BMRB Entry 30970

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30970
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
NMR structure of a designed cold unfolding four helix bundle
Deposition date:
2021-11-29
Original release date:
2022-02-25
Authors:
Pulavarti, S.; Szyperski, T.; Yuen, S.; Maguire, J.; Griffin, J.; Kuhlman, B.
Citation:

Citation: Pulavarti, Surya; Maguire, Jack; Yuen, Shirley; Harrison, Joseph; Griffin, Jermel; Premkumar, Lakshmanane; Esposito, Edward; Makhatadze, George; Garcia, Angel; Weiss, Thomas; Snell, Edward; Kuhlman, Brian; Szyperski, Thomas. "From Protein Design to the Energy Landscape of a Cold Unfolding Protein"  J. Phys. Chem. B 126, 1212-1231 (2022).
PubMed: 35128921

Assembly members:

Assembly members:
entity_1, polymer, 104 residues, 12099.824 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHQEYIKKVADELKENSQN INDLLKEVEKNPEDMEYWNK IYRLLHTNKEIAETAGFSSV AKVEHTAMNLVDKMLNSEIK ITSDLIDKIKKKVDMSTREI DKKV

Data typeCount
13C chemical shifts461
15N chemical shifts109
1H chemical shifts764

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 104 residues - 12099.824 Da.

1   GLYSERHISGLNGLUTYRILELYSLYSVAL
2   ALAASPGLULEULYSGLUASNSERGLNASN
3   ILEASNASPLEULEULYSGLUVALGLULYS
4   ASNPROGLUASPMETGLUTYRTRPASNLYS
5   ILETYRARGLEULEUHISTHRASNLYSGLU
6   ILEALAGLUTHRALAGLYPHESERSERVAL
7   ALALYSVALGLUHISTHRALAMETASNLEU
8   VALASPLYSMETLEUASNSERGLUILELYS
9   ILETHRSERASPLEUILEASPLYSILELYS
10   LYSLYSVALASPMETSERTHRARGGLUILE
11   ASPLYSLYSVAL

Samples:

sample_1: DCUB1, [U-100% 13C; U-100% 15N], 1.2 mM; sodium phosphate 50 mM; sodium chloride 100 mM

sample_2: DCUB1, [U-5% 13C; U-100% 15N], 1.2 mM; sodium phosphate 50 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 8; 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
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

CARA, Keller and Wuthrich - chemical shift assignment

XEASY, Bartels et al. - data analysis

CARA v1.8, Keller and Wuthrich - peak picking

PROSA, Guntert - processing

AutoStructure, Huang, Tejero, Powers and Montelione - structure calculation

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Agilent Agilent DDR2 600 MHz

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