BMRB Entry 15335

Name: Structure of Staphylococcus saprophyticus CHAP domain protein. Northeast Structural Genomics Target SyR11.
Published: 2007-08-07

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15335

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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 Staphylococcus saprophyticus CHAP domain protein. Northeast Structural Genomics Target SyR11.

Deposition date:

2007-06-27

Original release date:

2007-08-07

Authors:

Rossi, Paolo; Aramini, James; Chen, Chen; Nwosu, Chioma; Cunningham, Kellie; Owens, Leah; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation:

Citation: Rossi, Paolo; Aramini, James; Xiao, Rong; Chen, Chen; Nwosu, Chioma; Owens, Leah; Maglaqui, Melissa; Nair, Rajesh; Fischer, Markus; Acton, Thomas; Honig, Barry; Rost, Burkhard; Montelione, Gaetano. "Structural elucidation of the Cys-His-Glu-Asn proteolytic relay in the secreted CHAP domain enzyme from the human pathogen Staphylococcus saprophyticus." Proteins 74, 515-9 (2009).
PubMed: 18951393

Assembly members:

Assembly members:
SyR11, polymer, 163 residues, 16997.244 Da.

Natural source:

Natural source: Common Name: Staphylococcus saprophyticus Taxonomy ID: 29385 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus saprophyticus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: SyR11-21.5

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SyR11: MKKLVTATTLTAGIGAAIVG LDHGNEADAAEQTQPTNQST TQSTSGSSANLYTAGQCTWY VYDKVGGNIGSTWGNANNWA SAASSAGYTVNNSPEAGSIL QSTAGGYGHVAYVENVNSDG SVEVSEMNYNGGPFSVSERT ISAGEASSYNYIHLNLEHHH HHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	608
15N chemical shifts	178
1H chemical shifts	954

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SyR11	1

Entities:

Entity 1, SyR11 163 residues - 16997.244 Da.

C term LEHHHHHH tag

1

MET

LYS

LEU

VAL

THR

ALA

THR

LEU

2

THR

ALA

GLY

ILE

GLY

ALA

ILE

VAL

GLY

3

LEU

ASP

HIS

GLY

ASN

GLU

ALA

ASP

ALA

4

GLU

GLN

THR

GLN

PRO

THR

ASN

GLN

SER

THR

5

THR

GLN

SER

THR

SER

GLY

SER

ALA

ASN

6

LEU

TYR

THR

ALA

GLY

GLN

CYS

THR

TRP

TYR

7

VAL

TYR

ASP

LYS

VAL

GLY

ASN

ILE

GLY

8

SER

THR

TRP

GLY

ASN

ALA

ASN

TRP

ALA

9

SER

ALA

SER

ALA

GLY

TYR

THR

VAL

10

ASN

SER

PRO

GLU

ALA

GLY

SER

ILE

LEU

11

GLN

SER

THR

ALA

GLY

TYR

GLY

HIS

VAL

12

ALA

TYR

VAL

GLU

ASN

VAL

ASN

SER

ASP

GLY

13

SER

VAL

GLU

VAL

SER

GLU

MET

ASN

TYR

ASN

14

GLY

PRO

PHE

SER

VAL

SER

GLU

ARG

THR

15

ILE

SER

ALA

GLY

GLU

ALA

SER

TYR

ASN

16

TYR

ILE

HIS

LEU

ASN

LEU

GLU

HIS

17

HIS

Samples:

sample_1: SyR11, [U-100% 13C; U-100% 15N], 0.66 mM; MES 20 mM; sodium azide 0.02%; DTT 100 mM; calcium chloride 5 mM; sodium chloride 100 mM

sample_2: SyR11, [U-100% 13C; U-100% 15N], 0.66 mM; MES 20 mM; sodium azide 0.02%; DTT 100 mM; calcium chloride 5 mM; sodium chloride 100 mM

sample_3: SyR11, [U-5% 13C; U-100% 15N], 0.94 mM; MES 20 mM; sodium azide 0.02%; DTT 100 mM; calcium chloride 5 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCOCACB	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 HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY (aliph)	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY (arom)	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
HETnoe	sample_3	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC (aliph)	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC (arom)	sample_1	isotropic	sample_conditions_1

Software:

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - structure solution

SPARKY v3.110, Goddard - data analysis

TOPSPIN v1.3, Bruker Biospin - collection

Molmol v2K.2, Koradi, Billeter and Wuthrich - visualization

X-PLOR NIH v2.11.2, Schwieters, Kuszewski, Tjandra and Clore - refinement

PSVS v1.3, Bhattacharya and Montelione - validation

DYANA, Guntert, Braun and Wuthrich - refinement

CNSSOLVE v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

MolProbity, Richardson - validation

PDBStat v5.0, PDBStat (Tejero) - refinement

ProcheckNMR, Laskowski and MacArthur - refinement

NMRPipe v2.4, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

EMBL	AP008934 CRV28521
SWS	Q49ZM2_STAS1
PDB	2K3A
DBJ	BAE17754
GB	EHY93150 KIJ87710
REF	WP_002482559