BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17752

Title: SOLUTION STRUCTURE OF THE HUMAN PROLACTIN RECEPTOR ECD DOMAIN D2

Deposition date: 2011-06-30 Original release date: 2012-02-13

Authors: Dagil, Robert; Knudsen, Maiken; Kragelund, Birthe; O'Shea, Charlotte

Citation: Dagil, Robert; Knudsen, Maiken; Olsen, Johan; O'Shea, Charlotte; Franzmann, Magnus; Goffin, Vincent; Teilum, Kaare; Breinholt, Jens; Kragelund, Birthe. "The WSXWS Motif in Cytokine Receptors Is a Molecular Switch Involved in Receptor Activation: Insight from Structures of the Prolactin Receptor"  Structure 20, 270-282 (2012).

Assembly members:
hPRLR-D2, polymer, 113 residues, 13328.4 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

Entity Sequences (FASTA):
hPRLR-D2: MYIVQPDPPLELAVEVKQPE DRKPYLWIKWSPPTLIDLKT GWFTLLYEIRLKPEKAAEWE IHFAGQQTEFKILSLHPGQK YLVQVRCKPDHGYWSAWSPA TFIQIPSDFTMND

Data sets:
Data typeCount
13C chemical shifts549
15N chemical shifts112
1H chemical shifts809

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hPRLR-D21

Entities:

Entity 1, hPRLR-D2 113 residues - 13328.4 Da.

1   METTYRILEVALGLNPROASPPROPROLEU
2   GLULEUALAVALGLUVALLYSGLNPROGLU
3   ASPARGLYSPROTYRLEUTRPILELYSTRP
4   SERPROPROTHRLEUILEASPLEULYSTHR
5   GLYTRPPHETHRLEULEUTYRGLUILEARG
6   LEULYSPROGLULYSALAALAGLUTRPGLU
7   ILEHISPHEALAGLYGLNGLNTHRGLUPHE
8   LYSILELEUSERLEUHISPROGLYGLNLYS
9   TYRLEUVALGLNVALARGCYSLYSPROASP
10   HISGLYTYRTRPSERALATRPSERPROALA
11   THRPHEILEGLNILEPROSERASPPHETHR
12   METASNASP

Samples:

sample_1: hPRLR-D2, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 10 mM; TCEP 10 mM; DSS 1 mM; sodium azide 0.02%; D2O 10%; H2O 90%

sample_2: hPRLR-D2, [U-100% 13C(1)], 0.5 mM; sodium phosphate 10 mM; TCEP 10 mM; sodium azide 0.02%; DSS 1 mM; D2O 100%

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1

Software:

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

CYANA v2.2.1, Guntert, Mumenthaler and Wuthrich - chemical shift assignment

X-PLOR NIH v2.25, Schwieters, Kuszewski, Tjandra and Clore - structure solution

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

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

CCPN v2.1.5, CCPN - peak picking

ARIA v2.3.2, Linge, O, . - Water refinement

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAG36079 BAG73583
EMBL CAH91100 CAL38328 CAL38451
GB AAA60174 AAB34470 AAD32032 AAD49855 AAH59392
REF NP_000940 NP_001153263 NP_001191243 NP_001191244 NP_001191245
SP P16471

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