BMRB Entry 27690

Name: MtFKBP
Published: 2019-03-28

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PDB ID: 6wbu
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27690
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:

MtFKBP

Deposition date:

2018-11-13

Original release date:

2019-03-28

Authors:

Andrade, Guilherme; Silva, Luis; Oliveira, Danielle; Pires, Jose; Almeida, Fabio; Anobom, Cristiane

Citation:

Citation: Andrade, Guilherme; Silva, Luis; Oliveira, Danielle; Pires, Jose; Almeida, Fabio; Anobom, Cristiane. "Backbone and side chain 1H, 15N and 13C assignments of a putative peptidyl prolyl cis-trans isomerase FKBP12 from Mycobacterium tuberculosis" Biomol. NMR Assignments 13, 239-243 (2019).
PubMed: 30879170

Assembly members:

Assembly members:
MtFKBP, polymer, 126 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mycobacterium tuberculosis Taxonomy ID: 1773 Superkingdom: Bacteria Kingdom: Terrabacteria Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28-a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MtFKBP: GAMALERPEIDFPEGQPPEY LDITDITEGDGPEAVKGSNV SMHYVGVSWSTGEEFDASWN RGSTLDFTLGTGRVIKGWDM GIAGMKVGGRRKLVIPPHLA YGDRSPSPAIKPGETLIFVV DLVGVG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	517
15N chemical shifts	133
1H chemical shifts	813

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FKBP12 monomer	1

Entities:

Entity 1, FKBP12 monomer 126 residues - Formula weight is not available

1

GLY

ALA

MET

ALA

LEU

GLU

ARG

PRO

GLU

ILE

2

ASP

PHE

PRO

GLU

GLY

GLN

PRO

GLU

TYR

3

LEU

ASP

ILE

THR

ASP

ILE

THR

GLU

GLY

ASP

4

GLY

PRO

GLU

ALA

VAL

LYS

GLY

SER

ASN

VAL

5

SER

MET

HIS

TYR

VAL

GLY

VAL

SER

TRP

SER

6

THR

GLY

GLU

PHE

ASP

ALA

SER

TRP

ASN

7

ARG

GLY

SER

THR

LEU

ASP

PHE

THR

LEU

GLY

8

THR

GLY

ARG

VAL

ILE

LYS

GLY

TRP

ASP

MET

9

GLY

ILE

ALA

GLY

MET

LYS

VAL

GLY

ARG

10

ARG

LYS

LEU

VAL

ILE

PRO

HIS

LEU

ALA

11

TYR

GLY

ASP

ARG

SER

PRO

SER

PRO

ALA

ILE

12

LYS

PRO

GLY

GLU

THR

LEU

ILE

PHE

VAL

13

ASP

LEU

VAL

GLY

VAL

GLY

Samples:

sample_1: PMSF 2 mM; EDTA 5 mM; sodium azide 5 mM; sodium chloride 150 mM; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 0.22 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin - processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker DRX 600 MHz
Bruker Avance 900 MHz

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