BMRB Entry 19463

Name: p87m-BMRB
Published: 2014-02-12

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PDB ID: 2n67
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19463
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: p87m-BMRB PubMed: 24234348

Deposition date: 2013-08-28 Original release date: 2014-02-12

Authors: Kaplan, Anne; Maciejewski, Mark; Olson, Rich; Alexandrescu, Andrei

Citation: Kaplan, Anne; Maciejewski, Mark; Olson, Rich; Alexandrescu, Andrei. "NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain." Biomol. NMR Assignments ., .-. (2013).

Assembly members:
p87m-HlyIIC, polymer, 94 residues, 10449.7 Da.

Natural source: Common Name: Bacillus cereus Taxonomy ID: 1396 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus cereus

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

Entity Sequences (FASTA):
p87m-HlyIIC: DNQKALEEQMNSINSVNDKL NKGKGKLSLSMNGNQLKATS SNAGYGISYEDKNWGIFVNG EKVYTFNEKSTVGNISNDIN KLNIKGMYIEIKQI

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	377
15N chemical shifts	112
1H chemical shifts	663

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	p87m-HlyIIc	1

Entities:

Entity 1, p87m-HlyIIc 94 residues - 10449.7 Da.

1

ASP

ASN

GLN

LYS

ALA

LEU

GLU

GLN

MET

2

ASN

SER

ILE

ASN

SER

VAL

ASN

ASP

LYS

LEU

3

ASN

LYS

GLY

LYS

GLY

LYS

LEU

SER

LEU

SER

4

MET

ASN

GLY

ASN

GLN

LEU

LYS

ALA

THR

SER

5

SER

ASN

ALA

GLY

TYR

GLY

ILE

SER

TYR

GLU

6

ASP

LYS

ASN

TRP

GLY

ILE

PHE

VAL

ASN

GLY

7

GLU

LYS

VAL

TYR

THR

PHE

ASN

GLU

LYS

SER

8

THR

VAL

GLY

ASN

ILE

SER

ASN

ASP

ILE

ASN

9

LYS

LEU

ASN

ILE

LYS

GLY

MET

TYR

ILE

GLU

10

ILE

LYS

GLN

ILE

Samples:

sample_1: p87m-HlyIIC, [U-99% 13C; U-99% 15N], 0.4 mM; sodium phosphate 20 mM; EDTA 1 mM; AEBSF 1 mM; sodium azide 0.05 % w/v

sample_2: p87m-HlyIIC, [U-99% 15N], 0.4 mM; sodium phosphate 20 mM; EDTA 1 mM; AEBSF 1 mM; sodium azide 0.05 % w/v

sample_3: p87m-HlyIIC, [U-99% 15N], 0.4 mM; sodium phosphate 20 mM; EDTA 1 mM; AEBSF 1 mM; sodium azide 0.05 % w/v

sample_conditions_1: ionic strength: 0 M; pH: 6.0; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
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 DQF-COSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_3	isotropic	sample_conditions_1
3D HNHB	sample_3	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_3	isotropic	sample_conditions_1

Software:

ANALYSIS v2.1, CCPN -

DANGLE v1.1 -

FELIX-NMR, Accelrys Software Inc. - processing

NMR spectrometers:

Varian INOVA 800 MHz
Varian INOVA 600 MHz

BMRB	19461 19462
DBJ	BAR83236
EMBL	CCW09093
GB	AAM21564 AAP10457 ACK95641 AEA17128 AFQ27182
REF	NP_833256 WP_000709367 WP_000709368 WP_000709369 WP_000709372

Biological Magnetic Resonance Data Bank