BMRB Entry 27321

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27321

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Title:
1H, 13C and 15N Chemical Shift Assignments and 15N backbone relaxation data for intracellular loop 2 of the human ZIP4 protein
Deposition date:
2017-11-30
Original release date:
2019-06-21
Authors:
Bafaro, Elizabeth; Maciejewski, Mark; Hoch, Jeffrey; Dempski, Robert
Citation:

Citation: Bafaro, Elizabeth; Maciejewski, Mark; Hoch, Jeffrey; Dempski, Robert. "Concomitant disorder and high-affinity zinc binding in the human zinc- and iron-regulated transport protein 4 intracellular loop"  Protein Sci. 28, 868-880 (2019).
PubMed: 30793391

Assembly members:

Assembly members:
hZIP4_ICL2, polymer, 100 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hZIP4_ICL2: GDRGPEFELGTLPRDPEDLE DGPCGHSSHSHGGHSHGVSL QLAPSELRQPKPPHEGSRAD LVAEESPELLNPEPRRLSPE LRLLPYGHGLSAWSHPQFEK

Data sets:
Data typeCount
13C chemical shifts350
15N chemical shifts156
1H chemical shifts385
T1 relaxation values79
T2 relaxation values79
heteronuclear NOE values80

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hZIP4 ICL21

Entities:

Entity 1, hZIP4 ICL2 100 residues - Formula weight is not available

Residues 1-11 represent a cloning scar. Residues 87-100 represent a non-native affinity tag. Residues 12-86 are the intracellular loop of a membrane protein.

1   GLYASPARGGLYPROGLUPHEGLULEUGLY
2   THRLEUPROARGASPPROGLUASPLEUGLU
3   ASPGLYPROCYSGLYHISSERSERHISSER
4   HISGLYGLYHISSERHISGLYVALSERLEU
5   GLNLEUALAPROSERGLULEUARGGLNPRO
6   LYSPROPROHISGLUGLYSERARGALAASP
7   LEUVALALAGLUGLUSERPROGLULEULEU
8   ASNPROGLUPROARGARGLEUSERPROGLU
9   LEUARGLEULEUPROTYRGLYHISGLYLEU
10   SERALATRPSERHISPROGLNPHEGLULYS

Samples:

sample_1: hZIP4 intracellular loop 2, [U-100% 13C; U-100% 15N], 0.3 mM; HEPES 20 mM; glycerol 20 % v/v; TCEP 5 mM; sodium azide 0.02 % w/v; D2O, [U-100% 2H], 7 % v/v; H2O 73 % v/v; protease inhibitors (Roche) 1 tablet/10mL

sample_2: hZIP4 intracellular loop 2, [U-100% 13C; U-100% 15N], 0.3 mM; HEPES 20 mM; glycerol, [U-2H], 20 % v/v; TCEP 5 mM; sodium azide 0.02 % w/v; D2O, [U-100% 2H], 7 % v/v; protease inhibitors (Roche) 1 tablet/10mL

sample_3: hZIP4 intracellular loop 2, [U-100% 15N], 0.3 mM; HEPES 20 mM; glycerol 20 % v/v; TCEP 5 mM; sodium azide 0.02 % w/v; D2O, [U-100% 2H], 7 % v/v; H2O 73 % v/v; protease inhibitors (Roche) 1 tablet/10mL

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

sample_conditions_2: pH: 7.0; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_2
3D 1H-15N NOESYsample_3isotropicsample_conditions_2
T1_relaxation_800sample_3isotropicsample_conditions_2
T2_relaxation_800sample_3isotropicsample_conditions_2
HetNOE_relaxation_800sample_3isotropicsample_conditions_2

Software:

CcpNMR, CCPN - chemical shift assignment

RNMRTK vv3, Alan Stern, Jeffrey Hoch - processing

VNMRJ, Varian - collection

NMR spectrometers:

  • Agilent INOVA 800 MHz

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