BMRB Entry 30960

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30960
MolProbity Validation Chart

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Title:
Solution NMR Structure of Immunoglobulin-like Domain of Human Neuregulin-1
Deposition date:
2021-10-18
Original release date:
2022-05-11
Authors:
Eletsky, A.; Kim, Y.; Rogals, M.; Prestegard, J.
Citation:

Citation: Khaje, N.; Mobley, C.; Eletsky, A.; Rogals, M.; Kim, Y.; Biehn, S.; Mishra, S.; Lindert, S.; Prestegard, J.; Sharp, J.. "Validated determination of NRG1 Ig-like domain structure by mass spectrometry coupled with computational modeling"  Nat. Comm. Biol. 5, 452-452 (2022).
PubMed: 35551273

Assembly members:

Assembly members:
entity_1, polymer, 118 residues, 13350.179 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(DE3)   Vector: pET-21b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MHHHHHHSSGRENLYFQGAL PPRLKEMKSQESAAGSKLVL RCETSSEYSSLRFKWFKNGN ELNRKNKPQNIKIQKKPGKS ELRINKASLADSGEYMCKVI SKLGNDSASANITIVESN

Data typeCount
13C chemical shifts493
15N chemical shifts124
1H chemical shifts801

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 118 residues - 13350.179 Da.

1   METHISHISHISHISHISHISSERSERGLY
2   ARGGLUASNLEUTYRPHEGLNGLYALALEU
3   PROPROARGLEULYSGLUMETLYSSERGLN
4   GLUSERALAALAGLYSERLYSLEUVALLEU
5   ARGCYSGLUTHRSERSERGLUTYRSERSER
6   LEUARGPHELYSTRPPHELYSASNGLYASN
7   GLULEUASNARGLYSASNLYSPROGLNASN
8   ILELYSILEGLNLYSLYSPROGLYLYSSER
9   GLULEUARGILEASNLYSALASERLEUALA
10   ASPSERGLYGLUTYRMETCYSLYSVALILE
11   SERLYSLEUGLYASNASPSERALASERALA
12   ASNILETHRILEVALGLUSERASN

Samples:

sample_1: NRG1-Ig, [U-13C; U-15N], 2.0 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DSS 4 uM; sodium azide 0.05 % w/w

sample_2: NRG1-Ig, [U-13C; U-15N], 0.45 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DSS 4 uM; sodium azide 0.05 % w/w

sample_3: NRG1-Ig, [5% 13C; U-15N], 0.34 mM; sodium chloride 300 mM; DSS 5 uM; sodium azide 0.05 % w/w; TRIS 20 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 300 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C CT-HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C CT-HSQC aromaticsample_1isotropicsample_conditions_1
3D (HACA)CONHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSY aliphaticsample_1isotropicsample_conditions_1
3D (H)CCH-COSY aliphaticsample_1isotropicsample_conditions_1
3D (H)CCH-COSY aromaticsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C CT-HSQC methylsample_3isotropicsample_conditions_2
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D 1H-13C,15N NOESYsample_1isotropicsample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - structure calculation

ASDP v1.0, Huang, Mao, Xu and Montelione - structure calculation

CARA v1.9.1.7, Keller and Wuthrich - chemical shift assignment, peak picking

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

TopSpin v4.0, Bruker Biospin - processing

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

TALOS-N, Shen and Bax - data analysis

PSVS v1.5, Bhattacharya and Montelione - data analysis

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz

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