BMRBj - BMREntryMaster

	Total	¹H
All	87.3 % (172 of 197)	87.3 % (172 of 197)
Backbone	94.2 % (65 of 69)	94.2 % (65 of 69)
Sidechain	83.6 % (107 of 128)	83.6 % (107 of 128)
Aromatic	86.7 % (13 of 15)	86.7 % (13 of 15)
Methyl	72.7 % (8 of 11)	72.7 % (8 of 11)

1. (R7G)-Crp4

GLLCYCGKGH CKRGERVRGT CGIRFLYCCP RR

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Temperature 298 K, pH 4

#	Name	Isotope labeling	Concentration
1	(R7G)-Crp4	natural abundance	1 mg
2	H2O	natural abundance	90 %
3	D2O	natural abundance	10 %

Protein Blocks Logo

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

Release date

2012-05-08

Citation

The α-defensin salt-bridge induces backbone stability to facilitate folding and confer proteolytic resistance
Andersson, H.S., Figueredo, S.M., Haugaard-Kedstrom, L.M., Bengtsson, E., Daly, N.L., Qu, X., Craik, D.J., Ouellette, A.J., Rosengren, K.
Amino Acids (2012), 43, 1471-1483, PubMed 22286872 , DOI 10.1007/s00726-012-1220-3 , Abstract

Related entities 1. (R7G)-Crp4, : 1 : 7 : 36 entities Detail

Experiments performed 3 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_17733_2ley.nef
Input source #2: Coordindates	2ley.cif
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
A:4:CYS:SG	A:29:CYS:SG	unknown	unknown	2.031
A:6:CYS:SG	A:21:CYS:SG	unknown	unknown	2.032
A:11:CYS:SG	A:28:CYS:SG	unknown	unknown	2.028

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--
GLLCYCGKGHCKRGERVRGTCGIRFLYCCPRR
||||||||||||||||||||||||||||||||
GLLCYCGKGHCKRGERVRGTCGIRFLYCCPRR

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	32	0	0	100.0

Content subtype: combined_17733_2ley.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	3		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	172		96.9 (chain: A, length: 32)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	187 (1)	noe	96.9 (chain: A, length: 32)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	28 (1)	hbond	50.0 (chain: A, length: 32)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	31 (31)	.	93.8 (chain: A, length: 32)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 32, Sequence coverage: 96.9%
- Total number of assignments
  - ¹H chemical shifts: 172
- Completeness of assignments
  - Entity_assemble_ID: A
- 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	197	172	87.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	69	65	94.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	128	107	83.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	11	8	72.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	15	13	86.7

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 32, Sequence coverage: 96.9%
- Total number of restraints: 187
- Weight of restraints: 1.0 (187)
- Potential type of restraints: square-well-parabolic (187)
- Range of distance target values: 2.1, 5.16 (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_4
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 32, Sequence coverage: 50.0%
  - Total number of restraints: 28
  - Weight of restraints: 1.0 (28)
  - Potential type of restraints: square-well-parabolic (28)
  - Range of distance target values: 1.9, 2.4 (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_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 32, Sequence coverage: 93.8%
- Total number of restraints: 31
- Total number of restraints per polymer type: 31
- Weight of restraints: 1.0 (31)
- Potential type of restraints: square-well-parabolic (31)
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords cryptdin-4, peptide

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 (0.587 seconds)

BMRB: 17733

Sample

Related entities 1. (R7G)-Crp4, : 1 : 7 : 36 entities Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail