BMRB Entry 30295

Name: Solution Structure of BlsM
Published: 2018-05-17

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PDB ID: 5vto
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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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution Structure of BlsM

Deposition date:

2017-05-17

Original release date:

2018-05-17

Authors:

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

Citation:

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).
PubMed: 31876335

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	621
15N chemical shifts	140
1H chemical shifts	925

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1, 1	1
2	entity_1, 2	1

Entities:

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

1

LYS

ALA

GLY

VAL

ARG

SER

VAL

PHE

LEU

ALA

2

GLY

PRO

PHE

MET

GLY

LEU

VAL

ASN

PRO

GLU

3

THR

ASN

SER

MET

PRO

SER

ALA

GLU

GLN

LEU

4

PRO

PHE

LEU

THR

LEU

ILE

GLU

HIS

PHE

GLU

5

LYS

GLN

GLY

LEU

GLU

VAL

PHE

ASN

ALA

HIS

6

ARG

GLU

ALA

TRP

GLY

ALA

GLN

VAL

LEU

7

THR

PRO

GLU

CYS

THR

PRO

LEU

ASP

GLN

8

LEU

GLU

ILE

ARG

LYS

ALA

ASP

VAL

PHE

VAL

9

ALA

ILE

PRO

GLY

ILE

PRO

SER

PRO

GLY

10

THR

HIS

VAL

GLU

ILE

GLY

TRP

ALA

SER

ALA

11

PHE

ASP

LYS

PRO

ILE

VAL

LEU

GLU

12

GLU

GLY

ARG

GLU

TYR

GLY

PHE

LEU

13

VAL

ARG

GLY

LEU

GLY

THR

VAL

ALA

VAL

14

GLU

PHE

VAL

HIS

TYR

LYS

ASP

ILE

ALA

LEU

15

ALA

LYS

PRO

GLN

ILE

ASP

ALA

ILE

ARG

16

LYS

VAL

ASP

ARG

VAL

ASN

PRO

ALA

17

ALA

THR

PRO

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HN(CO)CA	sample_3	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_4	isotropic	sample_conditions_1
3D 15N NOESY-TROSY	sample_1	isotropic	sample_conditions_1
3D HMQC-NOESY-HSQC	sample_2	isotropic	sample_conditions_1
3D 15N/13C-filtered 13C-edited NOESY	sample_5	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_6	isotropic	sample_conditions_1

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

BMRB Entry 30295

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: