BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	95.5 % (1085 of 1136)	95.4 % (559 of 586)	95.5 % (420 of 440)	96.4 % (106 of 110)
Backbone	96.6 % (564 of 584)	96.4 % (189 of 196)	96.9 % (283 of 292)	95.8 % (92 of 96)
Sidechain	94.8 % (614 of 648)	94.9 % (370 of 390)	94.3 % (230 of 244)	100.0 % (14 of 14)
Aromatic	84.6 % (66 of 78)	84.6 % (33 of 39)	83.3 % (30 of 36)	100.0 % (3 of 3)
Methyl	97.8 % (131 of 134)	98.5 % (66 of 67)	97.0 % (65 of 67)

1. PriC N-terminal domain

MKTALLLEKL EGQLATLRQR CAPVSQFATL SARFDRHLFQ TRATTLQACL DEAGDNLAAL RHAVEQQQLP QVAWLAEHLA AQLEAIAREA SAWSLREW

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	PriC N-terminal domain	[U-99% 13C; U-99% 15N]	protein	0.5 mM
2	sodium chloride	natural abundance		150 mM
3	H2O		solvent	90 %
4	D2O		solvent	10 %

LACS Plot; CA

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

Referencing offset: -0.1 ppm, Outliers: 3 Detail

LACS Plot; CB

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

Referencing offset: -0.1 ppm, Outliers: 3 Detail

LACS Plot; HA

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

Referencing offset: 0.03 ppm, Outliers: 1 Detail

LACS Plot; CO

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

Referencing offset: -0.32 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2RT6, Strand ID: A Detail

Release date

2013-08-04

Citation

Solution structure of the N-terminal domain of a replication restart primosome factor, PriC, in Escherichia coli
Aramaki, T., Abe, Y., Katayama, T., Ueda, T.
Protein Sci. (2013), 22, 1279-1286, PubMed 23868391 , DOI 10.1002/pro.2314 , Abstract

Related entities 1. PriC N-temrinal domain, : 1 : 2 : 3 entities Detail

Interaction partners 1. PriC N-temrinal domain, : 20 interactors Detail

More details for 20 interactors identified by 3 citations

Experiments performed 18 experiments Detail

1 2D 1H-15N HSQC

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	PriC N-terminal domain	[U-99% 13C; U-99% 15N]	protein	0.5 mM
2	sodium chloride	natural abundance		150 mM
3	H2O		solvent	90 %
4	D2O		solvent	10 %

2 2D 1H-15N HSQC

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
5	PriC N-terminal domain	[U-98% 15N]	protein	0.2 mM
6	sodium chloride	natural abundance		150 mM
7	D2O		solvent	100 %

3 2D 1H-13C HSQC aliphatic

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	PriC N-terminal domain	[U-99% 13C; U-99% 15N]	protein	0.5 mM
2	sodium chloride	natural abundance		150 mM
3	H2O		solvent	90 %
4	D2O		solvent	10 %

4 2D 1H-13C HSQC aromatic

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	PriC N-terminal domain	[U-99% 13C; U-99% 15N]	protein	0.5 mM
2	sodium chloride	natural abundance		150 mM
3	H2O		solvent	90 %
4	D2O		solvent	10 %

5 3D CBCA(CO)NH

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	PriC N-terminal domain	[U-99% 13C; U-99% 15N]	protein	0.5 mM
2	sodium chloride	natural abundance		150 mM
3	H2O		solvent	90 %
4	D2O		solvent	10 %

6 3D C(CO)NH

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	PriC N-terminal domain	[U-99% 13C; U-99% 15N]	protein	0.5 mM
2	sodium chloride	natural abundance		150 mM
3	H2O		solvent	90 %
4	D2O		solvent	10 %

7 3D HNCO

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	PriC N-terminal domain	[U-99% 13C; U-99% 15N]	protein	0.5 mM
2	sodium chloride	natural abundance		150 mM
3	H2O		solvent	90 %
4	D2O		solvent	10 %

8 3D HNCA

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	PriC N-terminal domain	[U-99% 13C; U-99% 15N]	protein	0.5 mM
2	sodium chloride	natural abundance		150 mM
3	H2O		solvent	90 %
4	D2O		solvent	10 %

9 3D HNCACB

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	PriC N-terminal domain	[U-99% 13C; U-99% 15N]	protein	0.5 mM
2	sodium chloride	natural abundance		150 mM
3	H2O		solvent	90 %
4	D2O		solvent	10 %

10 3D HBHA(CO)NH

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	PriC N-terminal domain	[U-99% 13C; U-99% 15N]	protein	0.5 mM
2	sodium chloride	natural abundance		150 mM
3	H2O		solvent	90 %
4	D2O		solvent	10 %

11 3D HN(CO)CA

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	PriC N-terminal domain	[U-99% 13C; U-99% 15N]	protein	0.5 mM
2	sodium chloride	natural abundance		150 mM
3	H2O		solvent	90 %
4	D2O		solvent	10 %

12 3D H(CCO)NH

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	PriC N-terminal domain	[U-99% 13C; U-99% 15N]	protein	0.5 mM
2	sodium chloride	natural abundance		150 mM
3	H2O		solvent	90 %
4	D2O		solvent	10 %

13 3D HCCH-TOCSY

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	PriC N-terminal domain	[U-99% 13C; U-99% 15N]	protein	0.5 mM
2	sodium chloride	natural abundance		150 mM
3	H2O		solvent	90 %
4	D2O		solvent	10 %

14 3D 1H-15N NOESY

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	PriC N-terminal domain	[U-99% 13C; U-99% 15N]	protein	0.5 mM
2	sodium chloride	natural abundance		150 mM
3	H2O		solvent	90 %
4	D2O		solvent	10 %

15 3D 1H-15N TOCSY

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	PriC N-terminal domain	[U-99% 13C; U-99% 15N]	protein	0.5 mM
2	sodium chloride	natural abundance		150 mM
3	H2O		solvent	90 %
4	D2O		solvent	10 %

16 3D 1H-13C NOESY aliphatic

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	PriC N-terminal domain	[U-99% 13C; U-99% 15N]	protein	0.5 mM
2	sodium chloride	natural abundance		150 mM
3	H2O		solvent	90 %
4	D2O		solvent	10 %

17 3D 1H-13C NOESY aromatic

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	PriC N-terminal domain	[U-99% 13C; U-99% 15N]	protein	0.5 mM
2	sodium chloride	natural abundance		150 mM
3	H2O		solvent	90 %
4	D2O		solvent	10 %

18 3D HCCH-COSY

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	PriC N-terminal domain	[U-99% 13C; U-99% 15N]	protein	0.5 mM
2	sodium chloride	natural abundance		150 mM
3	H2O		solvent	90 %
4	D2O		solvent	10 %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_11525_2rt6.nef
Input source #2: Coordindates	2rt6.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--------
MKTALLLEKLEGQLATLRQRCAPVSQFATLSARFDRHLFQTRATTLQACLDEAGDNLAALRHAVEQQQLPQVAWLAEHLAAQLEAIAREASAWSLREW
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MKTALLLEKLEGQLATLRQRCAPVSQFATLSARFDRHLFQTRATTLQACLDEAGDNLAALRHAVEQQQLPQVAWLAEHLAAQLEAIAREASAWSLREW

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	98	0	0	100.0

Content subtype: combined_11525_2rt6.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1097		99.0 (chain: A, length: 98)
1	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	1310 (1)	noe	99.0 (chain: A, length: 98)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	92 (1)	hbond	60.2 (chain: A, length: 98)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	174 (174)	.	94.9 (chain: A, length: 98)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 98, Sequence coverage: 99.0%
- Total number of assignments
  - ¹H chemical shifts: 562
  - ¹³C chemical shifts: 423
  - ¹⁵N chemical shifts: 112
- 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	586	562	95.9
¹³C chemical shifts	440	423	96.1
¹⁵N chemical shifts	118	112	94.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	196	191	97.4
¹³C chemical shifts	196	192	98.0
¹⁵N chemical shifts	96	93	96.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	390	371	95.1
¹³C chemical shifts	244	231	94.7
¹⁵N chemical shifts	22	19	86.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	68	67	98.5
¹³C chemical shifts	68	66	97.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	39	33	84.6
¹³C chemical shifts	36	30	83.3
¹⁵N chemical shifts	3	3	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_4
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 98, Sequence coverage: 99.0%
- Total number of restraints: 1298
- Weight of restraints: 1.0 (1298)
- Potential type of restraints: square-well-parabolic (1298)
- Range of distance target values: 2.45, 4.15 (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: 98, Sequence coverage: 60.2%
  - Total number of restraints: 92
  - Weight of restraints: 1.0 (92)
  - Potential type of restraints: square-well-parabolic (92)
  - Range of distance target values: 2.0, 2.95 (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: 98, Sequence coverage: 94.9%
- Total number of restraints: 174
- Total number of restraints per polymer type: 174
- Weight of restraints: 1.0 (174)
- Potential type of restraints: square-well-parabolic (174)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords PriC, Primosome, Protein structure, Replication restart

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Link destinations for BMRB, PDB and EMDB

Found 1 Document (0.807 seconds)

BMRB: 11525

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. PriC N-temrinal domain, : 1 : 2 : 3 entities Detail

Interaction partners 1. PriC N-temrinal domain, : 20 interactors Detail

Experiments performed 18 experiments Detail

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NMR combined restraints 5 contents Detail