BMRB Entry 6416

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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/BMR6416
MolProbity Validation Chart

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Title:
Backbone 1H, 13C, and 15N assignments of a 56 kDa E. coli nickel binding protein NikA
Deposition date:
2004-12-08
Original release date:
2005-08-16
Authors:
Rajesh, Sundaresan; Heddle, Jonathan; Kurashima-Ito, Kaori; Nietlispach, Daniel; Shirakawa, Masahiro; Tame, Jeremy; Ito, Yutaka
Citation:

Citation: Rajesh, Sundaresan; Heddle, Jonathan; Kurashima-Ito, Kaori; Nietlispach, Daniel; Shirakawa, Masahiro; Tame, Jeremy; Ito, Yutaka. "Backbone 1H, 13C, and 15N resonance assignments of a 56 kDa E. coli nickel binding protein NikA"  J. Biomol. NMR 32, 177-177 (2005).

Assembly members:

Assembly members:
periplasmic nickel binding protein A, polymer, 502 residues, 56302 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
periplasmic nickel binding protein A: AAPDEITTAWPVNVGPLNPH LYTPNQMFAQSMVYEPLVKY QADGSVIPWLAKSWTHSEDG KTWTFTLRDDVKFSNGEPFD AEAAAENFRAVLDNRQRHAW LELANQIVDVKALSKTELQI TLKSAYYPFLQELALPRPFR FIAPSQFKNHETMNGIKAPI GTGPWILQESKLNQYDVFVR NENYWGEKPAIKKITFNVIP DPTTRAVAFETGDIDLLYGN EGLLPLDTFARFSQNPAYHT QLSQPIETVMLALNTAKAPT NELAVREALNYAVNKKSLID NALYGTQQVADTLFAPSVPY ANLGLKPSQYDPQKAKALLE KAGWTLPAGKDIREKNGQPL RIELSFIGTDALSKSMAEII RADMRQIGADVSLIGEEESS IYARQRDGRFGMIFHRTWGA PYDPHAFLSSMRVPSHADFQ AQQGLADKPLIDKEIGEVLA THDETQRQALYRDILTRLHD EAVYLPISYISMMVVSKPEL GNIPYAPIATEIPFEQIKPV KP

Data sets:
Data typeCount
1H chemical shifts396
13C chemical shifts1275
15N chemical shifts396

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1NikA monomer1

Entities:

Entity 1, NikA monomer 502 residues - 56302 Da.

1   ALAALAPROASPGLUILETHRTHRALATRP
2   PROVALASNVALGLYPROLEUASNPROHIS
3   LEUTYRTHRPROASNGLNMETPHEALAGLN
4   SERMETVALTYRGLUPROLEUVALLYSTYR
5   GLNALAASPGLYSERVALILEPROTRPLEU
6   ALALYSSERTRPTHRHISSERGLUASPGLY
7   LYSTHRTRPTHRPHETHRLEUARGASPASP
8   VALLYSPHESERASNGLYGLUPROPHEASP
9   ALAGLUALAALAALAGLUASNPHEARGALA
10   VALLEUASPASNARGGLNARGHISALATRP
11   LEUGLULEUALAASNGLNILEVALASPVAL
12   LYSALALEUSERLYSTHRGLULEUGLNILE
13   THRLEULYSSERALATYRTYRPROPHELEU
14   GLNGLULEUALALEUPROARGPROPHEARG
15   PHEILEALAPROSERGLNPHELYSASNHIS
16   GLUTHRMETASNGLYILELYSALAPROILE
17   GLYTHRGLYPROTRPILELEUGLNGLUSER
18   LYSLEUASNGLNTYRASPVALPHEVALARG
19   ASNGLUASNTYRTRPGLYGLULYSPROALA
20   ILELYSLYSILETHRPHEASNVALILEPRO
21   ASPPROTHRTHRARGALAVALALAPHEGLU
22   THRGLYASPILEASPLEULEUTYRGLYASN
23   GLUGLYLEULEUPROLEUASPTHRPHEALA
24   ARGPHESERGLNASNPROALATYRHISTHR
25   GLNLEUSERGLNPROILEGLUTHRVALMET
26   LEUALALEUASNTHRALALYSALAPROTHR
27   ASNGLULEUALAVALARGGLUALALEUASN
28   TYRALAVALASNLYSLYSSERLEUILEASP
29   ASNALALEUTYRGLYTHRGLNGLNVALALA
30   ASPTHRLEUPHEALAPROSERVALPROTYR
31   ALAASNLEUGLYLEULYSPROSERGLNTYR
32   ASPPROGLNLYSALALYSALALEULEUGLU
33   LYSALAGLYTRPTHRLEUPROALAGLYLYS
34   ASPILEARGGLULYSASNGLYGLNPROLEU
35   ARGILEGLULEUSERPHEILEGLYTHRASP
36   ALALEUSERLYSSERMETALAGLUILEILE
37   ARGALAASPMETARGGLNILEGLYALAASP
38   VALSERLEUILEGLYGLUGLUGLUSERSER
39   ILETYRALAARGGLNARGASPGLYARGPHE
40   GLYMETILEPHEHISARGTHRTRPGLYALA
41   PROTYRASPPROHISALAPHELEUSERSER
42   METARGVALPROSERHISALAASPPHEGLN
43   ALAGLNGLNGLYLEUALAASPLYSPROLEU
44   ILEASPLYSGLUILEGLYGLUVALLEUALA
45   THRHISASPGLUTHRGLNARGGLNALALEU
46   TYRARGASPILELEUTHRARGLEUHISASP
47   GLUALAVALTYRLEUPROILESERTYRILE
48   SERMETMETVALVALSERLYSPROGLULEU
49   GLYASNILEPROTYRALAPROILEALATHR
50   GLUILEPROPHEGLUGLNILELYSPROVAL
51   LYSPRO

Samples:

sample_1: periplasmic nickel binding protein A, [U-99% 2H; U-13C; U-15N], 1.5 – 2.0 mM

cond-1: pH: 7.5; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
Six Trosy-based experiments: HNCA, HN(CO)CA, HN(CA)CB, HN(COCA)CB, HN(CA)CO, and HNCO.sample_1not availablecond-1
Also a 3D 15N-HMQC-NOE {15N,1H} TROSY spectra was recorded to confirmsample_1not availablecond-1
sequential assignments.sample_1not availablecond-1
A MQ-HN(CA)CO experiment was recorded due to the low sensitivity of SQ-HN(CA)COsample_1not availablecond-1
experiment.sample_1not availablecond-1

Software:

Azara v2.7 - Processing

Ansig for OpenGL v1.0.3 - Analysis

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAB37766 BAE77817 BAG79268 BAI27733 BAI32904
EMBL CAA51659 CAP77927 CAQ33795 CAR00421 CAR05091
GB AAB18451 AAC76501 AAG58603 AAN44953 AAN82705
REF NP_290042 NP_312370 NP_417933 NP_709246 NP_756131
SP P33590
AlphaFold P33590

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