BMRB Entry 17031
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17031
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution NMR structure of the PBS linker polypeptide domain of phycobilisome linker protein apcE from Synechocystis sp. Northeast Structural Genomics Consortium Target SgR209C
Deposition date: 2010-06-30 Original release date: 2010-08-24
Authors: Ramelot, Theresa; Yang, Yunhuang; Cort, John; Hamilton, Keith; Ciccosanti, Colleen; Lee, Dan; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael
Citation: Ramelot, Theresa; Yang, Yunhuang; Cort, John; Hamilton, Keith; Ciccosanti, Colleen; Lee, Dan; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of the PBS linker polypeptide domain of phycobilisome linker protein apcE from Synechocystis sp. Northeast Structural Genomics Consortium Target SgR209C" Not known ., .-..
Assembly members:
SLR0335, polymer, 155 residues, 17840 Da.
Natural source: Common Name: Synechocystis sp. Taxonomy ID: 1143 Superkingdom: Bacteria Kingdom: not available Genus/species: Synechocystis not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SLR0335: PQSYFNAAAKRQKYAMKPGL
SALEKNAVIKAAYRQIFERD
ITKAYSQSISYLESQVRNGD
ISMKEFVRRLAKSPLYRKQF
FEPFINSRALELAFRHILGR
GPSSREEVQKYFSIVSSGGL
PALVDALVDSQEYADYFGEE
TVPYLRGLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 652 |
| 15N chemical shifts | 156 |
| 1H chemical shifts | 1025 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SLR0335 | 1 |
Entities:
Entity 1, SLR0335 155 residues - 17840 Da.
| 1 | PRO | GLN | SER | TYR | PHE | ASN | ALA | ALA | ALA | LYS | ||||
| 2 | ARG | GLN | LYS | TYR | ALA | MET | LYS | PRO | GLY | LEU | ||||
| 3 | SER | ALA | LEU | GLU | LYS | ASN | ALA | VAL | ILE | LYS | ||||
| 4 | ALA | ALA | TYR | ARG | GLN | ILE | PHE | GLU | ARG | ASP | ||||
| 5 | ILE | THR | LYS | ALA | TYR | SER | GLN | SER | ILE | SER | ||||
| 6 | TYR | LEU | GLU | SER | GLN | VAL | ARG | ASN | GLY | ASP | ||||
| 7 | ILE | SER | MET | LYS | GLU | PHE | VAL | ARG | ARG | LEU | ||||
| 8 | ALA | LYS | SER | PRO | LEU | TYR | ARG | LYS | GLN | PHE | ||||
| 9 | PHE | GLU | PRO | PHE | ILE | ASN | SER | ARG | ALA | LEU | ||||
| 10 | GLU | LEU | ALA | PHE | ARG | HIS | ILE | LEU | GLY | ARG | ||||
| 11 | GLY | PRO | SER | SER | ARG | GLU | GLU | VAL | GLN | LYS | ||||
| 12 | TYR | PHE | SER | ILE | VAL | SER | SER | GLY | GLY | LEU | ||||
| 13 | PRO | ALA | LEU | VAL | ASP | ALA | LEU | VAL | ASP | SER | ||||
| 14 | GLN | GLU | TYR | ALA | ASP | TYR | PHE | GLY | GLU | GLU | ||||
| 15 | THR | VAL | PRO | TYR | LEU | ARG | GLY | LEU | GLU | HIS | ||||
| 16 | HIS | HIS | HIS | HIS | HIS |
Samples:
NC_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± .25 mM; DTT 100 ± 1 mM; sodium azide 0.02 ± .001 %; protein, [U-100% 13C; U-100% 15N], 1.4 ± .05 mM; H2O 95%; D2O 5%
NC_sample_in_D2O: MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± .25 mM; DTT 100 ± 1 mM; sodium azide 0.02 ± .001 %; protein, [U-100% 13C; U-100% 15N], 1.4 ± .05 mM; H2O 95%; D2O 5%
NC5_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± .25 mM; DTT 100 ± 1 mM; sodium azide 0.02 ± .001 %; protein, [U-5% 13C; U-100% 15N], 1.2 ± .05 mM; H2O 95%; D2O 5%
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 | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC_sample | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | NC_sample | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliph | NC_sample | isotropic | sample_conditions_1 |
| 4D 1H-13C NOESY | NC_sample_in_D2O | isotropic | sample_conditions_1 |
| 3D HNCO | NC_sample | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | NC_sample | isotropic | sample_conditions_1 |
| 3D HNCACB | NC_sample | isotropic | sample_conditions_1 |
| 3D (H)CC(CO)NH-TOCSY | NC_sample | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | NC_sample_in_D2O | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | NC_sample_in_D2O | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | NC_sample_in_D2O | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC5_sample | isotropic | sample_conditions_1 |
| 3D H(CC)(CO)NH-TOCSY | NC_sample | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY arom | NC_sample | isotropic | sample_conditions_1 |
| (H)CCH-TOCSY | NC_sample_in_D2O | isotropic | sample_conditions_1 |
| 3D HNCA | NC_sample | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | NC_sample | isotropic | sample_conditions_1 |
Software:
NMRPipe vlinux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
VNMR v6.1C, Varian - collection
TOPSPIN v2.1.4, Bruker Biospin - collection
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis
X-PLOR NIH v2.25, Schwieters, Kuszewski, Tjandra and Clore - structure solution
SPARKY v3.113, Goddard - data analysis
PSVS v1.4, Bhattacharya and Montelione - structure validation
AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
PDBStat v5.0, (PDBStat) R. Tejero, G.T. Montelione - data analysis
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker AvanceIII 850 MHz
- Varian INOVA 500 MHz
- Varian INOVA 750 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts