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BMRB Entry 51500

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51500

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Title: Miro2 N-terminal GTPase domain bound to GTP

Deposition date: 2022-06-21 Original release date: 2022-06-27

Authors: Smith, Cassandra; Jones, David

Citation: Smith, Cassandra; Jones, David. "Backbone Chemical Shift Assignment of the N-terminal GTPase domain of Miro2 bound to GTP"  Biomol. NMR Assignments ., .-..

Assembly members:
entity_1, polymer, 200 residues, 22218.23 Da.
entity_GTP, non-polymer, 523.180 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MRRDVRILLLGEAQVGKTSL ILSLVGEEFPEEVPPRAEEI TIPADVTPEKVPTHIVDYSE AEQTDEELREEIHKANVVCV VYDVSEEATIEKIRTKWIPL VNGGTTQGPRVPIILVGNKS DLRSGSSMEAVLPIMSQFPE IETCVECSAKNLRNISELFY YAQKAVLHPTAPLYDPEAKQ

Data sets:
Data typeCount
13C chemical shifts643
15N chemical shifts169
1H chemical shifts169

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Protein1
2Nucleotide2

Entities:

Entity 1, Protein 200 residues - 22218.23 Da.

Residues 1-20 represent the non-native affinity tag for purification. The remainder represent the first residues 1-180 of the native protein.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METARGARGASPVALARGILELEULEULEU
4   GLYGLUALAGLNVALGLYLYSTHRSERLEU
5   ILELEUSERLEUVALGLYGLUGLUPHEPRO
6   GLUGLUVALPROPROARGALAGLUGLUILE
7   THRILEPROALAASPVALTHRPROGLULYS
8   VALPROTHRHISILEVALASPTYRSERGLU
9   ALAGLUGLNTHRASPGLUGLULEUARGGLU
10   GLUILEHISLYSALAASNVALVALCYSVAL
11   VALTYRASPVALSERGLUGLUALATHRILE
12   GLULYSILEARGTHRLYSTRPILEPROLEU
13   VALASNGLYGLYTHRTHRGLNGLYPROARG
14   VALPROILEILELEUVALGLYASNLYSSER
15   ASPLEUARGSERGLYSERSERMETGLUALA
16   VALLEUPROILEMETSERGLNPHEPROGLU
17   ILEGLUTHRCYSVALGLUCYSSERALALYS
18   ASNLEUARGASNILESERGLULEUPHETYR
19   TYRALAGLNLYSALAVALLEUHISPROTHR
20   ALAPROLEUTYRASPPROGLUALALYSGLN

Entity 2, Nucleotide - C10 H16 N5 O14 P3 - 523.180 Da.

1   GTP

Samples:

sample_1: N-terminal GTPase Domain, [U-99% 13C; U-99% 15N], 350 ± 7 uM; GUANOSINE-5'-TRIPHOSPHATE 200 ± 4 uM; D2O 10 ± 0.01 %; DSS 100 ± 5 uM; sodium chloride 150 ± 1 mM; HEPES 25 ± 0.5 mM; magnesium chloride 1 ± 0.01 mM; H2O 90 ± 1 %

sample_2: N-terminal GTPase Domain, [U-99% 13C; U-99% 15N; U-80% 2H], 350 ± 7 uM; GUANOSINE-5'-TRIPHOSPHATE 200 ± 4 uM; D2O 10 ± 0.01 %; DSS 100 ± 5 uM; sodium chloride 150 ± 1 mM; HEPES 25 ± 0.5 mM; magnesium chloride 1 ± 0.01 mM; H2O 90 ± 1 %

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
1D 1Hsample_1isotropicsample_conditions_1

Software:

VNMRj v4.2A - collection

TOPSPIN v4.1 - collection

ANALYSIS v2.5 - chemical shift assignment, data analysis, peak picking

istHMS - collection, processing

NMRPipe v10.9 - processing

NMR spectrometers:

  • Varian DD2 900 MHz
  • Bruker AVANCE NEO 600 MHz

Related Database Links:

Uniprot Q8IXI1
AlphaFold Q9H7M8

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts