BMRB Entry 18942

Name: alpha-1 integrin I-domain in complex with GLOGEN triple helical peptide
Published: 2013-11-08

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PDB ID: 2m32
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/BMR18942
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:

alpha-1 integrin I-domain in complex with GLOGEN triple helical peptide

Deposition date:

2013-01-07

Original release date:

2013-11-08

Authors:

Chin, Yanni; Headey, Stephen; Mohanty, Biswaranjan; McEwan, Paul; Swarbrick, James; Mulhern, Terrence; Emsley, Jonas; Simpson, Jamie; Scanlon, Martin

Citation:

Citation: Chin, Yanni K-Y; Headey, Stephen; Mohanty, Biswaranjan; Patil, Rahul; McEwan, Paul; Swarbrick, James; Mulhern, Terrence; Emsley, Jonas; Simpson, Jamie; Scanlon, Martin. "The structure of integrin 1I domain in complex with a collagen-mimetic peptide." J. Biol. Chem. 288, 36796-36809 (2013).
PubMed: 24187131

Assembly members:

Assembly members:
entity_1, polymer, 192 residues, 21513.508 Da.
entity_2, polymer, 23 residues, 1936.040 Da.
entity_MG, non-polymer, 24.305 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: STQLDIVIVLDGSNSIYPWD SVTAFLNDLLERMDIGPKQT QVGIVQYGENVTHEFNLNKY SSTEEVLVAAKKIVQRGGRQ TMTALGIDTARKEAFTEARG ARRGVKKVMVIVTDGESHDN HRLKKVIQDCEDENIQRFSI AILGSYNRGNLSTEKFVEEI KSIASEPTEKHFFNVSDELA LVTIVKTLGERI
entity_2: XGPXGPXGLXGENGPXGPXG PXX

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	740
15N chemical shifts	189
1H chemical shifts	1214

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	alpha-1 integrin I-domain	1
2	GLOGEN triple helical peptide, 1	2
3	GLOGEN triple helical peptide, 2	2
4	GLOGEN triple helical peptide, 3	2
5	MG2	3

Entities:

Entity 1, alpha-1 integrin I-domain 192 residues - 21513.508 Da.

1

SER

THR

GLN

LEU

ASP

ILE

VAL

ILE

VAL

LEU

2

ASP

GLY

SER

ASN

SER

ILE

TYR

PRO

TRP

ASP

3

SER

VAL

THR

ALA

PHE

LEU

ASN

ASP

LEU

4

GLU

ARG

MET

ASP

ILE

GLY

PRO

LYS

GLN

THR

5

GLN

VAL

GLY

ILE

VAL

GLN

TYR

GLY

GLU

ASN

6

VAL

THR

HIS

GLU

PHE

ASN

LEU

ASN

LYS

TYR

7

SER

THR

GLU

VAL

LEU

VAL

ALA

8

LYS

ILE

VAL

GLN

ARG

GLY

ARG

GLN

9

THR

MET

THR

ALA

LEU

GLY

ILE

ASP

THR

ALA

10

ARG

LYS

GLU

ALA

PHE

THR

GLU

ALA

ARG

GLY

11

ALA

ARG

GLY

VAL

LYS

VAL

MET

VAL

12

ILE

VAL

THR

ASP

GLY

GLU

SER

HIS

ASP

ASN

13

HIS

ARG

LEU

LYS

VAL

ILE

GLN

ASP

CYS

14

GLU

ASP

GLU

ASN

ILE

GLN

ARG

PHE

SER

ILE

15

ALA

ILE

LEU

GLY

SER

TYR

ASN

ARG

GLY

ASN

16

LEU

SER

THR

GLU

LYS

PHE

VAL

GLU

ILE

17

LYS

SER

ILE

ALA

SER

GLU

PRO

THR

GLU

LYS

18

HIS

PHE

ASN

VAL

SER

ASP

GLU

LEU

ALA

19

LEU

VAL

THR

ILE

VAL

LYS

THR

LEU

GLY

GLU

20

ARG

ILE

Entity 2, GLOGEN triple helical peptide, 1 23 residues - 1936.040 Da.

1

ACE

GLY

PRO

HYP

GLY

PRO

HYP

GLY

LEU

HYP

2

GLY

GLU

ASN

GLY

PRO

HYP

GLY

PRO

HYP

GLY

3

PRO

HYP

NH2

Entity 3, MG2 - Mg - 24.305 Da.

1

MG

Samples:

sample_1: entity_1, [U-98% 13C; U-98% 15N], 1.2 mM; entity_2 2.4 mM; HEPES 50 mM; NaCl 50 mM; MgCl2 5 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	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

Software:

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

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 900 MHz

BMRB	18020 18021
PDB	1PT6 1QC5 1QCY 2M32 4A0Q
DBJ	BAG62150
GB	AAI37122 AAI37123 EAW54866 EAW54867 EAW54868
REF	NP_852478 XP_001094788 XP_002815595 XP_003276564 XP_003827398
SP	P56199
AlphaFold	P56199