BMRB Entry 17002

Name: Solution NMR structure of the protein YP_510488.1
Published: 2010-09-02

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PDB ID: 2kzc
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17002
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of the protein YP_510488.1

Deposition date:

2010-06-15

Original release date:

2010-09-02

Authors:

MOHANTY, BISWARANJAN; SERRANO, PEDRO; GERALT, MICHAEL; HORST, RETO; WILSON, IAN; WUTHRICH, KURT

Citation:

Citation: MOHANTY, BISWARANJAN; SERRANO, PEDRO; GERALT, MICHAEL; HORST, RETO; WILSON, IAN; WUTHRICH, KURT. "Solution NMR structure of the protein YP_510488.1" .
PubMed: NA

Assembly members:

Assembly members:
entity, polymer, 85 residues, 9367.771 Da.

Natural source:

Natural source: Common Name: Jannaschia sp. CCS1 Taxonomy ID: 290400 Superkingdom: Bacteria Kingdom: not available Genus/species: Jannaschia not available

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GMQFKAEARRNKLMGLWVAE VLGKSGDEANAYAAEVVKAD FEEAGHEDVMRKVLGDLDGK RPEAEVRAKYEGLMAVAKAQ LMDEL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	352
15N chemical shifts	90
1H chemical shifts	595

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	YP_510488.1	1

Entities:

Entity 1, YP_510488.1 85 residues - 9367.771 Da.

1

GLY

MET

GLN

PHE

LYS

ALA

GLU

ALA

ARG

2

ASN

LYS

LEU

MET

GLY

LEU

TRP

VAL

ALA

GLU

3

VAL

LEU

GLY

LYS

SER

GLY

ASP

GLU

ALA

ASN

4

ALA

TYR

ALA

GLU

VAL

LYS

ALA

ASP

5

PHE

GLU

ALA

GLY

HIS

GLU

ASP

VAL

MET

6

ARG

LYS

VAL

LEU

GLY

ASP

LEU

ASP

GLY

LYS

7

ARG

PRO

GLU

ALA

GLU

VAL

ARG

ALA

LYS

TYR

8

GLU

GLY

LEU

MET

ALA

VAL

ALA

LYS

ALA

GLN

9

LEU

MET

ASP

GLU

LEU

Samples:

sample_1: PC07345C, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 4.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.113 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
4D APSY - HACANH	sample_1	isotropic	sample_conditions_1
5D APSY - HACACONH	sample_1	isotropic	sample_conditions_1
5D APSY - CBCACONH	sample_1	isotropic	sample_conditions_1
15N Resolved [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1
13Cali Resolved [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1
13Caro Resolved [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1

Software:

CYANA vCYANA3.0, Guntert, Mumenthaler and Wuthrich - TORSION ANGLE DYNAMICS

UNIO vUNIO2.0.0, Torsten Herrmann - structure solution

TOPSPIN v1.3, Bruker Biospin - processing

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2KZC
GB	ABD55463
REF	WP_011455667