BMRB Entry 16252

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16252
MolProbity Validation Chart

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Title:
1H, 13C, 15N Chemical shift assignments of A13 homeodomain
Deposition date:
2009-04-10
Original release date:
2009-07-10
Authors:
Ames, James
Citation:

Citation: Zhang, Yonghong; Thornburg, Chelsea; Stadler, H. Scott; Ames, James. "(1)H, (15)N, and (13)C chemical shift assignments of mouse HOXA13 DNA binding domain."  Biomol. NMR Assignments 3, 199-201 (2009).
PubMed: 19888690

Assembly members:

Assembly members:
A13, polymer, 73 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET23

Entity Sequences (FASTA):

Entity Sequences (FASTA):
A13: MSHMLEGRKKRVPYTKVQLK ELEREYATNKFITKDKRRRI SATTNLSERQVTIWFQNRRV KEKKVINKLKTTS

Data sets:
Data typeCount
13C chemical shifts232
15N chemical shifts70
1H chemical shifts486

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1A131

Entities:

Entity 1, A13 73 residues - Formula weight is not available

Residues 1-6 are due to a cloning artifact.

1   METSERHISMETLEUGLUGLYARGLYSLYS
2   ARGVALPROTYRTHRLYSVALGLNLEULYS
3   GLULEUGLUARGGLUTYRALATHRASNLYS
4   PHEILETHRLYSASPLYSARGARGARGILE
5   SERALATHRTHRASNLEUSERGLUARGGLN
6   VALTHRILETRPPHEGLNASNARGARGVAL
7   LYSGLULYSLYSVALILEASNLYSLEULYS
8   THRTHRSER

Samples:

sample_1: A13, [U-98% 13C; U-98% 15N], 0.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.02 M; pH: 7.0; pressure: 1.0 atm; temperature: 285 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 16577
PDB
EMBL CAC44975
GB AAA86506 AAB03322 AAC50993 AAH75791 AAI00732
REF NP_000513 NP_001079321 NP_001162372 NP_001182271 NP_001258284
SP P31271 P50210 Q62424 Q90X25
TPG DAA30521
AlphaFold P31271 P50210 Q62424 Q90X25

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