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 4289

Title: 1H and 15N Chemical-Shift Assignments of a Carboxy-Terminal Functional Domain of the Bacteriophage P22 Scaffolding Protein

Deposition date: 1998-12-29 Original release date: 2001-03-02

Authors: Sun, Yahong; Krishna, N.

Citation: Sun, Yahong; Krishna, N.. "1H and 15N Chemical-Shift Assignments of a Carboxy-Terminal Functional Domain of the Bacteriophage P22 Scaffolding Protein"  Magn. Reson. Chem. 37, 602-604 (1999).

Assembly members:
P22 scaffolding protein, polymer, 67 residues, Formula weight is not available

Natural source:   Common Name: bacteriophage P22   Taxonomy ID: 10754   Superkingdom: not available   Kingdom: not available   Genus/species: not available bacteriophage P22

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
P22 scaffolding protein: ALTRLSERLTLKPRGKQISS APHADQPITGDVSAANKDAI RKQMDAAASKGDVETYRKLK AKLKGIR

Data sets:
Data typeCount
1H chemical shifts424
15N chemical shifts62

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C-terminal P22 scaffolding protein1

Entities:

Entity 1, C-terminal P22 scaffolding protein 67 residues - Formula weight is not available

1   ALALEUTHRARGLEUSERGLUARGLEUTHR
2   LEULYSPROARGGLYLYSGLNILESERSER
3   ALAPROHISALAASPGLNPROILETHRGLY
4   ASPVALSERALAALAASNLYSASPALAILE
5   ARGLYSGLNMETASPALAALAALASERLYS
6   GLYASPVALGLUTHRTYRARGLYSLEULYS
7   ALALYSLEULYSGLYILEARG

Samples:

sample_1: P22 scaffolding protein, [U-99% 15N], 1.1 mM; NaCl 25 mM; phosphate 50 mM; EDTA 2 mM

sample_2: P22 scaffolding protein 1.1 mM; NaCl 25 mM; phosphate 50 mM; EDTA 2 mM

Ex-cond_1: pH: 4.4; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
NOESYnot availablenot availableEx-cond_1
TOCSYnot availablenot availableEx-cond_1
DQF-COSYnot availablenot availableEx-cond_1
1H-15N NOESY-HSQCnot availablenot availableEx-cond_1
1H-15N TOCSY-HMQCnot availablenot availableEx-cond_1

Software:

FELIX v97.2 -

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Varian INOVA 600 MHz
  • Bruker AM 600 MHz

Related Database Links:

PDB
DBJ BAD15214 BAF80719 BAG12602 BAJ35316 BAP06069
EMBL CAR60453 CBG23390 CBY96613 CCR48949 CCT11723
GB AAA72962 AAF75046 AAL15526 AAM81388 AAX21428
REF NP_720328 WP_000433851 WP_000433852 WP_000433853 WP_000433854
SP P26748
TPG DAA00986
AlphaFold P26748

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