BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 30956

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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/BMR30956
MolProbity Validation Chart

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Title: Solution structure of the zinc finger domain of murine MetAP1, complexed with ZNG N-terminal peptide   PubMed: 35584702

Deposition date: 2021-09-30 Original release date: 2022-05-26

Authors: Edmonds, K.; Jordan, M.; Thalluri, K.; Wu, H.; Di Marchi, R.; Giedroc, D.

Citation: Weiss, Andy; Murdoch, Caitlin; Edmonds, Katherine; Jordan, Matthew; Monteith, Andrew; Perera, Yasiru; Rodriguez Nassif, Aslin; Petoletti, Amber; Beavers, William; Munneke, Matthew; Drury, Sydney; Krystofiak, Evan; Thalluri, Kishore; Wu, Hongwei; Kruse, Angela; DiMarchi, Richard; Caprioli, Richard; Spraggins, Jeffrey; Chazin, Walter; Giedroc, David; Skaar, Eric. "Zn-regulated GTPase metalloprotein activator 1 modulates vertebrate zinc homeostasis"  Cell 185, 2148-2163 (2022).

Assembly members:
entity_1, polymer, 80 residues, 8956.125 Da.
entity_ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: AEEEYAEDCPELVPIETKNQ EMAAVETRVCETDGCSSEAK LQCPTCIKLGIQGSYFCSQE CFKGSWATHKLLHKKAKDEK

Data typeCount
13C chemical shifts347
15N chemical shifts85
1H chemical shifts547

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22
3unit_32

Entities:

Entity 1, unit_1 80 residues - 8956.125 Da.

1   ALAGLUGLUGLUTYRALAGLUASPCYSPRO
2   GLULEUVALPROILEGLUTHRLYSASNGLN
3   GLUMETALAALAVALGLUTHRARGVALCYS
4   GLUTHRASPGLYCYSSERSERGLUALALYS
5   LEUGLNCYSPROTHRCYSILELYSLEUGLY
6   ILEGLNGLYSERTYRPHECYSSERGLNGLU
7   CYSPHELYSGLYSERTRPALATHRHISLYS
8   LEULEUHISLYSLYSALALYSASPGLULYS

Entity 2, unit_2 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: ZNG-Metap1 fusion, [U-13C; U-15N], 2 ± 0.01 mM; sodium chloride 150 ± 0.01 mM; sodium phosphate 10 ± 0.01 mM; TCEP 2 ± 0.01 mM; DSS 0.3 ± 0.01 mM

sample_2: ZNG-Metap1 fusion, [U-13C; U-15N], 2 ± 0.01 mM; sodium chloride 150 ± 0.01 mM; sodium phosphate 10 ± 0.01 mM; TCEP 2 ± 0.01 mM; DSS 0.3 ± 0.01 mM

sample_3: ZNG-Metap1 fusion, [U-10% 13C; U-100% 15N], 2 ± 0.01 mM; sodium chloride 150 ± 0.01 mM; sodium phosphate 10 ± 0.01 mM; TCEP 2 ± 0.01 mM; DSS 0.3 ± 0.01 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3d Har(CC-TOCSY-CGCBCACO)NHsample_1isotropicsample_conditions_1
2D hbCBcgcdceHEsample_2isotropicsample_conditions_1
2D hbCBcgcdHDsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-15N HSQC long-rangesample_1isotropicsample_conditions_1
2D 1H-13C HSQC CTsample_3isotropicsample_conditions_1
2D 1H-13C HSQC CTsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1

Software:

CYANA v3.98.13, Guntert P. - refinement, structure calculation

CARA, Keller and Wuthrich - chemical shift assignment

TopSpin v4.0.9, Bruker Biospin - collection

VnmrJ, Varian - collection

NMRFAM-SPARKY, NMRFAM - data analysis

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

hmsIST, Hyberts, Wagner - processing

NMR spectrometers:

  • Bruker AVANCE NEO 600 MHz
  • Varian VNMRS 800 MHz

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