BMRB Entry 18869

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PDB ID: 2m1l
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18869
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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:

Solution NMR Structure of Cyclin-dependent kinase 2-associated protein 2 (CDK2AP2, DOC-1R) from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8910C

Deposition date:

2012-11-30

Original release date:

2013-01-24

Authors:

Ertekin, Asli; Janjua, Haleema; Kohan, Eitan; Shastry, Ritu; Pederson, Kari; Prestegard, James; Montelione, Gaetano

Citation:

Citation: Ertekin, Asli; Janjua, Haleema; Shastry, Ritu; Pederson, Kari; Prestegard, James; Montelione, Gaetano. "Solution NMR Structure of CDK2-associated protein 2 (CDK2AP2; Deleted in Oral Cancer 1 Related protein, DOC-1R)" .

Assembly members:

Assembly members:
HR8910C, polymer, 69 residues, 7644.846 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: pET15Nano6HT_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HR8910C: SHMAMKPPGAQGSQSTYTDL LSVIEEMGKEIRPTYAGSKS AMERLKRGIIHARALVRECL AETERNART

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	283
15N chemical shifts	65
1H chemical shifts	435

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HR8910C_1	1
2	HR8910C_2	1

Entities:

Entity 1, HR8910C_1 69 residues - 7644.846 Da.

Protein is a dimer, residues 58-60 are part of N-terminal tag.

1

SER

HIS

MET

ALA

MET

LYS

PRO

GLY

ALA

2

GLN

GLY

SER

GLN

SER

THR

TYR

THR

ASP

LEU

3

LEU

SER

VAL

ILE

GLU

MET

GLY

LYS

GLU

4

ILE

ARG

PRO

THR

TYR

ALA

GLY

SER

LYS

SER

5

ALA

MET

GLU

ARG

LEU

LYS

ARG

GLY

ILE

6

HIS

ALA

ARG

ALA

LEU

VAL

ARG

GLU

CYS

LEU

7

ALA

GLU

THR

GLU

ARG

ASN

ALA

ARG

THR

Samples:

sample_4: HR8910C.005, [U-5% 13C; U-100% 15N], 5.0 mg/mL; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 5%

sample_1: HR8910C.003, [U-100% 13C; U-100% 15N], 5.0 mg/mL; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 5%

sample_2: HR8910C, [U-100% 13C; U-100% 15N], 5.0 mg/mL; HR8910C 15.0 mg/mL; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 5%; Proteinase Inhibitors 1 x

sample_3: HR8910C, [U-100% 15N], 0.3 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 5%; Proteinase Inhibitors 1 x; PEG 4.2%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 13C-filtered NOESY aliphatic	sample_2	isotropic	sample_conditions_1
2D 13C-filtered NOESY aromatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C high res (L/V methyl stereospecific assignment)	sample_4	isotropic	sample_conditions_1
3D HC(C)H-TOCSY	sample_1	isotropic	sample_conditions_1
3D HC(C)H-COSY	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement,structure solution,geometry optimization

CYANA v3.02, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

NMRPipe v2.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN v2.1, Bruker Biospin - collection

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY v3.112, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

PSVS v1.4, Bhattacharya, Montelione - structure validation

NMR spectrometers:

Bruker Avance 800 MHz

UNP	O75956
PDB	2M1L
DBJ	BAB22939 BAB28046 BAB31046 BAG50926
EMBL	CAG33331 CAG46839
GB	AAC61745 AAH02850 AAH16704 AAH25656 AAP35555
REF	NP_001030397 NP_001102968 NP_001253515 NP_001258778 NP_005842
SP	O75956 Q58CN7 Q9CPY4
TPG	DAA13560
AlphaFold	O75956 O75956 Q58CN7 Q9CPY4