BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 30763

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30763

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Title: Solution NMR Structure of DE NOVO DESIGNED Rossmann 2x3 Fold Protein r2x3_168, Northeast Structural Genomics Consortium (NESG) Target OR386

Deposition date: 2020-06-12 Original release date: 2020-08-03

Authors: Liu, G.; Montelione, G.

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 Accurate de novo design of asymetric alpha/beta proteins with ten or more secondary structure elements requires consideration of backbone strain Design principle proposed from designed larger alpha/beta-proteins not folded as designed: Consistency between local, non-local, and global structures"  . ., .-..

Assembly members:
entity_1, polymer, 125 residues, 14535.344 Da.

Natural source:   Common Name: not available   Taxonomy ID: 32630   Superkingdom: not available   Kingdom: not available   Genus/species: synthetic construct

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

Entity Sequences (FASTA):
entity_1: MGKVVFLSDDQEIIEEVSKK AEEEGYDIQTSNDKKEIIDR LKRRNIDMIIVKTEDKESIS EIIKQVLDSGAKVLILSSDE NIIESIRKQYPKVETRRAQD KEEVKDAVEEFLKEGGSLEH HHHHH

Data sets:
Data typeCount
13C chemical shifts539
15N chemical shifts127
1H chemical shifts886

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 125 residues - 14535.344 Da.

1   METGLYLYSVALVALPHELEUSERASPASP
2   GLNGLUILEILEGLUGLUVALSERLYSLYS
3   ALAGLUGLUGLUGLYTYRASPILEGLNTHR
4   SERASNASPLYSLYSGLUILEILEASPARG
5   LEULYSARGARGASNILEASPMETILEILE
6   VALLYSTHRGLUASPLYSGLUSERILESER
7   GLUILEILELYSGLNVALLEUASPSERGLY
8   ALALYSVALLEUILELEUSERSERASPGLU
9   ASNILEILEGLUSERILEARGLYSGLNTYR
10   PROLYSVALGLUTHRARGARGALAGLNASP
11   LYSGLUGLUVALLYSASPALAVALGLUGLU
12   PHELEULYSGLUGLYGLYSERLEUGLUHIS
13   HISHISHISHISHIS

Samples:

sample_1: OR386, [U-13C; U-15N], 0.6 mM

sample_2: OR386, [U-10% 13C; U-100% 15N], 0.6 mM

sample_3: OR386, [U-10% 13C; U-100% 15N], 0.6 mM

sample_conditions_1: ionic strength: 100 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 aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D SIMUTANEOUS 1H, 15N, 13C NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3anisotropicsample_conditions_1

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

ASDP, Huang, Montelione - structure calculation

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

XEASY, Bartels et al. - peak picking

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

NMR spectrometers:

  • Bruker AVANCE III 800 MHz
  • Bruker AVANCE 600 MHz

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