BMRB Entry 30163

Name: NMR Structure of Apo-form Human Tear Lipocalin
Published: 2017-08-22

Click here to enlarge.

PDB ID: 5t43
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30163
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

NMR Structure of Apo-form Human Tear Lipocalin

Deposition date:

2016-08-28

Original release date:

2017-08-22

Authors:

Vogel, H.; Liu, Z.

Citation:

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

Assembly members:

Assembly members:
entity_1, polymer, 158 residues, 17453.652 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: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	132
1H chemical shifts	132

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 158 residues - 17453.652 Da.

1

HIS

LEU

ALA

SER

ASP

GLU

ILE

2

GLN

ASP

VAL

SER

GLY

THR

TRP

TYR

LEU

LYS

3

ALA

MET

THR

VAL

ASP

ARG

GLU

PHE

PRO

GLU

4

MET

ASN

LEU

GLU

SER

VAL

THR

PRO

MET

THR

5

LEU

THR

LEU

GLU

GLY

ASN

LEU

GLU

6

ALA

LYS

VAL

THR

MET

LEU

ILE

SER

GLY

ARG

7

CYS

GLN

GLU

VAL

LYS

ALA

VAL

LEU

GLU

LYS

8

THR

ASP

GLU

PRO

GLY

LYS

TYR

THR

ALA

ASP

9

GLY

LYS

HIS

VAL

ALA

TYR

ILE

ARG

10

SER

HIS

VAL

LYS

ASP

HIS

TYR

ILE

PHE

TYR

11

SER

GLU

GLY

GLU

LEU

HIS

GLY

LYS

PRO

VAL

12

ARG

GLY

VAL

LYS

LEU

VAL

GLY

ARG

ASP

PRO

13

LYS

ASN

LEU

GLU

ALA

LEU

GLU

ASP

PHE

14

GLU

LYS

ALA

GLY

ALA

ARG

GLY

LEU

SER

15

THR

GLU

SER

ILE

LEU

ILE

PRO

ARG

GLN

SER

16

GLU

THR

CYS

SER

PRO

GLY

SER

ASP

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_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

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