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Found 1 Document (0.71 seconds)

BMRB: 15320

2JR5

Solution structure of UPF0350 protein VC_2471: Northeast Structural Genomics Target VcR36

Authors

Wu, Y., Parish, D., Singarapu, K., Sukumaran, D., Eletski, A., Shastry, R., Nwosu, C., Maglaqui, M., Xiao, R., Liu, J., Baran, M.C., Swapna, G., Acton, T.B., Rost, B., Montelione, G.T., Szyperski, T.

Assembly

UPF0350 protein VC 2471

Entity

1. UPF0350 protein VC 2471 (polymer, Thiol state: all free), 94 monomers, 10919.34 Da Detail

MYTAEQKARI KWACRRGMLE LDVVIMPFFE ECFDSLTESE QDDFVALLES DDPDLFAWVM GHGRCENLGL AAMVDKIVAH NLSKVRLEHH HHHH

Formula weight

10919.34 Da

Source organism

Vibrio cholerae

Exptl. method

solution NMR

Refine. method

torsion angle dynamics, simulated annealing

Data set

assigned_chemical_shifts, spectral_peak_list

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 90.4 %, Completeness (bb): 85.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	90.4 % (994 of 1100)	98.2 % (557 of 567)	77.9 % (339 of 435)	100.0 % (98 of 98)
Backbone	85.4 % (478 of 560)	100.0 % (190 of 190)	70.5 % (196 of 278)	100.0 % (92 of 92)
Sidechain	96.2 % (606 of 630)	97.3 % (367 of 377)	94.3 % (233 of 247)	100.0 % (6 of 6)
Aromatic	92.1 % (105 of 114)	100.0 % (57 of 57)	83.6 % (46 of 55)	100.0 % (2 of 2)
Methyl	100.0 % (100 of 100)	100.0 % (50 of 50)	100.0 % (50 of 50)

1. UPF0350 protein VC 2471

MYTAEQKARI KWACRRGMLE LDVVIMPFFE ECFDSLTESE QDDFVALLES DDPDLFAWVM GHGRCENLGL AAMVDKIVAH NLSKVRLEHH HHHH

Show sample condition

Sample #1

Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]		1.2 mM

Sample #2

Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
2	entity	[U-5% 13C; U-100% 15N]		1.1 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: -0.52 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: -0.52 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: 0.07 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2JR5, Strand ID: A Detail

Release date

2007-08-14

Citation

Solution structure of UPF0350 protein VC_2471: Northeast Structural Genomics Target VcR36
Wu, Y., Parish, D., Singarapu, K., Sukumaran, D., Eletski, A., Shastry, R., Nwosu, C., Maglaqui, M., Xiao, R., Liu, J., Baran, M., Swapna, G., Rost, B., Montelione, G., Szyperski, T.

Related entities 1. UPF0350 protein VC 2471, : 1 : 1 : 28 entities Detail

Experiments performed 9 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_15320_2jr5.nef
Input source #2: Coordindates	2jr5.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----
MYTAEQKARIKWACRRGMLELDVVIMPFFEECFDSLTESEQDDFVALLESDDPDLFAWVMGHGRCENLGLAAMVDKIVAHNLSKVRLEHHHHHH
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MYTAEQKARIKWACRRGMLELDVVIMPFFEECFDSLTESEQDDFVALLESDDPDLFAWVMGHGRCENLGLAAMVDKIVAHNLSKVRLEHHHHHH

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_15320_2jr5.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	979		100.0 (chain: A, length: 94)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	1423 (1)	noe	93.6 (chain: A, length: 94)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	46 (1)	hbond	42.6 (chain: A, length: 94)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	184 (184)	.	90.4 (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: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 557
  - ¹³C chemical shifts: 324
  - ¹⁵N chemical shifts: 98
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- 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	567	556	98.1
¹³C chemical shifts	435	324	74.5
¹⁵N chemical shifts	103	98	95.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	190	189	99.5
¹³C chemical shifts	188	94	50.0
¹⁵N chemical shifts	92	92	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	377	367	97.3
¹³C chemical shifts	247	230	93.1
¹⁵N chemical shifts	11	6	54.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	55	50	90.9
¹³C chemical shifts	55	50	90.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	57	57	100.0
¹³C chemical shifts	55	43	78.2
¹⁵N chemical shifts	2	2	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: 93.6%
- Total number of restraints: 1423
- Weight of restraints: 1.0 (1423)
- Potential type of restraints: square-well-parabolic (1423)
- Range of distance target values: 2.07, 6.01 (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_3
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 94, Sequence coverage: 42.6%
  - Total number of restraints: 46
  - Weight of restraints: 1.0 (46)
  - Potential type of restraints: square-well-parabolic (46)
  - Range of distance target values: 2.05, 3.0 (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_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 94, Sequence coverage: 90.4%
- Total number of restraints: 184
- Total number of restraints per polymer type: 184
- Weight of restraints: 1.0 (184)
- Potential type of restraints: square-well-parabolic (184)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords NESG, NMR, UPF0350 protein VC_2471, solution structure

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Found 1 Document (0.71 seconds)

BMRB: 15320

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. UPF0350 protein VC 2471, : 1 : 1 : 28 entities Detail

Experiments performed 9 experiments Detail

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NMR combined restraints 5 contents Detail