BMRBj - BMREntryMaster

Found 1 Document (0.803 seconds)

BMRB: 16038

2KB3

NMR Structure of the phosphorylated form of OdhI, pOdhI.

Authors

Barthe, P.P.B., Roumestand, C.C.R., Canova, M.M.C., Hurard, C.C.H., Molle, V.V.M., Cohen-Gonsaud, M.M.C.G.

Assembly

pOdhI

Entity

1. pOdhI (polymer, Thiol state: not present), 143 monomers, 15481.86 Da Detail

MSDNNGTPEP QVETXSVFRA DLLKEMESST GTAPASTGAE NLPAGSALLV VKRGPNAGAR FLLDQPTTTA GRHPESDIFL DDVTVSRRHA EFRINEGEFE VVDVGSLNGT YVNREPRNAQ VMQTGDEIQI GKFRLVFLAG PAE

Formula weight

15481.86 Da

Source organism

Corynebacterium glutamicum

Exptl. method

solution NMR

Refine. method

DGSA-distance geometry simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.3 %, Completeness: 84.6 %, Completeness (bb): 98.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	84.6 % (1320 of 1561)	93.4 % (755 of 808)	69.7 % (423 of 607)	97.3 % (142 of 146)
Backbone	98.6 % (822 of 834)	98.6 % (284 of 288)	98.3 % (406 of 413)	99.2 % (132 of 133)
Sidechain	72.4 % (620 of 856)	90.6 % (471 of 520)	43.0 % (139 of 323)	76.9 % (10 of 13)
Aromatic	46.5 % (40 of 86)	93.0 % (40 of 43)	0.0 % (0 of 43)
Methyl	65.4 % (102 of 156)	98.7 % (77 of 78)	32.1 % (25 of 78)

1. pOdhI

MSDNNGTPEP QVETXSVFRA DLLKEMESST GTAPASTGAE NLPAGSALLV VKRGPNAGAR FLLDQPTTTA GRHPESDIFL DDVTVSRRHA EFRINEGEFE VVDVGSLNGT YVNREPRNAQ VMQTGDEIQI GKFRLVFLAG PAE

Show sample condition

Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 293 K, pH 6.2

#	Name	Isotope labeling	Concentration
1	pOdhI	[U-100% 15N]	0.3 mM
2	H2O	natural abundance	95 %
3	D2O	natural abundance	5 %

Sample #2

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 293 K, pH 6.2

#	Name	Isotope labeling	Concentration
4	pOdhI	[U-100% 13C; U-100% 15N]	0.3 mM
5	H2O	natural abundance	95 %
6	D2O	natural abundance	5 %
7	NaCl	natural abundance	150 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: -0.22 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: -0.22 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: -0.07 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: 0.57 ppm, Outliers: 4 Detail

Protein Blocks Logo

Calculated from 30 models in PDB: 2KB3, Strand ID: A Detail

Release date

2009-04-28

Citation

Dynamic and structural characterization of a bacterial FHA protein reveals a new autoinhibition mechanism
Barthe, P., Roumestand, C., Canova, M.J., Kremer, L., Hurard, C., Molle, V., Cohen-Gonsaud, M.
Structure (2009), 17, 568-578, PubMed 19368890 , DOI 10.1016/j.str.2009.02.012 , Abstract

Related entities 1. pOdhI, : 1 : 4 : 12 entities Detail

Interaction partners 1. pOdhI, : 3 interactors Detail

More details for 3 interactors identified by 2 citations

Experiments performed 6 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_16038_2kb3.nef
Input source #2: Coordindates	2kb3.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	True (see coodinates for details)
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)

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:14:THR:C	1:15:TPO:N	unknown	unknown	n/a
1:15:TPO:C	1:16:SER:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	15	TPO	PHOSPHOTHREONINE	Assigned chemical shifts, Coordinates

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100
MSDNNGTPEPQVETXSVFRADLLKEMESSTGTAPASTGAENLPAGSALLVVKRGPNAGARFLLDQPTTTAGRHPESDIFLDDVTVSRRHAEFRINEGEFE
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MSDNNGTPEPQVETXSVFRADLLKEMESSTGTAPASTGAENLPAGSALLVVKRGPNAGARFLLDQPTTTAGRHPESDIFLDDVTVSRRHAEFRINEGEFE

-------110-------120-------130-------140---
VVDVGSLNGTYVNREPRNAQVMQTGDEIQIGKFRLVFLAGPAE
|||||||||||||||||||||||||||||||||||||||||||
VVDVGSLNGTYVNREPRNAQVMQTGDEIQIGKFRLVFLAGPAE

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	143	0	0	100.0

Content subtype: combined_16038_2kb3.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	2		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1321		100.0 (chain: A, length: 143)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	1342 (1)	undefined	94.4 (chain: A, length: 143)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	229 (229)	.	92.3 (chain: A, length: 143)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 143, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 408
  - ¹H chemical shifts: 763
  - ¹⁵N chemical shifts: 150
- Completeness of assignments
  - Entity_assemble_ID: A
- Peptide bond of PRO
- Tautomeric state of HIS
- 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)
89	HIS	HE2	10.78
89	HIS	NE2	168.35

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	611	408	66.8
¹H chemical shifts	812	762	93.8
¹⁵N chemical shifts	157	149	94.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	286	286	100.0
¹H chemical shifts	290	288	99.3
¹⁵N chemical shifts	134	133	99.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	325	122	37.5
¹H chemical shifts	522	474	90.8
¹⁵N chemical shifts	23	16	69.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	82	12	14.6
¹H chemical shifts	82	81	98.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	43	0	0.0
¹H chemical shifts	43	40	93.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: undefined
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 143, Sequence coverage: 94.4%
- Total number of restraints: 1342
- Weight of restraints: 1.0 (1342)
- Potential type of restraints: square-well-parabolic (1342)
- Range of distance target values: 2.05, 5.43 (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: 143, Sequence coverage: 92.3%
- Total number of restraints: 229
- Total number of restraints per polymer type: 229
- Weight of restraints: 1.0 (229)
- Potential type of restraints: square-well-parabolic (229)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords FHA, Forkhead-associated domain, GarA, Kinase substrate

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Found 1 Document (0.803 seconds)

BMRB: 16038

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. pOdhI, : 1 : 4 : 12 entities Detail

Interaction partners 1. pOdhI, : 3 interactors Detail

Experiments performed 6 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail