BMRBj - BMREntryMaster

Found 1 Document (0.498 seconds)

BMRB: 15812

2K4Y

NMR Structure of FeoA-like protein from Clostridium acetobutylicum: Northeast Structural Genomics Consortium Target CaR178

Authors

SINGARAPU, K., WU, Y., HUA, J., SUKUMARAN, D., Zhao, L., Jiang, M., Foote, E.L., Xiao, R., Nair, R., Baran, M.C., G.V.T, S., Acton, T., Rost, B., Montelione, G.T., SZYPERSKI, T.

Assembly

FeoA-like protein

Entity

1. FeoA-like protein (polymer, Thiol state: all free), 86 monomers, 9703.386 Da Detail

MTKGIGLNEV EIKSKVKVIG IVPESKVRRK IMDMGIVRGT EIYIEGKAPM GDPIALRLRG YSLSLRKSEA KDILVEVLLE HHHHHH

Formula weight

9703.386 Da

Source organism

Clostridium acetobutylicum

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 95.3 %, Completeness: 91.5 %, Completeness (bb): 92.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	91.5 % (938 of 1025)	91.8 % (494 of 538)	90.8 % (366 of 403)	92.9 % (78 of 84)
Backbone	92.4 % (471 of 510)	93.8 % (166 of 177)	91.2 % (228 of 250)	92.8 % (77 of 83)
Sidechain	90.9 % (539 of 593)	90.9 % (328 of 361)	90.9 % (210 of 231)	100.0 % (1 of 1)
Aromatic	50.0 % (20 of 40)	60.0 % (12 of 20)	40.0 % (8 of 20)
Methyl	98.2 % (112 of 114)	96.5 % (55 of 57)	100.0 % (57 of 57)

1. FeoA-like protein

MTKGIGLNEV EIKSKVKVIG IVPESKVRRK IMDMGIVRGT EIYIEGKAPM GDPIALRLRG YSLSLRKSEA KDILVEVLLE HHHHHH

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]		0.91 mM

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: -0.07 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: -0.07 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: -0.1 ppm, Outliers: 1 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: 0.56 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2K4Y, Strand ID: A Detail

Release date

2008-08-07

Citation

NMR Structure of FeoA-like protein from Clostridium acetobutylicum: Northeast Structural Genomics Consortium Target CaR178
SINGARAPU, K., WU, Y., HUA, J., SUKUMARAN, D., Zhao, L., Jiang, M., Foote, E.L., Xiao, R., Nair, R., Baran, M.C., G.V.T, S., Acton, T., Rost, B., Montelione, G.T., SZYPERSKI, T.
Not known

Related entities 1. FeoA-like protein, : 1 : 4 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_15812_2k4y.nef
Input source #2: Coordindates	2k4y.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------
MTKGIGLNEVEIKSKVKVIGIVPESKVRRKIMDMGIVRGTEIYIEGKAPMGDPIALRLRGYSLSLRKSEAKDILVEVLLEHHHHHH
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MTKGIGLNEVEIKSKVKVIGIVPESKVRRKIMDMGIVRGTEIYIEGKAPMGDPIALRLRGYSLSLRKSEAKDILVEVLLEHHHHHH

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	86	0	0	100.0

Content subtype: combined_15812_2k4y.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	947		95.3 (chain: A, length: 86)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	2219 (1)	noe	90.7 (chain: A, length: 86)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_3	Warning	334 (325)	.	90.7 (chain: A, length: 86)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 86, Sequence coverage: 95.3%
- Total number of assignments
  - ¹H chemical shifts: 501
  - ¹³C chemical shifts: 368
  - ¹⁵N chemical shifts: 78
- 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	538	501	93.1
¹³C chemical shifts	403	368	91.3
¹⁵N chemical shifts	90	78	86.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	177	168	94.9
¹³C chemical shifts	172	157	91.3
¹⁵N chemical shifts	83	77	92.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	361	333	92.2
¹³C chemical shifts	231	211	91.3
¹⁵N chemical shifts	7	1	14.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	61	59	96.7
¹³C chemical shifts	61	59	96.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	20	12	60.0
¹³C chemical shifts	20	8	40.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 86, Sequence coverage: 90.7%
- Total number of restraints: 2214
- Weight of restraints: 1.0 (2214)
- Potential type of restraints: upper-bound-parabolic (2214)
- Range of distance target values: 2.47, 10.7 (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: Warning
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 86, Sequence coverage: 90.7%
- Total number of restraints: 325
- Total number of restraints per polymer type: 325
- Weight of restraints: 1.0 (325)
- Potential type of restraints: square-well-parabolic (325)
- Plot of Phi-Psi angle restraints
- Plot of Chi1-Chi2 angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords GFT NMR, Iron binding protein, Structural Genomics

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (0.498 seconds)

BMRB: 15812

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. FeoA-like protein, : 1 : 4 entities Detail

Experiments performed 7 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail