BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	94.0 % (770 of 819)	94.8 % (402 of 424)	92.1 % (291 of 316)	97.5 % (77 of 79)
Backbone	96.7 % (406 of 420)	95.2 % (140 of 147)	97.5 % (198 of 203)	97.1 % (68 of 70)
Sidechain	92.2 % (426 of 462)	94.6 % (262 of 277)	88.1 % (155 of 176)	100.0 % (9 of 9)
Aromatic	76.3 % (58 of 76)	86.8 % (33 of 38)	64.9 % (24 of 37)	100.0 % (1 of 1)
Methyl	97.4 % (74 of 76)	100.0 % (38 of 38)	94.7 % (36 of 38)

1. cold shock-like protein [Rickettsia rickettsii str. 'Sheila Smith']

MATNIVGKVK WYNSTKNFGF IEQDNGGKDV FVHKSAVDAA GLHSLEEGQD VIFDLEEKQG KAYAVNLRIK

Show sample condition

Sample

Solvent system 90% H2O, 10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0, Details 1.50 mM Rr-Csp U-15N/13C pH 6.0 20mM sodium phosphate buffer, 50 mM sodium chloride

#	Name	Isotope labeling	Concentration
1	[U-100% 13C; U-100% 15N]	natural abundance	1.5 mM
2	sodium phosphate	natural abundance	20 mM
3	sodium chloride	natural abundance	50 mM
4	sodium azide	natural abundance	0.02 %
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: -0.92 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: -0.92 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: -0.03 ppm, Outliers: 1 Detail

LACS Plot; CO

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

Referencing offset: 0.38 ppm, Outliers: 4 Detail

Protein Blocks Logo

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

Release date

2012-06-04

Citation

Solution structure of the cold-shock-like protein from Rickettsia rickettsii
Gerarden, K.P., Fuchs, A.M., Koch, J.M., Mueller, M.M., Graupner, D.R., Frost, J.T., Heinen, C.D., Lackner, H.A., Schoeller, E.R., House, S.J., Peterson, P.G., Veldkamp, F.C.
Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. (2012), 68, 1284-1288, PubMed 23143233 , DOI 10.1107/S174430911203881X , Abstract

Related entities 1. R. rickettsii cold shock-like protein, : 1 : 1 : 1 : 178 entities Detail

Experiments performed 3 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_18442_2lss.nef
Input source #2: Coordindates	2lss.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
MATNIVGKVKWYNSTKNFGFIEQDNGGKDVFVHKSAVDAAGLHSLEEGQDVIFDLEEKQGKAYAVNLRIK
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MATNIVGKVKWYNSTKNFGFIEQDNGGKDVFVHKSAVDAAGLHSLEEGQDVIFDLEEKQGKAYAVNLRIK

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	70	0	0	100.0

Content subtype: combined_18442_2lss.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	783		98.6 (chain: A, length: 70)
1	Distance restraints	DYANA/DIANA_distance_constraints_3	OK	4418 (1)	noe	98.6 (chain: A, length: 70)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_2	OK	120 (120)	.	98.6 (chain: A, length: 70)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 70, Sequence coverage: 98.6%
- Total number of assignments
  - ¹H chemical shifts: 413
  - ¹³C chemical shifts: 293
  - ¹⁵N chemical shifts: 77
- Completeness of assignments
  - Entity_assemble_ID: A
- 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	424	413	97.4
¹³C chemical shifts	316	293	92.7
¹⁵N chemical shifts	80	77	96.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	147	144	98.0
¹³C chemical shifts	140	138	98.6
¹⁵N chemical shifts	70	68	97.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	277	269	97.1
¹³C chemical shifts	176	155	88.1
¹⁵N chemical shifts	10	9	90.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	39	38	97.4
¹³C chemical shifts	39	36	92.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	38	37	97.4
¹³C chemical shifts	37	24	64.9
¹⁵N chemical shifts	1	1	100.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_3
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 70, Sequence coverage: 98.6%
- Total number of restraints: 4246
- Weight of restraints: 1.0 (4246)
- Potential type of restraints: upper-bound-parabolic (4246)
- Range of distance target values: 2.4, 5.5 (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: DYANA/DIANA_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 70, Sequence coverage: 98.6%
- Total number of restraints: 120
- Total number of restraints per polymer type: 120
- Weight of restraints: 1.0 (120)
- Potential type of restraints: square-well-parabolic (120)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords cold shock-like protein, cold shock protein, CSD, Csp, rickettsii

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Found 1 Document (0.692 seconds)

BMRB: 18442

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. R. rickettsii cold shock-like protein, : 1 : 1 : 1 : 178 entities Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail