BMRB Entry 17683
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17683
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Title: Solution NMR Structure of Heat shock factor protein 1 DNA binding domain from homo sapiens, Northeast Structural Genomics Consortium Target HR3023C
Deposition date: 2011-06-01 Original release date: 2011-07-05
Authors: Liu, G.; Xiao, R.; Ciccosanti, C.; Janjua, H.; Acton, T.; Lee, Hsiau-wei; Wang, H.; Huang, Yuanpeng; Everett, J.; Montelione, G.
Citation: Liu, G.; Xiao, R.; Ciccosanti, C.; Janjua, H.; Acton, T.; Wang, H.; Lee, Hsiau-wei; Huang, Yuanpeng; Everett, J.; Montelione, G.. "Northeast Structural Genomics Consortium Target HR3023C" To be published ., .-..
Assembly members:
HR3023C, polymer, 125 residues, 14401.479 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
HR3023C: MGHHHHHHSHMAGPSNVPAF
LTKLWTLVSDPDTDALICWS
PSGNSFHVFDQGQFAKEVLP
KYFKHNNMASFVRQLNMYGF
RKVVHIEQGGLVKPERDDTE
FQHPCFLRGQEQLLENIKRK
VTSVS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 528 |
| 15N chemical shifts | 120 |
| 1H chemical shifts | 830 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HR3023C | 1 |
Entities:
Entity 1, HR3023C 125 residues - 14401.479 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | MET | ALA | GLY | PRO | SER | ASN | VAL | PRO | ALA | PHE | ||||
| 3 | LEU | THR | LYS | LEU | TRP | THR | LEU | VAL | SER | ASP | ||||
| 4 | PRO | ASP | THR | ASP | ALA | LEU | ILE | CYS | TRP | SER | ||||
| 5 | PRO | SER | GLY | ASN | SER | PHE | HIS | VAL | PHE | ASP | ||||
| 6 | GLN | GLY | GLN | PHE | ALA | LYS | GLU | VAL | LEU | PRO | ||||
| 7 | LYS | TYR | PHE | LYS | HIS | ASN | ASN | MET | ALA | SER | ||||
| 8 | PHE | VAL | ARG | GLN | LEU | ASN | MET | TYR | GLY | PHE | ||||
| 9 | ARG | LYS | VAL | VAL | HIS | ILE | GLU | GLN | GLY | GLY | ||||
| 10 | LEU | VAL | LYS | PRO | GLU | ARG | ASP | ASP | THR | GLU | ||||
| 11 | PHE | GLN | HIS | PRO | CYS | PHE | LEU | ARG | GLY | GLN | ||||
| 12 | GLU | GLN | LEU | LEU | GLU | ASN | ILE | LYS | ARG | LYS | ||||
| 13 | VAL | THR | SER | VAL | SER |
Samples:
sample_NC: HR3023C, [U-100% 13C; U-100% 15N], 0.51 mM; H2O 90%; D2O 10%
sample_NC5: HR3023C, [U-100% 13C; U-100% 15N], 0.43 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES 20 mM; DSS 50 uM; D2O 10%; H2O 90%
sample_NC5_pol: HR3023C, [U-100% 13C; U-100% 15N], 0.43 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES 20 mM; DSS 50 uM; D2O 10%; H2O 90%
sample_NC5_peg: HR3023C, [U-100% 13C; U-100% 15N], 0.43 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES 20 mM; DSS 50 uM; D2O 10%; H2O 90%
sample_conditions_1: pH: 6.5; 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_NC5 | 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-13C HSQC aromatic | sample_NC | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_NC5_pol | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_NC5_peg | 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
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAD96217 BAF83664 BAG73234 BAK63583 |
| EMBL | CAA43892 CAD58796 |
| GB | AAA52695 AAC80425 AAH13716 AAH14638 AAH94064 |
| PRF | 2102256A |
| REF | NP_001070277 NP_001230748 NP_001266850 NP_001301273 NP_005517 |
| SP | P38532 Q00613 Q08DJ8 |
| TPG | DAA22852 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts