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Biological Magnetic Resonance Data Bank


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BMRB Entry 26047

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR26047
MolProbity Validation Chart

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Title: Lysine dimethylated FKBP12

Deposition date: 2016-05-05 Original release date: 2017-05-15

Authors: Hattori, Yoshikazu; Sebera, Jukab; Sychrovsky, Vladimir; Furuita, Kyoko; Sugiki, Toshihiko; Ohki, Izuru; Ikegami, Takahisa; Kobayashi, Naohiro; Tanaka, Yoshiyuki; Fujiwara, Toshimichi; Kojima, Chojiro

Citation: Hattori, Yoshikazu; Sebera, Jukab; Sychrovsky, Vladimir; Furuita, Kyoko; Sugiki, Toshihiko; Ohki, Izuru; Ikegami, Takahisa; Kobayashi, Naohiro; Tanaka, Yoshiyuki; Fujiwara, Toshimichi; Kojima, Chojiro. "NMR Observation of Protein Surface Salt Bridges at Neutral pH"  J. Am. Chem. Soc. ., .-..

Assembly members:
entity, polymer, 111 residues, 12425.415 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):
entity: GPSMGVQVETISPGDGRTFP XRGQTCVVHYTGMLEDGXXF DSSRDRNXPFXFMLGXQEVI RGWEEGVAQMSVGQRAXLTI SPDYAYGATGHPGIIPPHAT LVFDVELLXLE

Data sets:
Data typeCount
13C chemical shifts494
15N chemical shifts109
1H chemical shifts791

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 111 residues - 12425.415 Da.

1   GLYPROSERMETGLYVALGLNVALGLUTHR
2   ILESERPROGLYASPGLYARGTHRPHEPRO
3   MLYARGGLYGLNTHRCYSVALVALHISTYR
4   THRGLYMETLEUGLUASPGLYMLYMLYPHE
5   ASPSERSERARGASPARGASNMLYPROPHE
6   MLYPHEMETLEUGLYMLYGLNGLUVALILE
7   ARGGLYTRPGLUGLUGLYVALALAGLNMET
8   SERVALGLYGLNARGALAMLYLEUTHRILE
9   SERPROASPTYRALATYRGLYALATHRGLY
10   HISPROGLYILEILEPROPROHISALATHR
11   LEUVALPHEASPVALGLULEULEUMLYLEU
12   GLU

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1.2 mM; sodium chloride 30 mM; DTT 3 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.8; temperature: 303 K

Experiments:

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

Software:

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

MagRO-NMRView, Kobayashi, Naohiro - chemical shift assignment, data analysis, peak picking

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

NMR spectrometers:

  • Bruker Avance III 800 MHz

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