BMRB Entry 15357

Name: the solution structure of SNase complex
Published: 2007-07-01

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PDB ID: 2khs
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15357
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

the solution structure of SNase complex

Deposition date:

2007-07-01

Original release date:

2007-07-01

Authors:

Geng, Yong; Shan, Lu; Feng, Yingang; Wang, Jinfeng

Citation:

Citation: Geng, Yong; Feng, Yingang; Xie, Tao; Shan, Lu; Wang, Jinfeng. "The native-like interactions between SNase121 and SNase(111-143) fragments induce the recovery of their native-like structures and the ability to degrade DNA." Biochemistry 48, 8692-8703 (2009).
PubMed: 19658434

Assembly members:

Assembly members:
SNase complex -subdomain, polymer, 156 residues, 17686.604 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: Pet-3d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SNase complex -subdomain: ATSTKKLHKEPATLIKAIDG DTVKLMYKGQPMTFRLLLVD TPETKHPKKGVEKYGPEASA FTKKMVENAKKIEVEFDKGQ RTDKYGRGLAYIYADGKMVN EALVRQGLAKVAYVYKPNNT HGSVAYVYKPNNTHEQLLRK SEAQAKKEKLNIWSED

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	580
15N chemical shifts	141
1H chemical shifts	903

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	-subdomain	1

Entities:

Entity 1, -subdomain 156 residues - 17686.604 Da.

1

ALA

THR

SER

THR

LYS

LEU

HIS

LYS

GLU

2

PRO

ALA

THR

LEU

ILE

LYS

ALA

ILE

ASP

GLY

3

ASP

THR

VAL

LYS

LEU

MET

TYR

LYS

GLY

GLN

4

PRO

MET

THR

PHE

ARG

LEU

VAL

ASP

5

THR

PRO

GLU

THR

LYS

HIS

PRO

LYS

GLY

6

VAL

GLU

LYS

TYR

GLY

PRO

GLU

ALA

SER

ALA

7

PHE

THR

LYS

MET

VAL

GLU

ASN

ALA

LYS

8

LYS

ILE

GLU

VAL

GLU

PHE

ASP

LYS

GLY

GLN

9

ARG

THR

ASP

LYS

TYR

GLY

ARG

GLY

LEU

ALA

10

TYR

ILE

TYR

ALA

ASP

GLY

LYS

MET

VAL

ASN

11

GLU

ALA

LEU

VAL

ARG

GLN

GLY

LEU

ALA

LYS

12

VAL

ALA

TYR

VAL

TYR

LYS

PRO

ASN

THR

13

HIS

GLY

SER

VAL

ALA

TYR

VAL

TYR

LYS

PRO

14

ASN

THR

HIS

GLU

GLN

LEU

ARG

LYS

15

SER

GLU

ALA

GLN

ALA

LYS

GLU

LYS

LEU

16

ASN

ILE

TRP

SER

GLU

ASP

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1 mM; deuterated acetate buffer 50 mM; KCl 100 mM; NaN3 0.01 (%w/v); H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 5.0; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

Bruker Avance 600 MHz

BMRB	4010
PDB	1RKN 2F3V 2F3W 2KHS 2SOB
DBJ	BAT21500
GB	AFR11891 AFR11892 AFR11893 AHG12631 AKU89572
REF	WP_049881958