BMRB Entry 15404

Name: Backbone and sidechain 1H, 13C, and 15N Chemical Shift Assignments for H. capsulatum CBP
Published: 2007-08-13

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15404

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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 and sidechain 1H, 13C, and 15N Chemical Shift Assignments for H. capsulatum CBP

Deposition date:

2007-07-23

Original release date:

2007-08-13

Authors:

Beck, Moriah; DeKoster, Gregory; Cistola, David; Goldman, William

Citation:

Citation: Beck, Moriah; DeKoster, Gregory; Hambly, David; Gross, Micheal; Cistola, David; Goldman, William. "Structural features responsible for the biological stability of Histoplasma's virulence factor CBP" Biochemistry 47, 4427-4438 (2008).
PubMed: 18361504

Assembly members:

Assembly members:
CBP, polymer, 78 residues, 7855 Da.

Natural source:

Natural source: Common Name: Ajellomyces capsulata Taxonomy ID: 5037 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Histoplasma capsulatum

Experimental source:

Experimental source: Production method: purified from the natural source Host organism: Histoplasma capsulatum Vector: pTS404

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CBP: DQPSVGDAFDKYNEAVRVFT QLSSAANCDWAACLSSLSAS SAACIAAVGELGLDVPLDLA CAATATSSATEACKGCLW

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
coupling_constants
- coupling_constant_list_1

Data type	Count
13C chemical shifts	276
15N chemical shifts	80
1H chemical shifts	455
coupling constants	66

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CBP, monomer 1	1
2	CBP, monomer 2	1

Entities:

Entity 1, CBP, monomer 1 78 residues - 7855 Da.

G186AR strain mature peptide

1

ASP

GLN

PRO

SER

VAL

GLY

ASP

ALA

PHE

ASP

2

LYS

TYR

ASN

GLU

ALA

VAL

ARG

VAL

PHE

THR

3

GLN

LEU

SER

ALA

ASN

CYS

ASP

TRP

4

ALA

CYS

LEU

SER

LEU

SER

ALA

SER

5

SER

ALA

CYS

ILE

ALA

VAL

GLY

GLU

6

LEU

GLY

LEU

ASP

VAL

PRO

LEU

ASP

LEU

ALA

7

CYS

ALA

THR

ALA

THR

SER

ALA

THR

8

GLU

ALA

CYS

LYS

GLY

CYS

LEU

TRP

Samples:

CBP-13C_15N: CBP, [U-99% 13C; U-99% 15N], 2 ± 1 mM; D2O, [U-99% 2H], 5%; H2O 95%; potassium chloride 100 mM; HEPES, [U-98% 2H], 10 mM; sodium azide 0.05%

CBP-15N: CBP, [U-99% 15N], 1 ± 0.2 mM; D2O, [U-99% 2H], 5%; H2O 95%; potassium chloride 100 mM; HEPES, [U-98% 2H], 10 mM; sodium azide 0.05%

CBP-13C_15N-cys: CBP, [U-99% 13C; U-99% 15N], 2 ± 1 mM; D2O, [U-99% 2H], 5%; H2O 95%; potassium chloride 100 mM; HEPES, [U-98% 2H], 10 mM; sodium azide 0.05%

CBP-normal: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	CBP-15N	isotropic	CBP-normal
3D HNCACB	CBP-13C_15N	isotropic	CBP-normal
3D CBCA(CO)NH	CBP-13C_15N-cys	isotropic	CBP-normal
3D HBHA(CO)NH	CBP-13C_15N-cys	isotropic	CBP-normal
3D HNCO	CBP-13C_15N	isotropic	CBP-normal
3D CBCA(CO)CAHA	CBP-13C_15N	isotropic	CBP-normal
3D HCCH-TOCSY	CBP-13C_15N	isotropic	CBP-normal
3D HCC(TOCSY)NNH	CBP-13C_15N	isotropic	CBP-normal
3D CC(TOCSY)NNH	CBP-13C_15N	isotropic	CBP-normal
3D aromatic HC(C)H-TOCSY	CBP-13C_15N	isotropic	CBP-normal
2D aromatic 13C-HSQC	CBP-13C_15N	isotropic	CBP-normal
2D hbCBcgcdHD	CBP-13C_15N	isotropic	CBP-normal
2D hbCBcgcdHDHE	CBP-13C_15N	isotropic	CBP-normal
3D 1H-13C NOESY	CBP-13C_15N-cys	isotropic	CBP-normal
3D HNHA	CBP-13C_15N-cys	isotropic	CBP-normal

Software:

FELIX v2001, Accelrys Software Inc. - chemical shift assignment, peak picking, processing

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 700 MHz
Varian INOVA 500 MHz