BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15252

Title: Solution Structure of T4 Bacteriophage Helicase Uvsw.1   PubMed: 17878153

Deposition date: 2007-05-17 Original release date: 2007-10-29

Authors: Sivakolundu, Sivashankar; Lee, Tracy; White, Stephen; Kriwacki, Richard

Citation: Kerr, Iain; Sivakolundu, Sivashankar; Li, Zhenmei; Buchsbaum, Jeffrey; Knox, Luke; Kriwacki, Richard; White, Stephen. "Crystallographic and NMR analyses of UvsW and UvsW.1 from bacteriophage T4"  J. Biol. Chem. 282, 34392-34400 (2007).

Assembly members:
UvsW.1, polymer, 79 residues, 9096.122 Da.

Natural source:   Common Name: Bacteriophage T4   Taxonomy ID: 10665   Superkingdom: Viruses   Kingdom: not available   Genus/species: T4-like viruses T4

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):
UvsW.1: GSHMLLEFKQFLYEASIDEF MGKIASCQTLEGLEELEAYY KKRVKETELKDTDDISVRDA LAGKRAELEDSDDEVEESF

Data sets:
Data typeCount
13C chemical shifts231
15N chemical shifts78
1H chemical shifts442
heteronuclear NOE values72

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit 11

Entities:

Entity 1, subunit 1 79 residues - 9096.122 Da.

1   GLYSERHISMETLEULEUGLUPHELYSGLN
2   PHELEUTYRGLUALASERILEASPGLUPHE
3   METGLYLYSILEALASERCYSGLNTHRLEU
4   GLUGLYLEUGLUGLULEUGLUALATYRTYR
5   LYSLYSARGVALLYSGLUTHRGLULEULYS
6   ASPTHRASPASPILESERVALARGASPALA
7   LEUALAGLYLYSARGALAGLULEUGLUASP
8   SERASPASPGLUVALGLUGLUSERPHE

Samples:

sample_1: UvsW.1, [U-99% 13C; U-99% 15N], 1.66 ± 0.1 mM; sodium phosphate 10 mM; NaCl 10 mM; DTT 1 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.02 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC, Steady state {1H}-15N NOEsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

FELIX v2000, Accelrys Software Inc. - chemical shift assignment, peak picking, processing

ARIA v1.2, Linge, O'Donoghue and Nilges - chemical shift assignment, structure solution

AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Koll - refinement

ProcheckNMR, Laskowski and MacArthur - data analysis

TALOS, Cornilescu, Delaglio and Bax - restraint generation

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAI83196
EMBL CCI89077 CUL01145 CUL01694 CUL02025 CUL02331
GB AAD42668 ABI95005 ACP30825 ACP31101 ADJ39905
REF NP_049796 YP_002854138 YP_002854517 YP_004415076 YP_006986738
SP P20703
AlphaFold P20703

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