BMRB Entry 11570
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR11570
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Title: Solution Structure of the Bacillus anthracis Sortase A-substrate Complex
Deposition date: 2014-06-21 Original release date: 2015-09-10
Authors: Chan, Albert; Yi, Sung Wook; Jung, Michael; Clubb, Robert
Citation: Chan, Albert; Yi, Sung Wook; Jung, Michael; Clubb, Robert. "Structure of the Bacillus anthracis Sortase-Substrate Complex Reveals Important Roles of the N-terminus Tail in Transpeptidation Reaction" J. Biol. Chem. ., .-..
Assembly members:
BaSrtA, polymer, 158 residues, 17110.521 Da.
Boc-LPAT*, polymer, 5 residues, 402.551 Da.
Natural source: Common Name: Bacillus anthracis Taxonomy ID: 1392 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus anthracis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
BaSrtA: GSHMDASKIDQPDLAEVANA
SLDKKQVIGRISIPSVSLEL
PVLKSSTEKNLLSGAATVKE
NQVMGKGNYALAGHNMSKKG
VLFSDIASLKKGDKIYLYDN
ENEYEYAVTGVSEVTPDKWE
VVEDHGKDEITLITCVSVKD
NSKRYVVAGDLVGTKAKK
Boc-LPAT*: XLPAX
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 642 |
| 15N chemical shifts | 152 |
| 1H chemical shifts | 1004 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 158 residues - 17110.521 Da.
First four residues represent a non-native tag left over from cleaving off the 6xHis tag using Thrombin
| 1 | GLY | SER | HIS | MET | ASP | ALA | SER | LYS | ILE | ASP | ||||
| 2 | GLN | PRO | ASP | LEU | ALA | GLU | VAL | ALA | ASN | ALA | ||||
| 3 | SER | LEU | ASP | LYS | LYS | GLN | VAL | ILE | GLY | ARG | ||||
| 4 | ILE | SER | ILE | PRO | SER | VAL | SER | LEU | GLU | LEU | ||||
| 5 | PRO | VAL | LEU | LYS | SER | SER | THR | GLU | LYS | ASN | ||||
| 6 | LEU | LEU | SER | GLY | ALA | ALA | THR | VAL | LYS | GLU | ||||
| 7 | ASN | GLN | VAL | MET | GLY | LYS | GLY | ASN | TYR | ALA | ||||
| 8 | LEU | ALA | GLY | HIS | ASN | MET | SER | LYS | LYS | GLY | ||||
| 9 | VAL | LEU | PHE | SER | ASP | ILE | ALA | SER | LEU | LYS | ||||
| 10 | LYS | GLY | ASP | LYS | ILE | TYR | LEU | TYR | ASP | ASN | ||||
| 11 | GLU | ASN | GLU | TYR | GLU | TYR | ALA | VAL | THR | GLY | ||||
| 12 | VAL | SER | GLU | VAL | THR | PRO | ASP | LYS | TRP | GLU | ||||
| 13 | VAL | VAL | GLU | ASP | HIS | GLY | LYS | ASP | GLU | ILE | ||||
| 14 | THR | LEU | ILE | THR | CYS | VAL | SER | VAL | LYS | ASP | ||||
| 15 | ASN | SER | LYS | ARG | TYR | VAL | VAL | ALA | GLY | ASP | ||||
| 16 | LEU | VAL | GLY | THR | LYS | ALA | LYS | LYS |
Entity 2, entity_2 5 residues - 402.551 Da.
| 1 | BOC | LEU | PRO | ALA | B27 |
Samples:
sample_1: BaSrtA, [U-100% 13C; U-100% 15N], 2.6 mM; Boc-LPAT 2.6 mM; sodium phosphate 50 mM; sodium azide 0.01%; H2O 93%; D2O, [U-2H], 7%
sample_2: BaSrtA, [U-100% 13C; U-100% 15N], 2.6 mM; Boc-LPAT 2.6 mM; sodium phosphate 50 mM; sodium azide 0.01%; D2O, [U-2H], 100%
sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR_NIH v2.25, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
ModelFree, Palmer - data analysis
Molmol, Koradi, Billeter and Wuthrich - data analysis
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PIPP, Garrett - peak picking
Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton - data analysis
SPARKY, Goddard - data analysis
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
xwinnmr, Bruker Biospin - collection, data analysis
CARA, Keller and Wuthrich - chemical shift assignment, peak picking
UNIO v10, Herrmann, Guntert and Wuthrich - peak picking, structure solution
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| BMRB | 16811 26510 |
| PDB | |
| DBJ | BAL16456 BAR78533 GAE96182 GAO57723 GAO63420 |
| EMBL | CJA38300 CJJ39486 CKE38654 CKE81514 CKE96545 |
| GB | AAP24701 AAS39688 AAT29792 AAT52982 AAU19641 |
| REF | NP_843215 WP_001041406 WP_001041710 WP_001041711 WP_001041715 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts