BMRB Entry 15806
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15806
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Title: 1H and 15N Chemical Shift Assignments and Experimental NMR Restraints for the Neurotrypsin Kringle Domain PubMed: 18956887
Deposition date: 2008-06-16 Original release date: 2008-07-02
Authors: Ozhogina, Olga
Citation: Ozhogina, Olga; Grishaev, Alexander; Bominaar, Emile; Llinas, Miguel. "NMR Solution Structure of the Neurotrypsin Kringle Domain" Biochemistry 47, 12290-12298 (2008).
Assembly members:
Neurotrypsin_kringle_domain, polymer, 77 residues, 8533 Da.
Natural source: Common Name: Norway rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pmed23
Entity Sequences (FASTA):
Neurotrypsin_kringle_domain: RCGAGEPWGNATNLGVPCLH
WDEVPPFLERSPPASWAELR
GQPHNFCRSPDGAGRPWCFY
RNAQGKVDWGYCDCGQG
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 84 |
| 1H chemical shifts | 473 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Neurotrypsin kringle domain | 1 |
Entities:
Entity 1, Neurotrypsin kringle domain 77 residues - 8533 Da.
| 1 | ARG | CYS | GLY | ALA | GLY | GLU | PRO | TRP | GLY | ASN | ||||
| 2 | ALA | THR | ASN | LEU | GLY | VAL | PRO | CYS | LEU | HIS | ||||
| 3 | TRP | ASP | GLU | VAL | PRO | PRO | PHE | LEU | GLU | ARG | ||||
| 4 | SER | PRO | PRO | ALA | SER | TRP | ALA | GLU | LEU | ARG | ||||
| 5 | GLY | GLN | PRO | HIS | ASN | PHE | CYS | ARG | SER | PRO | ||||
| 6 | ASP | GLY | ALA | GLY | ARG | PRO | TRP | CYS | PHE | TYR | ||||
| 7 | ARG | ASN | ALA | GLN | GLY | LYS | VAL | ASP | TRP | GLY | ||||
| 8 | TYR | CYS | ASP | CYS | GLY | GLN | GLY |
Samples:
sample_1: Neurotrypsin, [U-100% 15N], 1 mM; H2O 90%; D2O, [U-100% 2H], 10%
sample_conditions_1: ionic strength: 0.0 mM; pH: 5.2; pressure: 1 atm; temperature: 300.0 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D [1H-15N]-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D [1H-15N]-HMBC | sample_1 | isotropic | sample_conditions_1 |
| 2D [1H-13C]-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D [1H-1H]-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D [1H-1H]-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D [1H-1H]-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D [1H-15N]-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D [1H-15N]-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHB | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA v2.0, Linge, O'Donoghue and Nilges - refinement
ANALYSIS v1.4, CCPN - data analysis
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
FELIX v97, Accelrys Software Inc. - processing
Molmol v2K.2, Koradi, Billeter and Wuthrich - display
ProcheckNMR v3.5.4, Laskowski and MacArthur - geometry plots
QUEEN v1.1, Nabuurs, Spronk, Krieger, Maassen, Vriend and Vuister - quantitative evaluation of experimental distance restraints
NMR spectrometers:
- Bruker Avance DRX 600 MHz
Related Database Links:
| BMRB | 15806 |
| PDB | |
| DDBJ | Q99JC8 |
| EMBL | AJ311671 Q99JC8 CAA73646 CAC35028 |
| GB | NP_445956 AAH31429 EDL12300 EDL82129 |
| IUBMB | EC: 3.4.21 |
| MEROPS | S01.237 |
| NCBI | CAC35028 NP_445956 |
| PFAM | PF00051 |
| PIR | PIRSF037929 |
| REFSEQ | NM_053504 |
| SCOP | 57441 |
| SWS | Q99JC8 |
| UNP | Q99JC8 |
| DBJ | BAA23986 |
| REF | NP_032965 NP_445956 |
| SP | G3V801 O08762 |
| AlphaFold | Q99JC8 G3V801 O08762 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts