BMRB Entry 18489
Click here to enlarge.
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
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
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: 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:
HR2876B, polymer, 107 residues, 12201.979 Da.
Natural source: Common Name: Humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
HR2876B: MGHHHHHHSHMFIQTQDTPN
PNSLKFIPGKPVLETRTMDF
PTPAAAFRSPLARQLFRIEG
VKSVFFGPDSITVTKENEEL
DWNLLKPDIYATIMDFFASG
LPLVTEE
- assigned_chemical_shifts
- RDCs
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 448 |
| 15N chemical shifts | 90 |
| 1H chemical shifts | 713 |
| residual dipolar couplings | 147 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HR2876B | 1 |
Entities:
Entity 1, HR2876B 107 residues - 12201.979 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | MET | PHE | ILE | GLN | THR | GLN | ASP | THR | PRO | ASN | ||||
| 3 | PRO | ASN | SER | LEU | LYS | PHE | ILE | PRO | GLY | LYS | ||||
| 4 | PRO | VAL | LEU | GLU | THR | ARG | THR | MET | ASP | PHE | ||||
| 5 | PRO | THR | PRO | ALA | ALA | ALA | PHE | ARG | SER | PRO | ||||
| 6 | LEU | ALA | ARG | GLN | LEU | PHE | ARG | ILE | GLU | GLY | ||||
| 7 | VAL | LYS | SER | VAL | PHE | PHE | GLY | PRO | ASP | SER | ||||
| 8 | ILE | THR | VAL | THR | LYS | GLU | ASN | GLU | GLU | LEU | ||||
| 9 | ASP | TRP | ASN | LEU | LEU | LYS | PRO | ASP | ILE | TYR | ||||
| 10 | ALA | THR | ILE | MET | ASP | PHE | PHE | ALA | SER | GLY | ||||
| 11 | LEU | PRO | LEU | VAL | THR | GLU | GLU |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_NC | isotropic | sample_conditions_1 |
| 3D HNCO | sample_NC | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_NC | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_NC | isotropic | sample_conditions_1 |
| 3D 1H-13C arom NOESY | sample_NC | isotropic | sample_conditions_1 |
| 3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | sample_NC | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_NC5_RDC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_NC5 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_NC | isotropic | sample_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 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts