BMRB Entry 30684

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30684
MolProbity Validation Chart

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Title:
NMR structure of the HACS1 SH3 domain
Deposition date:
2019-11-15
Original release date:
2019-11-20
Authors:
Donaldson, L.
Citation:

Citation: Kwan, Jamie; Slavkovic, Sladjana; Piazza, Michael; Wang, Dingyan; Dieckmann, Thorsten; Johnson, Philip; Wen, Xiao-Yan; Donaldson, Logan. "The HACS1 signaling adaptor protein recognizes a unique motif in the Paired Immunoglobulin Receptor B (PIRB) cytoplasmic domain"  Commun. Biol. 3, 672-672 (2020).
PubMed: 33188360

Assembly members:

Assembly members:
entity_1, polymer, 87 residues, 9656.987 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 BL21   Vector: pGEX2T

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSDITSLYKKAGSSFRLDDD GPYSGPFCGRARVHTDFTPS PYDTDSLKIKKGDIIDIICK TPMGMWTGMLNNKVGNFKFI YVDVISE

Data sets:
Data typeCount
13C chemical shifts266
15N chemical shifts62
1H chemical shifts429

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 87 residues - 9656.987 Da.

1   GLYSERASPILETHRSERLEUTYRLYSLYS
2   ALAGLYSERSERPHEARGLEUASPASPASP
3   GLYPROTYRSERGLYPROPHECYSGLYARG
4   ALAARGVALHISTHRASPPHETHRPROSER
5   PROTYRASPTHRASPSERLEULYSILELYS
6   LYSGLYASPILEILEASPILEILECYSLYS
7   THRPROMETGLYMETTRPTHRGLYMETLEU
8   ASNASNLYSVALGLYASNPHELYSPHEILE
9   TYRVALASPVALILESERGLU

Samples:

sample_1: entity_1, [U-99% 13C; U-99% 15N], 0.6 mM; sodium phosphate 20 mM; sodium chloride 150 mM; sodium azide 0.05 % w/v

sample_2: entity_1, [U-99% 13C; U-99% 15N], 0.6 mM; sodium phosphate 20 mM; sodium chloride 150 mM; sodium azide 0.05 % w/v; Pf1 phage 10 mg/mL

sample_conditions_1: ionic strength: 150 mM; pH: 7.7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-15N IPAP HSQCsample_2anisotropicsample_conditions_1

Software:

CcpNmr Analysis, CCPN - chemical shift assignment, data analysis, peak picking

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Varian Uniform NMR System 600 MHz

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