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BMRB: 19449

2MCQ

NMR structure of a BolA-like hypothetical protein RP812 from RICKETTSIA PROWAZEKII, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)

Authors

Chen, Y., BARNWAL, R., Yang, F., Varani, G.

Assembly

BolA-like hypothetical protein RP812

Entity

1. BolA-like hypothetical protein RP812 (polymer, Thiol state: not present), 75 monomers, 8318.549 Da Detail

MAISAEELEK ILKKSFPSSV IKITDLVGDQ DHYALEISDA QFNGLSLINQ HKLVKNALSE ILNKKLHSIS IKTIS

Formula weight

8318.549 Da

Source organism

Rickettsia prowazekii

Exptl. method

Refine. method

torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 87.6 %, Completeness (bb): 96.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	87.6 % (786 of 897)	84.1 % (392 of 466)	89.7 % (314 of 350)	98.8 % (80 of 81)
Backbone	96.7 % (433 of 448)	96.0 % (145 of 151)	96.4 % (215 of 223)	98.6 % (73 of 74)
Sidechain	81.4 % (425 of 522)	78.4 % (247 of 315)	85.5 % (171 of 200)	100.0 % (7 of 7)
Aromatic	0.0 % (0 of 40)	0.0 % (0 of 20)	0.0 % (0 of 20)
Methyl	93.4 % (99 of 106)	94.3 % (50 of 53)	92.5 % (49 of 53)

1. entity

MAISAEELEK ILKKSFPSSV IKITDLVGDQ DHYALEISDA QFNGLSLINQ HKLVKNALSE ILNKKLHSIS IKTIS

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	BolA-like hypothetical protein RP812	[U-98% 13C; U-98% 15N]		1.5 mM
2	D2O	natural abundance		10 %
3	H2O	natural abundance		90 %

LACS Plot; CA

Referencing offset: -0.16 ppm, Outliers: 1 Detail

LACS Plot; CB

Referencing offset: -0.16 ppm, Outliers: 1 Detail

LACS Plot; HA

Referencing offset: -0.01 ppm, Outliers: 1 Detail

LACS Plot; CO

Referencing offset: 0.11 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 2MCQ, Strand ID: A Detail

Release date

2013-10-07

Related entities 1. BolA-like hypothetical protein RP812, : 1 : 1 : 42 entities Detail

Experiments performed 10 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	BolA-like hypothetical protein RP812	[U-98% 13C; U-98% 15N]		1.5 mM
2	D2O	natural abundance		10 %
3	H2O	natural abundance		90 %

2 2D 1H-13C HSQC

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	BolA-like hypothetical protein RP812	[U-98% 13C; U-98% 15N]		1.5 mM
2	D2O	natural abundance		10 %
3	H2O	natural abundance		90 %

3 3D CBCA(CO)NH

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	BolA-like hypothetical protein RP812	[U-98% 13C; U-98% 15N]		1.5 mM
2	D2O	natural abundance		10 %
3	H2O	natural abundance		90 %

4 3D HNCACB

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	BolA-like hypothetical protein RP812	[U-98% 13C; U-98% 15N]		1.5 mM
2	D2O	natural abundance		10 %
3	H2O	natural abundance		90 %

5 3D HNCO

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	BolA-like hypothetical protein RP812	[U-98% 13C; U-98% 15N]		1.5 mM
2	D2O	natural abundance		10 %
3	H2O	natural abundance		90 %

6 3D HBHA(CO)NH

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	BolA-like hypothetical protein RP812	[U-98% 13C; U-98% 15N]		1.5 mM
2	D2O	natural abundance		10 %
3	H2O	natural abundance		90 %

7 3D 1H-15N NOESY

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	BolA-like hypothetical protein RP812	[U-98% 13C; U-98% 15N]		1.5 mM
2	D2O	natural abundance		10 %
3	H2O	natural abundance		90 %

8 3D 1H-13C NOESY

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	BolA-like hypothetical protein RP812	[U-98% 13C; U-98% 15N]		1.5 mM
2	D2O	natural abundance		10 %
3	H2O	natural abundance		90 %

9 3D HNHA

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	BolA-like hypothetical protein RP812	[U-98% 13C; U-98% 15N]		1.5 mM
2	D2O	natural abundance		10 %
3	H2O	natural abundance		90 %

10 3D HCCH-TOCSY

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	BolA-like hypothetical protein RP812	[U-98% 13C; U-98% 15N]		1.5 mM
2	D2O	natural abundance		10 %
3	H2O	natural abundance		90 %

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_19449_2mcq.nef
Input source #2: Coordindates	2mcq.cif
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10--------20--------30--------40--------50--------60--------70-------
MAISAEELEKILKKSFPSSVIKITDLVGDQDHYALEISDAQFNGLSLINQHKLVKNALSEILNKKLHSISIKTISIP
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MAISAEELEKILKKSFPSSVIKITDLVGDQDHYALEISDAQFNGLSLINQHKLVKNALSEILNKKLHSISIKTISIP

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	77	0	0	100.0

Content subtype: combined_19449_2mcq.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	803		97.4 (chain: A, length: 77)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	Warning	1691 (1)	noe	97.4 (chain: A, length: 77)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_3	OK	90 (90)	.	71.4 (chain: A, length: 77)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 77, Sequence coverage: 97.4%
- Total number of assignments
  - ¹H chemical shifts: 403
  - ¹³C chemical shifts: 320
  - ¹⁵N chemical shifts: 80
- Completeness of assignments
  - Entity_assemble_ID: A
- Peptide bond of PRO
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 77, Sequence coverage: 97.4%
- Total number of restraints: 1691
- Weight of restraints: 1.0 (1691)
- Potential type of restraints: upper-bound-parabolic (1691)
- Range of distance target values: 2.27, 5.5 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 77, Sequence coverage: 71.4%
- Total number of restraints: 90
- Total number of restraints per polymer type: 90
- Weight of restraints: 1.0 (90)
- Potential type of restraints: square-well-parabolic (90)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords protein