BMRB Entry 4267

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4267

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Title:
Chemical shift assignments, 3JHNHA coupling constants and secondary structure of HNGAL (Human Neutrophil Gelatinase-Associated Lipocalin) in its apo form.
Deposition date:
1998-11-11
Original release date:
2011-03-03
Authors:
Coles, Murray; Diercks, Tammo; Muehlenweg, Bernd; Bartsch, Stefan; Zoelzer, Volker; Tschesche, Harald; Kessler, Horst
Citation:

Citation: Coles, Murray; Diercks, Tammo; Muehlenweg, Bernd; Bartsch, Stefan; Zoelzer, Volker; Tschesche, Harald; Kessler, Horst. "The Solution Strucuture and Dynamics of Human Neutrophil Gelatinase-associated Lipocalin."  J. Mol. Biol. 289, 139-157 (1999).

Assembly members:

Assembly members:
HNGAL Human Neutrophil Gelatinase-Associated Lipocalin, polymer, 179 residues, 20660 Da.

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: Bl21[DE3] Escherichia   Vector: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HNGAL Human Neutrophil Gelatinase-Associated Lipocalin: MQDSTSDLIPAPPLSKVPLQ QNFQDNQFQGKWYVVGLAGN AILREDKDPQKMYATIYELK EDKSYNVTSVLFRKKKCDYW IRTFVPGCQPGEFTLGNIKS YPGLTSYLVRVVSTNYNQHA MVFFKKVSQNREYFKITLYG RTKELTSELKENFIRFSKSL GLPENHIVFPVPIDQCIDG

Data typeCount
13C chemical shifts737
15N chemical shifts188
1H chemical shifts1266
coupling constants125
order parameters152
T1 relaxation values443
T2 relaxation values445

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1HNGAL1

Entities:

Entity 1, HNGAL 179 residues - 20660 Da.

1   METGLNASPSERTHRSERASPLEUILEPRO
2   ALAPROPROLEUSERLYSVALPROLEUGLN
3   GLNASNPHEGLNASPASNGLNPHEGLNGLY
4   LYSTRPTYRVALVALGLYLEUALAGLYASN
5   ALAILELEUARGGLUASPLYSASPPROGLN
6   LYSMETTYRALATHRILETYRGLULEULYS
7   GLUASPLYSSERTYRASNVALTHRSERVAL
8   LEUPHEARGLYSLYSLYSCYSASPTYRTRP
9   ILEARGTHRPHEVALPROGLYCYSGLNPRO
10   GLYGLUPHETHRLEUGLYASNILELYSSER
11   TYRPROGLYLEUTHRSERTYRLEUVALARG
12   VALVALSERTHRASNTYRASNGLNHISALA
13   METVALPHEPHELYSLYSVALSERGLNASN
14   ARGGLUTYRPHELYSILETHRLEUTYRGLY
15   ARGTHRLYSGLULEUTHRSERGLULEULYS
16   GLUASNPHEILEARGPHESERLYSSERLEU
17   GLYLEUPROGLUASNHISILEVALPHEPRO
18   VALPROILEASPGLNCYSILEASPGLY

Samples:

HNGAL_sample_N15: HNGAL Human Neutrophil Gelatinase-Associated Lipocalin, [U-15N], 1.43 mM; sodium acetate 50 mM; acetic acid 50 mM; sodium chloride 50 mM; sodium azide 0.02%; D2O 10.0%; H2O 90.0%

HNGAL_sample_dl: HNGAL Human Neutrophil Gelatinase-Associated Lipocalin, [U-15N; U-13C], 1.15 mM; sodium acetate 50 mM; acetic acid 50 mM; sodium chloride 50 mM; sodium azide 0.02%; D2O 10.0%; H2O 90.0%

sample_conditions_all: pH: 6.0; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
not availablenot availablenot availablesample_conditions_all

Software:

No software information available

NMR spectrometers:

  • Bruker DMX 750 MHz
  • Bruker DMX 600 MHz

Related Database Links:

PDB
DBJ BAG63166 BAH14588 BAJ21166
EMBL CAA58127 CAA67574 CAG46889
GB AAB26529 AAD14168 AAH33089 AAV38204 AAX36313
REF NP_005555 XP_003822366 XP_004048725 XP_520287
SP P80188
AlphaFold P80188

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