BMRB Entry 18156
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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/BMR18156
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Title: Solution NMR Structure of the mitochondrial inner membrane domain (residues 164-251), FtsH_ext, from the paraplegin-like protein AFGL32 from Homo sapiens, Northeast Structural Genomics Consortium Target HR6741A
Deposition date: 2011-12-20 Original release date: 2012-02-06
Authors: Ramelot, Theresa; Yang, Yunhuang; Lee, Hsiau-Wei; Janua, Haleema; Kohan, Eitan; Shastry, Ritu; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Kennedy, Michael
Citation: Ramelot, Theresa; Yang, Yunhuang; Lee, Hsiau-Wei; Janua, Haleema; Kohan, Eitan; Shastry, Ritu; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Kennedy, Michael. "Northeast Structural Genomics Consortium Target HR6741A" To be published ., .-..
Assembly members:
HR6741A, polymer, 99 residues, 11999.1 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):
HR6741A: MGHHHHHHSHMKRSGREITW
KDFVNNYLSKGVVDRLEVVN
KRFVRVTFTPGKTPVDGQYV
WFNIGSVDTFERNLETLQQE
LGIEGENRVPVVYIAESDG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 420 |
| 15N chemical shifts | 101 |
| 1H chemical shifts | 657 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HR6741A | 1 |
Entities:
Entity 1, HR6741A 99 residues - 11999.1 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | MET | LYS | ARG | SER | GLY | ARG | GLU | ILE | THR | TRP | ||||
| 3 | LYS | ASP | PHE | VAL | ASN | ASN | TYR | LEU | SER | LYS | ||||
| 4 | GLY | VAL | VAL | ASP | ARG | LEU | GLU | VAL | VAL | ASN | ||||
| 5 | LYS | ARG | PHE | VAL | ARG | VAL | THR | PHE | THR | PRO | ||||
| 6 | GLY | LYS | THR | PRO | VAL | ASP | GLY | GLN | TYR | VAL | ||||
| 7 | TRP | PHE | ASN | ILE | GLY | SER | VAL | ASP | THR | PHE | ||||
| 8 | GLU | ARG | ASN | LEU | GLU | THR | LEU | GLN | GLN | GLU | ||||
| 9 | LEU | GLY | ILE | GLU | GLY | GLU | ASN | ARG | VAL | PRO | ||||
| 10 | VAL | VAL | TYR | ILE | ALA | GLU | SER | ASP | GLY |
Samples:
HR6741.001: HR6741A, [U-100% 13C; U-100% 15N], 0.7 mM; sodium chloride 200 mM; MES 20 mM; calcium chloride 5 mM; DTT 10 mM; DSS 10 uM; sodium azide 0.02%; H2O 90%; D2O 10%
HR6741.002: HR6741A, NC5, 1.0 mM; sodium chloride 200 mM; MES 20 mM; calcium chloride 5 mM; DTT 10 mM; DSS 10 uM; sodium azide 0.02%; H2O 90%; D2O 10%
HR6741.001_D2O: HR6741A, [U-100% 13C; U-100% 15N], 0.7 mM; sodium chloride 200 mM; MES 20 mM; calcium chloride 5 mM; DTT 10 mM; DSS 10 uM; sodium azide 0.02%; D2O 100%
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | HR6741.001 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | HR6741.001 | isotropic | sample_conditions_1 |
| 3D HNCO | HR6741.001 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | HR6741.001 | isotropic | sample_conditions_1 |
| 3D HNCACB | HR6741.001 | isotropic | sample_conditions_1 |
| 3D 1H-13C arom NOESY | HR6741.001 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESYaliph | HR6741.001 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | HR6741.001 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | HR6741.002 | isotropic | sample_conditions_1 |
| 2D 1H-15N hetNOE | HR6741.002 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | HR6741.001 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | HR6741.001 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | HR6741.001 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | HR6741.001 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | HR6741.001 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | HR6741.001 | isotropic | sample_conditions_1 |
| 4D CC-HMQC-NOESY-HMQC | HR6741.001_D2O | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | HR6741.001_D2O | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | HR6741.001_D2O | isotropic | sample_conditions_1 |
Software:
CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement,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
NMRPipe v2008 linux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN v2.1.4 and 3.1, Bruker Biospin - collection
VNMRJ, Varian - collection
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
SPARKY v3.113, Goddard - data analysis
TALOS+ v1.2009.0721.18, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PALES v2000, PALES (Zweckstetter, Bax) - geometry optimization
PSVS v1.4, Bhattacharya, Montelione - structure validation
X-PLOR NIH v2.25, Schwieters, Kuszewski, Tjandra and Clore - structure determination
NMR spectrometers:
- Bruker AvanceIII 850 MHz
- Varian INOVA 600 MHz
- Bruker AvanceIII 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAE29204 BAE30959 BAE31449 |
| EMBL | CAB48398 |
| GB | AAH24282 AAH36999 AAH43056 AAH65016 AAI05323 |
| REF | NP_001039676 NP_001128336 NP_006787 NP_081406 XP_001094146 |
| SP | Q2KJI7 Q8JZQ2 Q9Y4W6 |
| TPG | DAA15802 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts