BMRB Entry 17736

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17736
MolProbity Validation Chart

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Title:
Solution NMR structure of the AHSA1-like protein CHU_1110 from Cytophaga hutchinsonii, Northeast Structural Genomics Consortium Target ChR152.
Deposition date:
2011-06-28
Original release date:
2011-07-18
Authors:
Yang, Yunhuang; Ramelot, Theresa; Lee, Dan; Ciccosanti, Colleen; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael
Citation:

Citation: Yang, Yunhuang; Ramelot, Theresa; Lee, Dan; Ciccosanti, Colleen; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of the AHSA1-like protein CHU_1110 from Cytophaga hutchinsonii, Northeast Structural Genomics Consortium Target ChR152."  .

Assembly members:

Assembly members:
AHSA1-like_protein_CHU_1110_from_Cytophaga_hutchinsonii, polymer, 175 residues, 20303.1 Da.

Natural source:

Natural source:   Common Name: CFB group bacteria   Taxonomy ID: 985   Superkingdom: bacteria   Kingdom: not available   Genus/species: Cytophaga hutchinsonii

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
AHSA1-like_protein_CHU_1110_from_Cytophaga_hutchinsonii: MRTDLALDFSVNKENKTITI KREFAAVRAIVWEAFTRAEI LDQWWAPKPWKAKTKSMDFK EGGTWLYAMVGPNGEEHWSI CEYAIIKPIERFTGKDGFTD ASGKLNTEMPRSNWDMRFID KGEITEVQYHISYDDVAQLE ATIQMGFKEGITMAMENLDE LLVSGKKLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts757
15N chemical shifts182
1H chemical shifts1189

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AHSA1-like protein CHU_11101

Entities:

Entity 1, AHSA1-like protein CHU_1110 175 residues - 20303.1 Da.

1   METARGTHRASPLEUALALEUASPPHESER
2   VALASNLYSGLUASNLYSTHRILETHRILE
3   LYSARGGLUPHEALAALAVALARGALAILE
4   VALTRPGLUALAPHETHRARGALAGLUILE
5   LEUASPGLNTRPTRPALAPROLYSPROTRP
6   LYSALALYSTHRLYSSERMETASPPHELYS
7   GLUGLYGLYTHRTRPLEUTYRALAMETVAL
8   GLYPROASNGLYGLUGLUHISTRPSERILE
9   CYSGLUTYRALAILEILELYSPROILEGLU
10   ARGPHETHRGLYLYSASPGLYPHETHRASP
11   ALASERGLYLYSLEUASNTHRGLUMETPRO
12   ARGSERASNTRPASPMETARGPHEILEASP
13   LYSGLYGLUILETHRGLUVALGLNTYRHIS
14   ILESERTYRASPASPVALALAGLNLEUGLU
15   ALATHRILEGLNMETGLYPHELYSGLUGLY
16   ILETHRMETALAMETGLUASNLEUASPGLU
17   LEULEUVALSERGLYLYSLYSLEUGLUHIS
18   HISHISHISHISHIS

Samples:

NC_sample: AHSA1-like protein CHU_1110 from Cytophaga hutchinsonii, [U-100% 13C; U-100% 15N], 1.05 ± 0.11 mM; Tris-HCl 10 ± 1 mM; sodium chloride 100 ± 5 mM; sodium azide 0.02 ± 0.001 %; DTT 5 ± 0.25 mM; H20 90%; D20 10%

NC5_sample: AHSA1-like protein CHU_1110 from Cytophaga hutchinsonii, [U-5% 13C; U-100% 15N], 1.07 ± 0.11 mM; Tris-HCl 10 ± 1 mM; sodium chloride 100 ± 5 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; H20 90%; D20 10%

NC_sample_in_D2O: AHSA1-like protein CHU_1110 from Cytophaga hutchinsonii, [U-100% 13C; U-100% 15N], 1.05 ± 0.11 mM; Tris-HCl 10 ± 1 mM; sodium chloride 100 ± 5 mM; sodium azide 0.02 ± 0.001 %; DTT 10 ± 0.5 mM; D2O 100%

sample_conditions_1: ionic strength: 0.2 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC-aromaticNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQCNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-13C HSQCNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-13C HSQC-CTNC5_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC5_sampleisotropicsample_conditions_1
3D 1H-13C NOESY_aliphNC_sampleisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HNCANC_sampleisotropicsample_conditions_1
3D HN(CO)CANC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D H(CCO)NHNC_sampleisotropicsample_conditions_1
3D C(CCO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-COSYNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D CCH-TOCSYNC_sample_in_D2Oisotropicsample_conditions_1
4D CC-NOESYNC_sample_in_D2Oisotropicsample_conditions_1

Software:

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1.4, Bruker Biospin - collection

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis

X-PLOR NIH v2.25, Schwieters, Kuszewski, Tjandra and Clore - structure solution

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.113, Goddard - data analysis

PSVS v1.4, Bhattacharya and Montelione - refinement

AutoAssign v2.30, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, chemical shift assignment

PDBStat v5.1, (PdbStat)-Roberto Tejero and Gaetano T. Montelione - structure solution

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift autoassignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance III 850 MHz

Related Database Links:

PDB
GB ABG58386
REF WP_011584501

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