BMRB Entry 17613

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17613
MolProbity Validation Chart

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Title:
Solution NMR Structure of DE NOVO DESIGNED PROTEIN, P-LOOP NTPASE FOLD, Northeast Structural Genomics Consortium Target OR36
Deposition date:
2011-04-29
Original release date:
2011-06-01
Authors:
Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Janjua, Haleema; Ciccosanti, colleen; Lee, Hsiau-Wei; Acton, Thomas; Everett, John; Baker, David; Montelione, Gaetano; Northeast Structural Genomics Consortium, NESG
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:
OR36, polymer, 134 residues, 16031.576 Da.

Natural source:

Natural source:   Common Name: Denove Design   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   Vector: pET29b+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
OR36: MKILILINTNNDELIKKIKK EVENQGYQVRDVNDSDELKK EMKKLAEEKNFEKILIISND KQLLKEMLELISKLGYKVFL LLQDQDENELEEFKRKIESQ GYEVRKVTDDEEALKIVREF MQKAGSLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts598
15N chemical shifts139
1H chemical shifts1003

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OR361

Entities:

Entity 1, OR36 134 residues - 16031.576 Da.

1   METLYSILELEUILELEUILEASNTHRASN
2   ASNASPGLULEUILELYSLYSILELYSLYS
3   GLUVALGLUASNGLNGLYTYRGLNVALARG
4   ASPVALASNASPSERASPGLULEULYSLYS
5   GLUMETLYSLYSLEUALAGLUGLULYSASN
6   PHEGLULYSILELEUILEILESERASNASP
7   LYSGLNLEULEULYSGLUMETLEUGLULEU
8   ILESERLYSLEUGLYTYRLYSVALPHELEU
9   LEULEUGLNASPGLNASPGLUASNGLULEU
10   GLUGLUPHELYSARGLYSILEGLUSERGLN
11   GLYTYRGLUVALARGLYSVALTHRASPASP
12   GLUGLUALALEULYSILEVALARGGLUPHE
13   METGLNLYSALAGLYSERLEUGLUHISHIS
14   HISHISHISHIS

Samples:

sample_NC: OR36, [U-100% 13C; U-100% 15N], 0.71 mM; H2O 90%; D2O 10%; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; MES 20 mM; DSS 50 uM; Proteinase Inhibitors 1 x

sample_NC5: OR36, [U-10% 13C; U-100% 15N], 0.95 mM; H2O 90%; D2O 10%; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; MES 20 mM; DSS 50 uM; Proteinase Inhibitors 1 x

sample_NC5_RDC: OR36, [U-10% 13C; U-100% 15N], 0.95 mM; H2O 90%; D2O 10%; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; MES 20 mM; DSS 50 uM; Proteinase Inhibitors 1 x

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_NC5isotropicsample_conditions_1
3D HNCOsample_NCisotropicsample_conditions_1
3D CBCA(CO)NHsample_NCisotropicsample_conditions_1
3D HNCACBsample_NCisotropicsample_conditions_1
3D 1H-13C arom NOESYsample_NCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_NCisotropicsample_conditions_1
2D 1H-15N HSQCsample_NC5_RDCisotropicsample_conditions_1
2D HetNOEsample_NC5isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

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

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 600 MHz

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