BMRB Entry 6185

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6185
MolProbity Validation Chart

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Title:
Solution structure of P22 Cro
Deposition date:
2004-04-22
Original release date:
2004-06-04
Authors:
Newlove, T.; Konieczka, J.; Cordes, M.
Citation:

Citation: Newlove, T.; Konieczka, J.; Cordes, M.. "Secondary structure switching in Cro protein evolution"  Structure 12, 569-581 (2004).
PubMed: 15062080

Assembly members:

Assembly members:
Regulatory protein cro, polymer, 61 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Bacteria phage P22   Taxonomy ID: 10754   Superkingdom: Viruses   Kingdom: not available   Genus/species: P22-like viruses Bacteria phage P22

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Regulatory protein cro: MYKKDVIDHFGTQRAVAKAL GISDAAVSQWKEVIPEKDAY RLEIVTAGALKYQENAYRQA A

Data sets:
Data typeCount
1H chemical shifts439
13C chemical shifts214
15N chemical shifts68

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Regulatory protein cro1

Entities:

Entity 1, Regulatory protein cro 61 residues - Formula weight is not available

1   METTYRLYSLYSASPVALILEASPHISPHE
2   GLYTHRGLNARGALAVALALALYSALALEU
3   GLYILESERASPALAALAVALSERGLNTRP
4   LYSGLUVALILEPROGLULYSASPALATYR
5   ARGLEUGLUILEVALTHRALAGLYALALEU
6   LYSTYRGLNGLUASNALATYRARGGLNALA
7   ALA

Samples:

sample_1: Regulatory protein cro 6 mM; sodium phosphate buffer 50 mM; H2O 90%; D2O 10%

sample_2: Regulatory protein cro, [U-15N], 3.5 mM; sodium phosphate buffer 50 mM; H2O 90%; D2O 10%

sample_3: Regulatory protein cro, [U-13C; U-15N], 2.75 mM; sodium phosphate buffer 50 mM; H2O 90%; D2O 10%

sample_4: Regulatory protein cro, [U-15N], 3.5 mM; sodium phosphate buffer 50 mM; D2O 100%

sample_cond_1: pH: 6.4; temperature: 293 K; ionic strength: 50 mM; pressure: 1 atm

sample_cond_2: pH: 6.4; temperature: 300 K; ionic strength: 50 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
2D NOESYnot availablenot availablenot available
HNHAnot availablenot availablenot available
HNHBnot availablenot availablenot available
3D 15N-separated NOESYnot availablenot availablenot available
3D 13C-separated NOESYnot availablenot availablenot available
hydrogen exchangenot availablenot availablenot available

Software:

XWINNMR v3.1 - collection

NMRPipe - processing

NMRView v4.1.3 - data analysis

CNS v1.1 - structure solution, refinement

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAF80763 BAG12646 BAI26412
EMBL CAA60874 CAB39982 CEK05850
GB AAA32268 AAF75025 AAM81424 AAW70527 ABV04679
REF NP_059607 WP_000276884 WP_000276885 WP_032160967 YP_001457062
SP P09964
TPG DAA01022
AlphaFold P09964

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