BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	95.3 % (1510 of 1584)	96.0 % (793 of 826)	93.5 % (576 of 616)	99.3 % (141 of 142)
Backbone	98.7 % (762 of 772)	98.1 % (255 of 260)	99.0 % (380 of 384)	99.2 % (127 of 128)
Sidechain	93.1 % (873 of 938)	95.1 % (538 of 566)	89.7 % (321 of 358)	100.0 % (14 of 14)
Aromatic	62.9 % (88 of 140)	74.3 % (52 of 70)	49.3 % (33 of 67)	100.0 % (3 of 3)
Methyl	100.0 % (150 of 150)	100.0 % (75 of 75)	100.0 % (75 of 75)

1. Orf c02003 protein

MSISTSAEVY YEEAEEFLSK GDLVQACEKY YKAAEEAIKL LVIENNLKEI TNNVKNKGRW KSENLFKASK LLRSNNTEIP ILWKSAWTLH VEGFHELSLN EKEVKKLKED VRKLVIFAVN SLEHHHHHH

Show sample condition

Sample #1

Pressure 1 atm, Temperature 298 K, pH 4.5

#	Name	Isotope labeling	Type	Concentration
1	entity	natural abundance		1.1 mM

Sample #2

Pressure 1 atm, Temperature 298 K, pH 4.5

#	Name	Isotope labeling	Type	Concentration
2	entity	natural abundance		1.0 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: -0.2 ppm, Outliers: 1 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: -0.2 ppm, Outliers: 1 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: 0.01 ppm, Outliers: 1 Detail

LACS Plot; CO

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: -0.29 ppm, Outliers: 1 Detail

Protein Blocks Logo

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

Release date

2007-07-17

Citation

solution structure of NESG target SsR10, Orf c02003 protein
Wu, Y., Singarapu, K., Zhang, Q., Eletski, A., Xu, D., Sukumaran, D., Parish, D., Wang, D., Jiang, M., Cunningham, K., Maglaqui, M., Owens, L., Xiao, R., Liu, J., Baran, M., Swapna, G., Acton, T., Rost, B., Montelione, G., Szyperski, T.

Related entities 1. Orf c02003 protein, : 1 : 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_15265_2jpu.nef
Input source #2: Coordindates	2jpu.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-------100
MSISTSAEVYYEEAEEFLSKGDLVQACEKYYKAAEEAIKLLVIENNLKEITNNVKNKGRWKSENLFKASKLLRSNNTEIPILWKSAWTLHVEGFHELSLN
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MSISTSAEVYYEEAEEFLSKGDLVQACEKYYKAAEEAIKLLVIENNLKEITNNVKNKGRWKSENLFKASKLLRSNNTEIPILWKSAWTLHVEGFHELSLN

-------110-------120---------
EKEVKKLKEDVRKLVIFAVNSLEHHHHHH
|||||||||||||||||||||||||||||
EKEVKKLKEDVRKLVIFAVNSLEHHHHHH

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	129	0	0	100.0

Content subtype: combined_15265_2jpu.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1511		100.0 (chain: A, length: 129)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	2032 (1)	noe	96.1 (chain: A, length: 129)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	273 (273)	.	95.3 (chain: A, length: 129)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 129, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 574
  - ¹H chemical shifts: 796
  - ¹⁵N chemical shifts: 141
- 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 (%)
¹³C chemical shifts	616	574	93.2
¹H chemical shifts	826	796	96.4
¹⁵N chemical shifts	145	141	97.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	258	255	98.8
¹H chemical shifts	260	258	99.2
¹⁵N chemical shifts	128	127	99.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	358	319	89.1
¹H chemical shifts	566	538	95.1
¹⁵N chemical shifts	17	14	82.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	76	75	98.7
¹H chemical shifts	76	75	98.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	67	31	46.3
¹H chemical shifts	70	50	71.4
¹⁵N chemical shifts	3	3	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_3
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 129, Sequence coverage: 96.1%
- Total number of restraints: 2032
- Weight of restraints: 1.0 (2032)
- Potential type of restraints: square-well-parabolic (2032)
- Range of distance target values: 2.12, 5.47 (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: 129, Sequence coverage: 95.3%
- Total number of restraints: 273
- Total number of restraints per polymer type: 273
- Weight of restraints: 1.0 (273)
- Potential type of restraints: square-well-parabolic (273)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords NESG, NMR, solution structure

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BMRB: 15265

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Orf c02003 protein, : 1 : 1 : 2 entities Detail

Experiments performed 7 experiments Detail

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NMR combined restraints 4 contents Detail