BMRB Entry 19486

Name: Solution NMR Structure of Zinc finger protein 423 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR7298F
Published: 2013-09-23

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PDB ID: 2mdg
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19486
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of Zinc finger protein 423 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR7298F

Deposition date:

2013-09-10

Original release date:

2013-09-23

Authors:

Pederson, Kari; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Everett, John; Acton, Thomas; Montelione, Gaetano; Prestegard, James

Citation:

Citation: Pederson, Kari; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Everett, John; Acton, Thomas; Montelione, Gaetano; Prestegard, James. "Solution NMR Structure of Zinc finger protein 423 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR7298F" To be published ., .-..

Assembly members:

Assembly members:
HR7298F, polymer, 55 residues, 6432.094 Da.
ZINC ION, non-polymer, 65.409 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 Vector: pET15Avi6HT_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HR7298F: MGSHKCNVCSRTFFSENGLR EHLQTHRGPAKHYMCPICGE RFPSLLTLTEHKVTH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	212
15N chemical shifts	51
1H chemical shifts	335

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HR7298F	1
2	Zn ion 1	2
3	Zn ion 2	2

Entities:

Entity 1, HR7298F 55 residues - 6432.094 Da.

M at N-terminal is part of His-Tag.

1

MET

GLY

SER

HIS

LYS

CYS

ASN

VAL

CYS

SER

2

ARG

THR

PHE

SER

GLU

ASN

GLY

LEU

ARG

3

GLU

HIS

LEU

GLN

THR

HIS

ARG

GLY

PRO

ALA

4

LYS

HIS

TYR

MET

CYS

PRO

ILE

CYS

GLY

GLU

5

ARG

PHE

PRO

SER

LEU

THR

LEU

THR

GLU

6

HIS

LYS

VAL

THR

HIS

Entity 2, Zn ion 1 - Zn - 65.409 Da.

1

ZN

Samples:

NC: HR7298F.005, [U-100% 13C; U-100% 15N], 0.17 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O, [U-100% 2H], 10%; DSS 50 uM; ZnSO4 50 uM; H2O 90%

C12E5_NC5: HR7298F.0059, [U-5% 13C; U-100% 15N], 0.51 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O, [U-100% 2H], 5%; DSS 50 uM; C12E5 PEG/Hexanol 4.2%; ZnSO4 50 uM; H2O 95%

NC5: HR7298F.009, [U-5% 13C; U-100% 15N], 0.51 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O, [U-100% 2H], 5%; DSS 50 uM; ZnSO4 50 uM; H2O 95%

C12E5_NC: HR7298F.005, [U-100% 13C; U-100% 15N], 0.17 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O, [U-100% 2H], 10%; DSS 50 uM; ZnSO4 50 uM; C12E5 PEG?Hexanol 4.2%; H2O 90%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	NC	isotropic	sample_conditions_1
3D HNCO	NC	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC	isotropic	sample_conditions_1
3D HNCACB	NC	isotropic	sample_conditions_1
3D H(CCO)NH	NC	isotropic	sample_conditions_1
3D HCCH-TOCSY	NC	isotropic	sample_conditions_1
3D 1H-15N NOESY	NC5	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	NC	isotropic	sample_conditions_1
2D 1H-13C CT HSQC	NC5	isotropic	sample_conditions_1
2D 1H-15N J-modulation HSQC	NC	isotropic	sample_conditions_1
2D 1H-15N J-modulation HSQC	C12E5_NC5	anisotropic	sample_conditions_1
2D 1H-15N CO filtered TROSY	NC	isotropic	sample_conditions_1
2D 1H-15N CO-filtered TROSY	C12E5_NC	anisotropic	sample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

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

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMRJ, Varian - collection

SPARKY v3.113, Goddard - chemical shift assignment

PALES, PALES (Zweckstetter, Bax) - structure validation

PSVS v1.5, Bhattacharya, Montelione - structure validation

NMR spectrometers:

Varian INOVA 600 MHz
Varian Avance 900 MHz
Varian Avance 600 MHz

EMBL	ZN423_HUMAN
PDB	2MDG
DBJ	BAA34480 BAC65647 BAE21688 BAG51329 BAG72439
GB	AAB58646 AAF28354 AAG17053 AAH59234 AAI12316
REF	NP_001095363 NP_001258549 NP_001297449 NP_055884 NP_201584
SP	O08961 Q2M1K9 Q80TS5
TPG	DAA20039
AlphaFold	O08961 Q2M1K9 Q80TS5