BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	87.5 % (958 of 1095)	96.5 % (545 of 565)	72.5 % (303 of 418)	98.2 % (110 of 112)
Backbone	99.3 % (592 of 596)	98.6 % (208 of 211)	100.0 % (287 of 287)	99.0 % (97 of 98)
Sidechain	77.3 % (453 of 586)	95.2 % (337 of 354)	47.2 % (103 of 218)	92.9 % (13 of 14)
Aromatic	51.7 % (30 of 58)	96.6 % (28 of 29)	0.0 % (0 of 27)	100.0 % (2 of 2)
Methyl	61.9 % (73 of 118)	98.3 % (58 of 59)	25.4 % (15 of 59)

1. Rv0020c FHA

GHGSAGTSVT LQLDDGSGRT YQLREGSNII GRGQDAQFRL PDTGVSRRHL EIRWDGQVAL LADLNSTNGT TVNNAPVQEW QLADGDVIRL GHSEIIVRMH

Show sample condition

Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 293 (±0.1) K, pH 6.8 (±0.1), Details Rv0020c_FHA

#	Name	Isotope labeling	Type	Concentration
1	Rv0020c_FHA	[U-15N]		0.5 (±0.01) mM

Sample #2

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 293 (±0.1) K, pH 6.8 (±0.1), Details Rv0020c_FHA

#	Name	Isotope labeling	Type	Concentration
2	Rv0020c_FHA	[U-13C; U-15N]		0.5 (±0.01) 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: -0.31 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: -0.31 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: -0.15 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: 0.53 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 30 models in PDB: 2LC1, Strand ID: A Detail

Release date

2011-10-25

Citation

Structural insight into the Mycobacterium tuberculosis Rv0020c protein and its interaction with the PknB kinase
Roumestand, C., Leiba, J., Galophe, N., Margeat, E., Padilla, A., Bessin, Y., Barthe, P., Molle, V., Cohen-Gonsaud, M.
Structure (2011), 19, 1525-1534, PubMed 22000520 , DOI 10.1016/j.str.2011.07.011 , Abstract

Entries sharing articles BMRB: 1, Swiss-Prot: 2 entries Detail

  BMRB: 17585 released on 2011-10-25
    Title Rv0020c_Nter structure
  Swiss-Prot: P9WI81 released on 2014-04-16
    Title PKNB_MYCTU Entity Serine/threonine-protein kinase PknB
  Swiss-Prot: P71590 released on 2012-10-03
    Title FHAA_MYCTU Entity FHA domain-containing protein FhaA

Related entities 1. Rv0020c FHA, : 1 : 2 : 2 : 56 entities Detail

Interaction partners 1. Rv0020c FHA, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

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_17586_2lc1.nef
Input source #2: Coordindates	2lc1.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
GHGSAGTSVTLQLDDGSGRTYQLREGSNIIGRGQDAQFRLPDTGVSRRHLEIRWDGQVALLADLNSTNGTTVNNAPVQEWQLADGDVIRLGHSEIIVRMH
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GHGSAGTSVTLQLDDGSGRTYQLREGSNIIGRGQDAQFRLPDTGVSRRHLEIRWDGQVALLADLNSTNGTTVNNAPVQEWQLADGDVIRLGHSEIIVRMH

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	100	0	0	100.0

Content subtype: combined_17586_2lc1.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	954		100.0 (chain: A, length: 100)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	1714 (1)	noe	100.0 (chain: A, length: 100)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	64 (1)	hbond	42.0 (chain: A, length: 100)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	152 (152)	.	92.0 (chain: A, length: 100)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 100, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 553
  - ¹³C chemical shifts: 287
  - ¹⁵N chemical shifts: 114
- 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)
49	HIS	HE2	10.58
49	HIS	NE2	170.16
70	THR	HG1	7.103

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	565	550	97.3
¹³C chemical shifts	418	287	68.7
¹⁵N chemical shifts	121	113	93.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	211	209	99.1
¹³C chemical shifts	200	200	100.0
¹⁵N chemical shifts	98	97	99.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	354	341	96.3
¹³C chemical shifts	218	87	39.9
¹⁵N chemical shifts	23	16	69.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	60	60	100.0
¹³C chemical shifts	60	6	10.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	29	28	96.6
¹³C chemical shifts	27	0	0.0
¹⁵N chemical shifts	2	2	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_3
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 100, Sequence coverage: 100.0%
- Total number of restraints: 1714
- Weight of restraints: 1.0 (1714)
- Potential type of restraints: square-well-parabolic (1714)
- Range of distance target values: 2.21, 3.81 (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: CNS/XPLOR_distance_constraints_4
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 100, Sequence coverage: 42.0%
  - Total number of restraints: 64
  - Weight of restraints: 1.0 (64)
  - Potential type of restraints: square-well-parabolic (64)
  - Range of distance target values: 2.05, 2.55 (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_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 100, Sequence coverage: 92.0%
- Total number of restraints: 152
- Total number of restraints per polymer type: 152
- Weight of restraints: 1.0 (152)
- Potential type of restraints: square-well-parabolic (152)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords FhaA, PROTEIN

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BMRB: 17586

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 1, Swiss-Prot: 2 entries Detail

Related entities 1. Rv0020c FHA, : 1 : 2 : 2 : 56 entities Detail

Interaction partners 1. Rv0020c FHA, : 1 interactors Detail

Experiments performed 7 experiments Detail

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NMR combined restraints 5 contents Detail