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 19395

Title: Solution Structure of human holo-PRL-3 in complex with vanadate

Deposition date: 2013-07-29 Original release date: 2013-10-08

Authors: Jeong, Ki-Woong; Kang, Dong-Il; Kim, Jin-Kyoung; Shin, Soyoung; Jin, Bonghwan; Lee, Chung-Kyoung; Kim, Eun-Hee; Jeon, Young; Kim, Yangmee

Citation: Kim, Kyoung-Ah; Song, Jin-Sue; Jee, Jungoo; Sheen, Mee; Lee, Chulhyun; Lee, Tae; Ro, Seonggu; Cho, Joong; Lee, Weontae; Yamazaki, Toshio; Jeon, Young; Cheong, Chaejoon. "Structure of human PRL-3, the phosphatase associated with cancer metastasis"  FEBS Lett. ., .-..

Assembly members:
holo-PRL-3_in_complex_with_vanadate, polymer, 162 residues, 18268.441 Da.
(2S)-2-amino-3-methyl-1-{4-[3-(thiophen-2-yl)-1,2,4-oxadiazol-5-yl]piperidin-1-yl}butan-1-one, non-polymer, 334.436 Da.
4-[(E)-(4-hydroxynaphthalen-1-yl)diazenyl]benzenesulfonic acid, non-polymer, 328.342 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   Vector: pET-21b

Entity Sequences (FASTA):
holo-PRL-3_in_complex_with_vanadate: MARMNRPAPVEVSYKHMRFL ITHNPTNATLSTFIEDLKKY GATTVVRVCEVTYDKTPLEK DGITVVDWPFDDGAPPPGKV VEDWLSLVKAKFCEAPGSCV AVHCVAGLGRAPVLVALALI ESGMKYEDAIQFIRQKRRGA INSKQLTYLEKYRPKQRLRF KD

Data sets:
Data typeCount
13C chemical shifts427
15N chemical shifts130
1H chemical shifts913

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1holo PRL-3 in complex with vanadate1
2LL5_12
3LL5_22
4LL5_32
5LL5_42
6LL5_52
7ORI3

Entities:

Entity 1, holo PRL-3 in complex with vanadate 162 residues - 18268.441 Da.

1   METALAARGMETASNARGPROALAPROVAL
2   GLUVALSERTYRLYSHISMETARGPHELEU
3   ILETHRHISASNPROTHRASNALATHRLEU
4   SERTHRPHEILEGLUASPLEULYSLYSTYR
5   GLYALATHRTHRVALVALARGVALCYSGLU
6   VALTHRTYRASPLYSTHRPROLEUGLULYS
7   ASPGLYILETHRVALVALASPTRPPROPHE
8   ASPASPGLYALAPROPROPROGLYLYSVAL
9   VALGLUASPTRPLEUSERLEUVALLYSALA
10   LYSPHECYSGLUALAPROGLYSERCYSVAL
11   ALAVALHISCYSVALALAGLYLEUGLYARG
12   ALAPROVALLEUVALALALEUALALEUILE
13   GLUSERGLYMETLYSTYRGLUASPALAILE
14   GLNPHEILEARGGLNLYSARGARGGLYALA
15   ILEASNSERLYSGLNLEUTHRTYRLEUGLU
16   LYSTYRARGPROLYSGLNARGLEUARGPHE
17   LYSASP

Entity 2, LL5_1 - C16 H22 N4 O2 S - 334.436 Da.

1   LL5

Entity 3, ORI - C16 H12 N2 O4 S - 328.342 Da.

1   ORI

Samples:

sample_1: holo PRL-3 in complex with vanadate; HEPES 50 mM; NaCl 100 mM; DTT 10 mM; sodium orthovanadate 3 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.3; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard, Guntert, Mumenthaler and Wuthrich, Schwieters, Kuszewski, Tjandra and Clore - chemical shift assignment, processing, refinement, structure solution

NMR spectrometers:

  • Bruker DRX 800 MHz

Related Database Links:

PDB
DBJ BAJ20896
GB AAC29314 EHH25482 EHH64453
REF NP_001180623 NP_116000 XP_001500033 XP_002819531 XP_003819536
SP O75365

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