BMRB Entry 18758
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18758
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Title: Refined solution structure and dynamics of First Catalytic Cysteine Half-domain from mouse E1 enzyme PubMed: 24211821
Deposition date: 2012-10-03 Original release date: 2013-09-16
Authors: Jaremko, Mariusz; Jaremko, Lukasz; Nowakowski, Michal; Szczepanowski, Roman; Filipek, Renata; Wojciechowski, Marek; Bochtler, Matthias; Ejchart, Andrzej
Citation: Jaremko, Mariusz; Jaremko, ukasz; Nowakowski, Micha; Wojciechowski, Marek; Szczepanowski, Roman; Panecka, Renata; Zhukov, Igor; Bochtler, Matthias; Ejchart, Andrzej. "NMR structural studies of the first catalytic half-domain of ubiquitin activating enzyme." J. Struct. Biol. 185, 69-78 (2014).
Assembly members:
entity, polymer, 112 residues, 12195.902 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Saccharomyces cerevisiae
Entity Sequences (FASTA):
entity: EFGEEMVLTDSNGEQPLSAM
VSMVTKDNPGVVTCLDEARH
GFETGDFVSFSEVQGMIQLN
GCQPMEIKVLGPYTFSICDT
SNFSDYIRGGIVSQVKVPKK
ISFKSLPASLVE
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
- order_parameters
| Data type | Count |
| 13C chemical shifts | 469 |
| 15N chemical shifts | 110 |
| 1H chemical shifts | 769 |
| heteronuclear NOE values | 99 |
| order parameters | 71 |
| T1 relaxation values | 100 |
| T2 relaxation values | 99 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | First Catalytic Cysteine Half-domain | 1 |
Entities:
Entity 1, First Catalytic Cysteine Half-domain 112 residues - 12195.902 Da.
| 1 | GLU | PHE | GLY | GLU | GLU | MET | VAL | LEU | THR | ASP | ||||
| 2 | SER | ASN | GLY | GLU | GLN | PRO | LEU | SER | ALA | MET | ||||
| 3 | VAL | SER | MET | VAL | THR | LYS | ASP | ASN | PRO | GLY | ||||
| 4 | VAL | VAL | THR | CYS | LEU | ASP | GLU | ALA | ARG | HIS | ||||
| 5 | GLY | PHE | GLU | THR | GLY | ASP | PHE | VAL | SER | PHE | ||||
| 6 | SER | GLU | VAL | GLN | GLY | MET | ILE | GLN | LEU | ASN | ||||
| 7 | GLY | CYS | GLN | PRO | MET | GLU | ILE | LYS | VAL | LEU | ||||
| 8 | GLY | PRO | TYR | THR | PHE | SER | ILE | CYS | ASP | THR | ||||
| 9 | SER | ASN | PHE | SER | ASP | TYR | ILE | ARG | GLY | GLY | ||||
| 10 | ILE | VAL | SER | GLN | VAL | LYS | VAL | PRO | LYS | LYS | ||||
| 11 | ILE | SER | PHE | LYS | SER | LEU | PRO | ALA | SER | LEU | ||||
| 12 | VAL | GLU |
Samples:
sample_1: First Cysteine Catalytic Half-domain, [U-100% 13C; U-100% 15N], 1 mM; H2O 90 mM; D2O 10 mM
sample_2: First Cysteine Catalytic Half-domain, [U-100% 15N], 1 mM; H2O 90 mM; D2O 10 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | 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 HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH v2.26, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - peak picking
SPARKY, Goddard - chemical shift assignment
WhatIF, Vriend - refinement
NMR spectrometers:
- Varian UnityPlus 500 MHz
- Bruker Avance 700 MHz
- Varian INOVA 400 MHz
Related Database Links:
| PDB | |
| DBJ | BAA01433 BAC40121 BAC40405 BAE25369 BAE42599 |
| GB | AAH58630 AAI38201 AAI45985 EDL00743 |
| REF | NP_001129557 NP_001263245 NP_001263246 NP_033483 |
| SP | Q02053 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts