BMRB Entry 15481

Name: 15N and 1HN assignments of the EVH1 domain of human HOMER3A
Published: 2007-09-27

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15481

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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:

15N and 1HN assignments of the EVH1 domain of human HOMER3A

Deposition date:

2007-09-20

Original release date:

2007-09-27

Authors:

Higman, Victoria; Schmieder, Peter; Diehl, Anne; Bishop, Shurene; Oschkinat, Hartmut; Arrowsmith, Cheryl; Wiegelt, Johan; Edwards, Aled; Sundstrom, Michael; Ball, Linda

Citation:

Citation: Higman, Victoria; Schmieder, Peter; Bishop, Shurene; Diehl, Anne; Oschkinat, Hartmut; Arrowsmith, Cheryl; Edwards, Aled; Sundstrom, Michael; Wiegelt, Johan; Ball, Linda. "15N and 1HN assignments of the EVH1 domain of human HOMER3A" Biomol. NMR Assignments ., .-..

Assembly members:

Assembly members:
HOMER3A_EVH1_domain, polymer, 117 residues, Formula weight is not available

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: pNIC28-Bsa4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HOMER3A_EVH1_domain: SMAREQPIFSTRAHVFQIDP ATKRNWIPAGKHALTVSYFY DATRNVYRIISIGGAKAIIN STVTPNMTFTKTSQKFGQWA DSRANTVYGLGFASEQHLTQ FAEKFQEVKEAARLARE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1

Data type	Count
15N chemical shifts	114
1H chemical shifts	114
T1 relaxation values	91
T2 relaxation values	91

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HOMER3A EVH1 domain	1

Entities:

Entity 1, HOMER3A EVH1 domain 117 residues - Formula weight is not available

The first two residues (SM) are from the vector.

1

SER

MET

ALA

ARG

GLU

GLN

PRO

ILE

PHE

SER

2

THR

ARG

ALA

HIS

VAL

PHE

GLN

ILE

ASP

PRO

3

ALA

THR

LYS

ARG

ASN

TRP

ILE

PRO

ALA

GLY

4

LYS

HIS

ALA

LEU

THR

VAL

SER

TYR

PHE

TYR

5

ASP

ALA

THR

ARG

ASN

VAL

TYR

ARG

ILE

6

SER

ILE

GLY

ALA

LYS

ALA

ILE

ASN

7

SER

THR

VAL

THR

PRO

ASN

MET

THR

PHE

THR

8

LYS

THR

SER

GLN

LYS

PHE

GLY

GLN

TRP

ALA

9

ASP

SER

ARG

ALA

ASN

THR

VAL

TYR

GLY

LEU

10

GLY

PHE

ALA

SER

GLU

GLN

HIS

LEU

THR

GLN

11

PHE

ALA

GLU

LYS

PHE

GLN

GLU

VAL

LYS

GLU

12

ALA

ARG

LEU

ALA

ARG

GLU

Samples:

sample_1: HOMER3A EVH1 domain, [U-99% 15N], 0.7 mM; potassium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.15 mM; DTT 1 mM

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 297 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC - T1 series	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC - T2 series	sample_1	isotropic	sample_conditions_1

Software:

xwinnmr v3.5, Bruker Biospin - collection

TOPSPIN v1.3, Bruker Biospin - processing

ANALYSIS v1.0.15, CCPNMR - chemical shift assignment, peak picking

NMR spectrometers:

Bruker DRX 600 MHz

SWS	Q9NSC5
PDB	2P8V 2P8V
NCBI	gi:21361157
DBJ	BAA35110 BAG36707 BAG54040
EMBL	CAB75536 CAB75543 CAB75544 CAB75545 CAC35223
GB	AAB81545 AAC71025 AAC71029 AAH05773 AAH12113
REF	NP_001139193 NP_001139194 NP_001139196 NP_001139625 NP_001244618
SP	Q99JP6 Q9NSC5 Q9Z2X5
AlphaFold	Q99JP6 Q9NSC5 Q9Z2X5