BMRB Entry 16562

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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/BMR16562
MolProbity Validation Chart

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Title:
SOLUTION NMR STRUCTURE OF DE NOVO DESIGNED ROSSMANN 2x2 FOLD PROTEIN, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR16
Deposition date:
2009-10-17
Original release date:
2009-11-02
Authors:
Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; CICCOSANTI, C.; Acton, Thomas; Baker, David; Montelione, Gaetano
Citation:

Citation: Liu, Gaohua; Koga, Nobuyasu; Baker, David; Montelione, Gaetano. "SOLUTION NMR STRUCTURE OF DENOVO DESIGNED ROSSMANN 2x2 FOLD PROTEIN, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR16"  .

Assembly members:

Assembly members:
2x2, polymer, 110 residues, 13078.123 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   Vector: pET29b+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
2x2: MLLYVLIISNDKKLIEEARK MAEKANLELRTVKTEDELKK YLEEFRKESQNIKVLILVSN DEELDKAKELAQKMEIDVRT RKVTSPDEAKRWIKEFSEEG GSLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts497
15N chemical shifts115
1H chemical shifts818

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OR161

Entities:

Entity 1, OR16 110 residues - 13078.123 Da.

1   METLEULEUTYRVALLEUILEILESERASN
2   ASPLYSLYSLEUILEGLUGLUALAARGLYS
3   METALAGLULYSALAASNLEUGLULEUARG
4   THRVALLYSTHRGLUASPGLULEULYSLYS
5   TYRLEUGLUGLUPHEARGLYSGLUSERGLN
6   ASNILELYSVALLEUILELEUVALSERASN
7   ASPGLUGLULEUASPLYSALALYSGLULEU
8   ALAGLNLYSMETGLUILEASPVALARGTHR
9   ARGLYSVALTHRSERPROASPGLUALALYS
10   ARGTRPILELYSGLUPHESERGLUGLUGLY
11   GLYSERLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.859 mM; H2O 93%; D2O 7%; NaCl 200 mM

sample_2: entity, [U-10% 13C; U-100% 15N], 0.867 mM; H2O 93%; D2O 7%; NaCl 200 mM

sample_conditions_1: ionic strength: 200 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_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
GFT (4,3)D HABCABcoNHNsample_1isotropicsample_conditions_1
SIMUTANEOUS 1H, 15N, 13C NOESYsample_1isotropicsample_conditions_1
3D CCHTOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
AROMATIC 1H, 15N, 13C NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

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

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

AutoStruct, Huang, Tejero, Powers and Montelione - data analysis, geometry optimization, refinement

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

TOPSPIN, Bruker Biospin - collection

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

VNMRJ, Varian - collection

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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 18558
PDB

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