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Biological Magnetic Resonance Data Bank


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BMRB Entry 34007

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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/BMR34007
MolProbity Validation Chart

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Title: Solution structure of the complex between human ZNHIT3 and NUFIP1 proteins

Deposition date: 2016-06-07 Original release date: 2016-08-26

Authors: Quinternet, M.; Chagot, M.; Manival, X.

Citation: Quinternet, M.; Chagot, M.; Rothe, B.; Tiotu, D.; Charpentier, B.; Manival, X.. "Structural features of the box C/D snoRNP pre-assembly process are conserved through species"  (2016).

Assembly members:
Zinc finger HIT domain-containing protein 3, polymer, 75 residues, 8492.720 Da.
Nuclear fragile X mental retardation-interacting protein 1, polymer, 34 residues, 4030.654 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
Zinc finger HIT domain-containing protein 3: GPHMDRVSLQNLKNLGESAT LRSLLLNPHLRQLMVNLDQG EDKAKLMRAYMQEPLFVEFA DCCLGIVEPSQNEES
Nuclear fragile X mental retardation-interacting protein 1: DIRHERNVILQCVRYIIKKD FFGLDTNSAKSKDV

Data sets:
Data typeCount
13C chemical shifts488
15N chemical shifts125
1H chemical shifts805

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 75 residues - 8492.720 Da.

1   GLYPROHISMETASPARGVALSERLEUGLN
2   ASNLEULYSASNLEUGLYGLUSERALATHR
3   LEUARGSERLEULEULEUASNPROHISLEU
4   ARGGLNLEUMETVALASNLEUASPGLNGLY
5   GLUASPLYSALALYSLEUMETARGALATYR
6   METGLNGLUPROLEUPHEVALGLUPHEALA
7   ASPCYSCYSLEUGLYILEVALGLUPROSER
8   GLNASNGLUGLUSER

Entity 2, entity_2 34 residues - 4030.654 Da.

1   ASPILEARGHISGLUARGASNVALILELEU
2   GLNCYSVALARGTYRILEILELYSLYSASP
3   PHEPHEGLYLEUASPTHRASNSERALALYS
4   SERLYSASPVAL

Samples:

sample_1: NUFIP1, [U-13C; U-15N], 1 mM; ZNHIT3, [U-13C; U-15N], 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 150 mM; pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

TOPSPIN v3.2, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AvanceIII 600 MHz

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