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 15509

Title: NMR Solution Structure of PARC CPH Domain. NESG Target HR3443B/SGC-Toronto

Authors: Kaustov, Lilia; Liao, Jack; Lemak, Sasha; Duan, Shili; Muhandiram, Ranjith; Karra, Murthy; Srisailam, Sampath; Sundstrom, Martin; Weigelt, Johan; Edwards, Aled; Dhe-Paganon, Sirano; Arrowsmith, Cheryl

Citation: Kaustov, Lilia; Liao, Jack; Lemak, Sasha; Duan, Shili; Muhandiram, Ranjith; Karra, Murthy; Srisailam, Sampath; Dhe-Paganon, Sirano; Arrowsmith, Cheryl. "NMR Solution Structure of PARC CPH Domain"  . ., .-..

Assembly members:
PARC, polymer, 105 residues, 15094.872 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):
PARC: GSHMRSEFSSRGGYGEYVQQ TLQPGMRVRMLDDYEEISAG DEGEFRQSNNGIPPVQVFWQ STGRTYWVHWHMLEILGPEE ATEDKASAAVEKGAGATVLG TAFPS

Data sets:
Data typeCount
13C chemical shifts372
15N chemical shifts105
1H chemical shifts639

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 105 residues - 15094.872 Da.

Residues 1-4 represent a residual tag after His-tag cleavage

1   GLYSERHISMETARGSERGLUPHESERSER
2   ARGGLYGLYTYRGLYGLUTYRVALGLNGLN
3   THRLEUGLNPROGLYMETARGVALARGMET
4   LEUASPASPTYRGLUGLUILESERALAGLY
5   ASPGLUGLYGLUPHEARGGLNSERASNASN
6   GLYILEPROPROVALGLNVALPHETRPGLN
7   SERTHRGLYARGTHRTYRTRPVALHISTRP
8   HISMETLEUGLUILELEUGLYPROGLUGLU
9   ALATHRGLUASPLYSALASERALAALAVAL
10   GLULYSGLYALAGLYALATHRVALLEUGLY
11   THRALAPHEPROSER

Samples:

PARC_sample: TRIS, [U-13C; U-15N], 25 mM; sodium chloride 250 mM; H2O 90%; PMSF 0.5 mM; Benzamidine 1 mM; D2O 10%; H2O 55 mM

PARC_cond: ionic strength: 0.25 M; pH: 7.4; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCPARC_sampleisotropicPARC_cond
2D 1H-13C HSQCPARC_sampleisotropicPARC_cond
3D HNCACBPARC_sampleisotropicPARC_cond
3D CBCA(CO)NHPARC_sampleisotropicPARC_cond
3D Cc(CO)NH-TOCSYPARC_sampleisotropicPARC_cond
3D 1H-15N NOESYPARC_sampleisotropicPARC_cond
3D 1H-13C NOESYPARC_sampleisotropicPARC_cond
3D HCCH-TOCSYPARC_sampleisotropicPARC_cond
3D HNCOPARC_sampleisotropicPARC_cond
3D HBHA(CO)NHPARC_sampleisotropicPARC_cond
Hc(CO)NH-TOCSYPARC_sampleisotropicPARC_cond

Software:

CYANA, Brunger, Adams, Clore, Gros, Nilges and Read, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, peak picking, processing, refinement, structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
DBJ BAI45256
EMBL CAC85756 CAH18328 CAH18696
GB AAH28159 AAI48598 AAN61516 EAX04163 EAX04164
REF NP_055904 XP_002746613 XP_002808431 XP_003833312 XP_003897675
SP Q8IWT3