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Solution Structure of the SPOR domain from E. coli DamX
Authors
Williams, K.B., Arends, S.RYAN., Popham, D.L., Fowler, C.ANDREW., Weiss, D.S.
Assembly
DamX SPOR domain
Entity
1. DamX SPOR domain (polymer, Thiol state: not present), 106 monomers, 11855.99 Da Detail

MRGSHHHHHH GSNNNGSLKS APSSHYTLQL SSSSNYDNLN GWAKKENLKN YVVYETTRNG QPWYVLVSGV YASKEEAKKA VSTLPADVQA KNPWAKPLRQ VQADLK


Formula weight
11855.99 Da
Source organism
Escherichia coli
Exptl. method
solution NMR
Refine. method
torsion angle dynamics
Data set
assigned_chemical_shifts, heteronucl_NOEs, heteronucl_T1_relaxation, heteronucl_T2_relaxation
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 94.1 %, Completeness (bb): 93.3 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All94.1 % (1156 of 1229)93.8 % (601 of 641)94.5 % (443 of 469)94.1 % (112 of 119)
Backbone93.3 % (584 of 626)92.5 % (197 of 213)93.9 % (293 of 312)93.1 % (94 of 101)
Sidechain95.0 % (668 of 703)94.4 % (404 of 428)95.7 % (246 of 257)100.0 % (18 of 18)
Aromatic95.5 % (107 of 112)100.0 % (56 of 56)90.6 % (48 of 53)100.0 % (3 of 3)
Methyl100.0 % (94 of 94)100.0 % (47 of 47)100.0 % (47 of 47)

1. DamX SPOR domain polypeptide

MRGSHHHHHH GSNNNGSLKS APSSHYTLQL SSSSNYDNLN GWAKKENLKN YVVYETTRNG QPWYVLVSGV YASKEEAKKA VSTLPADVQA KNPWAKPLRQ VQADLK

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5


#NameIsotope labelingTypeConcentration
1DamX SPOR domain polypeptide[U-99% 15N]0.7 mM
2H2Onatural abundance90 %
3D2O[U-99% 2H]10 %
4potassium phosphatenatural abundance50 mM
5potassium chloridenatural abundance50 mM
Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5


#NameIsotope labelingTypeConcentration
6DamX SPOR domain polypeptide[U-99% 13C; U-99% 15N]0.7 mM
7D2O[U-99% 2H]100 %
8potassium phosphatenatural abundance50 mM
9potassium chloridenatural abundance50 mM
Sample #3

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5


#NameIsotope labelingTypeConcentration
10DamX SPOR domain polypeptide[U-99% 13C; U-99% 15N]0.7 mM
11H2Onatural abundance90 %
12D2O[U-99% 2H]10 %
13potassium phosphatenatural abundance50 mM
14potassium chloridenatural abundance50 mM
Sample #4

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5


#NameIsotope labelingTypeConcentration
15DamX SPOR domain polypeptide[U-99% 15N]0.7 mM
16H2Onatural abundance90 %
17D2O[U-99% 2H]10 %
18potassium phosphatenatural abundance50 mM
19potassium chloridenatural abundance50 mM
20PEG(C12E5):n-hexanolnatural abundance5 %

LACS Plot; CA
Referencing offset: -0.09 ppm, Outliers: 1 Detail
LACS Plot; CB
Referencing offset: -0.09 ppm, Outliers: 1 Detail
LACS Plot; HA
Referencing offset: 0.02 ppm, Outliers: 3 Detail
LACS Plot; CO
Referencing offset: 0.32 ppm, Outliers: 1 Detail
Protein Blocks Logo
Calculated from 25 models in PDB: 2LFV, Strand ID: A Detail


Heteronucl. T1
94 T1 values in 1 lists
Coherence Sz, Field strength (1H) 600 MHz, Pressure 1 atm, Temperature 298 K, pH 6.5 Detail
Heteronucl. T2
94 T2 values in 1 lists
Coherence S(+,-), Field strength (1H) 600 MHz, Pressure 1 atm, Temperature 298 K, pH 6.5 Detail
Heteronucl. NOE
94 NOE values in 1 lists
Value type peak integral, Field strength (1H) 600 MHz, Pressure 1 atm, Temperature 298 K, pH 6.5 Detail
Heteronucl. T1/T2
94 T1/T2 values in 1 lists
Field strength (1H) 600 MHz, Pressure 1 atm, Temperature 298 K, pH 6.5 Detail
Release date
2012-07-16
Citation
Nuclear magnetic resonance solution structure of the peptidoglycan-binding SPOR domain from Escherichia coli DamX: insights into septal localization
Williams, K.B., Yahashiri, A., Arends, S.RYAN., Popham, D.L., Fowler, C.ANDREW., Weiss, D.S.
Biochemistry (2013), 52, 627-639, PubMed 23290046 , DOI 10.1021/bi301609e ,
Related entities 1. DamX SPOR domain, : 1 : 3 : 2 entities Detail
Interaction partners 1. DamX SPOR domain, : 11 interactors Detail
Experiments performed 25 experiments Detail
NMR combined restraints 5 contents Detail
Keywords cell division, DamX, peptidoglycan binding protein, protein, RNP domain, SPOR domain