BMRB Entry 51117

Name: Backbone resonance assignments and relaxation rates of the zinc finger domain of murine methionine amino peptidase 1
Published: 2022-06-01

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51117

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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:

Backbone resonance assignments and relaxation rates of the zinc finger domain of murine methionine amino peptidase 1

Deposition date:

2021-09-30

Original release date:

2022-06-01

Authors:

Edmonds, Katherine; Jordan, Matthew; Thalluri, Kishore; Hongwei, Wu; Di Marchi, Richard; Giedroc, David

Citation:

Citation: Weiss, Andy; Murdoch, Caitlin; Edmonds, Katherine; Jordan, Matthew; Monteith, Andrew; Perera, Yasiru; Rodriguez Nassif, Aslin; Petoletti, Amber; Beavers, William; Munneke, Matthew; Drury, Sydney; Krystofiak, Evan; Thalluri, Kishore; Wu, Hongwei; Kruse, Angela; DiMarchi, Richard; Caprioli, Richard; Spraggins, Jeffrey; Chazin, Walter; Giedroc, David; Skaar, Eric. "Zn-regulated GTPase metalloprotein activator 1 modulates vertebrate zinc homeostasis" Cell 185, 2148-2163 (2022).
PubMed: 35584702

Assembly members:

Assembly members:
entity_1, polymer, 59 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAAVETRVCETDGCSSEAKL QCPTCIKLGIQGSYFCSQEC FKGSWATHKLLHKKAKDEK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
heteronucl_NOEs
- heteronucl_NOEs_1
heteronucl_T1_relaxation
- heteronucl_T1_relaxation_1
heteronucl_T2_relaxation
- heteronucl_T2_relaxation_1

Data type	Count
13C chemical shifts	168
15N chemical shifts	57
1H chemical shifts	57
T1 relaxation values	57
T2 relaxation values	57
heteronuclear NOE values	57

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	zf	1
2	zn1	2
3	zn1	2

Entities:

Entity 1, zf 59 residues - Formula weight is not available

1

MET

ALA

VAL

GLU

THR

ARG

VAL

CYS

GLU

2

THR

ASP

GLY

CYS

SER

GLU

ALA

LYS

LEU

3

GLN

CYS

PRO

THR

CYS

ILE

LYS

LEU

GLY

ILE

4

GLN

GLY

SER

TYR

PHE

CYS

SER

GLN

GLU

CYS

5

PHE

LYS

GLY

SER

TRP

ALA

THR

HIS

LYS

LEU

6

LEU

HIS

LYS

ALA

LYS

ASP

GLU

LYS

Entity 2, zn1 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: Metap1 zinc finger, [U-100% 13C; U-100% 15N], 1 ± 0.01 mM; ZINC ION 2 ± 0.001 mM; DSS 0.3 ± 0.01 mM; sodium chloride 150 ± 0.01 mM; sodium phosphate 10 ± 0.01 mM; TCEP 2 ± 0.01 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
T1/R1 relaxation	sample_1	isotropic	sample_conditions_1
T2/R2 relaxation	sample_1	isotropic	sample_conditions_1
1H-15N heteronoe	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v4.0.9 - collection

NMRFAM-SPARKY - data analysis

NMRPipe - processing

istHMS - processing

CARA - data analysis

NMR spectrometers:

Bruker AVANCE NEO 600 MHz

UNP	Q8BP48
AlphaFold	Q8BP48