BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 18696

Title: 1H, 13C and 15N resonance assignment of the N-terminal domain of human lysyl aminoacyl tRNA synthetase   PubMed: 23065336

Deposition date: 2012-08-31 Original release date: 2012-10-18

Authors: Liu, Sheng; Tsang, Pearl

Citation: Liu, Sheng; Decker, Aaron; Howell, Mike; Caperelli, Carol; Tsang, Pearl. "1H, 13C and 15N resonance assignment of the N-terminal domain of human lysyl aminoacyl tRNA synthetase."  Biomol. NMR Assignments 7, 289-292 (2013).

Assembly members:
rmodN, polymer, 76 residues, 8311 Da.
rmodN_isoD62, polymer, 76 residues, 8312 Da.

Natural source:   Common Name: not available   Taxonomy ID: 9606   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: recombinant technology' 'Escherichia coli' . . . Escherichia coli 'BL21 DE3   Vector: 18696

Entity Sequences (FASTA):
rmodN: MAAVQAAEVKVDGSEPKLSK NELKRRLKAEKKVAEKEAKQ KELSEKQLSQATAAATNHTT DNGVLPETGGHHHHHH
rmodN_isoD62: MAAVQAAEVKVDGSEPKLSK NELKRRLKAEKKVAEKEAKQ KELSEKQLSQATAAATNHTT DDGVLPETGGHHHHHH

Data sets:
Data typeCount
13C chemical shifts574
15N chemical shifts143
1H chemical shifts660

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1rmodN1
2rmodN_isoD622

Entities:

Entity 1, rmodN 76 residues - 8311 Da.

1   METALAALAVALGLNALAALAGLUVALLYS
2   VALASPGLYSERGLUPROLYSLEUSERLYS
3   ASNGLULEULYSARGARGLEULYSALAGLU
4   LYSLYSVALALAGLULYSGLUALALYSGLN
5   LYSGLULEUSERGLULYSGLNLEUSERGLN
6   ALATHRALAALAALATHRASNHISTHRTHR
7   ASPASNGLYVALLEUPROGLUTHRGLYGLY
8   HISHISHISHISHISHIS

Entity 2, rmodN_isoD62 76 residues - 8312 Da.

N62 deamidate into isoD62

1   METALAALAVALGLNALAALAGLUVALLYS
2   VALASPGLYSERGLUPROLYSLEUSERLYS
3   ASNGLULEULYSARGARGLEULYSALAGLU
4   LYSLYSVALALAGLULYSGLUALALYSGLN
5   LYSGLULEUSERGLULYSGLNLEUSERGLN
6   ALATHRALAALAALATHRASNHISTHRTHR
7   ASPASPGLYVALLEUPROGLUTHRGLYGLY
8   HISHISHISHISHISHIS

Samples:

sample_1: rmodN, [U-100% 13C; U-100% 15N], 1.5 ± 0.1 mM; sodium phosphate' 'natural abundance 0.1; natural abundance 0.1; natural abundance 0.1; natural abundance 0.1; natural abundance 0.1; natural abundance 0.1; natural abundance 0.1

sample_conditions_1: ionic strength: 70 mM; pH: 6.0; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 18697 18697
DBJ BAA06688 BAA22084 BAC86604 BAG09591 BAA06688 BAA22084 BAC86604 BAG09591
GB AAH04132 ABM83227 ABM86426 AIC54646 EAW95620 AAH04132 ABM83227 ABM86426 AIC54646 EAW95620
REF NP_005539 XP_003260017 XP_003829594 XP_004058057 XP_009249230 NP_005539 XP_003260017 XP_003829594 XP_009249230 XP_511115
SP Q15046 Q15046

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