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BMRB: 15835

2K5G

Solution NMR structure of protein encoded by gene BPP1335 from Bordetella parapertussis: Northeast Structural Genomics Target BpR195

Authors

SINGARAPU, K., ELETSKY, A., SATHYAMOORTHY, B., SUKUMARAN, D., Wang, D., Jiang, M., Ciccosanti, C., Xiao, R., Liu, J., Baran, M.C., Swapna, G., Acton, T.B., Rost, B., Montelione, G.T., SZYPERSKI, T.

Assembly

BpR195

Entity

1. BpR195 (polymer, Thiol state: not present), 191 monomers, 21136.57 Da Detail

MTSPSSAFPD GHGARLDAQS IRFERLLPGP IERVWAWLAD ADKRARWLAG GELPRQPGQT FELHFNHAAL TAETAPARYA QYDRPIVARH TLLRCEPPRV LALTWGGGAG EAPSEVLFEL SEAGEQVRLV LTHTRLADRA AMLDVAGGWH AHLAVLAGKL AGQAPPPFWT TLAQAEQDYE QRLLEHHHHH H

Formula weight

21136.57 Da

Source organism

Bordetella parapertussis

Exptl. method

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 94.2 %, Completeness: 89.2 %, Completeness (bb): 90.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	89.2 % (1933 of 2167)	90.3 % (1009 of 1118)	87.0 % (745 of 856)	92.7 % (179 of 193)
Backbone	90.3 % (1009 of 1118)	92.2 % (353 of 383)	88.0 % (491 of 558)	93.2 % (165 of 177)
Sidechain	88.7 % (1086 of 1225)	89.3 % (656 of 735)	87.8 % (416 of 474)	87.5 % (14 of 16)
Aromatic	77.9 % (162 of 208)	86.5 % (90 of 104)	67.3 % (66 of 98)	100.0 % (6 of 6)
Methyl	95.5 % (210 of 220)	95.5 % (105 of 110)	95.5 % (105 of 110)

1. BpR195

MTSPSSAFPD GHGARLDAQS IRFERLLPGP IERVWAWLAD ADKRARWLAG GELPRQPGQT FELHFNHAAL TAETAPARYA QYDRPIVARH TLLRCEPPRV LALTWGGGAG EAPSEVLFEL SEAGEQVRLV LTHTRLADRA AMLDVAGGWH AHLAVLAGKL AGQAPPPFWT TLAQAEQDYE QRLLEHHHHH H

Show sample condition

Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]		1.069 mM
2	H2O	natural abundance		95 %
3	D2O	[U-100% 2H]		5 %

Sample #2

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
4	entity	[U-100% 15N; U-5% 13C]		1.1 mM
5	H2O	natural abundance		95 %
6	D2O	[U-100% 2H]		5 %

Protein Blocks Logo

Calculated from 20 models in PDB: 2K5G, Strand ID: A Detail

Release date

2008-08-18

Citation

Solution NMR structure of protein encoded by gene BPP1335 from Bordetella parapertussis: Northeast Structural Genomics Target BpR195
SINGARAPU, K., ELETSKY, A., SATHYAMOORTHY, B., SUKUMARAN, D., Wang, D., Jiang, M., Ciccosanti, C., Xiao, R., Liu, J., Baran, M.C., Swapna, G., Acton, T.B., Rost, B., Montelione, G.T., SZYPERSKI, T.
Not known

Related entities 1. BpR195, : 1 entities Detail

Experiments performed 10 experiments Detail

1 2D 1H-15N HSQC

Instrument

Varian INOVA - 750 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]		1.069 mM
2	H2O	natural abundance		95 %
3	D2O	[U-100% 2H]		5 %

2 3D CBCA(CO)NH

Instrument

Varian INOVA - 750 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]		1.069 mM
2	H2O	natural abundance		95 %
3	D2O	[U-100% 2H]		5 %

3 3D HNCACB

Instrument

Varian INOVA - 750 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]		1.069 mM
2	H2O	natural abundance		95 %
3	D2O	[U-100% 2H]		5 %

4 3D HBHA(CO)NH

Instrument

Varian INOVA - 750 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]		1.069 mM
2	H2O	natural abundance		95 %
3	D2O	[U-100% 2H]		5 %

5 4,3D GFT HCCH COSY

Instrument

Varian INOVA - 750 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]		1.069 mM
2	H2O	natural abundance		95 %
3	D2O	[U-100% 2H]		5 %

6 3D 15N-13C simultanious NOESY

Instrument

Varian INOVA - 750 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]		1.069 mM
2	H2O	natural abundance		95 %
3	D2O	[U-100% 2H]		5 %

7 3D HNCO

Instrument

Varian INOVA - 750 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]		1.069 mM
2	H2O	natural abundance		95 %
3	D2O	[U-100% 2H]		5 %

8 3D HCCH-TOCSY

Instrument

Varian INOVA - 750 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]		1.069 mM
2	H2O	natural abundance		95 %
3	D2O	[U-100% 2H]		5 %

9 2D 1H-13C HSQC

Instrument

Varian INOVA - 750 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]		1.069 mM
2	H2O	natural abundance		95 %
3	D2O	[U-100% 2H]		5 %

10 2D 1H-13C HSQC

Instrument

Varian INOVA - 750 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
4	entity	[U-100% 15N; U-5% 13C]		1.1 mM
5	H2O	natural abundance		95 %
6	D2O	[U-100% 2H]		5 %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_15835_2k5g.nef
Input source #2: Coordindates	2k5g.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--------80--------90-------100
MTSPSSAFPDGHGARLDAQSIRFERLLPGPIERVWAWLADADKRARWLAGGELPRQPGQTFELHFNHAALTAETAPARYAQYDRPIVARHTLLRCEPPRV
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MTSPSSAFPDGHGARLDAQSIRFERLLPGPIERVWAWLADADKRARWLAGGELPRQPGQTFELHFNHAALTAETAPARYAQYDRPIVARHTLLRCEPPRV

-------110-------120-------130-------140-------150-------160-------170-------180-------190-
LALTWGGGAGEAPSEVLFELSEAGEQVRLVLTHTRLADRAAMLDVAGGWHAHLAVLAGKLAGQAPPPFWTTLAQAEQDYEQRLLEHHHHHH
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LALTWGGGAGEAPSEVLFELSEAGEQVRLVLTHTRLADRAAMLDVAGGWHAHLAVLAGKLAGQAPPPFWTTLAQAEQDYEQRLLEHHHHHH

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	191	0	0	100.0

Content subtype: combined_15835_2k5g.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1923		92.1 (chain: A, length: 191)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	3756 (1)	noe	89.5 (chain: A, length: 191)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	86 (1)	hbond	34.0 (chain: A, length: 191)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	Warning	682 (669)	.	85.3 (chain: A, length: 191)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 191, Sequence coverage: 92.1%
- Total number of assignments
  - ¹³C chemical shifts: 738
  - ¹H chemical shifts: 1010
  - ¹⁵N chemical shifts: 175
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- Tautomeric state of HIS
- 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: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 191, Sequence coverage: 89.5%
- Total number of restraints: 3752
- Weight of restraints: 1.0 (3752)
- Potential type of restraints: square-well-parabolic (3752)
- Range of distance target values: 1.31, 5.57 (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
- Saveframe: CNS/XPLOR_distance_constraints_3
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 191, Sequence coverage: 34.0%
  - Total number of restraints: 86
  - Weight of restraints: 1.0 (86)
  - Potential type of restraints: square-well-parabolic (86)
  - Range of distance target values: 1.0, 1.5 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_4
- Status: Warning
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 191, Sequence coverage: 85.3%
- Total number of restraints: 669
- Total number of restraints per polymer type: 669
- Weight of restraints: 1.0 (669)
- Potential type of restraints: square-well-parabolic (669)
- Plot of Phi-Psi angle restraints
- Plot of Chi1-Chi2 angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A