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Found 1 Document (0.777 seconds)

BMRB: 16576

2KQ1

Solution Structure Of Protein BH0266 From Bacillus halodurans. Northeast Structural Genomics Consortium Target BhR97a

Authors

Wu, Y., Eletsky, A., Lee, D., Sathyamoorthy, B., Buchwald, W., Hua, J., Ciccosanti, C., He, Y., Hamilton, K., Acton, T., Xiao, R., Everett, J., Lee, H., Prestegard, J., Montelione, G., Szyperski, T.

Assembly

Protein BH0266 From Bacillus halodurans

Entity

1. Protein BH0266 From Bacillus halodurans (polymer, Thiol state: not present), 119 monomers, 13571.91 Da Detail

MPTFDHGNLS LGELELTVLY DEERYDIVEQ TETVQVDLEG PRGVLTVFRF ARPSYEVFVD LTEAGEGSHT VDVEHRGFPG DLAVTVEPRM ARVQLEERQT VSVPVTVEMI NLEHHHHHH

Formula weight

13571.91 Da

Source organism

Escherichia coli

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts, spectral_peak_list

Chem. Shift Complete

Sequence coverage: 92.4 %, Completeness: 80.7 %, Completeness (bb): 78.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	80.7 % (1093 of 1354)	87.5 % (607 of 694)	69.7 % (377 of 541)	91.6 % (109 of 119)
Backbone	78.9 % (554 of 702)	91.3 % (219 of 240)	66.2 % (231 of 349)	92.0 % (104 of 113)
Sidechain	84.0 % (641 of 763)	85.5 % (388 of 454)	81.8 % (248 of 303)	83.3 % (5 of 6)
Aromatic	45.5 % (50 of 110)	58.2 % (32 of 55)	32.7 % (18 of 55)
Methyl	98.6 % (146 of 148)	97.3 % (72 of 74)	100.0 % (74 of 74)

1. BH0266

MPTFDHGNLS LGELELTVLY DEERYDIVEQ TETVQVDLEG PRGVLTVFRF ARPSYEVFVD LTEAGEGSHT VDVEHRGFPG DLAVTVEPRM ARVQLEERQT VSVPVTVEMI NLEHHHHHH

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 288 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	entity	[U-100% 13C; U-100% 15N]	1.0 mM
2	H2O	natural abundance	90 %
3	D2O	natural abundance	10 %

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 288 K, pH 6.5

#	Name	Isotope labeling	Concentration
4	entity	[U-5% 13C; U-99% 15N]	1.0 mM
5	H2O	natural abundance	90 %
6	D2O	natural abundance	10 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.25 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.25 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: -0.02 ppm, Outliers: 4 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2KQ1, Strand ID: A Detail

Release date

2010-01-06

Citation

Structures of domains I and IV from YbbR are representative of a widely distributed protein family
Barb, A.W., Cort, J.R., Seetharaman, J., Lew, S., Lee, H., Acton, T., Xiao, R., Kennedy, M.A., Tong, L., Montelione, G.T., Prestegard, J.H.
Protein Sci. (2011), 20, 396-405, PubMed 21154411 , DOI 10.1002/pro.571 , Abstract

Related entities 1. Protein BH0266 From Bacillus halodurans, : 1 : 15 entities Detail

Experiments performed 7 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_16576_2kq1.nef
Input source #2: Coordindates	2kq1.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
MPTFDHGNLSLGELELTVLYDEERYDIVEQTETVQVDLEGPRGVLTVFRFARPSYEVFVDLTEAGEGSHTVDVEHRGFPGDLAVTVEPRMARVQLEERQT
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MPTFDHGNLSLGELELTVLYDEERYDIVEQTETVQVDLEGPRGVLTVFRFARPSYEVFVDLTEAGEGSHTVDVEHRGFPGDLAVTVEPRMARVQLEERQT

-------110---------
VSVPVTVEMINLEHHHHHH
|||||||||||||||||||
VSVPVTVEMINLEHHHHHH

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	119	0	0	100.0

Content subtype: combined_16576_2kq1.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1084		92.4 (chain: A, length: 119)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	1324 (1)	noe	92.4 (chain: A, length: 119)
2	Distance restraints	DYANA/DIANA_distance_constraints_3	Warning	22 (1)	hbond	18.5 (chain: A, length: 119)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	203 (203)	.	79.8 (chain: A, length: 119)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 119, Sequence coverage: 92.4%
- Total number of assignments
  - ¹H chemical shifts: 613
  - ¹³C chemical shifts: 358
  - ¹⁵N chemical shifts: 113
- Completeness of assignments
  - Entity_assemble_ID: A
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	694	613	88.3
¹³C chemical shifts	541	358	66.2
¹⁵N chemical shifts	127	113	89.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	240	222	92.5
¹³C chemical shifts	238	110	46.2
¹⁵N chemical shifts	113	104	92.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	454	391	86.1
¹³C chemical shifts	303	248	81.8
¹⁵N chemical shifts	14	9	64.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	77	75	97.4
¹³C chemical shifts	77	75	97.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	55	32	58.2
¹³C chemical shifts	55	18	32.7

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 119, Sequence coverage: 92.4%
- Total number of restraints: 1324
- Weight of restraints: 1.0 (1324)
- Potential type of restraints: upper-bound-parabolic (1324)
- Range of distance target values: 2.4, 9.15 (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: DYANA/DIANA_distance_constraints_3
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 119, Sequence coverage: 18.5%
  - Total number of restraints: 22
  - Weight of restraints: 1.0 (22)
  - Potential type of restraints: upper-bound-parabolic (22)
  - Range of distance target values: 2.0, 3.0 (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: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 119, Sequence coverage: 79.8%
- Total number of restraints: 203
- Total number of restraints per polymer type: 203
- Weight of restraints: 1.0 (203)
- Potential type of restraints: square-well-parabolic (203)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

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Found 1 Document (0.777 seconds)

BMRB: 16576

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Protein BH0266 From Bacillus halodurans, : 1 : 15 entities Detail

Experiments performed 7 experiments Detail

Instrument

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NMR combined restraints 5 contents Detail