BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15335

Title: Structure of Staphylococcus saprophyticus CHAP domain protein. Northeast Structural Genomics Target SyR11.   PubMed: 18951393

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: 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).

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

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

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

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

Data typeCount
13C chemical shifts608
15N chemical shifts178
1H chemical shifts954

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1SyR111

Entities:

Entity 1, SyR11 163 residues - 16997.244 Da.

C term LEHHHHHH tag

1   METLYSLYSLEUVALTHRALATHRTHRLEU
2   THRALAGLYILEGLYALAALAILEVALGLY
3   LEUASPHISGLYASNGLUALAASPALAALA
4   GLUGLNTHRGLNPROTHRASNGLNSERTHR
5   THRGLNSERTHRSERGLYSERSERALAASN
6   LEUTYRTHRALAGLYGLNCYSTHRTRPTYR
7   VALTYRASPLYSVALGLYGLYASNILEGLY
8   SERTHRTRPGLYASNALAASNASNTRPALA
9   SERALAALASERSERALAGLYTYRTHRVAL
10   ASNASNSERPROGLUALAGLYSERILELEU
11   GLNSERTHRALAGLYGLYTYRGLYHISVAL
12   ALATYRVALGLUASNVALASNSERASPGLY
13   SERVALGLUVALSERGLUMETASNTYRASN
14   GLYGLYPROPHESERVALSERGLUARGTHR
15   ILESERALAGLYGLUALASERSERTYRASN
16   TYRILEHISLEUASNLEUGLUHISHISHIS
17   HISHISHIS

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:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCOCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY (aliph)sample_1isotropicsample_conditions_1
3D 1H-13C NOESY (arom)sample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
HETnoesample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC (aliph)sample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQC (arom)sample_1isotropicsample_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

Related Database Links:

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