BMRB Entry 18228

Name: Backbone and side chain assignment of TpbA
Published: 2012-03-08

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PDB ID: 2m3v
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18228
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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:

Backbone and side chain assignment of TpbA

Deposition date:

2012-01-27

Original release date:

2012-03-08

Authors:

Koveal, Dorothy; Peti, Wolfgang; Page, Rebecca

Citation:

Citation: Koveal, Dorothy; Jayasundera, Thusitha; Wood, Thomas; Peti, Wolfgang; Page, Rebecca. "Backbone and sidechain (1)H, (15)N and (13)C assignments of Tyrosine Phosphatase related to Biofilm formation A (TpbA) of Pseudomonas aeruginosa." Biomol. NMR Assignments 7, 57-59 (2013).
PubMed: 22392344

Assembly members:

Assembly members:
TpbA, polymer, 193 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Pseudomonas aeruginosa Taxonomy ID: 287 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas aeruginosa

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pRP1B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TpbA: GHMAETAAPRSPAWAQAVDP SINLYRMSPTLYRSALPNAQ SVALLQRLQVKTVVSFIKDD DRAWLGQAPVRVVSLPTHAD RVDDAEVLSVLRQLQAAERE GPVLMHCKHGNNRTGLFAAM YRIVVQGWDKQAALEEMQRG GFGDEDDMRDASAYVRGADV DGLRLAMANGECSPSRFALC HVREWMAQALDRP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	542
15N chemical shifts	172
1H chemical shifts	1205

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TpbA monomer	1

Entities:

Entity 1, TpbA monomer 193 residues - Formula weight is not available

G26, H27 and M28 are cloning artifacts.

1

GLY

HIS

MET

ALA

GLU

THR

ALA

PRO

ARG

2

SER

PRO

ALA

TRP

ALA

GLN

ALA

VAL

ASP

PRO

3

SER

ILE

ASN

LEU

TYR

ARG

MET

SER

PRO

THR

4

LEU

TYR

ARG

SER

ALA

LEU

PRO

ASN

ALA

GLN

5

SER

VAL

ALA

LEU

GLN

ARG

LEU

GLN

VAL

6

LYS

THR

VAL

SER

PHE

ILE

LYS

ASP

7

ASP

ARG

ALA

TRP

LEU

GLY

GLN

ALA

PRO

VAL

8

ARG

VAL

SER

LEU

PRO

THR

HIS

ALA

ASP

9

ARG

VAL

ASP

ALA

GLU

VAL

LEU

SER

VAL

10

LEU

ARG

GLN

LEU

GLN

ALA

GLU

ARG

GLU

11

GLY

PRO

VAL

LEU

MET

HIS

CYS

LYS

HIS

GLY

12

ASN

ARG

THR

GLY

LEU

PHE

ALA

MET

13

TYR

ARG

ILE

VAL

GLN

GLY

TRP

ASP

LYS

14

GLN

ALA

LEU

GLU

MET

GLN

ARG

GLY

15

GLY

PHE

GLY

ASP

GLU

ASP

MET

ARG

ASP

16

ALA

SER

ALA

TYR

VAL

ARG

GLY

ALA

ASP

VAL

17

ASP

GLY

LEU

ARG

LEU

ALA

MET

ALA

ASN

GLY

18

GLU

CYS

SER

PRO

SER

ARG

PHE

ALA

LEU

CYS

19

HIS

VAL

ARG

GLU

TRP

MET

ALA

GLN

ALA

LEU

20

ASP

ARG

PRO

Samples:

sample_1: TpbA, [U-15N], 1.1 mM; TRIS 10 mM; sodium chloride 100 mM; TCEP 0.5 mM

sample_2: TpbA, [U-13C, U-15N], 1.0 mM; TRIS 10 mM; sodium chloride 100 mM; TCEP 0.5 mM

sample_3: TpbA 1.0 mM; TRIS 10 mM; sodium chloride 100 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_3	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 800 MHz

BMRB	18977
PDB	2M3V 4R0S
DBJ	BAK91895 BAP20213 BAP49072 BAQ37900 BAR66014
EMBL	CDH75498 CDM50177 CDO83381 CEI03735 CEI78250
GB	AAG07272 AAT49761 ABJ13157 AFM63275 AGI79981
REF	NP_252574 WP_003092976 WP_003105672 WP_003111594 WP_003118289