BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 30163

Title: NMR Structure of Apo-form Human Tear Lipocalin

Authors: Vogel, H.; Liu, Z.

Citation: Vogel, H.; Liu, Z.. "NMR Structure of Apo-form Human Tear Lipocalin"  . ., .-..

Assembly members:
entity_1, polymer, 158 residues, 17453.652 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):
entity_1: HHLLASDEEIQDVSGTWYLK AMTVDREFPEMNLESVTPMT LTTLEGGNLEAKVTMLISGR CQEVKAVLEKTDEPGKYTAD GGKHVAYIIRSHVKDHYIFY SEGELHGKPVRGVKLVGRDP KNNLEALEDFEKAAGARGLS TESILIPRQSETCSPGSD

Data sets:
Data typeCount
15N chemical shifts132
1H chemical shifts132

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 158 residues - 17453.652 Da.

1   HISHISLEULEUALASERASPGLUGLUILE
2   GLNASPVALSERGLYTHRTRPTYRLEULYS
3   ALAMETTHRVALASPARGGLUPHEPROGLU
4   METASNLEUGLUSERVALTHRPROMETTHR
5   LEUTHRTHRLEUGLUGLYGLYASNLEUGLU
6   ALALYSVALTHRMETLEUILESERGLYARG
7   CYSGLNGLUVALLYSALAVALLEUGLULYS
8   THRASPGLUPROGLYLYSTYRTHRALAASP
9   GLYGLYLYSHISVALALATYRILEILEARG
10   SERHISVALLYSASPHISTYRILEPHETYR
11   SERGLUGLYGLULEUHISGLYLYSPROVAL
12   ARGGLYVALLYSLEUVALGLYARGASPPRO
13   LYSASNASNLEUGLUALALEUGLUASPPHE
14   GLULYSALAALAGLYALAARGGLYLEUSER
15   THRGLUSERILELEUILEPROARGGLNSER
16   GLUTHRCYSSERPROGLYSERASP

Samples:

sample_1: D2O 10 ± 1 %; H2O 90 ± 1 %; Lipocalin, [U-99% 13C; U-99% 15N], 1.0 ± 0.1 mM; sodium azide 0.04 ± 0.001 %; sodium phosphate 50 ± 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.4; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker Avance 700 MHz

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