BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	96.3 % (926 of 962)	96.0 % (479 of 499)	96.2 % (354 of 368)	97.9 % (93 of 95)
Backbone	98.6 % (509 of 516)	98.9 % (181 of 183)	98.8 % (244 of 247)	97.7 % (84 of 86)
Sidechain	94.6 % (493 of 521)	94.6 % (299 of 316)	94.4 % (185 of 196)	100.0 % (9 of 9)
Aromatic	73.8 % (59 of 80)	75.0 % (30 of 40)	71.8 % (28 of 39)	100.0 % (1 of 1)
Methyl	100.0 % (78 of 78)	100.0 % (39 of 39)	100.0 % (39 of 39)

1. RNA-BINDING GLYCINE-RICH PROTEIN

GMAEVEYRCF VGGLAWATTD QTLGEAFSQF GEILDSKIIN DRETGRSRGF GFVTFKDEKA MRDAIEGMNG QDLDGRNITV NEAQSR

Show sample condition

Sample

Solvent system 10% water/90% D2O, Pressure 1.000 atm, Temperature 298.000 K, pH 7.000, Details 0.4 mM RRM domain

#	Name	Isotope labeling	Type	Concentration
1	RNA-BINDING GLYCINE-RICH PROTEIN	[U-13C; U-15N]		0.4 mM

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	indirect	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: -0.4 ppm, Outliers: 1 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	indirect	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: -0.4 ppm, Outliers: 1 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	indirect	1.0
¹⁵N	DSS	methyl protons	internal	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	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	indirect	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: -0.05 ppm, Outliers: 3 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 4C7Q, Strand ID: A Detail

Release date

2013-09-29

Citation

Structural basis of nucleic acid binding by Nicotiana tabacum glycine-rich RNA-binding protein: implications for its RNA chaperone function
Kahn, F., Boelens, R., Saqlan, S.M., van Ingen, H.
Nucleic Acids Res. (2014), 42, 8705-8718, PubMed 24957607 , DOI 10.1093/nar/gku468 , Abstract

Related entities 1. Solution structure of the Nt. GR-RBP1 RRM domain, : 1 : 356 entities Detail

Experiments performed 1 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_19525_4c7q.nef
Input source #2: Coordindates	4c7q.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

0--------10--------20--------30--------40--------50--------60--------70--------80-----
GMAEVEYRCFVGGLAWATTDQTLGEAFSQFGEILDSKIINDRETGRSRGFGFVTFKDEKAMRDAIEGMNGQDLDGRNITVNEAQSR
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GMAEVEYRCFVGGLAWATTDQTLGEAFSQFGEILDSKIINDRETGRSRGFGFVTFKDEKAMRDAIEGMNGQDLDGRNITVNEAQSR
--------10--------20--------30--------40--------50--------60--------70--------80------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	86	0	0	100.0

Content subtype: combined_19525_4c7q.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list	Warning	934		100.0 (chain: A, length: 86)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	1805 (1)	noe	97.7 (chain: A, length: 86)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	138 (138)	.	90.7 (chain: A, length: 86)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 86, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 479
  - ¹³C chemical shifts: 362
  - ¹⁵N chemical shifts: 93
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- 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	GLN	CD	180.247
28	GLN	CD	180.086
39	ASN	CG	174.704
68	ASN	CG	177.078
70	GLN	CD	180.515
76	ASN	CG	177.323
80	ASN	CG	175.681
83	GLN	CD	180.562

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	499	479	96.0
¹³C chemical shifts	368	354	96.2
¹⁵N chemical shifts	102	93	91.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	183	181	98.9
¹³C chemical shifts	172	169	98.3
¹⁵N chemical shifts	86	84	97.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	316	298	94.3
¹³C chemical shifts	196	185	94.4
¹⁵N chemical shifts	16	9	56.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	42	42	100.0
¹³C chemical shifts	42	42	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	40	29	72.5
¹³C chemical shifts	39	28	71.8
¹⁵N chemical shifts	1	1	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: 86, Sequence coverage: 97.7%
- Total number of restraints: 1800
- Weight of restraints: 1.0 (1800)
- Potential type of restraints: square-well-parabolic (1800)
- Range of distance target values: 1.34, 2.75 (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_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 86, Sequence coverage: 90.7%
- Total number of restraints: 138
- Total number of restraints per polymer type: 138
- Weight of restraints: 1.0 (138)
- Potential type of restraints: square-well-parabolic (138)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords RNA BINDING PROTEIN, RRM domain

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (0.649 seconds)

BMRB: 19525

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Solution structure of the Nt. GR-RBP1 RRM domain, : 1 : 356 entities Detail

Experiments performed 1 experiments Detail

Instrument

Sample

NMR combined restraints 4 contents Detail