BMRB Entry 10053

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10053

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Title:
Backbone 1H, 13C, and 15N assignments of a 59 kDa Salmonella typhimurium periplasmic oligopeptide binding protein OppA
Deposition date:
2006-11-26
Original release date:
2007-08-22
Authors:
Kurashima-Ito, Kaori; Moromisato, Kayano; Nishimura, Kaoru; Waelchli, Markus; Tame, Jeremy; Ito, Yutaka
Citation:

Citation: Kurashima-Ito, Kaori; Moromisato, Kayano; Nishimura, Kaoru; Walchli, Markus; Tame, Jeremy; Ito, Yutaka. "Backbone 1H, 13C and 15N assignments of a 59 kDa Salmonella typhimurium periplasmic oligopeptide binding protein, OppA"  Biomol. NMR Assignments 1, 37-39 (2007).
PubMed: 19636820

Assembly members:

Assembly members:
OppA, polymer, 517 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Salmonella typhimurium   Taxonomy ID: 602   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Salmonella typhimurium

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
OppA: ADVPAGVQLADKQTLVRNNG SEVQSLDPHKIEGVPESNVS RDLFEGLLISDVEGHPSPGV AEKWENKDFKVWTFHLRENA KWSDGTPVTAHDFVYSWQRL ADPNTASPYASYLQYGHIAN IDDIIAGKKPATDLGVKALD DHTFEVTLSEPVPYFYKLLV HPSVSPVPKSAVEKFGDKWT QPANIVTNGAYKLKNWVVNE RIVLERNPQYWDNAKTVINQ VTYLPISSEVTDVNRYRSGE IDMTYNNMPIELFQKLKKEI PNEVRVDPYLCTYYYEINNQ KAPFNDVRVRTALKLALDRD IIVNKVKNQGDLPAYSYTPP YTDGAKLVEPEWFKWSQQKR NEEAKKLLAEAGFTADKPLT FDLLYNTSDLHKKLAIAVAS IWKKNLGVNVNLENQEWKTF LDTRHQGTFDVARAGWCANY NEPTSFLNTMLSDSSNNTAH YKSPAFDKLIADTLKVADDT QRSELYAKAEQQLDKDSAIV PVYYYVNARLVKPWVGGYTG KDPLDNIYVKNLYIIKH

Data sets:
  • assigned_chemical_shifts
Data typeCount
13C chemical shifts1371
15N chemical shifts434
1H chemical shifts435

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OppA1

Entities:

Entity 1, OppA 517 residues - Formula weight is not available

1   ALAASPVALPROALAGLYVALGLNLEUALA
2   ASPLYSGLNTHRLEUVALARGASNASNGLY
3   SERGLUVALGLNSERLEUASPPROHISLYS
4   ILEGLUGLYVALPROGLUSERASNVALSER
5   ARGASPLEUPHEGLUGLYLEULEUILESER
6   ASPVALGLUGLYHISPROSERPROGLYVAL
7   ALAGLULYSTRPGLUASNLYSASPPHELYS
8   VALTRPTHRPHEHISLEUARGGLUASNALA
9   LYSTRPSERASPGLYTHRPROVALTHRALA
10   HISASPPHEVALTYRSERTRPGLNARGLEU
11   ALAASPPROASNTHRALASERPROTYRALA
12   SERTYRLEUGLNTYRGLYHISILEALAASN
13   ILEASPASPILEILEALAGLYLYSLYSPRO
14   ALATHRASPLEUGLYVALLYSALALEUASP
15   ASPHISTHRPHEGLUVALTHRLEUSERGLU
16   PROVALPROTYRPHETYRLYSLEULEUVAL
17   HISPROSERVALSERPROVALPROLYSSER
18   ALAVALGLULYSPHEGLYASPLYSTRPTHR
19   GLNPROALAASNILEVALTHRASNGLYALA
20   TYRLYSLEULYSASNTRPVALVALASNGLU
21   ARGILEVALLEUGLUARGASNPROGLNTYR
22   TRPASPASNALALYSTHRVALILEASNGLN
23   VALTHRTYRLEUPROILESERSERGLUVAL
24   THRASPVALASNARGTYRARGSERGLYGLU
25   ILEASPMETTHRTYRASNASNMETPROILE
26   GLULEUPHEGLNLYSLEULYSLYSGLUILE
27   PROASNGLUVALARGVALASPPROTYRLEU
28   CYSTHRTYRTYRTYRGLUILEASNASNGLN
29   LYSALAPROPHEASNASPVALARGVALARG
30   THRALALEULYSLEUALALEUASPARGASP
31   ILEILEVALASNLYSVALLYSASNGLNGLY
32   ASPLEUPROALATYRSERTYRTHRPROPRO
33   TYRTHRASPGLYALALYSLEUVALGLUPRO
34   GLUTRPPHELYSTRPSERGLNGLNLYSARG
35   ASNGLUGLUALALYSLYSLEULEUALAGLU
36   ALAGLYPHETHRALAASPLYSPROLEUTHR
37   PHEASPLEULEUTYRASNTHRSERASPLEU
38   HISLYSLYSLEUALAILEALAVALALASER
39   ILETRPLYSLYSASNLEUGLYVALASNVAL
40   ASNLEUGLUASNGLNGLUTRPLYSTHRPHE
41   LEUASPTHRARGHISGLNGLYTHRPHEASP
42   VALALAARGALAGLYTRPCYSALAASNTYR
43   ASNGLUPROTHRSERPHELEUASNTHRMET
44   LEUSERASPSERSERASNASNTHRALAHIS
45   TYRLYSSERPROALAPHEASPLYSLEUILE
46   ALAASPTHRLEULYSVALALAASPASPTHR
47   GLNARGSERGLULEUTYRALALYSALAGLU
48   GLNGLNLEUASPLYSASPSERALAILEVAL
49   PROVALTYRTYRTYRVALASNALAARGLEU
50   VALLYSPROTRPVALGLYGLYTYRTHRGLY
51   LYSASPPROLEUASPASNILETYRVALLYS
52   ASNLEUTYRILEILELYSHIS

Samples:

sample_1: OppA, [U-2H; U-13C; U-15N], 0.7 – 0.8 mM

condition_1: pH: 5.6; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H-15N TROSY-HSQCsample_1not availablecondition_1
3D TROSY-HNCAsample_1not availablecondition_1
3D TROSY-HN(CO)CAsample_1not availablecondition_1
3D TROSY-HN(CA)CBsample_1not availablecondition_1
3D TROSY-HN(COCA)CBsample_1not availablecondition_1
3D TROSY-HN(CA)COsample_1not availablecondition_1
3D TROSY-HNCOsample_1not availablecondition_1
1H-15N TROSY-HSQC 800MHzsample_1not availablecondition_1

Software:

xwinnmr v3.5, Bruker - data collection

TOPSPIN v1.3, Bruker - data collection

AZARA v2.7, Wayne Boucher & Univ. Cambridge - processing

ANSIG-for-OpenGL v1.0.6 - assignment

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

PDB
DBJ BAJ36712 BAP07611
EMBL CAA27785 CAA29039 CAD08386 CAR32867 CAR37243
GB AAL20664 AAO69284 AAV77092 AAX65648 ABX66895
PIR AG0650
REF NP_455753 NP_460705 WP_000065807 WP_000065811 WP_000065812
SP P06202
AlphaFold P06202

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