BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 50998

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50998

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Title: Backbone assignment of human prolactin at pH 7.0 and 5.5   PubMed: 35192840

Deposition date: 2021-06-30 Original release date: 2022-03-03

Authors: Vang, Janus; Pustovalova, Yulia; Hoch, Jeffrey

Citation: Vang, Janus; Pustovalova, Yulia; Korzhnev, Dmitry; Gorbatyuk, Oksana; Keeler, Camille; Hodsdon, Michael; Hoch, Jeffrey. "Architecture of the two metal binding sites in prolactin"  Biophys. J. 121, 1312-1321 (2022).

Assembly members:
entity_1, polymer, 199 residues, Formula weight is not available

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   Vector: pT7

Entity Sequences (FASTA):
entity_1: LPICPGGAARCQVTLRDLFD RAVVLSHYIHNLSSEMFSEF DKRYTHGRGFITKAINSCHT SSLATPEDKEQAQQMNQKDF LSLIVSILRSWNEPLYHLVT EVRGMQEAPEAILSKAVEIE EQTKRLLEGMELIVSQVHPE TKENEIYPVWSGLPSLQMAD EESRLSAYYNLLHCLRRDSH KIDNYLKLLKCRIIHNNNC

Data sets:
Data typeCount
13C chemical shifts548
15N chemical shifts301
1H chemical shifts301

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human prolactin1

Entities:

Entity 1, human prolactin 199 residues - Formula weight is not available

1   LEUPROILECYSPROGLYGLYALAALAARG
2   CYSGLNVALTHRLEUARGASPLEUPHEASP
3   ARGALAVALVALLEUSERHISTYRILEHIS
4   ASNLEUSERSERGLUMETPHESERGLUPHE
5   ASPLYSARGTYRTHRHISGLYARGGLYPHE
6   ILETHRLYSALAILEASNSERCYSHISTHR
7   SERSERLEUALATHRPROGLUASPLYSGLU
8   GLNALAGLNGLNMETASNGLNLYSASPPHE
9   LEUSERLEUILEVALSERILELEUARGSER
10   TRPASNGLUPROLEUTYRHISLEUVALTHR
11   GLUVALARGGLYMETGLNGLUALAPROGLU
12   ALAILELEUSERLYSALAVALGLUILEGLU
13   GLUGLNTHRLYSARGLEULEUGLUGLYMET
14   GLULEUILEVALSERGLNVALHISPROGLU
15   THRLYSGLUASNGLUILETYRPROVALTRP
16   SERGLYLEUPROSERLEUGLNMETALAASP
17   GLUGLUSERARGLEUSERALATYRTYRASN
18   LEULEUHISCYSLEUARGARGASPSERHIS
19   LYSILEASPASNTYRLEULYSLEULEULYS
20   CYSARGILEILEHISASNASNASNCYS

Samples:

sample_1: prolactin, [U-13C; U-15N; U-2H], 0.4 mM; potassium phosphate 50 mM; sodium azide 0.02%

sample_2: prolactin, [U-15N; U-2H], 0.2 mM; MOPS 20 mM; sodium chloride 20 mM

sample_3: prolactin, [U-15N; U-2H], 0.1 mM; MES 10 mM; sodium chloride 20 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 308 K

sample_conditions_2: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 308 K

sample_conditions_3: ionic strength: 30 mM; pH: 5.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_3
2D 1H-15N HSQCsample_2isotropicsample_conditions_3
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

RNMRTK - processing

SPARKY - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

UNP P01236
AlphaFold Q92996

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