BMRB Entry 15085
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15085
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Title: Complete Assignment of a hypothetical portein RP4601 (NESG ID: RpT2)from Rhodopseudomonas palustris.
Deposition date: 2006-12-22 Original release date: 2007-02-09
Authors: Lemak, Alexander; Srisailam, Sampath; Yee, Adelinda; Karra, Murthy; Lukin, Jonathan; Arrowsmith, Cheryl
Citation: Lemak, Alexander. "Assignment of a hypothetical protein RP4601 from Rhodopseudomonas palustris" The BMRB entry is the only known published source for the data..
Assembly members:
RP4601, polymer, 66 residues, 7260.643 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
RP4601: MKVMIRKTATGHSAYVAKKD
LEELIVEMENPALWGGKVTL
ANGWQLELPAMAADTPLPIT
VEARKL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 267 |
| 15N chemical shifts | 62 |
| 1H chemical shifts | 460 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RP4601_aasem | 1 |
Entities:
Entity 1, RP4601_aasem 66 residues - 7260.643 Da.
| 1 | MET | LYS | VAL | MET | ILE | ARG | LYS | THR | ALA | THR | ||||
| 2 | GLY | HIS | SER | ALA | TYR | VAL | ALA | LYS | LYS | ASP | ||||
| 3 | LEU | GLU | GLU | LEU | ILE | VAL | GLU | MET | GLU | ASN | ||||
| 4 | PRO | ALA | LEU | TRP | GLY | GLY | LYS | VAL | THR | LEU | ||||
| 5 | ALA | ASN | GLY | TRP | GLN | LEU | GLU | LEU | PRO | ALA | ||||
| 6 | MET | ALA | ALA | ASP | THR | PRO | LEU | PRO | ILE | THR | ||||
| 7 | VAL | GLU | ALA | ARG | LYS | LEU |
Samples:
RP4601_sample1: RP4601, [U-100% 13C; U-100% 15N], 0.7 – 1.2 mM; NaN3 0.01%; Zn 10 uM; DTT 10 mM; H2O 90%; D2O 10%; Benzamidine 1 mM
RP4601_sample2: RP4601, [U-100% 13C; U-100% 15N], 0.6 – 1.1 mM; D2O 100%; NaN3 0.01%; Zn 10 uM; DTT 10 mM; Benzamidine 1 mM
rp4601_conditions_1: ionic strength: 500 mM; pH: 5.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | RP4601_sample1 | isotropic | rp4601_conditions_1 |
| 2D 1H-13C HSQC | RP4601_sample1 | isotropic | rp4601_conditions_1 |
| 3D HNCA | RP4601_sample1 | isotropic | rp4601_conditions_1 |
| 3D CBCA(CO)NH | RP4601_sample1 | isotropic | rp4601_conditions_1 |
| 3D H(CCO)NH | RP4601_sample1 | isotropic | rp4601_conditions_1 |
| HBHACBCAcoNH 4D projection Reconstruction | RP4601_sample1 | isotropic | rp4601_conditions_1 |
| HCCCcoNH Tocsy 4D Projection Reconstruction | RP4601_sample1 | isotropic | rp4601_conditions_1 |
| 3D 1H-15N NOESY | RP4601_sample1 | isotropic | rp4601_conditions_1 |
| 3D 1H-13C NOESY | RP4601_sample1 | isotropic | rp4601_conditions_1 |
| 3D HN(COCA)CB | RP4601_sample1 | isotropic | rp4601_conditions_1 |
| 3D HCCH-TOCSY (H-Tocsy) | RP4601_sample2 | isotropic | rp4601_conditions_1 |
| HCCH-TOCSY (C-Tocsy) | RP4601_sample2 | isotropic | rp4601_conditions_1 |
| 3D 1H-13C NOESY | RP4601_sample2 | isotropic | rp4601_conditions_1 |
Software:
TOPSPIN v1.3, Bruker Biospin - collection
NMRPipe v2.6, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v3.106, Goddard - chemical shift assignment, data analysis, peak picking
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance 500 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