BMRB Entry 17753

Name: Solution NMR Structure of the Helix-loop-Helix Domain of Human ID3 Protein, Northeast Structural Genomics Consortium Target HR3111A
Published: 2011-08-03

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PDB ID: 2lfh
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17753
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of the Helix-loop-Helix Domain of Human ID3 Protein, Northeast Structural Genomics Consortium Target HR3111A

Deposition date:

2011-06-30

Original release date:

2011-08-03

Authors:

Eletsky, Alexander; Wang, Dongyan; Kohan, Eitan; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas

Citation:

Citation: Eletsky, Alexander; Wang, Dongyan; Kohan, Eitan; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of the Helix-loop-Helix Domain of Human ID3 Protein, Northeast Structural Genomics Consortium Target HR3111A" To be published ., .-..

Assembly members:

Assembly members:
HR3111A, polymer, 68 residues, 7639.775 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: pET 14-15C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HR3111A: MGHHHHHHSHMGGGKGPAAE EPLSLLDDMNHCYSRLRELV PGVPRGTQLSQVEILQRVID YILDLQVV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	236
15N chemical shifts	51
1H chemical shifts	389

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HR3111A, strand 1	1
2	HR3111A, strand 2	1

Entities:

Entity 1, HR3111A, strand 1 68 residues - 7639.775 Da.

Residues 14-68 correspond to the range 29-83 in the native protein. Residues 1-13 represent a non-native affinity tag.

1

MET

GLY

HIS

SER

HIS

2

MET

GLY

LYS

GLY

PRO

ALA

GLU

3

GLU

PRO

LEU

SER

LEU

ASP

MET

ASN

4

HIS

CYS

TYR

SER

ARG

LEU

ARG

GLU

LEU

VAL

5

PRO

GLY

VAL

PRO

ARG

GLY

THR

GLN

LEU

SER

6

GLN

VAL

GLU

ILE

LEU

GLN

ARG

VAL

ILE

ASP

7

TYR

ILE

LEU

ASP

LEU

GLN

VAL

Samples:

NC: HR3111A, [U-100% 13C; U-100% 15N], 0.9 mM; sodium chloride 100 mM; DTT 10 mM; TRIS 10 mM; sodium azide 0.02%; H2O 90%; D2O 10%

NC5: HR3111A, [5% 13C; U-100% 15N], 0.5 mM; sodium chloride 100 mM; DTT 10 mM; TRIS 10 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.5; 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 CT-HSQC aliphatic	NC	isotropic	sample_conditions_1
3D HNCO	NC	isotropic	sample_conditions_1
(4,3)D GFT CABCA(CO)NHN	NC	isotropic	sample_conditions_1
(4,3)D GFT HNNCABCA	NC	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	NC	isotropic	sample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY	NC	isotropic	sample_conditions_1
3D HN(CA)CO	NC	isotropic	sample_conditions_1
3D (H)CCH-COSY aliphatic	NC	isotropic	sample_conditions_1
3D (H)CCH-TOCSY aliphatic	NC	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC	isotropic	sample_conditions_1
2D 1H-15N LR-HSQC for histidines	NC	isotropic	sample_conditions_1
1D 15N T1	NC	isotropic	sample_conditions_1
1D 15N T2	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC methyl	NC5	isotropic	sample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement,structure solution,geometry optimization

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

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

XEASY v1.3.13, Bartels et al. - data analysis

PROSA v6.4, Guntert - processing

VNMRJ v2.2D, Varian - collection

TALOS+ v1.2009.0721.18, Shen, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

Varian INOVA 750 MHz
Varian INOVA 500 MHz

PDB	2LFH
DBJ	BAF82692 BAI46669
EMBL	CAA47360 CAA48862 CAA51827 CAB70600 CAQ64597
GB	AAH03107 AAP35437 AAP36573 AAX32359 AAX32360
PIR	S71405
PRF	2104289A
REF	NP_001003025 NP_001230531 NP_002158 XP_002716031 XP_002811352
SP	Q02535 Q712G9
AlphaFold	Q02535 Q712G9