BMRB Entry 15335
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15335
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Title: Structure of Staphylococcus saprophyticus CHAP domain protein. Northeast Structural Genomics Target SyR11. PubMed: 18951393
Deposition date: 2007-06-27 Original release date: 2007-08-07
Authors: Rossi, Paolo; Aramini, James; Chen, Chen; Nwosu, Chioma; Cunningham, Kellie; Owens, Leah; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano
Citation: Rossi, Paolo; Aramini, James; Xiao, Rong; Chen, Chen; Nwosu, Chioma; Owens, Leah; Maglaqui, Melissa; Nair, Rajesh; Fischer, Markus; Acton, Thomas; Honig, Barry; Rost, Burkhard; Montelione, Gaetano. "Structural elucidation of the Cys-His-Glu-Asn proteolytic relay in the secreted CHAP domain enzyme from the human pathogen Staphylococcus saprophyticus." Proteins 74, 515-9 (2009).
Assembly members:
SyR11, polymer, 163 residues, 16997.244 Da.
Natural source: Common Name: Staphylococcus saprophyticus Taxonomy ID: 29385 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus saprophyticus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SyR11: MKKLVTATTLTAGIGAAIVG
LDHGNEADAAEQTQPTNQST
TQSTSGSSANLYTAGQCTWY
VYDKVGGNIGSTWGNANNWA
SAASSAGYTVNNSPEAGSIL
QSTAGGYGHVAYVENVNSDG
SVEVSEMNYNGGPFSVSERT
ISAGEASSYNYIHLNLEHHH
HHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 608 |
| 15N chemical shifts | 178 |
| 1H chemical shifts | 954 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SyR11 | 1 |
Entities:
Entity 1, SyR11 163 residues - 16997.244 Da.
C term LEHHHHHH tag
| 1 | MET | LYS | LYS | LEU | VAL | THR | ALA | THR | THR | LEU | ||||
| 2 | THR | ALA | GLY | ILE | GLY | ALA | ALA | ILE | VAL | GLY | ||||
| 3 | LEU | ASP | HIS | GLY | ASN | GLU | ALA | ASP | ALA | ALA | ||||
| 4 | GLU | GLN | THR | GLN | PRO | THR | ASN | GLN | SER | THR | ||||
| 5 | THR | GLN | SER | THR | SER | GLY | SER | SER | ALA | ASN | ||||
| 6 | LEU | TYR | THR | ALA | GLY | GLN | CYS | THR | TRP | TYR | ||||
| 7 | VAL | TYR | ASP | LYS | VAL | GLY | GLY | ASN | ILE | GLY | ||||
| 8 | SER | THR | TRP | GLY | ASN | ALA | ASN | ASN | TRP | ALA | ||||
| 9 | SER | ALA | ALA | SER | SER | ALA | GLY | TYR | THR | VAL | ||||
| 10 | ASN | ASN | SER | PRO | GLU | ALA | GLY | SER | ILE | LEU | ||||
| 11 | GLN | SER | THR | ALA | GLY | GLY | TYR | GLY | HIS | VAL | ||||
| 12 | ALA | TYR | VAL | GLU | ASN | VAL | ASN | SER | ASP | GLY | ||||
| 13 | SER | VAL | GLU | VAL | SER | GLU | MET | ASN | TYR | ASN | ||||
| 14 | GLY | GLY | PRO | PHE | SER | VAL | SER | GLU | ARG | THR | ||||
| 15 | ILE | SER | ALA | GLY | GLU | ALA | SER | SER | TYR | ASN | ||||
| 16 | TYR | ILE | HIS | LEU | ASN | LEU | GLU | HIS | HIS | HIS | ||||
| 17 | HIS | HIS | HIS |
Samples:
sample_1: SyR11, [U-100% 13C; U-100% 15N], 0.66 mM; MES 20 mM; sodium azide 0.02%; DTT 100 mM; calcium chloride 5 mM; sodium chloride 100 mM
sample_2: SyR11, [U-100% 13C; U-100% 15N], 0.66 mM; MES 20 mM; sodium azide 0.02%; DTT 100 mM; calcium chloride 5 mM; sodium chloride 100 mM
sample_3: SyR11, [U-5% 13C; U-100% 15N], 0.94 mM; MES 20 mM; sodium azide 0.02%; DTT 100 mM; calcium chloride 5 mM; sodium chloride 100 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCOCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY (aliph) | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY (arom) | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| HETnoe | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (aliph) | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (arom) | sample_1 | isotropic | sample_conditions_1 |
Software:
AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - structure solution
SPARKY v3.110, Goddard - data analysis
TOPSPIN v1.3, Bruker Biospin - collection
Molmol v2K.2, Koradi, Billeter and Wuthrich - visualization
X-PLOR NIH v2.11.2, Schwieters, Kuszewski, Tjandra and Clore - refinement
PSVS v1.3, Bhattacharya and Montelione - validation
DYANA, Guntert, Braun and Wuthrich - refinement
CNSSOLVE v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
MolProbity, Richardson - validation
PDBStat v5.0, PDBStat (Tejero) - refinement
ProcheckNMR, Laskowski and MacArthur - refinement
NMRPipe v2.4, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| EMBL | AP008934 CRV28521 |
| SWS | Q49ZM2_STAS1 |
| PDB | |
| DBJ | BAE17754 |
| GB | EHY93150 KIJ87710 |
| REF | WP_002482559 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts