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Found 1 Document (0.483 seconds)

BMRB: 15836

2K5H

Solution NMR structure of protein encoded by MTH693 from Methanobacterium thermoautotrophicum: Northeast Structural Genomics Consortium target tt824a

Authors

Wu, Y., Singarapu, K., Semesi, A., Sukumaran, D., Yee, A., Garcia, M., Arrowsmith, C., Szyperski, T.

Assembly

tt824a

Entity

1. tt824a (polymer, Thiol state: not present), 101 monomers, 10912.16 Da Detail

MGSSHHHHHH SSGRENLYFQ GHMAARITGE PSKKAVSDRL IGRKGVVMEA ISPQNSGLVK VDGETWRATS GTVLDVGEEV SVKAIEGVKL VVEKLEEQKG S

Formula weight

10912.16 Da

Source organism

Methanothermobacter thermautotrophicus

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 91.1 %, Completeness: 86.8 %, Completeness (bb): 87.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	86.8 % (972 of 1120)	85.9 % (499 of 581)	87.1 % (378 of 434)	90.5 % (95 of 105)
Backbone	87.5 % (527 of 602)	86.3 % (183 of 212)	87.6 % (255 of 291)	89.9 % (89 of 99)
Sidechain	86.3 % (524 of 607)	85.6 % (316 of 369)	87.1 % (202 of 232)	100.0 % (6 of 6)
Aromatic	51.7 % (30 of 58)	58.6 % (17 of 29)	42.9 % (12 of 28)	100.0 % (1 of 1)
Methyl	100.0 % (108 of 108)	100.0 % (54 of 54)	100.0 % (54 of 54)

1. tt824a

MGSSHHHHHH SSGRENLYFQ GHMAARITGE PSKKAVSDRL IGRKGVVMEA ISPQNSGLVK VDGETWRATS GTVLDVGEEV SVKAIEGVKL VVEKLEEQKG S

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
1	entity	[U-100% 13C; U-100% 15N]	0.7 mM
2	H2O	natural abundance	90 %
3	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: -0.08 ppm, Outliers: 2 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: -0.08 ppm, Outliers: 2 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: 0.0 ppm, Outliers: 5 Detail

LACS Plot; CO

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: 0.34 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2K5H, Strand ID: A Detail

Release date

2008-08-18

Citation

Solution NMR structure of protein encoded by MTH693 from Methanobacterium thermoautotrophicum: Northeast Structural Genomics Consortium target tt824a
Wu, Y., Singarapu, K., Semesi, A., Sukumaran, D., Yee, A., Garcia, M., Arrowsmith, C., Szyperski, T.
Not known

Related entities 1. tt824a, : 1 : 3 entities Detail

Experiments performed 7 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_15836_2k5h.nef
Input source #2: Coordindates	2k5h.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
MGSSHHHHHHSSGRENLYFQGHMAARITGEPSKKAVSDRLIGRKGVVMEAISPQNSGLVKVDGETWRATSGTVLDVGEEVSVKAIEGVKLVVEKLEEQKG
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MGSSHHHHHHSSGRENLYFQGHMAARITGEPSKKAVSDRLIGRKGVVMEAISPQNSGLVKVDGETWRATSGTVLDVGEEVSVKAIEGVKLVVEKLEEQKG

-
S
|
S

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	101	0	0	100.0

Content subtype: combined_15836_2k5h.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	975		90.1 (chain: A, length: 101)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	1393 (1)	noe	82.2 (chain: A, length: 101)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	Warning	179 (178)	.	75.2 (chain: A, length: 101)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 101, Sequence coverage: 90.1%
- Total number of assignments
  - ¹³C chemical shifts: 374
  - ¹H chemical shifts: 507
  - ¹⁵N chemical shifts: 94
- 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 (%)
¹³C chemical shifts	434	374	86.2
¹H chemical shifts	581	507	87.3
¹⁵N chemical shifts	110	94	85.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	202	174	86.1
¹H chemical shifts	212	185	87.3
¹⁵N chemical shifts	99	88	88.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	232	200	86.2
¹H chemical shifts	369	322	87.3
¹⁵N chemical shifts	11	6	54.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	57	55	96.5
¹H chemical shifts	57	55	96.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	28	12	42.9
¹H chemical shifts	29	17	58.6
¹⁵N chemical shifts	1	1	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 101, Sequence coverage: 82.2%
- Total number of restraints: 1393
- Weight of restraints: 1.0 (1393)
- Potential type of restraints: square-well-parabolic (1393)
- Range of distance target values: 2.09, 6.28 (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: Warning
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 101, Sequence coverage: 75.2%
- Total number of restraints: 178
- Total number of restraints per polymer type: 178
- Weight of restraints: 1.0 (178)
- Potential type of restraints: square-well-parabolic (178)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

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Found 1 Document (0.483 seconds)

BMRB: 15836

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. tt824a, : 1 : 3 entities Detail

Experiments performed 7 experiments Detail

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NMR combined restraints 4 contents Detail