BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	59.8 % (945 of 1579)	76.0 % (620 of 816)	31.7 % (196 of 619)	89.6 % (129 of 144)
Backbone	60.4 % (476 of 788)	96.7 % (266 of 275)	21.8 % (84 of 385)	98.4 % (126 of 128)
Sidechain	54.7 % (498 of 910)	65.4 % (354 of 541)	39.9 % (141 of 353)	18.8 % (3 of 16)
Aromatic	64.0 % (119 of 186)	64.5 % (60 of 93)	63.7 % (58 of 91)	50.0 % (1 of 2)
Methyl	85.6 % (125 of 146)	93.2 % (68 of 73)	78.1 % (57 of 73)

1. entity 1

EHPEFLKAGK EPGLQIWRVE KFDLVPVPTN LYGDFFTGDA YVILKTVQLR NGNLQYDLHY WLGNECSQDE SGAAAIFTVQ LDDYLNGRAV QHREVQGFES ATFLGYFKSG LKYKKGGVAS GFKHVVPNEV VVQ

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 (±0.01) atm, Temperature 298 (±0.1) K, pH 5.0 (±0.1), Details 0.65 mM 13C, 15N gelsolin domain 1, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	gelsolin domain 1	[U-13C; U-15N]	protein	0.65 (±0.1) mM
2	Acetate	natural abundance	buffer	10 mM
3	H2O	natural abundance	solvent	90 %
4	D2O	[U-2H]	solvent	10 %

Protein Blocks Logo

Calculated from 20 models in PDB: 5H3M, Strand ID: A Detail

Release date

2016-11-09

Citation

Structural Basis for pH-mediated Regulation of F-actin Severing by Gelsolin Domain 1
Fan, J.S., Goh, H., Ding, K., Xue, B., Robinson, R.C., Yang, D.
Sci. Rep. (2017), 7, 45230-45230, PubMed 28349924 , DOI 10.1038/srep45230 , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 36027 released on 2016-11-09
Title Solution structure of human Gelsolin protein domain 1 at pH 7.3

Related entities 1. Human Gelsolin protein domain 1, : 1 : 13 : 36 : 226 entities Detail

Interaction partners 1. Human Gelsolin protein domain 1, : 73 interactors Detail

More details for 73 interactors identified by 27 citations

Experiments performed 1 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_36026_5h3m.nef
Input source #2: Coordindates	5h3m.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
EHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFES
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
EHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFES

-------110-------120-------130---
ATFLGYFKSGLKYKKGGVASGFKHVVPNEVVVQ
|||||||||||||||||||||||||||||||||
ATFLGYFKSGLKYKKGGVASGFKHVVPNEVVVQ

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	133	0	0	100.0

Content subtype: combined_36026_5h3m.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	849		98.5 (chain: A, length: 133)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	1418 (1)	noe	99.2 (chain: A, length: 133)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	88 (1)	hbond	43.6 (chain: A, length: 133)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	173 (173)	.	88.7 (chain: A, length: 133)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 133, Sequence coverage: 98.5%
- Total number of assignments
  - ¹H chemical shifts: 608
  - ¹³C chemical shifts: 114
  - ¹⁵N chemical shifts: 127
- 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	816	608	74.5
¹³C chemical shifts	619	114	18.4
¹⁵N chemical shifts	148	127	85.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	275	265	96.4
¹³C chemical shifts	266	0	0.0
¹⁵N chemical shifts	128	125	97.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	541	343	63.4
¹³C chemical shifts	353	114	32.3
¹⁵N chemical shifts	20	2	10.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	73	67	91.8
¹³C chemical shifts	73	55	75.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	93	59	63.4
¹³C chemical shifts	91	56	61.5
¹⁵N chemical shifts	2	1	50.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 133, Sequence coverage: 99.2%
- Total number of restraints: 1418
- Weight of restraints: 1.0 (1418)
- Potential type of restraints: square-well-parabolic (1418)
- Range of distance target values: 2.35, 4.9 (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: 133, Sequence coverage: 43.6%
  - Total number of restraints: 88
  - Weight of restraints: 1.0 (88)
  - Potential type of restraints: square-well-parabolic (88)
  - Range of distance target values: 2.0, 2.75 (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_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 133, Sequence coverage: 88.7%
- Total number of restraints: 173
- Total number of restraints per polymer type: 173
- Weight of restraints: 1.0 (173)
- Potential type of restraints: square-well-parabolic (173)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords STRUCTURAL PROTEIN, gelsolin

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 (3.474 seconds)

BMRB: 36026

Sample

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. Human Gelsolin protein domain 1, : 1 : 13 : 36 : 226 entities Detail

Interaction partners 1. Human Gelsolin protein domain 1, : 73 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample

NMR combined restraints 5 contents Detail