BMRB Entry 19851

Name: NMR structure of the protein YP_001712342.1 from Acinetobacter baumannii
Published: 2014-04-22

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PDB ID: 2mmb
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19851
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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:

NMR structure of the protein YP_001712342.1 from Acinetobacter baumannii

Deposition date:

2014-03-14

Original release date:

2014-04-22

Authors:

Proudfoot, Andrew; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt

Citation:

Citation: Proudfoot, Andrew; Wuthrich, Kurt; Serrano, Pedro; Geralt, Michael; Dutta, Samit. "NMR structure of the protein YP_002937094.1 from Eubacterium rectale" .

Assembly members:

Assembly members:
entity, polymer, 107 residues, 12156.859 Da.

Natural source:

Natural source: Common Name: Acinetobacter baumannii Taxonomy ID: 470 Superkingdom: Bacteria Kingdom: not available Genus/species: Acinetobacter baumannii

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GTDFGTTNNFVSPNLQLKQN VLPPTPKNIPLPAFGQRIIG WGTGAEGARQRLENIQPADV SMIKKQGTTLEMITAWQDFY EQEQQRNENNPTAKYRARLM KKIADLW

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	362
15N chemical shifts	115
1H chemical shifts	750

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 107 residues - 12156.859 Da.

1

GLY

THR

ASP

PHE

GLY

THR

ASN

PHE

2

VAL

SER

PRO

ASN

LEU

GLN

LEU

LYS

GLN

ASN

3

VAL

LEU

PRO

THR

PRO

LYS

ASN

ILE

PRO

4

LEU

PRO

ALA

PHE

GLY

GLN

ARG

ILE

GLY

5

TRP

GLY

THR

GLY

ALA

GLU

GLY

ALA

ARG

GLN

6

ARG

LEU

GLU

ASN

ILE

GLN

PRO

ALA

ASP

VAL

7

SER

MET

ILE

LYS

GLN

GLY

THR

LEU

8

GLU

MET

ILE

THR

ALA

TRP

GLN

ASP

PHE

TYR

9

GLU

GLN

GLU

GLN

ARG

ASN

GLU

ASN

10

PRO

THR

ALA

LYS

TYR

ARG

ALA

ARG

LEU

MET

11

LYS

ILE

ALA

ASP

LEU

TRP

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 5 mM

sample_conditions_1: ionic strength: 0.220 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
APSY 4D-HACANH	sample_1	isotropic	sample_conditions_1
APSY 5D-CBCACONH	sample_1	isotropic	sample_conditions_1
APSY 5D-HACACONH	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Bruker Biospin, Guntert P. - chemical shift assignment, collection, processing, refinement

UNIO, Herrmann and Wuthrich - chemical shift assignment, structure solution

Opalp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

CARA, Keller and Wuthrich - chemical shift assignment, refinement

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

MDDNMR, Maxim Mayzel, Vladislav Orekhov - processing

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2MMB
DBJ	BAN88776 BAP67935
EMBL	CAM87951 CAP02179 CDG77613 CQR69588 CQR89098
GB	ABS89932 ACJ40142 ACJ58428 ADX02293 ADX91089
REF	WP_000266118 WP_000266120 WP_000266121 WP_000266122 WP_000266123