BMRB Entry 34471

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34471
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Haddock model of NDM-1/morin complex
Deposition date:
2019-12-25
Original release date:
2021-01-06
Authors:
Riviere, G.; Oueslati, S.; Gayral, M.; Crechet, J.; Nhiri, N.; Jacquet, E.; Cintrat, J.; Giraud, F.; van Heijenoort, C.; Lescop, E.; Pethe, S.; Iorga, B.; Naas, T.; Guittet, E.; Morellet, N.
Citation:

Citation: Marra, A.. "NDM-1: a local clone emerges with worldwide aspirations."  Future Microbiol. 6, 137-141 (2011).
PubMed: 21366414

Assembly members:

Assembly members:
entity_1, polymer, 227 residues, 23974.957 Da.
entity_ZN, non-polymer, 65.409 Da.
entity_MRI, non-polymer, 302.236 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 573   Superkingdom: not available   Kingdom: not available   Genus/species: Klebsiella pneumoniae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: DQRFGDLVFRQLAPNVWQHT SYLDMPGFGAVASNGLIVRD GGRVLVVDTAWTDDQTAQIL NWIKQEINLPVALAVVTHAH QDKMGGMDALHAAGIATYAN ALSNQLAPQEGMVAAQHSLT FAANGWVEPATAPNFGPLKV FYPGPGHTSDNITVGIDGTD IAFGGCLIKDSKAKSLGNLG DADTEHYAASARAFGAAFPK ASMIVMSHSAPDSRAAITHT ARMADKL

Data sets:
Data typeCount
13C chemical shifts581
15N chemical shifts206
1H chemical shifts206

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22
3unit_32
4unit_43

Entities:

Entity 1, unit_1 227 residues - 23974.957 Da.

1   ASPGLNARGPHEGLYASPLEUVALPHEARG
2   GLNLEUALAPROASNVALTRPGLNHISTHR
3   SERTYRLEUASPMETPROGLYPHEGLYALA
4   VALALASERASNGLYLEUILEVALARGASP
5   GLYGLYARGVALLEUVALVALASPTHRALA
6   TRPTHRASPASPGLNTHRALAGLNILELEU
7   ASNTRPILELYSGLNGLUILEASNLEUPRO
8   VALALALEUALAVALVALTHRHISALAHIS
9   GLNASPLYSMETGLYGLYMETASPALALEU
10   HISALAALAGLYILEALATHRTYRALAASN
11   ALALEUSERASNGLNLEUALAPROGLNGLU
12   GLYMETVALALAALAGLNHISSERLEUTHR
13   PHEALAALAASNGLYTRPVALGLUPROALA
14   THRALAPROASNPHEGLYPROLEULYSVAL
15   PHETYRPROGLYPROGLYHISTHRSERASP
16   ASNILETHRVALGLYILEASPGLYTHRASP
17   ILEALAPHEGLYGLYCYSLEUILELYSASP
18   SERLYSALALYSSERLEUGLYASNLEUGLY
19   ASPALAASPTHRGLUHISTYRALAALASER
20   ALAARGALAPHEGLYALAALAPHEPROLYS
21   ALASERMETILEVALMETSERHISSERALA
22   PROASPSERARGALAALAILETHRHISTHR
23   ALAARGMETALAASPLYSLEU

Entity 2, unit_2 - Zn - 65.409 Da.

1   ZN

Entity 3, unit_4 - C15 H10 O7 - 302.236 Da.

1   MRI

Samples:

sample_1: NDM-1, [U-13C; U-15N], 320 uM; morin 1280 uM; Bis-tris 0.1 mM; sodium chloride 150 mM; DMSO 2.5%

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

CcpNmr Analysis, CCPN - chemical shift assignment, data analysis

HADDOCK, Bonvin - structure calculation

NMR spectrometers:

  • Bruker AVANCE III 800 MHz
  • Bruker AVANCE II 600 MHz

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