BMRB Entry 25381

Name: Structure of the E. coli threonylcarbamoyl-AMP synthase TsaC
Published: 2015-06-15

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PDB ID: 2mx1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25381
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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:

Structure of the E. coli threonylcarbamoyl-AMP synthase TsaC

Deposition date:

2014-12-06

Original release date:

2015-06-15

Authors:

Harris, Kimberly; Bobay, Benjamin; Sarachan, Kathryn; Sims, Alexis; Bilbille, Yann; Deutsch, Christopher; Iwata-Reuyl, Dirk; Agris, Paul

Citation:

Citation: Harris, Kimberly; Bobay, Benjamin; Sarachan, Kathryn; Sims, Alexis; Bilbille, Yann; Deutsch, Christopher; Iwata-Reuyl, Dirk; Agris, Paul. "NMR-based Structural Analysis of Threonylcarbamoyl-AMP Synthase and Its Substrate Interactions" J. Biol. Chem. 290, 20032-20043 (2015).
PubMed: 26060251

Assembly members:

Assembly members:
entity, polymer, 189 residues, 20655.629 Da.

Natural source:

Natural source: Common Name: E.coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: NNNLQRDAIAAAIDVLNEER VIAYPTEAVFGVGCDPDSET AVMRLLELKQRPVDKGLILI AANYEQLKPYIDDTMLTDVQ RETIFSRWPGPVTFVFPAPA TTPRWLTGRFDSLAVRVTDH PLVVALCQAYGKPLVSTSAN LSGLPPCRTVDEVRAQFGAA FPVVPGETGGRLNPSEIRDA LTGELFRQG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	723
15N chemical shifts	168
1H chemical shifts	1102

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 189 residues - 20655.629 Da.

1

ASN

LEU

GLN

ARG

ASP

ALA

ILE

ALA

2

ALA

ILE

ASP

VAL

LEU

ASN

GLU

ARG

3

VAL

ILE

ALA

TYR

PRO

THR

GLU

ALA

VAL

PHE

4

GLY

VAL

GLY

CYS

ASP

PRO

ASP

SER

GLU

THR

5

ALA

VAL

MET

ARG

LEU

GLU

LEU

LYS

GLN

6

ARG

PRO

VAL

ASP

LYS

GLY

LEU

ILE

LEU

ILE

7

ALA

ASN

TYR

GLU

GLN

LEU

LYS

PRO

TYR

8

ILE

ASP

THR

MET

LEU

THR

ASP

VAL

GLN

9

ARG

GLU

THR

ILE

PHE

SER

ARG

TRP

PRO

GLY

10

PRO

VAL

THR

PHE

VAL

PHE

PRO

ALA

PRO

ALA

11

THR

PRO

ARG

TRP

LEU

THR

GLY

ARG

PHE

12

ASP

SER

LEU

ALA

VAL

ARG

VAL

THR

ASP

HIS

13

PRO

LEU

VAL

ALA

LEU

CYS

GLN

ALA

TYR

14

GLY

LYS

PRO

LEU

VAL

SER

THR

SER

ALA

ASN

15

LEU

SER

GLY

LEU

PRO

CYS

ARG

THR

VAL

16

ASP

GLU

VAL

ARG

ALA

GLN

PHE

GLY

ALA

17

PHE

PRO

VAL

PRO

GLY

GLU

THR

GLY

18

ARG

LEU

ASN

PRO

SER

GLU

ILE

ARG

ASP

ALA

19

LEU

THR

GLY

GLU

LEU

PHE

ARG

GLN

GLY

Samples:

sample_1: Recombinant TsaC protein, [U-100% 13C; U-100% 15N], 1 mM; D2O, [U-100% 2H], 10%; potassium phosphate 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_2: Recombinant TsaC protein, [U-100% 13C; U-100% 15N], 1 mM; D2O, [U-100% 2H], 10%; potassium phosphate 20 mM; sodium chloride 100 mM; Pf1 bacteriophage 12 mg/mL; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 15N TOCSY-HSQC	sample_1	isotropic	sample_conditions_1
1H-15N HSQC-IPAP	sample_2	isotropic	sample_conditions_1
1H-15N TROSY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

SPARKY, Goddard - peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

Varian Inova 600 MHz
Bruker Avance II 700 MHz

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