BMRB Entry 18551

Name: Solution NMR structure of C2H2-type Zinc-fingers 4 and 5 from human Insulinoma-associated protein 1 (fragment 424-497), Northeast Structural Genomics Consortium Target HR7614B.
Published: 2015-11-16

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PDB ID: 2lv2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18551
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 C2H2-type Zinc-fingers 4 and 5 from human Insulinoma-associated protein 1 (fragment 424-497), Northeast Structural Genomics Consortium Target HR7614B.

Deposition date: 2012-06-27 Original release date: 2015-11-16

Authors: Yang, Yunhuang; Ramelot, Theresa; Cort, John; Shastry, Ritu; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation: Yang, Yunhuang; Ramelot, Theresa; Cort, John; Shastry, Ritu; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of C2H2-type Zinc-fingers 4 and 5 from human Insulinoma-associated protein 1 (fragment 424-497), Northeast Structural Genomics Consortium Target HR7614B." To be published ., .-..

Assembly members:
HR7614B, polymer, 85 residues, 9350.260 Da.
entity_ZN, non-polymer, 65.409 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: Escherichia coli

Entity Sequences (FASTA):
HR7614B: MGHHHHHHSHMGDGEGAGVL GLSASAECHLCPVCGESFAS KGAQERHLRLLHAAQVFPCK YCPATFYSSPGLTRHINKCH PSENR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	307
15N chemical shifts	79
1H chemical shifts	474

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C2H2-type Zinc-fingers 4 and 5 from human Insulinoma-associated protein 1 (fragment 424-497)	1
2	Zinc ion, 1	2
3	Zinc ion, 2	2

Entities:

Entity 1, C2H2-type Zinc-fingers 4 and 5 from human Insulinoma-associated protein 1 (fragment 424-497) 85 residues - 9350.260 Da.

1

MET

GLY

HIS

SER

HIS

2

MET

GLY

ASP

GLY

GLU

GLY

ALA

GLY

VAL

LEU

3

GLY

LEU

SER

ALA

SER

ALA

GLU

CYS

HIS

LEU

4

CYS

PRO

VAL

CYS

GLY

GLU

SER

PHE

ALA

SER

5

LYS

GLY

ALA

GLN

GLU

ARG

HIS

LEU

ARG

LEU

6

LEU

HIS

ALA

GLN

VAL

PHE

PRO

CYS

LYS

7

TYR

CYS

PRO

ALA

THR

PHE

TYR

SER

PRO

8

GLY

LEU

THR

ARG

HIS

ILE

ASN

LYS

CYS

HIS

9

PRO

SER

GLU

ASN

ARG

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

1

ZN

Samples:

NC_sample: HR7614B.021, [U-100% 13C; U-100% 15N], 0.69 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl pH 7.5 10 mM

NC5_sample: HR7614B.023, [U-5% 13C; U-100% 15N], 1.25 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl pH 7.5 10 mM

NC_D2O_sample: HR7614B.023, [U-5% 13C; U-100% 15N], 1.25 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl pH 7.5 10 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC	NC_sample	isotropic	sample_conditions_1
3D HNCO	NC_sample	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D HNCACB	NC_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	NC_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	NC_sample	isotropic	sample_conditions_1
3D C(CO)NH	NC_sample	isotropic	sample_conditions_1
3D HNCA	NC_sample	isotropic	sample_conditions_1
3D HN(CO)CA	NC_sample	isotropic	sample_conditions_1
3D H(CCO)NH	NC_sample	isotropic	sample_conditions_1
3D HCCH-TOCSY	NC_sample	isotropic	sample_conditions_1
3D HNHA	NC_sample	isotropic	sample_conditions_1
4D CC-NOESY	NC_D2O_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC_CT aliphatic	NC5_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC_noCT aliphatic	NC5_sample	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	NC_D2O_sample	isotropic	sample_conditions_1
3D Nnoesy	NC_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY NUS	NC_sample	isotropic	sample_conditions_1

Software:

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

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

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

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

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

Bruker Avance 850 MHz
Varian INOVA 600 MHz

PDB	2LV2 3ZMS
GB	AAA58680
REF	NP_002187 XP_001091915 XP_001144246 XP_002830051 XP_003732871
SP	Q01101

Biological Magnetic Resonance Data Bank