BMRB Entry 15281
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15281
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Title: Solution NMR structure of CC0527 from Caulobacter crescentus. Northeast Structural Genomics target CcR55.
Deposition date: 2007-06-05 Original release date: 2007-08-16
Authors: Aramini, James; Rossi, Paolo; Moseley, Hunter; Wang, Dongyan; Nwosu, Chioma; Cunningham, Kellie; Ma, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Micheal; Swapna, Gurla; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano
Citation: Aramini, James; Rossi, Paolo; Moseley, Hunter; Wang, Dongyan; Nwosu, Chioma; Cunningham, Kellie; Ma, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Micheal; Swapna, Gurla; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano. "Solution NMR structure of CC0527 from Caulobacter crescentus. Northeast Structural Genomics target CcR55." Not known ., .-..
Assembly members:
CcR55, polymer, 122 residues, 13533.255 Da.
Natural source: Common Name: Caulobacter crescentus Taxonomy ID: 155892 Superkingdom: Bacteria Kingdom: not available Genus/species: Caulobacter crescentus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CcR55: MTLIYKILSRAEWDAAKAQG
RFEGSAVDLADGFIHLSAGE
QAQETAAKWFRGQANLVLLA
VEAEPLGEDLKWEASRGGAR
FPHLYRPLLVSEVTREADLD
LDADGVPQLGDHLALEHHHH
HH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 510 |
| 15N chemical shifts | 122 |
| 1H chemical shifts | 805 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CcR55 | 1 |
Entities:
Entity 1, CcR55 122 residues - 13533.255 Da.
Residues 115-122 represent a non-native affinity purification tag (LEHHHHHH)
| 1 | MET | THR | LEU | ILE | TYR | LYS | ILE | LEU | SER | ARG | ||||
| 2 | ALA | GLU | TRP | ASP | ALA | ALA | LYS | ALA | GLN | GLY | ||||
| 3 | ARG | PHE | GLU | GLY | SER | ALA | VAL | ASP | LEU | ALA | ||||
| 4 | ASP | GLY | PHE | ILE | HIS | LEU | SER | ALA | GLY | GLU | ||||
| 5 | GLN | ALA | GLN | GLU | THR | ALA | ALA | LYS | TRP | PHE | ||||
| 6 | ARG | GLY | GLN | ALA | ASN | LEU | VAL | LEU | LEU | ALA | ||||
| 7 | VAL | GLU | ALA | GLU | PRO | LEU | GLY | GLU | ASP | LEU | ||||
| 8 | LYS | TRP | GLU | ALA | SER | ARG | GLY | GLY | ALA | ARG | ||||
| 9 | PHE | PRO | HIS | LEU | TYR | ARG | PRO | LEU | LEU | VAL | ||||
| 10 | SER | GLU | VAL | THR | ARG | GLU | ALA | ASP | LEU | ASP | ||||
| 11 | LEU | ASP | ALA | ASP | GLY | VAL | PRO | GLN | LEU | GLY | ||||
| 12 | ASP | HIS | LEU | ALA | LEU | GLU | HIS | HIS | HIS | HIS | ||||
| 13 | HIS | HIS |
Samples:
sample_1: CcR55, [U-100% 13C; U-100% 15N], 0.98 mM; MES 20 mM; NaCl 100 mM; CaCl2 5 mM; DTT 10 mM; NaN3 0.02%
sample_2: CcR55, [U-100% 13C; U-100% 15N], 0.98 mM; MES 20 mM; NaCl 100 mM; CaCl2 5 mM; DTT 10 mM; NaN3 0.02%
sample_3: CcR55, [U-5% 13C; U-100% 15N], 0.58 mM; MES 20 mM; NaCl 100 mM; CaCl2 5 mM; DTT 10 mM; NaN3 0.02%
sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (aliph) | 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 aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D GFT HNNCACBCA | sample_1 | isotropic | sample_conditions_1 |
| 3D GFT CACB(CO)NHN | sample_1 | isotropic | sample_conditions_1 |
| 3D GFT HAHBCACB(CO)NHN | 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 HNHA | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC high res. | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (arom) | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v1.3, Bruker Biospin - collection
AutoAssign v2.2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
SPARKY v3.110, Goddard - data analysis, peak picking
AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - structure solution
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
X-PLOR NIH v2.11.2, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
PSVS v1.3, Bhattacharya and Montelione - data analysis
PDBStat v5.0, Tejero and Montelione - PDB analysis
VNMR v6.1C, Varian - collection
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts