BMRB Entry 34399

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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/BMR34399
MolProbity Validation Chart

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Title:
Extremely stable monomeric variant of human cystatin C with single amino acid substitution
Deposition date:
2019-05-14
Original release date:
2019-10-16
Authors:
Zhukov, I.; Rodziewicz-Motowidlo, S.; Maszota-Zieleniak, M.; Jurczak, P.; Kozak, M.
Citation:

Citation: Maszota-Zieleniak, M.; Jurczak, P.; Orlikowska, M.; Zhukov, I.; Borek, D.; Otwinowski, Z.; Skowron, P.; Pietralik, Z.; Kozak, M.; Szymanska, A.; Rodziewicz-Motowidlo, S.. "NMR and crystallographic structural studies of the extremely stable monomeric variant of human cystatin C with single amino acid substitution."  FEBS J. 287, 361-376 (2020).
PubMed: 31330077

Assembly members:

Assembly members:
entity_1, polymer, 120 residues, 13323.062 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SSPGKPPRLVGGPMDASVEE EGVRRALDFAVGEYNKASND MYHSRALQVVRARKQIGAGV NYFLDVELGRTTCTKTQPNL DNCPFHDQPHLKRKAFCSFQ IYAVPWQGTMTLSKSTCQDA

Data sets:
Data typeCount
13C chemical shifts449
15N chemical shifts99
1H chemical shifts712

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 120 residues - 13323.062 Da.

1   SERSERPROGLYLYSPROPROARGLEUVAL
2   GLYGLYPROMETASPALASERVALGLUGLU
3   GLUGLYVALARGARGALALEUASPPHEALA
4   VALGLYGLUTYRASNLYSALASERASNASP
5   METTYRHISSERARGALALEUGLNVALVAL
6   ARGALAARGLYSGLNILEGLYALAGLYVAL
7   ASNTYRPHELEUASPVALGLULEUGLYARG
8   THRTHRCYSTHRLYSTHRGLNPROASNLEU
9   ASPASNCYSPROPHEHISASPGLNPROHIS
10   LEULYSARGLYSALAPHECYSSERPHEGLN
11   ILETYRALAVALPROTRPGLNGLYTHRMET
12   THRLEUSERLYSSERTHRCYSGLNASPALA

Samples:

sample_1: hCC V57G, [U-99% 15N], 0.5 mM; phosphate buffer 50 mM; NaCl 50 mM

sample_2: hCC V57G, [U-99% 13C; U-99% 15N], 0.5 mM; phosphate buffer 50 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.4; pressure: 1 Pa; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

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

Sparky, Goddard - data analysis, peak picking

CS-ROSETTA, Shen, Vernon, Baker and Bax - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Xplor-NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

YASARA, Krieger E. - refinement

NMR spectrometers:

  • Agilent DDR2 800 MHz

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