BMRB Entry 6313

Click here to enlarge.

PDB ID: 1gm0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6313
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

1H,13C,and 15N NMR assignments of the Bombyx mori Pheromone-binding Protein fragment BmPBP(1-128) at pH 6.5.

Deposition date:

2004-09-03

Original release date:

2005-02-08

Authors:

Damberger, Fred; Michel, Erich; Wuthrich, Kurt

Citation:

Citation: Michel, Erich; Damberger, Fred; Chen, Angela; Ishida, Yuko; Leal, Walter; Wuthrich, Kurt. "Letter to the Editor: Assignments for the Bombyx mori pheromone-binding protein fragment BmPBP(1-128) at pH 6.5" J. Biomol. NMR 31, 65-65 (2005).

Assembly members:

Assembly members:
Bombyx mori Pheromone-binding protein, polymer, 128 residues, 14467 Da.

Natural source:

Natural source: Common Name: silkworm moth Taxonomy ID: 7091 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Bombyx mori

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Bombyx mori Pheromone-binding protein: SQEVMKNLSLNFGKALDECK KEMTLTDAINEDFYNFWKEG YEIKNRETGCAIMCLSTKLN MLDPEGNLHHGNAMEFAKKH GADETMAQQLIDIVHGCEKS TPANDDKCIWTLGVATCFKA EIHKLNWA

Data sets:

assigned_chemical_shifts
- BmPBP_1

Data type	Count
1H chemical shifts	902
13C chemical shifts	555
15N chemical shifts	145

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BmPBP	1

Entities:

Entity 1, BmPBP 128 residues - 14467 Da.

1

SER

GLN

GLU

VAL

MET

LYS

ASN

LEU

SER

LEU

2

ASN

PHE

GLY

LYS

ALA

LEU

ASP

GLU

CYS

LYS

3

LYS

GLU

MET

THR

LEU

THR

ASP

ALA

ILE

ASN

4

GLU

ASP

PHE

TYR

ASN

PHE

TRP

LYS

GLU

GLY

5

TYR

GLU

ILE

LYS

ASN

ARG

GLU

THR

GLY

CYS

6

ALA

ILE

MET

CYS

LEU

SER

THR

LYS

LEU

ASN

7

MET

LEU

ASP

PRO

GLU

GLY

ASN

LEU

HIS

8

GLY

ASN

ALA

MET

GLU

PHE

ALA

LYS

HIS

9

GLY

ALA

ASP

GLU

THR

MET

ALA

GLN

LEU

10

ILE

ASP

ILE

VAL

HIS

GLY

CYS

GLU

LYS

SER

11

THR

PRO

ALA

ASN

ASP

LYS

CYS

ILE

TRP

12

THR

LEU

GLY

VAL

ALA

THR

CYS

PHE

LYS

ALA

13

GLU

ILE

HIS

LYS

LEU

ASN

TRP

ALA

Samples:

sample_1: Bombyx mori Pheromone-binding protein, [U-99% 13C; U-98% 15N], 1.1 mM; potassium phosphate buffer 50 mM; H2O 95%; D2O 5%; NaN3 0.2%

Ex-cond_1: pH: 6.5; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
HNCA	sample_1	not available	Ex-cond_1
CBCA(CO)NH	sample_1	not available	Ex-cond_1
HNCACB	sample_1	not available	Ex-cond_1
HNCO	sample_1	not available	Ex-cond_1
HN(CA)CO	sample_1	not available	Ex-cond_1
(H)CCH-COSY	sample_1	not available	Ex-cond_1
15N-resolved [1H,1H]-TOCSY	sample_1	not available	Ex-cond_1
(HB)CB(CGCD)HD	sample_1	not available	Ex-cond_1
15N-resolved [1H,1H]-NOESY	sample_1	not available	Ex-cond_1
13C(aliphatic)-resolved [1H,1H]-NOESY	sample_1	not available	Ex-cond_1
13C(aromatic)-resolved [1H,1H]-NOESY	sample_1	not available	Ex-cond_1

Software:

CARA v1.1 - computer-aided resonance assignment

ATNOS - automated peak-picking, integration

CANDID - automated NOE crosspeak assignment for structure calculation

DYANA - automated structure calculation using NMR constraints

NMR spectrometers:

Bruker DRX 500 MHz
Bruker DRX 900 MHz

BMRB	4849
PDB	1DQE 1GM0 1LS8 1XFR 2FJY 2P70 2P71
EMBL	CAA64443
GB	ACT34881 AGR44744 AGR44745 AGR44746 AGR44747
REF	NP_001037494
SP	P34174
AlphaFold	P34174 P34174 P34174