BMRB Entry 17905

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17905

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Title:
1H, 13C and 15N resonance assignment of the Anticodon Binding Domain of Human Lysyl Aminoacyl tRNA Synthetase
Deposition date:
2011-08-31
Original release date:
2011-12-12
Authors:
Liu, Sheng; Tsang, Pearl
Citation:

Citation: Liu, Sheng; Howell, Michael; Melby, Joel; Tsang, Pearl. "1H, 13C and 15N resonance assignment of the anticodon binding domain of human lysyl aminoacyl tRNA synthetase."  Biomol. NMR Assignments 6, 173-176 (2012).
PubMed: 22105307

Assembly members:

Assembly members:
GED_rrACBcs, polymer, 126 residues, 14210.3 Da.

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: pET-30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GED_rrACBcs: GEDPYPHKFHVDISLTDFIQ KYSHLQPGDHLTDITLKVAG RIHAKRASGGKLIFYDLRGE GVKLQVMANSRNYKSEEEFI HINNKLRRGDIIGVQGNPGK TKKGELSIIPYEITLLSPSL HMLPHL

Data sets:
Data typeCount
13C chemical shifts490
15N chemical shifts111
1H chemical shifts761

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GED_rrACBcs1

Entities:

Entity 1, GED_rrACBcs 126 residues - 14210.3 Da.

This is a N-terminally truncated (21 residues) form of human LysRS anticodon binding domain

1   GLYGLUASPPROTYRPROHISLYSPHEHIS
2   VALASPILESERLEUTHRASPPHEILEGLN
3   LYSTYRSERHISLEUGLNPROGLYASPHIS
4   LEUTHRASPILETHRLEULYSVALALAGLY
5   ARGILEHISALALYSARGALASERGLYGLY
6   LYSLEUILEPHETYRASPLEUARGGLYGLU
7   GLYVALLYSLEUGLNVALMETALAASNSER
8   ARGASNTYRLYSSERGLUGLUGLUPHEILE
9   HISILEASNASNLYSLEUARGARGGLYASP
10   ILEILEGLYVALGLNGLYASNPROGLYLYS
11   THRLYSLYSGLYGLULEUSERILEILEPRO
12   TYRGLUILETHRLEULEUSERPROSERLEU
13   HISMETLEUPROHISLEU

Samples:

sample_1: GED_rrACBcs, [U-100% 13C; U-100% 15N], 1.3 mM

sample_conditions_1: ionic strength: 40 mM; pH: 6.8; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HN(CA)CBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz
  • Bruker DMX 500 MHz

Related Database Links:

PDB
DBJ BAA06688 BAA22084 BAG09591
EMBL CAH89490
GB AAG30114 AAH04132 ABM83227 ABM86426 AIC54646
REF NP_001123561 NP_001127155 NP_001244522 NP_005539 XP_002761205
SP Q15046
AlphaFold Q15046

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