BMRB Entry 7297

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PDB ID: 2ida
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7297
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Assignment of conserved hypothetical protein RPA1320 from Rhodopseudomonas Palustris; Northeast Structural Genomics Consortium Target RPT3 / Ontario Center for Structural Proteomics Target RP1313

Deposition date:

2006-09-14

Original release date:

2006-10-23

Authors:

Lemak, Alexander; Yee, Adelinda; Lukin, Jonathan; Karra, Murthy; Gutmanas, Aleksandras; Guido, Valeria; Arrowsmith, Cheryl

Citation:

Citation: Lemak, Alexander; Yee, Adelinda; Lukin, Jonathan; Karra, Murthy; Gutmanas, Aleksandras; Guido, Valeria; Arrowsmith, Cheryl. "Solution structure of RPA1320" The BMRB entry is the only known published source for the data..

Assembly members:

Assembly members:
conserved hypotetical protein rpa1320, polymer, 102 residues, 11412 Da.
ZN, non-polymer, 65.409 Da.

Natural source:

Natural source: Common Name: Rhodopseudomonas palustris Taxonomy ID: 258594 Superkingdom: Bacteria Kingdom: not available Genus/species: rhodopseudomonas palustris

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: P11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
conserved hypotetical protein rpa1320: MTMGCRHVAGIRTVTPSALG CEECLKIGSPWVHLRICRTC GHVGCCDDSPHKHATRHFHA TGHPIIEGYDPPEGWGWCYV DEVMFDLSDRMTPHNGPIPR YV

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	417
15N chemical shifts	95
1H chemical shifts	648

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	rpa1320	1
2	ZINC ion, 1	2
3	ZINC ion, 2	2

Entities:

Entity 1, rpa1320 102 residues - 11412 Da.

1

MET

THR

MET

GLY

CYS

ARG

HIS

VAL

ALA

GLY

2

ILE

ARG

THR

VAL

THR

PRO

SER

ALA

LEU

GLY

3

CYS

GLU

CYS

LEU

LYS

ILE

GLY

SER

PRO

4

TRP

VAL

HIS

LEU

ARG

ILE

CYS

ARG

THR

CYS

5

GLY

HIS

VAL

GLY

CYS

ASP

SER

PRO

6

HIS

LYS

HIS

ALA

THR

ARG

HIS

PHE

HIS

ALA

7

THR

GLY

HIS

PRO

ILE

GLU

GLY

TYR

ASP

8

PRO

GLU

GLY

TRP

GLY

TRP

CYS

TYR

VAL

9

ASP

GLU

VAL

MET

PHE

ASP

LEU

SER

ASP

ARG

10

MET

THR

PRO

HIS

ASN

GLY

PRO

ILE

PRO

ARG

11

TYR

VAL

Entity 2, ZINC ion, 1 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: conserved hypotetical protein rpa1320, [U-13C; U-15N], 0.6 mM; NaCl 250 mM; TRIS 10 mM

cond_set1: ionic strength: 0.25 M; pH: 7.3; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
15N HSQC	sample_1	not available	cond_set1
HNCO	sample_1	not available	cond_set1
4D HBHACBCAcoNH	sample_1	not available	cond_set1
4D HCCcoNH TOCSY	sample_1	not available	cond_set1
13C HSQC	sample_1	not available	cond_set1
HC(C)H TOCSY	sample_1	not available	cond_set1
HCC(H) TOCSY	sample_1	not available	cond_set1
15N NOESY	sample_1	not available	cond_set1
13C NOESY	sample_1	not available	cond_set1

Software:

SPARKY v3.95 - spectral analysis

NMR spectrometers:

Bruker Avance 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks