BMRB Entry 15028

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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/BMR15028
MolProbity Validation Chart

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Title:
1H, 13C, and 15N Chemical Shift Assignments of Trx-ArsC complex
Deposition date:
2006-11-13
Original release date:
2008-06-23
Authors:
Jin, Changwen; Hu, Yunfei; Li, You; Zhang, Xinxin
Citation:

Citation: Li, Y.; Hu, Y.; Zhang, X.; Xu, H.; Lescop, E.; Xia, B.; Jin, C.. "Conformational fluctuations coupled to the thiol-disulfide transfer between thioredoxin and arsenate reductase in Bacillus subtilis"  J. Biol. Chem. 282, 11078-11083 (2007).
PubMed: 17303556

Assembly members:

Assembly members:
thioredoxin, polymer, 104 residues, 11377.1 Da.
arsenate_reductase, polymer, 139 residues, 15531.3 Da.

Natural source:

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a & pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
thioredoxin: MAIVKATDQSFSAETSEGVV LADFWAPWCGPSKMIAPVLE ELDQEMGDKLKIVKIDVDEN QETAGKYGVMSIPTLLVLKD GEVVETSVGFKPKEALQELV NKHL
arsenate_reductase: MENKIIYFLSTGNSARSQMA EGWAKQYLGDEWKVYSAGIE AHGLNPNAVKAMKEVGIDIS NQTSDIIDSDILNNADLVVT LSGDAADKCPMTPPHVKREH WGFDDPARAQGTEEEKWAFF QRVRDEIGNRLKEFAETGK

Data sets:
Data typeCount
13C chemical shifts740
15N chemical shifts249
1H chemical shifts1543

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1thioredoxin1
2arsenate_reductase2

Entities:

Entity 1, thioredoxin 104 residues - 11377.1 Da.

1   METALAILEVALLYSALATHRASPGLNSER
2   PHESERALAGLUTHRSERGLUGLYVALVAL
3   LEUALAASPPHETRPALAPROTRPCYSGLY
4   PROSERLYSMETILEALAPROVALLEUGLU
5   GLULEUASPGLNGLUMETGLYASPLYSLEU
6   LYSILEVALLYSILEASPVALASPGLUASN
7   GLNGLUTHRALAGLYLYSTYRGLYVALMET
8   SERILEPROTHRLEULEUVALLEULYSASP
9   GLYGLUVALVALGLUTHRSERVALGLYPHE
10   LYSPROLYSGLUALALEUGLNGLULEUVAL
11   ASNLYSHISLEU

Entity 2, arsenate_reductase 139 residues - 15531.3 Da.

1   METGLUASNLYSILEILETYRPHELEUSER
2   THRGLYASNSERALAARGSERGLNMETALA
3   GLUGLYTRPALALYSGLNTYRLEUGLYASP
4   GLUTRPLYSVALTYRSERALAGLYILEGLU
5   ALAHISGLYLEUASNPROASNALAVALLYS
6   ALAMETLYSGLUVALGLYILEASPILESER
7   ASNGLNTHRSERASPILEILEASPSERASP
8   ILELEUASNASNALAASPLEUVALVALTHR
9   LEUSERGLYASPALAALAASPLYSCYSPRO
10   METTHRPROPROHISVALLYSARGGLUHIS
11   TRPGLYPHEASPASPPROALAARGALAGLN
12   GLYTHRGLUGLUGLULYSTRPALAPHEPHE
13   GLNARGVALARGASPGLUILEGLYASNARG
14   LEULYSGLUPHEALAGLUTHRGLYLYS

Samples:

sample_1: Trx-ArsC complex, [U-13C; U-15N], 1 – 2 mM; Trx-ArsC complex1 – 2 mM; Tris-HCl 20 mM; Na2SO4 20 mM; KCL 40 mM

sample_2: Trx-ArsC complex mM; Trx-ArsC complex, [U-13C; U-15N], mM; Tris-HCl 20 mM; Na2SO4 20 mM; KCL 40 mM

sample_conditions_1: ionic strength: 0.08 M; pH: 6.85; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1

Software:

NMRView, B Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAI86356 BAM54098 BAM58927 GAK79977 BAA06970 BAA12434 BAM58640
EMBL CAA99577 CAB14810 CBI43781 CCF06106 CCG50792 CAB14519 CEI57801 CEJ78223
GB AAA87315 ABS74914 ADM38802 ADP33333 ADV93643 ADV93326 AFH58698 AFH58699 AFH58701 AFH58702
REF NP_390728 WP_003152560 WP_003222500 WP_003325184 WP_014664890 NP_390455 WP_004398596 WP_029318100 YP_004204353 YP_007534562
SP P14949 P45947
BMRB 6075 6563
AlphaFold P14949 P45947

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