BMRB Entry 34913

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34913
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Title:
Solution structure of the Pyrococcus abyssi Rpa2 winged-helix domain
Deposition date:
2024-04-22
Original release date:
2024-12-02
Authors:
Le Meur, R.; Madru, C.; Cordier, F.; Sauguet, L.; Guijarro, J.
Citation:

Citation: Martinez-Carranza, M.; Vialle, L.; Madru, C.; Cordier, F.; Dizkirici Tekpinar, A.; Haouz, A.; Legrand, P.; Le Meur, R.; England, P.; Dulermo, R.; Guijarro, J.; Henneke, G.; Sauguet, L.. "Communication between DNA polymerases and Replication Protein A within the archaeal replisome"  .

Assembly members:

Assembly members:
entity_1, polymer, 94 residues, 11006.380 Da.

Natural source:

Natural source:   Common Name: Pyrococcus abyssi GE5   Taxonomy ID: 272844   Superkingdom: Archaea   Kingdom: not available   Genus/species: Pyrococcus abyssi

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GTGGIMMEERSIEEPMEELL EEEIPEEKEENELLEKAKED ILNILRQKRTAISRKYILKK LGDKYDEETIDDAITELLAQ GEIYEPETGYYKLL

Data sets:
Data typeCount
13C chemical shifts416
15N chemical shifts95
1H chemical shifts645

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 94 residues - 11006.380 Da.

1   GLYTHRGLYGLYILEMETMETGLUGLUARG
2   SERILEGLUGLUPROMETGLUGLULEULEU
3   GLUGLUGLUILEPROGLUGLULYSGLUGLU
4   ASNGLULEULEUGLULYSALALYSGLUASP
5   ILELEUASNILELEUARGGLNLYSARGTHR
6   ALAILESERARGLYSTYRILELEULYSLYS
7   LEUGLYASPLYSTYRASPGLUGLUTHRILE
8   ASPASPALAILETHRGLULEULEUALAGLN
9   GLYGLUILETYRGLUPROGLUTHRGLYTYR
10   TYRLYSLEULEU

Samples:

sample_1: RPA2WH, [U-98% 13C; U-98% 15N], 300 uM; MES 20 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 170 mM; pH: 6; pressure: 1 atm; temperature: 308.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHANsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D CB(CGCD)HDsample_1isotropicsample_conditions_1
2D CB(CGCDCE)HEsample_1isotropicsample_conditions_1

Software:

TopSpin v4.1.3, Bruker Biospin - collection

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

CcpNmr Analysis v2.5.2, CCPN - chemical shift assignment

CcpNmr Analysis, CCPN - peak picking

CNS v1.2.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

ARIA v2.3.2, Linge, O'Donoghue and Nilges - chemical shift calculation

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz

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