BMRB Entry 17971

Name: Solution NMR structure of homeobox domain (171-248) of human homeobox protein TGIF1, Northeast Structural Genomics Consortium Target HR4411B
Published: 2011-10-28

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PDB ID: 2lk2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17971
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of homeobox domain (171-248) of human homeobox protein TGIF1, Northeast Structural Genomics Consortium Target HR4411B

Deposition date:

2011-09-30

Original release date:

2011-10-28

Authors:

Yang, Yunhuang; Ramelot, Theresa; Cort, John; Shastry, Ritu; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation:

Citation: Yang, Yunhuang; Ramelot, Theresa; Cort, John; Shastry, Ritu; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of homeobox domain (171-248) of human homeobox protein TGIF1, Northeast Structural Genomics Consortium Target HR4411B." .

Assembly members:

Assembly members:
TGIF1, polymer, 89 residues, 10666.1 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: pET15_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TGIF1: MGHHHHHHSHMLPKESVQIL RDWLYEHRYNAYPSEQEKAL LSQQTHLSTLQVCNWFINAR RRLLPDMLRKDGKDPNQFTI SRRGAKISE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	380
15N chemical shifts	98
1H chemical shifts	604

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TGIF1	1

Entities:

Entity 1, TGIF1 89 residues - 10666.1 Da.

1

MET

GLY

HIS

SER

HIS

2

MET

LEU

PRO

LYS

GLU

SER

VAL

GLN

ILE

LEU

3

ARG

ASP

TRP

LEU

TYR

GLU

HIS

ARG

TYR

ASN

4

ALA

TYR

PRO

SER

GLU

GLN

GLU

LYS

ALA

LEU

5

LEU

SER

GLN

THR

HIS

LEU

SER

THR

LEU

6

GLN

VAL

CYS

ASN

TRP

PHE

ILE

ASN

ALA

ARG

7

ARG

LEU

PRO

ASP

MET

LEU

ARG

LYS

8

ASP

GLY

LYS

ASP

PRO

ASN

GLN

PHE

THR

ILE

9

SER

ARG

GLY

ALA

LYS

ILE

SER

GLU

Samples:

NC_sample: TGIF1, [U-100% 13C; U-100% 15N], 0.41 ± 0.04 mM; ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; sodium azide 0.02 ± 0.001 %; DTT 10 ± 0.5 mM; calcium chloride 5 ± 0.25 mM; H2O 90%; D2O 10%

NC5_sample: TGIF1, [U-5% 13C; U-100% 15N], 0.36 ± 0.04 mM; ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; calcium chloride 5 ± 0.25 mM; H2O 90%; D2O 10%

NC_sample_in_D2O: TGIF1, [U-100% 13C; U-100% 15N], 0.41 ± 0.04 mM; ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; sodium azide 0.02 ± 0.001 %; DTT 10 ± 0.5 mM; calcium chloride 5 ± 0.25 mM; D2O 100%

sample_conditions_1: ionic strength: 0.2 M; pH: 4.5; 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 aliphatic	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC-aromatic	NC_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC	NC_sample_in_D2O	isotropic	sample_conditions_1
2D 1H-13C HSQC	NC_sample_in_D2O	isotropic	sample_conditions_1
2D 1H-13C HSQC-CT	NC5_sample	isotropic	sample_conditions_1
3D 1H-15N NOESY	NC5_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY_aliph	NC_sample	isotropic	sample_conditions_1
3D HNCO	NC_sample	isotropic	sample_conditions_1
3D HNCACB	NC_sample	isotropic	sample_conditions_1
3D CBCA(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 HBHA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D H(CCO)NH	NC_sample	isotropic	sample_conditions_1
3D C(CCO)NH	NC_sample	isotropic	sample_conditions_1
3D HCCH-COSY	NC_sample	isotropic	sample_conditions_1
3D HCCH-TOCSY	NC_sample	isotropic	sample_conditions_1
3D CC-TOCSY	NC_sample_in_D2O	isotropic	sample_conditions_1
4D CC-NOESY	NC_sample_in_D2O	isotropic	sample_conditions_1
3D 1H-15N NOESY_NUS	NC_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC	NC_sample_in_D2O	isotropic	sample_conditions_1
2D 1H-15N HSQC	NC_sample_in_D2O	isotropic	sample_conditions_1

Software:

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1.4, Bruker Biospin - collection

ASDP v1.0, Huang, Tejero, Powers and Montelione - data analysis

X-PLOR NIH v2.25, Schwieters, Kuszewski, Tjandra and Clore - structure solution

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.113, Goddard - data analysis

PSVS v1.4, Bhattacharya and Montelione - refinement

AutoAssign v2.30, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, chemical shift assignment

PDBStat v5.4, (PdbStat)-Roberto Tejero and Gaetano T. Montelione - structure solution

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift autoassignment

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

NMR spectrometers:

Varian INOVA 600 MHz
Bruker Avance III 850 MHz

PDB	2LK2
DBJ	BAE35685 BAE90340 BAF83801 BAI45661
EMBL	CAA61896 CAA61897 CAG29329
GB	AAF81643 AAH00814 AAH05724 AAH12700 AAH31268
REF	NP_001009815 NP_001015020 NP_001157546 NP_001157547 NP_001157548
SP	P70284 Q15583 Q5IS58
AlphaFold	P70284 Q15583 Q5IS58