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Found 1 Document (0.631 seconds)

BMRB: 16795

2KVV

Solution NMR of Putative excisionase from Klebsiella pneumoniae, Northeast Structural Genomics Consortium Target Target KpR49

Authors

Liu, G., Hamilton, H., Xiao, R., Acton, T.B., Rost, B., Montelione, G.T.

Assembly

KpR49

Entity

1. KpR49 (polymer, Thiol state: not present), 78 monomers, 9287.415 Da Detail

MAQIIFNEEW MVEKALMVRT GLGARQIESY RQGAWIEGVH FKRVSPSGEK TLRGTTWYNY PEINKFIRDS LEHHHHHH

Formula weight

9287.415 Da

Source organism

Klebsiella pneumoniae

Exptl. method

solution NMR

Refine. method

molecular dynamics, simulated annealing, distance geometry, torsion angle dynamics

Data set

assigned_chemical_shifts, spectral_peak_list

Chem. Shift Complete

Sequence coverage: 94.9 %, Completeness: 84.7 %, Completeness (bb): 81.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	84.7 % (808 of 954)	91.6 % (456 of 498)	73.3 % (272 of 371)	94.1 % (80 of 85)
Backbone	81.5 % (378 of 464)	93.8 % (150 of 160)	68.4 % (156 of 228)	94.7 % (72 of 76)
Sidechain	88.6 % (498 of 562)	90.5 % (306 of 338)	85.6 % (184 of 215)	88.9 % (8 of 9)
Aromatic	66.1 % (78 of 118)	76.3 % (45 of 59)	55.4 % (31 of 56)	66.7 % (2 of 3)
Methyl	97.2 % (70 of 72)	97.2 % (35 of 36)	97.2 % (35 of 36)

1. KpR49

MAQIIFNEEW MVEKALMVRT GLGARQIESY RQGAWIEGVH FKRVSPSGEK TLRGTTWYNY PEINKFIRDS LEHHHHHH

Show sample condition

Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 0.7 mM [U-100% 13C; U-100% 15N]KpR49, 95% H2O/5% D2O

#	Name	Isotope labeling	Type	Concentration
1	KpR49	[U-100% 13C; U-100% 15N]		0.7 mM

Sample #2

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 0.8 mM [U-5% 13C; U-100% 15N]KpR49, 95% H2O/5% D2O

#	Name	Isotope labeling	Type	Concentration
2	KpR49	[U-10% 13C; U-100% 15N]		0.8 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: 0.15 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: 0.15 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: 0.02 ppm, Outliers: 2 Detail

Protein Blocks Logo

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

Release date

2010-04-25

Related entities 1. KpR49, : 1 : 2 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_16795_2kvv.nef
Input source #2: Coordindates	2kvv.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--------
MAQIIFNEEWMVEKALMVRTGLGARQIESYRQGAWIEGVHFKRVSPSGEKTLRGTTWYNYPEINKFIRDSLEHHHHHH
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MAQIIFNEEWMVEKALMVRTGLGARQIESYRQGAWIEGVHFKRVSPSGEKTLRGTTWYNYPEINKFIRDSLEHHHHHH

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	78	0	0	100.0

Content subtype: combined_16795_2kvv.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	776		92.3 (chain: A, length: 78)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	1687 (1)	noe	91.0 (chain: A, length: 78)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	86 (86)	.	69.2 (chain: A, length: 78)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 78, Sequence coverage: 92.3%
- Total number of assignments
  - ¹H chemical shifts: 448
  - ¹³C chemical shifts: 251
  - ¹⁵N chemical shifts: 77
- Completeness of assignments
  - Entity_assemble_ID: A
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
20	THR	HG1	4.36

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	498	447	89.8
¹³C chemical shifts	371	251	67.7
¹⁵N chemical shifts	91	77	84.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	160	146	91.2
¹³C chemical shifts	156	71	45.5
¹⁵N chemical shifts	76	69	90.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	338	301	89.1
¹³C chemical shifts	215	180	83.7
¹⁵N chemical shifts	15	8	53.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	39	37	94.9
¹³C chemical shifts	39	37	94.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	59	44	74.6
¹³C chemical shifts	56	30	53.6
¹⁵N chemical shifts	3	2	66.7

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_3
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 78, Sequence coverage: 91.0%
- Total number of restraints: 1687
- Weight of restraints: 1.0 (1687)
- Potential type of restraints: square-well-parabolic (1687)
- Range of distance target values: 2.11, 4.2 (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: 78, Sequence coverage: 69.2%
- Total number of restraints: 86
- Total number of restraints per polymer type: 86
- Weight of restraints: 1.0 (86)
- Potential type of restraints: square-well-parabolic (86)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords nesg, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG), PSI-2, Protein NMR, Protein Structure Initiative, Structural Genomics, Target KpR49

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Found 1 Document (0.631 seconds)

BMRB: 16795

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. KpR49, : 1 : 2 entities Detail

Experiments performed 7 experiments Detail

Instrument

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NMR combined restraints 4 contents Detail