BMRB Entry 16811

Name: Solution Structure of Bacillus anthracis Sortase A (SrtA) Transpeptidase
Published: 2010-05-28

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PDB ID: 2kw8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16811
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution Structure of Bacillus anthracis Sortase A (SrtA) Transpeptidase

Deposition date:

2010-03-31

Original release date:

2010-05-28

Authors:

Weiner, Ethan; Robson, Scott; Marohn, Melanie; Clubb, Robert

Citation:

Citation: Weiner, Ethan; Robson, Scott; Marohn, Melanie; Clubb, Robert. "The Sortase A enzyme that attaches proteins to the cell wall of Bacillus anthracis contains an unusual active site architecture." J. Biol. Chem. 285, 23433-23443 (2010).
PubMed: 20489200

Assembly members:

Assembly members:
SrtA, polymer, 158 residues, 17110.521 Da.

Natural source:

Natural source: Common Name: Bacillus anthracis Taxonomy ID: 1392 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus anthracis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SrtA: GSHMDASKIDQPDLAEVANA SLDKKQVIGRISIPSVSLEL PVLKSSTEKNLLSGAATVKE NQVMGKGNYALAGHNMSKKG VLFSDIASLKKGDKIYLYDN ENEYEYAVTGVSEVTPDKWE VVEDHGKDEITLITCVSVKD NSKRYVVAGDLVGTKAKK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	592
15N chemical shifts	146
1H chemical shifts	962

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SrtA	1

Entities:

Entity 1, SrtA 158 residues - 17110.521 Da.

Residues 52-56 represent a non-native affinity tag

1

GLY

SER

HIS

MET

ASP

ALA

SER

LYS

ILE

ASP

2

GLN

PRO

ASP

LEU

ALA

GLU

VAL

ALA

ASN

ALA

3

SER

LEU

ASP

LYS

GLN

VAL

ILE

GLY

ARG

4

ILE

SER

ILE

PRO

SER

VAL

SER

LEU

GLU

LEU

5

PRO

VAL

LEU

LYS

SER

THR

GLU

LYS

ASN

6

LEU

SER

GLY

ALA

THR

VAL

LYS

GLU

7

ASN

GLN

VAL

MET

GLY

LYS

GLY

ASN

TYR

ALA

8

LEU

ALA

GLY

HIS

ASN

MET

SER

LYS

GLY

9

VAL

LEU

PHE

SER

ASP

ILE

ALA

SER

LEU

LYS

10

LYS

GLY

ASP

LYS

ILE

TYR

LEU

TYR

ASP

ASN

11

GLU

ASN

GLU

TYR

GLU

TYR

ALA

VAL

THR

GLY

12

VAL

SER

GLU

VAL

THR

PRO

ASP

LYS

TRP

GLU

13

VAL

GLU

ASP

HIS

GLY

LYS

ASP

GLU

ILE

14

THR

LEU

ILE

THR

CYS

VAL

SER

VAL

LYS

ASP

15

ASN

SER

LYS

ARG

TYR

VAL

ALA

GLY

ASP

16

LEU

VAL

GLY

THR

LYS

ALA

LYS

Samples:

sample_1: SrtA, [U-100% 15N], 4 mM; MES 10 mM; Bis-Tris 20 mM; H2O 93%; D2O 7%

sample_2: SrtA, [U-100% 13C; U-100% 15N], 2.5 mM; MES 10 mM; Bis-Tris 20 mM; H2O 93%; D2O 7%

sample_3: SrtA, [U-100% 13C; U-100% 15N], 2.5 mM; MES 10 mM; Bis-Tris 20 mM; H2O 93%; D2O 7%

sample_conditions_1: pH: 6.0; 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	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	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 HNCO	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 HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D HNHA	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1
3D HNHB	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1
3D HCACO	sample_2	isotropic	sample_conditions_1
4D 15N-13C HMQC-NOESY-HSQC	sample_2	isotropic	sample_conditions_1
2D (HB)CB(CGCDCE)HE	sample_2	isotropic	sample_conditions_1
2D (HB)CB(CGCD)HD	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC NOE with interleaved presat and no sat	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

PIPP, Garrett - peak picking

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

ATHNOS-CANDID, Herrmann, Guntert, Wuthrich - chemical shift assignment

ModelFree, Palmer - data analysis

ProcheckNMR, Laskowski and MacArthur - geometry optimization

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

xwinnmr, Bruker Biospin - collection

CARA, Keller - chemical shift assignment

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 600 MHz
Bruker Avance 800 MHz

BMRB	11570 26510
PDB	2KW8 2RUI
DBJ	BAL16456 BAR78533 GAE96182 GAO57723 GAO63420
EMBL	CJA38300 CJJ39486 CKE38654 CKE81514 CKE96545
GB	AAP24701 AAS39688 AAT29792 AAT52982 AAU19641
REF	NP_843215 WP_001041406 WP_001041710 WP_001041711 WP_001041715