BMRB Entry 34007

Name: Solution structure of the complex between human ZNHIT3 and NUFIP1 proteins
Published: 2016-08-26

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PDB ID: 5l85
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34007
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of the complex between human ZNHIT3 and NUFIP1 proteins

Deposition date:

2016-06-07

Original release date:

2016-08-26

Authors:

Quinternet, M.; Chagot, M.; Manival, X.

Citation:

Citation: Quinternet, M.; Chagot, M.; Rothe, B.; Tiotu, D.; Charpentier, B.; Manival, X.. "Structural Features of the Box C/D snoRNP Pre-assembly Process Are Conserved through Species" Structure 24, 1693-1706 (2016).
PubMed: 27594683

Assembly members:

Assembly members:
Zinc finger HIT domain-containing protein 3, polymer, 75 residues, 8492.720 Da.
Nuclear fragile X mental retardation-interacting protein 1, polymer, 34 residues, 4030.654 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(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Zinc finger HIT domain-containing protein 3: GPHMDRVSLQNLKNLGESAT LRSLLLNPHLRQLMVNLDQG EDKAKLMRAYMQEPLFVEFA DCCLGIVEPSQNEES
Nuclear fragile X mental retardation-interacting protein 1: DIRHERNVILQCVRYIIKKD FFGLDTNSAKSKDV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	488
15N chemical shifts	125
1H chemical shifts	805

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 75 residues - 8492.720 Da.

1

GLY

PRO

HIS

MET

ASP

ARG

VAL

SER

LEU

GLN

2

ASN

LEU

LYS

ASN

LEU

GLY

GLU

SER

ALA

THR

3

LEU

ARG

SER

LEU

ASN

PRO

HIS

LEU

4

ARG

GLN

LEU

MET

VAL

ASN

LEU

ASP

GLN

GLY

5

GLU

ASP

LYS

ALA

LYS

LEU

MET

ARG

ALA

TYR

6

MET

GLN

GLU

PRO

LEU

PHE

VAL

GLU

PHE

ALA

7

ASP

CYS

LEU

GLY

ILE

VAL

GLU

PRO

SER

8

GLN

ASN

GLU

SER

Entity 2, entity_2 34 residues - 4030.654 Da.

1

ASP

ILE

ARG

HIS

GLU

ARG

ASN

VAL

ILE

LEU

2

GLN

CYS

VAL

ARG

TYR

ILE

LYS

ASP

3

PHE

GLY

LEU

ASP

THR

ASN

SER

ALA

LYS

4

SER

LYS

ASP

VAL

Samples:

sample_1: NUFIP1, [U-13C; U-15N], 1 mM; ZNHIT3, [U-13C; U-15N], 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 150 mM; pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

TOPSPIN v3.2, Bruker Biospin - collection

NMR spectrometers:

Bruker AvanceIII 600 MHz

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