly members:
HR2876B, polymer, 107 residues, 12201.979 Da.

Natural source:

Natural source:   Common Name: Humans   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HR2876B: MGHHHHHHSHMFIQTQDTPN PNSLKFIPGKPVLETRTMDF PTPAAAFRSPLARQLFRIEG VKSVFFGPDSITVTKENEEL DWNLLKPDIYATIMDFFASG LPLVTEE

Data sets:
Data typeCount
13C chemical shifts448
15N chemical shifts90
1H chemical shifts713
residual dipolar couplings147

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR2876B1

Entities:

Entity 1, HR2876B 107 residues - 12201.979 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METPHEILEGLNTHRGLNASPTHRPROASN
3   PROASNSERLEULYSPHEILEPROGLYLYS
4   PROVALLEUGLUTHRARGTHRMETASPPHE
5   PROTHRPROALAALAALAPHEARGSERPRO
6   LEUALAARGGLNLEUPHEARGILEGLUGLY
7   VALLYSSERVALPHEPHEGLYPROASPSER
8   ILETHRVALTHRLYSGLUASNGLUGLULEU
9   ASPTRPASNLEULEULYSPROASPILETYR
10   ALATHRILEMETASPPHEPHEALASERGLY
11   LEUPROLEUVALTHRGLUGLU

Samples:

sample_NC: HR2876B.035, [U-100% 13C; U-100% 15N], 0.896 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl pH 7.5 10 mM; H2O 90%; D2O 10%

sample_NC5: HR2876B.037, [U-5% 13C; U-100% 15N], 0.92 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl pH 7.5 10 mM; H2O 90%; D2O 10%

sample_NC5_RDC: HR2876B.039, [U-5% 13C; U-100% 15N], 0.92 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl pH 7.5 10 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_NCisotropicsample_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_NC5_RDCisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_NC5isotropicsample_conditions_1
3D HCCH-TOCSYsample_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

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 BAB22965 BAC24985 BAE26508 BAG36716
EMBL CAB53015 CAB57314
GB AAH18355 AAI05370 AAQ73785 AAY14828 EDK99197
REF NP_001040031 NP_001100076 NP_001164062 NP_064429 XP_001491099
SP Q9QZ23
TPG DAA24542
AlphaFold Q9QZ23

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