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Found 1 Document (0.556 seconds)

BMRB: 15833

2K5E

NMR CHEMICAL SHIFT ASSIGNMENTS OF PUTATIVE UNCHARACTERIZED PROTEIN. FROM METHANOCALDOCOCCUS JANNASCHII, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET GsR195

Authors

LIU, G., ZHAO, L., CICCOSANTI, C., JIANG, M., XIAO, R., SWAPNA, G., NAIR, R., EVERETT, J.K., ACTON, T.B., ROST, B., Montelione, G.T.

Assembly

GsR195

Entity

1. GsR195 (polymer, Thiol state: all free), 146 monomers, 15981.80 Da Detail

MTQKFTKDMT FAQALQTHPG VAGVLRSYNL GCIGCMGAQN ESLEQGANAH GLNVEDILRD LNALALEHHH HHHMTQKFTK DMTFAQALQT HPGVAGVLRS YNLGCIGCMG AQNESLEQGA NAHGLNVEDI LRDLNALALE HHHHHH

Formula weight

15981.8 Da

Source organism

Methanocaldococcus jannaschii

Exptl. method

solution NMR

Refine. method

simulated annealing, distance geometry, torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 56.2 %, Completeness: 46.0 %, Completeness (bb): 45.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	46.0 % (744 of 1618)	49.2 % (408 of 830)	39.4 % (246 of 624)	54.9 % (90 of 164)
Backbone	45.5 % (397 of 872)	52.3 % (159 of 304)	37.7 % (160 of 424)	54.2 % (78 of 144)
Sidechain	47.2 % (414 of 878)	47.3 % (249 of 526)	46.1 % (153 of 332)	60.0 % (12 of 20)
Aromatic	27.5 % (33 of 120)	31.7 % (19 of 60)	23.3 % (14 of 60)
Methyl	53.8 % (86 of 160)	53.8 % (43 of 80)	53.8 % (43 of 80)

1. GsR195

MTQKFTKDMT FAQALQTHPG VAGVLRSYNL GCIGCMGAQN ESLEQGANAH GLNVEDILRD LNALALEHHH HHHMTQKFTK DMTFAQALQT HPGVAGVLRS YNLGCIGCMG AQNESLEQGA NAHGLNVEDI LRDLNALALE HHHHHH

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4.5, Details 10% D2O, 50 uM DSS and protease inhibitors added NMR buffer pH 4.5

#	Name	Isotope labeling	Concentration
1	entity	[U-100% 13C; U-100% 15N]	1.11 mM
2	DSS	natural abundance	50 uM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4.5, Details NMR buffer pH 4.5,10% D2O, 50 uM DSS, 1x protease inhibitors.

#	Name	Isotope labeling	Concentration
5	entity	[U-10% 13C; U-100% 15N]	1.48 mM
6	DSS	natural abundance	50 uM
7	H2O	natural abundance	90 %
8	D2O	[U-100% 2H]	10 %

LACS Plot; CA

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

Referencing offset: 0.18 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: 0.18 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: 0.06 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2K5E, Strand ID: A Detail

Release date

2008-08-21

Citation

N.A
LIU, G., XIAO, R., Montelione, G.
Not known

Experiments performed 9 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4.5, Details 10% D2O, 50 uM DSS and protease inhibitors added NMR buffer pH 4.5

#	Name	Isotope labeling	Concentration
1	entity	[U-100% 13C; U-100% 15N]	1.11 mM
2	DSS	natural abundance	50 uM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

2 2D 1H-13C HSQC

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4.5, Details 10% D2O, 50 uM DSS and protease inhibitors added NMR buffer pH 4.5

#	Name	Isotope labeling	Concentration
1	entity	[U-100% 13C; U-100% 15N]	1.11 mM
2	DSS	natural abundance	50 uM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

3 2D 1H-13C HSQC

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4.5, Details NMR buffer pH 4.5,10% D2O, 50 uM DSS, 1x protease inhibitors.

#	Name	Isotope labeling	Concentration
5	entity	[U-10% 13C; U-100% 15N]	1.48 mM
6	DSS	natural abundance	50 uM
7	H2O	natural abundance	90 %
8	D2O	[U-100% 2H]	10 %

4 3D SIMULTANEOUS CN-NOESY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4.5, Details 10% D2O, 50 uM DSS and protease inhibitors added NMR buffer pH 4.5

#	Name	Isotope labeling	Concentration
1	entity	[U-100% 13C; U-100% 15N]	1.11 mM
2	DSS	natural abundance	50 uM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

5 4,3D GFT CABCACONHN

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4.5, Details 10% D2O, 50 uM DSS and protease inhibitors added NMR buffer pH 4.5

#	Name	Isotope labeling	Concentration
1	entity	[U-100% 13C; U-100% 15N]	1.11 mM
2	DSS	natural abundance	50 uM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

6 4,3D GFT HNNCABCA

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4.5, Details 10% D2O, 50 uM DSS and protease inhibitors added NMR buffer pH 4.5

#	Name	Isotope labeling	Concentration
1	entity	[U-100% 13C; U-100% 15N]	1.11 mM
2	DSS	natural abundance	50 uM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

7 4,3D GFT HABCABCONHN

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4.5, Details 10% D2O, 50 uM DSS and protease inhibitors added NMR buffer pH 4.5

#	Name	Isotope labeling	Concentration
1	entity	[U-100% 13C; U-100% 15N]	1.11 mM
2	DSS	natural abundance	50 uM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

8 3D HNCO

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4.5, Details 10% D2O, 50 uM DSS and protease inhibitors added NMR buffer pH 4.5

#	Name	Isotope labeling	Concentration
1	entity	[U-100% 13C; U-100% 15N]	1.11 mM
2	DSS	natural abundance	50 uM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

9 3D CCH-COSY

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4.5, Details 10% D2O, 50 uM DSS and protease inhibitors added NMR buffer pH 4.5

#	Name	Isotope labeling	Concentration
1	entity	[U-100% 13C; U-100% 15N]	1.11 mM
2	DSS	natural abundance	50 uM
3	H2O	natural abundance	90 %
4	D2O	[U-100% 2H]	10 %

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_15833_2k5e.nef
Input source #2: Coordindates	2k5e.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---
MTQKFTKDMTFAQALQTHPGVAGVLRSYNLGCIGCMGAQNESLEQGANAHGLNVEDILRDLNALALEHHHHHH
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MTQKFTKDMTFAQALQTHPGVAGVLRSYNLGCIGCMGAQNESLEQGANAHGLNVEDILRDLNALALEHHHHHH

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	73	0	0	100.0

Content subtype: combined_15833_2k5e.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	659		91.8 (chain: A, length: 73)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	2760 (1)	noe	91.8 (chain: A, length: 73)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	338 (338)	.	93.2 (chain: A, length: 73)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 73, Sequence coverage: 91.8%
- Total number of assignments
  - ¹H chemical shifts: 375
  - ¹³C chemical shifts: 207
  - ¹⁵N chemical shifts: 77
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
10	THR	HG1	5.78

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	415	374	90.1
¹³C chemical shifts	312	207	66.3
¹⁵N chemical shifts	84	77	91.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	152	139	91.4
¹³C chemical shifts	146	67	45.9
¹⁵N chemical shifts	72	65	90.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	263	235	89.4
¹³C chemical shifts	166	140	84.3
¹⁵N chemical shifts	12	12	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	43	42	97.7
¹³C chemical shifts	43	42	97.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	30	17	56.7
¹³C chemical shifts	30	12	40.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 73, Sequence coverage: 91.8%
- Total number of restraints: 2760
- Weight of restraints: 1.0 (2760)
- Potential type of restraints: square-well-parabolic (2760)
- Range of distance target values: 2.1, 4.8 (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: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 73, Sequence coverage: 93.2%
- Total number of restraints: 338
- Total number of restraints per polymer type: 338
- Weight of restraints: 1.0 (338)
- Potential type of restraints: square-well-parabolic (338)
- Plot of Phi-Psi angle restraints
- Plot of Chi1-Chi2 angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

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Found 1 Document (0.556 seconds)

BMRB: 15833

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Experiments performed 9 experiments Detail

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NMR combined restraints 4 contents Detail