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 4267

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: 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:
HNGAL Human Neutrophil Gelatinase-Associated Lipocalin, polymer, 179 residues, 20660 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: Bl21[DE3] Escherichia

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:

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Related Database Links:

PDB 1DFV 1L6M 1NGL 1QQS 1X71 1X89 1X8U 3BY0 3CBC 3CMP 3FW4 3FW5 3HWD 3HWE 3HWF 3HWG 3I0A 3K3L 3PEC 3PED 3T1D 3TF6 3TZS 3U03 3U0D 4K19 4ZFX 4ZHC 4ZHD 4ZHF 4ZHG 4ZHH
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

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