BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	93.6 % (964 of 1030)	96.6 % (516 of 534)	89.4 % (362 of 405)	94.5 % (86 of 91)
Backbone	96.8 % (509 of 526)	97.8 % (176 of 180)	96.6 % (252 of 261)	95.3 % (81 of 85)
Sidechain	91.7 % (538 of 587)	96.0 % (340 of 354)	85.0 % (193 of 227)	83.3 % (5 of 6)
Aromatic	46.6 % (27 of 58)	82.8 % (24 of 29)	7.1 % (2 of 28)	100.0 % (1 of 1)
Methyl	95.9 % (117 of 122)	100.0 % (61 of 61)	91.8 % (56 of 61)

1. entity

QEDPWRHFAR THAIGQIVPG KVTKLVPFGA FVRVEEGIEG LVHISELAER HVEVPDQVVA VGDDAMVKVI DIDLERRRIS LSLKQANED

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Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.3

#	Name	Isotope labeling	Concentration
1	MtRpsA_S4	[U-100% 13C; U-100% 15N]	0.6 mM
2	H2O	natural abundance	90 %
3	D2O	natural abundance	10 %

Protein Blocks Logo

Calculated from 2 models in PDB: 5IE8, Strand ID: A Detail

Release date

2016-02-15

Citation

¹H, ¹⁵N, ¹³C resonance assignments for pyrazinoic acid binding domain of ribosomal protein S1 from Mycobacterium tuberculosis
Huang, B., Fu, J., Guo, C., Wu, X., Lin, D., Liao, X.
Biomol. NMR Assign. (2016), 10, 321-324, PubMed 27412769 , DOI 10.1007/s12104-016-9692-9 , Abstract

Related entities 1. MtRpsA S4, : 1 : 3 : 3 : 304 entities Detail

Experiments performed 1 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_26725_5ie8.nef
Input source #2: Coordindates	5ie8.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

280-----290-------300-------310-------320-------330-------340-------350-------360--------
QEDPWRHFARTHAIGQIVPGKVTKLVPFGAFVRVEEGIEGLVHISELAERHVEVPDQVVAVGDDAMVKVIDIDLERRRISLSLKQANED
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
QEDPWRHFARTHAIGQIVPGKVTKLVPFGAFVRVEEGIEGLVHISELAERHVEVPDQVVAVGDDAMVKVIDIDLERRRISLSLKQANED
--------10--------20--------30--------40--------50--------60--------70--------80---------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	89	0	0	100.0

Content subtype: combined_26725_5ie8.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1009		100.0 (chain: A, length: 89)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	1389 (1)	noe	100.0 (chain: A, length: 89)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	148 (148)	.	94.4 (chain: A, length: 89)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1

Status: Warning

Sequence coverage of experimental data

Entity_assembly_ID: A, Chain length: 89, Sequence coverage: 100.0%

280-----290-------300-------310-------320-------330-------340-------350-------360--------
QEDPWRHFARTHAIGQIVPGKVTKLVPFGAFVRVEEGIEGLVHISELAERHVEVPDQVVAVGDDAMVKVIDIDLERRRISLSLKQANED
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
QEDPWRHFARTHAIGQIVPGKVTKLVPFGAFVRVEEGIEGLVHISELAERHVEVPDQVVAVGDDAMVKVIDIDLERRRISLSLKQANED

Total number of assignments
- ¹H chemical shifts: 567
- ¹³C chemical shifts: 355
- ¹⁵N chemical shifts: 87

Completeness of assignments

Entity_assemble_ID: A

Excluded Atom_ID in statistics

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
281	GLU	HE2	4.813
282	ASP	HD2	4.136
285	ARG	HH12	8.633
285	ARG	HH11	8.569
286	HIS	HD1	7.931
289	ARG	HH11	7.204
290	THR	HG1	4.189
291	HIS	HD1	7.806
300	LYS	HZ1	8.936
300	LYS	HZ2	8.936
300	LYS	HZ3	8.936
302	THR	HG1	6.898
303	LYS	HZ1	9.333
303	LYS	HZ2	9.333
303	LYS	HZ3	9.333
312	ARG	HH11	8.205
312	ARG	HH22	8.705
312	ARG	HH21	7.674
314	GLU	HE2	3.1
315	GLU	HE2	4.811
322	HIS	HD1	8.595
322	HIS	HE2	8.027
322	HIS	ND1	124.084
324	SER	HG	4.434
325	GLU	HE2	7.134
328	GLU	HE2	4.811
329	ARG	HH12	8.965
329	ARG	HH11	8.851
329	ARG	HH21	8.134
329	ARG	HH22	8.425
330	HIS	HE2	7.88
332	GLU	HE2	0.801
335	ASP	HD2	7.652
343	ASP	HD2	5.194
347	LYS	HZ1	8.814
347	LYS	HZ2	8.814
347	LYS	HZ3	8.814
350	ASP	HD2	3.482
354	GLU	HE2	4.527
355	ARG	HH11	8.178
355	ARG	HH21	8.61
356	ARG	HH11	6.995
356	ARG	HH12	8.27
356	ARG	HH21	8.247
356	ARG	HH22	8.406
357	ARG	HH11	8.634
359	SER	HG	4.295
361	SER	HG	4.801
363	LYS	HZ1	7.363
363	LYS	HZ2	7.363
363	LYS	HZ3	7.363
367	GLU	HE2	4.744
368	ASP	HD2	5.194

All atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	534	514	96.3
¹³C chemical shifts	405	355	87.7
¹⁵N chemical shifts	98	86	87.8

Backbone atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	180	175	97.2
¹³C chemical shifts	178	168	94.4
¹⁵N chemical shifts	85	80	94.1

Side chain atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	354	339	95.8
¹³C chemical shifts	227	187	82.4
¹⁵N chemical shifts	13	6	46.2

Methyl group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	62	62	100.0
¹³C chemical shifts	62	57	91.9

Aromatic group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	29	24	82.8
¹³C chemical shifts	28	0	0.0
¹⁵N chemical shifts	1	1	100.0

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

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_3
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 89, Sequence coverage: 100.0%
- Total number of restraints: 1389
- Weight of restraints: 1.0 (1389)
- Potential type of restraints: square-well-parabolic (1389)
- Range of distance target values: 0.87, 6.08 (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_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 89, Sequence coverage: 94.4%
- Total number of restraints: 148
- Total number of restraints per polymer type: 148
- Weight of restraints: 1.0 (148)
- Potential type of restraints: square-well-parabolic (148)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

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BMRB: 26725

Sample

Related entities 1. MtRpsA S4, : 1 : 3 : 3 : 304 entities Detail

Experiments performed 1 experiments Detail

Instrument

Sample

NMR combined restraints 4 contents Detail