Chemical shift assignments, 3JHNHA coupling constants and secondary structure of
HNGAL (Human Neutrophil Gelatinase-Associated Lipocalin) in its apo form.

apo-HNGAL Human Neutrophil Gelatinase-Associated Lipocalin

multimeric matrix-metalloproteinase component

Chain B, Crystal Structure Of Human Neutrophil Gelatinase Associated Lipocalin Monomer

Chain A, Human Neutrophil Gelatinase-Associated Lipocalin (Hngal), Regularised Average Nmr Structure

Many methylene and valine/luecine methyl groups have been stereospecifically assigned.
those not stereo-assigned are given ambiguity code 2 even where HB2,HB3 etc.
are stated as having different shifts. Glycine HA pairs are steroassigned (exception G178).

Internal TMS referencing for proton, 15N and 13C by frequency ratio

Coles, M., Diercks, T., Muehlenweg, B., Bartsch, S., Zoelzer, V., Tschesche, H.,
and Kessler, H., "The Solution Structure and Dynamics of Human Neutrophil
Gelatinase-associated Lipocalin," J. Mol. Biol. 289, 139-157 (1999).

The Solution Strucuture and Dynamics of Human Neutrophil Gelatinase-associated
Lipocalin.

3JHNHA couplings measured from ratio of cross to diagonal peaks in an HNHA
experiment.

Construct contains the mature protein sequence, without N-terminal signal
sequence, preceded by a N-terminal methionine. Residue numbering refers
to the mature sequence with the methionine designated M0.
Disulphide bridge C76-C175.

HNGAL Human Neutrophil Gelatinase-Associated Lipocalin

Crystal Structure Of Human Neutrophil Gelatinase Associated Lipocalin Monomer

Neutrophil Gelatinase-Associated Lipocalin Is A Novel Bacteriostatic Agent That Interferes With Siderophore- Mediated Iron Acqu

Human Neutrophil Gelatinase-Associated Lipocalin (Hngal), Regularised Average Nmr Structure

Neutrophil Gelatinase Associated Lipocalin Homodimer

Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Complexed With Trencam-3,2-Hopo, A Cepabactin Analogue

Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Complexed With Carboxymycobactin S

Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Complexed With Carboxymycobactin T

Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) W79a-R81a Complexed With Ferric Enterobactin

Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Y106f Complexed With Ferric Enterobactin

Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) K125a Mutant Complexed With Ferric Enterobactin

Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Complexed With Ferric Catechol

Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Complexed With Ferric 4-Methyl-Catechol

Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) K125a-K Mutant Complexed With Ferric Enterobactin

Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Complex Fe-Bishacam

Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Complex Fe-Trencam2-Hopo

Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Complex Fe-Trencam-Hopo2

Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) K134a M Complexed With Ferric Enterobactin

Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Complexed With Apo Enterobactin

Siderocalin Recognitin Of Carboxymycobactins: Interference By The Immune System In Intracellular Iron Acquisition By Mycobacter

The Mutant Structure Of Human Siderocalin W79a, R81a, Y106f Bound To Enterobactin

Crystal Structure Of Neutrophil Gelatinase-associated Lipocalin (c87s Mutant) In Complex With Europium And The Siderophore Anal

Crystal Structure Of Neutrophil Gelatinase-associated Lipocalin Ngal (c87s Mutant) In Complex With Fragment 1026, Phenylurea

The Structure Of Human Siderocalin Bound To The Bacterial Siderophore Pyochelin

The Structure Of Human Siderocalin Bound To The Bacterial Siderophore 2,3-dhba

The Structure Of Human Siderocalin Bound To The Bacterial Siderophore Fluvibactin

Siderocalin-mediated Recognition And Cellular Uptake Of Actinides

neutrophil gelatinase associated lipocalin [Homo sapiens]

neutrophil gelatinase-associated lipocalin, NGAL [human, neutrophils, Peptide, 178 aa]

neutrophil lipocalin, partial [Homo sapiens]

lipocalin 2 (oncogene 24p3) [synthetic construct]

neutrophil gelatinase-associated lipocalin precursor [Homo sapiens]

PREDICTED: neutrophil gelatinase-associated lipocalin [Pan paniscus]

PREDICTED: neutrophil gelatinase-associated lipocalin [Gorilla gorilla gorilla]

PREDICTED: neutrophil gelatinase-associated lipocalin [Pan troglodytes]

RecName: Full=Neutrophil gelatinase-associated lipocalin; Short=NGAL; AltName: Full=25 kDa alpha-2-microglobulin-related subuni

Expression controlled with the T7 lac promoter

The data presented are for apo-HNGAL (Human Neutrophil Gelatinase-Associated
Lipocalin), a member of the lipocalin family of extracellular proteins
which generally function as transporters of small, hydrophobic molecules.
HNGAL binds bacterially-derived chemotactic formyl-peptides which induce
leukocyte granule discharge. HNGAL aslo forms a protein-protein complex with
the proenzyme of matrix metalloproteinase-9, pro-MMP-9 (or progelatinase B)
which influences its subsequent complexations and metalloproteinase activity.
This is the first lipocalin structure solved by NMR methods.

N15{1H} Heteronuclear steady-state NOE using 3s 1H presat. time. water flipback.
Reference experiment (i.e. no presat.) interleaved with acquisition. 750 MHz.
Minimum error assumed to be 0.05.

N15{1H} Heteronuclear steady-state NOE using 3s 1H presat. time. water flipback.
Reference experiment (i.e. no presat.) interleaved with acquisition. 600 MHz.
Minimum error assumed to be 0.05.

N15{1H} Heteronuclear steady-state NOE using 3s 1H presat. time. water flipback.
Reference experiment (i.e. no presat.) interleaved with acquisition. 500 MHz.
Minimum error assumed to be 0.05.

N15 T1 relaxation data with decoupling of CSA/DD cross-relaxation,
water flipback. Interleaved acquisition mode. 750 MHz.

N15 T1 relaxation data with decoupling of CSA/DD cross-relaxation,
water flipback. Interleaved acquisition mode. 600 MHz.

N15 T1 relaxation data with decoupling of CSA/DD cross-relaxation,
water flipback. Interleaved acquisition mode. 500 MHz.

N15 T2 relaxation data with decoupling of CSA/DD cross-relaxation,
water flipback. Interleaved acquisition mode. 750 MHz.
CPMG echo delay delta=0.45 ms. Rex contributions also given where appropriate.

N15 T2 relaxation data with decoupling of CSA/DD cross-relaxation,
water flipback. Interleaved acquisition mode. 600 MHz.
CPMG echo delay delta=0.45 ms

N15 T2 relaxation data with decoupling of CSA/DD cross-relaxation,
water flipback. Interleaved acquisition mode. 500 MHz.
CPMG echo delay delta=0.45 ms

four channel, three gradient, triple resonance

Order parameters are generalised, where applicable (i.e. S2=S2f*S2s),
derived from model-free analysis using truncated Lipari-Szabo and the
extended Clore model function (No residues fitted the full Lipari-Szabo model).

sequence numbering corrected in several data loops

Uniformly 15N labelled sample, unliganded HNGAL.

Uniformly 15N,13C labelled sample, unliganded HNGAL.