BMRB Entry 25395

Name: Solution structure of the internal EH domain of gamma-synergin
Published: 2015-12-28

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PDB ID: 2mx7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25395
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of the internal EH domain of gamma-synergin

Deposition date: 2014-12-16 Original release date: 2015-12-28

Authors: Kovermann, Michael; Weininger, Ulrich; Loew, Christian

Citation: Kovermann, Michael; Weininger, Ulrich; Loew, Christian. "Solution structure of the internal EH domain of gamma-synergin" Not known ., .-..

Assembly members:
entity, polymer, 112 residues, 12294.373 Da.

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
entity: SMFPSQDPAQPRMPPWIYNE SLVPDAYKKILETTMTPTGI DTAKLYPILMSSGLPRETLG QIWALANRTTPGKLTKEELY TVLAMIAVTQRGVPAMSPDA LNQFPAAPIPTL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	382
15N chemical shifts	86
1H chemical shifts	776

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 112 residues - 12294.373 Da.

1

SER

MET

PHE

PRO

SER

GLN

ASP

PRO

ALA

GLN

2

PRO

ARG

MET

PRO

TRP

ILE

TYR

ASN

GLU

3

SER

LEU

VAL

PRO

ASP

ALA

TYR

LYS

ILE

4

LEU

GLU

THR

MET

THR

PRO

THR

GLY

ILE

5

ASP

THR

ALA

LYS

LEU

TYR

PRO

ILE

LEU

MET

6

SER

GLY

LEU

PRO

ARG

GLU

THR

LEU

GLY

7

GLN

ILE

TRP

ALA

LEU

ALA

ASN

ARG

THR

8

PRO

GLY

LYS

LEU

THR

LYS

GLU

LEU

TYR

9

THR

VAL

LEU

ALA

MET

ILE

ALA

VAL

THR

GLN

10

ARG

GLY

VAL

PRO

ALA

MET

SER

PRO

ASP

ALA

11

LEU

ASN

GLN

PHE

PRO

ALA

PRO

ILE

PRO

12

THR

LEU

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1 mM; TRIS 20 mM; sodium chloride 100 mM; calcium chloride 2 mM

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC IPAP	sample_1	anisotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific, Linge, O'Donoghue and Nilges - chemical shift assignment, collection, peak picking, processing, structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 850 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts