BMRB Entry 30977

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30977
MolProbity Validation Chart

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Title:
NMR structure of crosslinked cyclophilin A
Deposition date:
2021-12-20
Original release date:
2022-05-26
Authors:
Lu, M.; Toptygin, D.; Xiang, Y.; Shi, Y.; Schwieters, C.; Lipinski, E.; Ahn, J.; Byeon, I.; Gronenborn, A.
Citation:

Citation: Lu, M.; Toptygin, D.; Xiang, Y.; Shi, Y.; Schwieters, C.; Lipinski, E.; Ahn, J.; Byeon, I.; Gronenborn, A.. "The Magic of Linking Rings: Discovery of a Unique Photoinduced Fluorescent Protein Crosslink"  J. Am. Chem. Soc. 144, 10809-10816 (2022).
PubMed: 35574633

Assembly members:

Assembly members:
entity_1, polymer, 165 residues, 18065.502 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: MQNPTVFFDIAVDGEPLGRV SFELFADKVPKTAENFRALS TGEKGFGYKGSCFHRIIPGF MCQGGDFTRHNGTGGKSIYG EKFEDENFILKHTGPGILSM ANAGPNTNGSQFFICTAKTE WLDGKHVVFGKVKEGMNIVE AMERFGSRNGKTSKKITIAD CGQLE

Data sets:
Data typeCount
13C chemical shifts509
15N chemical shifts172
1H chemical shifts944

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 165 residues - 18065.502 Da.

1   METGLNASNPROTHRVALPHEPHEASPILE
2   ALAVALASPGLYGLUPROLEUGLYARGVAL
3   SERPHEGLULEUPHEALAASPLYSVALPRO
4   LYSTHRALAGLUASNPHEARGALALEUSER
5   THRGLYGLULYSGLYPHEGLYTYRLYSGLY
6   SERCYSPHEHISARGILEILEPROGLYPHE
7   METCYSGLNGLYGLYASPPHETHRARGHIS
8   ASNGLYTHRGLYGLYLYSSERILETYRGLY
9   GLULYSPHEGLUASPGLUASNPHEILELEU
10   LYSHISTHRGLYPROGLYILELEUSERMET
11   ALAASNALAGLYPROASNTHRASNGLYSER
12   GLNPHEPHEILECYSTHRALALYSTHRGLU
13   TRPLEUASPGLYLYSHISVALVALPHEGLY
14   LYSVALLYSGLUGLYMETASNILEVALGLU
15   ALAMETGLUARGPHEGLYSERARGASNGLY
16   LYSTHRSERLYSLYSILETHRILEALAASP
17   CYSGLYGLNLEUGLU

Samples:

sample_1: cyclophilin A, [U-13C; U-15N], 390 uM; sodium phosphate 25 mM; TCEP 1 mM; NaN3 0.02%

sample_conditions_1: ionic strength: 25 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C TROSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D simultaneous 13C,15N-edited NOESYsample_1isotropicsample_conditions_1

Software:

CcpNmr Analysis, CCPN - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

TopSpin, Bruker Biospin - collection

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

NMR spectrometers:

  • Bruker AVANCE 900 MHz
  • Bruker AVANCE III HD 600 MHz

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