BMRB Entry 16339

Name: NMR structures of a designed Cyanovirin-N homolog lectin; LKAMG
Published: 2009-11-16

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PDB ID: 2kjl
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16339
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structures of a designed Cyanovirin-N homolog lectin; LKAMG

Deposition date:

2009-06-08

Original release date:

2009-11-16

Authors:

Koharudin, Leonardus; Gronenborn, Angela

Citation:

Citation: Koharudin, Leonardus; Furey, William; Gronenborn, Angela. "A designed chimeric cyanovirin-N homolog lectin: structure and molecular basis of sucrose binding." Proteins 77, 904-915 (2009).
PubMed: 19639634

Assembly members:

Assembly members:
LKAMG, polymer, 107 residues, 12104.285 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
LKAMG: MSYADSSRNAVLTNGGRTLR AECRNADGNWVTSELDLDTI IGNNDGHFQWGGQNFTETAE DIRFHPKEGAAEQPILRARL RDCNGEFHDRDVNLNRIQNV NGRLVFQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	301
15N chemical shifts	121
1H chemical shifts	658

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	LKAMG	1

Entities:

Entity 1, LKAMG 107 residues - 12104.285 Da.

a triplet (GSH) artifact cloning is not included in the protein sequence and structure calculation.

1

MET

SER

TYR

ALA

ASP

SER

ARG

ASN

ALA

2

VAL

LEU

THR

ASN

GLY

ARG

THR

LEU

ARG

3

ALA

GLU

CYS

ARG

ASN

ALA

ASP

GLY

ASN

TRP

4

VAL

THR

SER

GLU

LEU

ASP

LEU

ASP

THR

ILE

5

ILE

GLY

ASN

ASP

GLY

HIS

PHE

GLN

TRP

6

GLY

GLN

ASN

PHE

THR

GLU

THR

ALA

GLU

7

ASP

ILE

ARG

PHE

HIS

PRO

LYS

GLU

GLY

ALA

8

ALA

GLU

GLN

PRO

ILE

LEU

ARG

ALA

ARG

LEU

9

ARG

ASP

CYS

ASN

GLY

GLU

PHE

HIS

ASP

ARG

10

ASP

VAL

ASN

LEU

ASN

ARG

ILE

GLN

ASN

VAL

11

ASN

GLY

ARG

LEU

VAL

PHE

GLN

Samples:

sample_1: LKAMG, [U-100% 15N], 0.5 mM; sodium phosphate 20 mM; sodium azide 0.02%

sample_2: LKAMG, [U-100% 13C; U-100% 15N], 1.2 mM; sodium phosphate 20 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 15N-1H HSQC	sample_1	isotropic	sample_conditions_1
3D CBCANH	sample_2	isotropic	sample_conditions_1
3D CBCA(co)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D H(c)CH-NH TOCSY	sample_2	isotropic	sample_conditions_1
(h)CCH-NH TOCSY	sample_2	isotropic	sample_conditions_1
3D HBHA(co)NH	sample_2	isotropic	sample_conditions_1
3D simultaneous 15N/13C NOESY-HSQC	sample_2	isotropic	sample_conditions_1

Software:

CNS v1.1, Brunger A. T. et.al. - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - Automatic NOE calibration

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 800 MHz
Bruker Avance 600 MHz