BMRB Entry 15343

Name: Solution NMR Structure of CAPER RRM2 Domain. Northeast Structural Genomics Target HR4730A.
Published: 2007-08-07

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PDB ID: 2jrs
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15343
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution NMR Structure of CAPER RRM2 Domain. Northeast Structural Genomics Target HR4730A.

Deposition date: 2007-06-28 Original release date: 2007-08-07

Authors: Rossi, Paolo; Zhao, Li; Nwosu, Chioma; Cunningham, Kellie; Owens, Leah; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation: Rossi, Paolo; Xiao, Rong; Acton, Thomas; Montelione, Gaetano. "Solution NMR Structure of CAPER RRM2 Domain. Northeast Structural Genomics Target HR4730A." Not known ., .-..

Assembly members:
HR4730A, polymer, 108 residues, 12041.6 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):
HR4730A: MGHHHHHHSHMAAAMANNLQ KGSAGPMRLYVGSLHFNITE DMLRGIFEPFGRIESIQLMM DSETGRSKGYGFITFSDSEC AKKALEQLNGFELAGRPMKV GHVTERTD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	430
15N chemical shifts	104
1H chemical shifts	680

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HR4730A	1

Entities:

Entity 1, HR4730A 108 residues - 12041.6 Da.

1

MET

GLY

HIS

SER

HIS

2

MET

ALA

MET

ALA

ASN

LEU

GLN

3

LYS

GLY

SER

ALA

GLY

PRO

MET

ARG

LEU

TYR

4

VAL

GLY

SER

LEU

HIS

PHE

ASN

ILE

THR

GLU

5

ASP

MET

LEU

ARG

GLY

ILE

PHE

GLU

PRO

PHE

6

GLY

ARG

ILE

GLU

SER

ILE

GLN

LEU

MET

7

ASP

SER

GLU

THR

GLY

ARG

SER

LYS

GLY

TYR

8

GLY

PHE

ILE

THR

PHE

SER

ASP

SER

GLU

CYS

9

ALA

LYS

ALA

LEU

GLU

GLN

LEU

ASN

GLY

10

PHE

GLU

LEU

ALA

GLY

ARG

PRO

MET

LYS

VAL

11

GLY

HIS

VAL

THR

GLU

ARG

THR

ASP

Samples:

sample_1: HR4730A, [U-100% 13C; U-100% 15N], 1.3 mM; sodium azide 0.02%; MES 20 mM; sodium chloride 100 mM; Calcium Chloride 5 mM; DTT 10 mM

sample_2: HR4730A, [U-5% 13C; U-100% 15N], 1.1 mM; sodium azide 0.02%; MES 20 mM; sodium chloride 100 mM; Calcium Chloride 5 mM; DTT 10 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 293 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
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC stereospecific methyl	sample_2	isotropic	sample_conditions_1
HETnoe	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCOCACB	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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - structure solution

NMRPipe v2.4, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v2.110, Goddard - data analysis

TOPSPIN v1.3, Bruker Biospin - collection

CNSSOLVE v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

X-PLOR NIH v2.11.2, Schwieters, Kuszewski, Tjandra and Clore - refinement

DYANA, Guntert, Mumenthaler and Wuthrich - structure solution

PSVS v1.3, Bhattacharya and Montelione - validation

PDBStat v5.0, (PDBStat) Tejero - data analysis

Molmol v2K.2, Koradi, Billeter and Wuthrich - visualization

MolProbity, Richardson - validation

ProcheckNMR, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Th - validation

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

PDB	2JRS
DBJ	BAE22477 BAE27657 BAE32977 BAG64839 BAJ21051
EMBL	CAD97833 CAE45833 CAE45890 CAH18281 CAH90627
GB	AAA16346 AAA16347 AAH30493 AAH82607 AAH86645
REF	NP_001013225 NP_001125339 NP_001162566 NP_001164806 NP_001193433
SP	Q14498 Q5RC80 Q8VH51
TPG	DAA23046

Biological Magnetic Resonance Data Bank