BMRB Entry 25760

Name: NMR structure of the 140-315 fragment of the N-acetylglucosamine-1-phosphate transferase, alpha and beta subunits
Published: 2015-10-12

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PDB ID: 2n6d
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25760
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR structure of the 140-315 fragment of the N-acetylglucosamine-1-phosphate transferase, alpha and beta subunits

Deposition date: 2015-08-19 Original release date: 2015-10-12

Authors: Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt

Citation: Serrano, Pedro; Wuthrich, Kurt; Geralt, Michael. "NMR structure of the 140-315 fragment of the N-acetylglucosamine-1-phosphate transferase, alpha and beta subunits" to be published ., .-..

Assembly members:
entity, polymer, 172 residues, 19155.244 Da.

Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
entity: MKVPMLVLDPALPANITLKD LPSLYPSFHSASDIFNVAKP KNPSTNVSVVVFDSTKDVED AHSGLLKGNSRQTVWRGYLT TDKEVPGLVLMQDLAFLSGF PPTFKETNQLKTKLPENLSS KVKLLQLYSEASVALLKLNN PKDFQELNKQTKKNMTIDGK ELTISPAYLLWD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	679
15N chemical shifts	179
1H chemical shifts	1183

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 172 residues - 19155.244 Da.

1

MET

LYS

VAL

PRO

MET

LEU

VAL

LEU

ASP

PRO

2

ALA

LEU

PRO

ALA

ASN

ILE

THR

LEU

LYS

ASP

3

LEU

PRO

SER

LEU

TYR

PRO

SER

PHE

HIS

SER

4

ALA

SER

ASP

ILE

PHE

ASN

VAL

ALA

LYS

PRO

5

LYS

ASN

PRO

SER

THR

ASN

VAL

SER

VAL

6

VAL

PHE

ASP

SER

THR

LYS

ASP

VAL

GLU

ASP

7

ALA

HIS

SER

GLY

LEU

LYS

GLY

ASN

SER

8

ARG

GLN

THR

VAL

TRP

ARG

GLY

TYR

LEU

THR

9

THR

ASP

LYS

GLU

VAL

PRO

GLY

LEU

VAL

LEU

10

MET

GLN

ASP

LEU

ALA

PHE

LEU

SER

GLY

PHE

11

PRO

THR

PHE

LYS

GLU

THR

ASN

GLN

LEU

12

LYS

THR

LYS

LEU

PRO

GLU

ASN

LEU

SER

13

LYS

VAL

LYS

LEU

GLN

LEU

TYR

SER

GLU

14

ALA

SER

VAL

ALA

LEU

LYS

LEU

ASN

15

PRO

LYS

ASP

PHE

GLN

GLU

LEU

ASN

LYS

GLN

16

THR

LYS

ASN

MET

THR

ILE

ASP

GLY

LYS

17

GLU

LEU

THR

ILE

SER

PRO

ALA

TYR

LEU

18

TRP

ASP

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.240 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
APSY 4D-HACANH	sample_1	isotropic	sample_conditions_1
APSY 5D-CBCACONH	sample_1	isotropic	sample_conditions_1
APSY 5D-HACACONH	sample_1	isotropic	sample_conditions_1

Software:

CYANA, G??ntert P. - refinement

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2N6D
DBJ	BAB71102
EMBL	CAJ30014
GB	AAH71687 AAI31788 AAV98624 EAW97682 EHH21112
REF	NP_077288 XP_001092998 XP_001155334 XP_002823695 XP_003832629
SP	Q3T906

Biological Magnetic Resonance Data Bank