BMRB Entry 51135

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51135

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Title:
Chemical shift assignments for D64Y mutant of holo Acyl Carrier Protein from Homo sapiens
Deposition date:
2021-10-13
Original release date:
2022-09-16
Authors:
Tang, Jingxuan; Tonelli, Marco; Lee, Yeongjoon; Lee, Woonghee; Frederick, Ronnie; Markley, John
Citation:

Citation: Tang, Jingxuan; Tonelli, Marco; Lee, Yeongjoon; Lee, Woonghee; Frederick, Ronnie; Markley, John. "Chemical shift assignments for D64Y mutant of holo Acyl Carrier Protein from Homo sapiens"  .

Assembly members:

Assembly members:
entity_1, polymer, 88 residues, Formula weight is not available
entity_PNS, non-polymer, 358.348 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: pE-SUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SDMPPLTLEGIQDRVLYVLK LYDKIDPEKLSVNSHFMKDL GLDSLDQVEIIMAMEDEFGF EIPYIDAEKLMCPQEIVDYI ADKKDVYE

Data sets:
Data typeCount
13C chemical shifts317
15N chemical shifts81
1H chemical shifts605

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein1
2cofactor2

Entities:

Entity 1, protein 88 residues - Formula weight is not available

1   SERASPMETPROPROLEUTHRLEUGLUGLY
2   ILEGLNASPARGVALLEUTYRVALLEULYS
3   LEUTYRASPLYSILEASPPROGLULYSLEU
4   SERVALASNSERHISPHEMETLYSASPLEU
5   GLYLEUASPSERLEUASPGLNVALGLUILE
6   ILEMETALAMETGLUASPGLUPHEGLYPHE
7   GLUILEPROTYRILEASPALAGLULYSLEU
8   METCYSPROGLNGLUILEVALASPTYRILE
9   ALAASPLYSLYSASPVALTYRGLU

Entity 2, cofactor - C11 H23 N2 O7 P S - 358.348 Da.

1   PNS

Samples:

sample_1: human Acyl Carrier Protein - D64Y mutant, [U-100% 13C; U-100% 15N], 0.450 mM; HEPES 50 mM; sodium chloride 150 mM; DTT 1 mM

sample_2: Acyl Carrier Protein, [U-100% 13C; U-100% 15N], 0.450 mM; HEPES 50 mM; sodium chloride 150 mM; DTT 1 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D H(C)CH TOCSYsample_1isotropicsample_conditions_1
3D 15N-separated NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
2D HBCBCGCDHDsample_2isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_2isotropicsample_conditions_1

Software:

TOPSPIN - collection

VNMRj - collection

NMRPipe - processing

SMILE - processing

NMRFAM-SPARKY - chemical shift assignment

PINE - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 900 MHz
  • Bruker AVANCE III 750 MHz
  • Varian VXRS 600 MHz

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