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Biological Magnetic Resonance Data Bank


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BMRB Entry 30295

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR30295
MolProbity Validation Chart

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Title: Solution Structure of BlsM   PubMed: 31876335

Deposition date: 2017-05-17 Original release date: 2018-05-17

Authors: Kang, M.; Doddapaneni, K.; Heppner, Z.; Wu, Z.

Citation: Kang, Minhee; Doddapaneni, Kiran; Sarni, Samantha; Heppner, Zach; Wysocki, Vicki; Wu, Zhengrong. "Solution structure of the nucleotide hydrolase BlsM: Implication of its substrate specificity"  Protein Sci. 29, 1760-1773 (2020).

Assembly members:
entity_1, polymer, 163 residues, 17857.422 Da.

Natural source:   Common Name: Streptomyces griseochromogenes   Taxonomy ID: 68214   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptomyces griseochromogenes

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

Entity Sequences (FASTA):
entity_1: KAGVRSVFLAGPFMGLVNPE TNSMPSAEQLPFLTLIEHFE KQGLEVFNAHRREAWGAQVL TPEECTPLDQLEIRKADVFV AIPGIPPSPGTHVEIGWASA FDKPIVLLLEEGREEEYGFL VRGLGTVAAVEFVHYKDIAL AKPQIDAAIRKVVDRVNNPA ATP

Data sets:
Data typeCount
13C chemical shifts621
15N chemical shifts140
1H chemical shifts925

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_1, 21

Entities:

Entity 1, entity_1, 1 163 residues - 17857.422 Da.

1   LYSALAGLYVALARGSERVALPHELEUALA
2   GLYPROPHEMETGLYLEUVALASNPROGLU
3   THRASNSERMETPROSERALAGLUGLNLEU
4   PROPHELEUTHRLEUILEGLUHISPHEGLU
5   LYSGLNGLYLEUGLUVALPHEASNALAHIS
6   ARGARGGLUALATRPGLYALAGLNVALLEU
7   THRPROGLUGLUCYSTHRPROLEUASPGLN
8   LEUGLUILEARGLYSALAASPVALPHEVAL
9   ALAILEPROGLYILEPROPROSERPROGLY
10   THRHISVALGLUILEGLYTRPALASERALA
11   PHEASPLYSPROILEVALLEULEULEUGLU
12   GLUGLYARGGLUGLUGLUTYRGLYPHELEU
13   VALARGGLYLEUGLYTHRVALALAALAVAL
14   GLUPHEVALHISTYRLYSASPILEALALEU
15   ALALYSPROGLNILEASPALAALAILEARG
16   LYSVALVALASPARGVALASNASNPROALA
17   ALATHRPRO

Samples:

sample_1: sodium phosphate 25 mM; DTT 2 mM; sodium chloride 25 mM; beta-mercaptoethanol 2 mM; sodium azide 0.02%; Blasticidin M, [U-15N], 0.8 mM

sample_2: sodium azide 0.02%; Blasticidin M, [U-13C; U-15N], 0.8 mM

sample_3: Blasticidin M, [U-100% 13C; U-100% 15N; U-95% 2H], 0.8 mM

sample_4: Blasticidin M, [U-10% 13C; U-100% 15N], 0.8 mM

sample_5: Blasticidin M, [U-15N], 1.25 mM; Blasticidin M, [U-13C; U-15N], 1.25 mM

sample_6: Blasticidin M, [U-15N], 0.8 mM

sample_conditions_1: ionic strength: 178 mM; pH: 6.50; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HN(COCA)CBsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_4isotropicsample_conditions_1
3D 15N NOESY-TROSYsample_1isotropicsample_conditions_1
3D HMQC-NOESY-HSQCsample_2isotropicsample_conditions_1
3D 15N/13C-filtered 13C-edited NOESYsample_5isotropicsample_conditions_1
2D 1H-15N HSQCsample_6isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz

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