BMRB Entry 5141

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PDB ID: 1t4y
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5141
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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:

Sequence-specific resonance assignments of the N-terminal, 105-residue KaiC-interacting domain of SasA, a protein necessary for a robust circadian rhythm in Synechococcus elongatus

Deposition date:

2001-09-01

Original release date:

2003-03-12

Authors:

Klewer, Douglas; Williams, Stanly; Golden, Susan; LiWang, Andy

Citation:

Citation: Klewer, Douglas; Williams, Stanly; Golden, Susan; LiWang, Andy. "Letter to the Editor: Sequence-specific resonance assignments of the N-terminal, 105-residue KaiC-interacting domain of SasA, a protein necessary for a robust circadian rhythm in Synechococcus elongatus" J. Biomol. NMR 24, 77-78 (2002).

Assembly members:

Assembly members:
SasA, polymer, 105 residues, 11476.3 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SasA: GSSLSPQALAQPLLLQLFVD TRPLSQHIVQRVKNILAAVE ATVPISLQVINVADQPQLVE YYRLVVTPALVKIGPGSRQV LSGIDLTDQLANQLPQWLVQ QEGIF

Data sets:

assigned_chemical_shifts
- shift_set_1

Data type	Count
13C chemical shifts	343
15N chemical shifts	104
1H chemical shifts	683

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SasA N-terminus	1

Entities:

Entity 1, SasA N-terminus 105 residues - 11476.3 Da.

1

GLY

SER

LEU

SER

PRO

GLN

ALA

LEU

ALA

2

GLN

PRO

LEU

GLN

LEU

PHE

VAL

ASP

3

THR

ARG

PRO

LEU

SER

GLN

HIS

ILE

VAL

GLN

4

ARG

VAL

LYS

ASN

ILE

LEU

ALA

VAL

GLU

5

ALA

THR

VAL

PRO

ILE

SER

LEU

GLN

VAL

ILE

6

ASN

VAL

ALA

ASP

GLN

PRO

GLN

LEU

VAL

GLU

7

TYR

ARG

LEU

VAL

THR

PRO

ALA

LEU

8

VAL

LYS

ILE

GLY

PRO

GLY

SER

ARG

GLN

VAL

9

LEU

SER

GLY

ILE

ASP

LEU

THR

ASP

GLN

LEU

10

ALA

ASN

GLN

LEU

PRO

GLN

TRP

LEU

VAL

GLN

11

GLN

GLU

GLY

ILE

PHE

Samples:

sample_SasA-105: SasA, [U-99% 13C; U-99% 15N], 0.6 mM

condition_1: ionic strength: 0.22 M; pH: 7.0 na; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
CBCA(CO)NH	not available	not available	not available
CBCANH	not available	not available	not available
HNHA	not available	not available	not available
HBHA(CO)NH	not available	not available	not available
C(CO)NH	not available	not available	not available
H(CCO)NH	not available	not available	not available
H(C)CH-COSY	not available	not available	not available
1H-15N HSQC	not available	not available	not available

Software:

NMRPipe v1.8 rev 2001.030.21.27 - NMR data processing

PIPP v4.2.6 - Spectra visualization

STAPP v4.2.6 - partial sequence specific assignments, spin system creation

NMR spectrometers:

Varian Inova 600 MHz

PDB	1T4Y 1T4Z
DBJ	BAA03145 BAD80168
GB	ABB58144 AJD57380
REF	WP_011244288 WP_011378322 WP_039755926 YP_172688 YP_401131
SP	Q06904
AlphaFold	Q06904 Q06904