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Found 1 Document (0.624 seconds)

BMRB: 16557

2KPJ

Solution Structure Of Protein SOS-response transcriptional repressor, LexA From Eubacterium rectale. Northeast Structural Genomics Consortium Target ErR9A

Authors

Wu, Y., Eletsky, A., Lee, D., Ghosh, A., Buchwald, W., Zhang, Q., Janjua, H., Garcia, E., Nair, R., Sukumaran, D., Rost, B., Acton, T., Xiao, R., Everett, J., Montelione, G., Szyperski, T.

Assembly

ErR9A

Entity

1. ErR9A (polymer, Thiol state: all free), 94 monomers, 10705.09 Da Detail

MVKDKQKAIF SENLNSYIAK SEKTQLEIAK SIGVSPQTFN TWCKGIAIPR MGKVQALADY FNINKSDLIE DKKLNIDTVP IESGYTLEHH HHHH

Formula weight

10705.09 Da

Source organism

Escherichia coli

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts, spectral_peak_list

Chem. Shift Complete

Sequence coverage: 89.4 %, Completeness: 80.3 %, Completeness (bb): 75.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	80.3 % (907 of 1129)	88.1 % (519 of 589)	67.8 % (297 of 438)	89.2 % (91 of 102)
Backbone	75.1 % (419 of 558)	88.9 % (168 of 189)	61.5 % (171 of 278)	87.9 % (80 of 91)
Sidechain	85.9 % (568 of 661)	87.7 % (351 of 400)	82.4 % (206 of 250)	100.0 % (11 of 11)
Aromatic	60.0 % (54 of 90)	73.3 % (33 of 45)	45.5 % (20 of 44)	100.0 % (1 of 1)
Methyl	96.1 % (98 of 102)	96.1 % (49 of 51)	96.1 % (49 of 51)

1. ErR9A

MVKDKQKAIF SENLNSYIAK SEKTQLEIAK SIGVSPQTFN TWCKGIAIPR MGKVQALADY FNINKSDLIE DKKLNIDTVP IESGYTLEHH HHHH

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	entity	[U-100% 13C; U-100% 15N]	1.0 mM
2	H2O	natural abundance	90 %
3	D2O	natural abundance	10 %

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Concentration
4	entity	[U-5% 13C; U-100% 15N]	1.0 mM
5	H2O	natural abundance	90 %
6	D2O	natural abundance	10 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.09 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.09 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.0 ppm, Outliers: 1 Detail

Protein Blocks Logo

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

Release date

2009-11-17

Citation

Solution Structure Of Protein SOS-response transcriptional repressor, LexA From Eubacterium rectale. Northeast Structural Genomics Consortium Target ErR9A
Wu, Y., Eletsky, A., Lee, D., Ghosh, A., Buchwald, W., Zhang, Q., Janjua, H., Garcia, E., Nair, R., Sukumaran, D., Rost, B., Acton, T., Everett, J., Montelione, G., Szyperski, T.
Not known

Related entities 1. ErR9A, : 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_16557_2kpj.nef
Input source #2: Coordindates	2kpj.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----
MVKDKQKAIFSENLNSYIAKSEKTQLEIAKSIGVSPQTFNTWCKGIAIPRMGKVQALADYFNINKSDLIEDKKLNIDTVPIESGYTLEHHHHHH
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MVKDKQKAIFSENLNSYIAKSEKTQLEIAKSIGVSPQTFNTWCKGIAIPRMGKVQALADYFNINKSDLIEDKKLNIDTVPIESGYTLEHHHHHH

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	94	0	0	100.0

Content subtype: combined_16557_2kpj.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	885		88.3 (chain: A, length: 94)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	1215 (1)	noe	86.2 (chain: A, length: 94)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	195 (195)	.	93.6 (chain: A, length: 94)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 94, Sequence coverage: 88.3%
- Total number of assignments
  - ¹H chemical shifts: 511
  - ¹³C chemical shifts: 285
  - ¹⁵N chemical shifts: 89
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- 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	589	511	86.8
¹³C chemical shifts	438	285	65.1
¹⁵N chemical shifts	103	89	86.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	189	165	87.3
¹³C chemical shifts	188	83	44.1
¹⁵N chemical shifts	91	78	85.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	400	346	86.5
¹³C chemical shifts	250	202	80.8
¹⁵N chemical shifts	12	11	91.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	53	48	90.6
¹³C chemical shifts	53	48	90.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	45	33	73.3
¹³C chemical shifts	44	20	45.5
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: 94, Sequence coverage: 86.2%
- Total number of restraints: 1215
- Weight of restraints: 1.0 (1215)
- Potential type of restraints: square-well-parabolic (1215)
- Range of distance target values: 2.12, 6.03 (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: 94, Sequence coverage: 93.6%
- Total number of restraints: 195
- Total number of restraints per polymer type: 195
- Weight of restraints: 1.0 (195)
- Potential type of restraints: square-well-parabolic (195)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

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Found 1 Document (0.624 seconds)

BMRB: 16557

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. ErR9A, : 1 : 3 entities Detail

Experiments performed 7 experiments Detail

Instrument

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NMR combined restraints 4 contents Detail