BMRB Entry 17104

Name: YP_001336205.1
Published: 2010-08-18

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PDB ID: 2l1s
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17104
MolProbity Validation Chart

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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:

YP_001336205.1

Deposition date:

2010-08-05

Original release date:

2010-08-18

Authors:

Wahab, Atia-tul; Serrano, Pedro; Geralt, Michael; Wilson, Ian; Wuthrich, Kurt

Citation:

Citation: Wahab, Atia-tul; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the Klebsiella pneumoniae protein YP_001336205" .

Assembly members:

Assembly members:
YP_001336205.1, polymer, 83 residues, 9498.662 Da.

Natural source:

Natural source: Common Name: enterobacteria Taxonomy ID: 573 Superkingdom: bacteria Kingdom: not available Genus/species: Klebsiella pneumoniae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
YP_001336205.1: GAAGIDQYALKEFTADFTQF HIGDTVPAMYLTPEYNIKQW QQRNLPAPDAGSHWTYMGGN YVLITDTEGKILKVYDGEIF YHR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	299
15N chemical shifts	87
1H chemical shifts	575

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	YP_001336205.1	1

Entities:

Entity 1, YP_001336205.1 83 residues - 9498.662 Da.

1

GLY

ALA

GLY

ILE

ASP

GLN

TYR

ALA

LEU

2

LYS

GLU

PHE

THR

ALA

ASP

PHE

THR

GLN

PHE

3

HIS

ILE

GLY

ASP

THR

VAL

PRO

ALA

MET

TYR

4

LEU

THR

PRO

GLU

TYR

ASN

ILE

LYS

GLN

TRP

5

GLN

ARG

ASN

LEU

PRO

ALA

PRO

ASP

ALA

6

GLY

SER

HIS

TRP

THR

TYR

MET

GLY

ASN

7

TYR

VAL

LEU

ILE

THR

ASP

THR

GLU

GLY

LYS

8

ILE

LEU

LYS

VAL

TYR

ASP

GLY

GLU

ILE

PHE

9

TYR

HIS

ARG

Samples:

sample_1: YP_001336205.1, [U-98% 13C; U-98% 15N], 1.4 mM; sodium phosphate buffer 20 mM; sodium chloride 50 mM; sodium azide 0.005 mM; D2O, [U-99% 2H], 5%

sample_conditions_1: ionic strength: 0.11 M; 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
4D APSY-HACANH	sample_1	isotropic	sample_conditions_1
5D APSY-HACACONH	sample_1	isotropic	sample_conditions_1
5D APSY-CBCACONH	sample_1	isotropic	sample_conditions_1
15N-resolved [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1
13C(aliphatic)-resolved [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1
13C(aromatic)-resolved [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1

Software:

UNIO v2.0.0, Torsten Herrmann - chemical shift assignment, peak picking, structure calculation

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - Structure calculation

TOPSPIN v1.3, Bruker Biospin - data collection, processing

Molmol, Koradi, Billeter and Wuthrich - analysis and display of molecule

CARA v1.8.4_linux, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

PDB	2L1S
DBJ	BAH64351 BAS34384
EMBL	CCI75772 CCM83848 CCM88948 CCM96984 CCN30640
GB	ABR77975 ACI08127 ADC57433 AEJ99058 AEW62316
REF	WP_002912749 WP_004201590 WP_016946916 WP_017899344 WP_025713092