BMRB Entry 30000

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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/BMR30000
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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All files associated with the entry

Title:
Solution NMR structure of De novo designed PLOOP2X3_50 fold protein, Northeast Structural Genomics Consortium (NESG) target OR258
Deposition date:
2015-12-01
Original release date:
2016-06-17
Authors:
Liu, G.; Castelllanos, J.; Koga, R.; Koga, N.; Xiao, R.; Pederson, K.; Janjua, H.; Kohan, E.; Acton, T.; Kornhaber, G.; Everett, J.; Baker, D.; Montelione, G.
Citation:

Citation: Koga, N.; Koga, R.; Liu, G.; Castellanos, J.; Montelione, G.; Baker, D.. "Role of backbone strain in de novo design of complex alpha/beta protein structures"  Nat. Commun. 12, 3921-3921 (2021).
PubMed: 34168113

Assembly members:

Assembly members:
entity_1, polymer, 134 residues, 15769.068 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli K-12

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGTVVIVVSRDERILEELLE VVLKSDPNVKTVRTDDKEKV KEEIEKARKQGRPIVIFIRG ATEEVVRDIVEYAQKEGLRV LVIMVDQDQEELERIYEQLK KDGVDVRVTDNEDEAKKRLK ELLEKVLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts594
15N chemical shifts130
1H chemical shifts994

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 134 residues - 15769.068 Da.

1   METGLYTHRVALVALILEVALVALSERARG
2   ASPGLUARGILELEUGLUGLULEULEUGLU
3   VALVALLEULYSSERASPPROASNVALLYS
4   THRVALARGTHRASPASPLYSGLULYSVAL
5   LYSGLUGLUILEGLULYSALAARGLYSGLN
6   GLYARGPROILEVALILEPHEILEARGGLY
7   ALATHRGLUGLUVALVALARGASPILEVAL
8   GLUTYRALAGLNLYSGLUGLYLEUARGVAL
9   LEUVALILEMETVALASPGLNASPGLNGLU
10   GLULEUGLUARGILETYRGLUGLNLEULYS
11   LYSASPGLYVALASPVALARGVALTHRASP
12   ASNGLUASPGLUALALYSLYSARGLEULYS
13   GLULEULEUGLULYSVALLEUGLUHISHIS
14   HISHISHISHIS

Samples:

sample_1: DTT 5 mM; OR258, [U-13C; U-15N], 0.89 mM; TRIS-HCl 10 mM; sodium azide 0.02%; sodium chloride 100 mM

sample_2: DTT 5 mM; OR258, [5%-13C; U-15N], 0.89 mM; TRIS-HCl 10 mM; sodium azide 0.02%; sodium chloride 100 mM

sample_conditions_1: ionic strength: 115 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D simutalneous 13C-aromatic, 13C-aliphatic, 15N edited 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC methylsample_2isotropicsample_conditions_1

Software:

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

XEASY, Bartels et al. - peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz

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