BMRBj - BMREntryMaster

Found 1 Document (1.081 seconds)

BMRB: 15778

2K3U

Structure of the tyrosine-O-sulfated C5a receptor N-terminus in complex with the immune evasive protein CHIPS.

Authors

Ippel, J.H., Bunschoten, A., Kemmink, J., Liskamp, R.

Assembly

CHIPS-C5aR(P7-28S)

Entity

1. CHIPS protein (polymer, Thiol state: not present), 91 monomers, 10459.83 Da Detail

NSGLPTTLGK LDERLRNYLK KGTKNSAQFE KMVILTENKG YYTVYLNTPL AEDRKNVELL GKMYKTYFFK KGESKSSYVI NGPGKTNEYA Y

2. C5aR(P7-28S) peptide (polymer, Thiol state: not present), 24 monomers, 2707.788 Da Detail

XTTPDXGHXD DKDTLDLNTP VDKX

Total weight

13167.618 Da

Max. entity weight

10459.83 Da

Exptl. method

solution NMR

Refine. method

simulated annealing, torsion angle dynamics, simulated annealing docking, molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 96.5 %, Completeness: 88.3 %, Completeness (bb): 86.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	88.3 % (1169 of 1324)	96.8 % (672 of 694)	78.0 % (401 of 514)	82.8 % (96 of 116)
Backbone	86.1 % (565 of 656)	96.9 % (219 of 226)	79.9 % (259 of 324)	82.1 % (87 of 106)
Sidechain	89.0 % (685 of 770)	96.8 % (453 of 468)	76.4 % (223 of 292)	90.0 % (9 of 10)
Aromatic	73.6 % (78 of 106)	90.6 % (48 of 53)	56.6 % (30 of 53)
Methyl	90.6 % (96 of 106)	100.0 % (53 of 53)	81.1 % (43 of 53)

1. CHIPS protein

NSGLPTTLGK LDERLRNYLK KGTKNSAQFE KMVILTENKG YYTVYLNTPL AEDRKNVELL GKMYKTYFFK KGESKSSYVI NGPGKTNEYA Y

2. C5aR(P7-28S) peptide

XTTPDXGHXD DKDTLDLNTP VDKX

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 6.5 (±0.1), Details Titrated 1:1 complex of uniformly [15N]-labelled CHIPS and unlabelled peptide C5aR(P7-28S). pH of the sample is buffered at pH 6.5.

#	Name	Isotope labeling	Concentration
1	entity_1	[U-99% 15N]	0.5 mM
2	entity_2	natural abundance	0.5 mM
3	sodium phosphate	natural abundance	20 mM
4	sodium azide	natural abundance	0.1 %
5	H2O	natural abundance	90 %
6	D2O	natural abundance	10 %

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 6.5 (±0.1), Details Titrated 1:1 complex of uniformly labelled [13C,15N] CHIPS and unlabelled C5aR(P7-28S) peptide. pH of the sample is buffered at 6.5.

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

Protein Blocks Logo

Calculated from 25 models in PDB: 2K3U, Strand ID: A, B Detail

Release date

2009-04-02

Citation

Structure of the tyrosine-sulfated C5a receptor N terminus in complex with chemotaxis inhibitory protein of Staphylococcus aureus
Ippel, J.H., de Haas, C.J.C., Bunschoten, A., van Strijp, J.A.G., Kruijtzer, J.A.W., Liskamp, R.M.J., Kemmink, J.
J. Biol. Chem. (2009), 284, 12363-12372, PubMed 19251703 , DOI 10.1074/jbc.M808179200 , Abstract

Related entities 1. CHIPS protein, : 3 : 1 entities Detail

Related entities 2. C5aR(P7-28S) peptide, : 1 entities Detail

Experiments performed 27 experiments Detail

1 2D 1H-15N HSQC

Instrument

Varian INOVA - 600 MHz triple [1H,13C,15N] probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 6.5 (±0.1), Details Titrated 1:1 complex of uniformly [15N]-labelled CHIPS and unlabelled peptide C5aR(P7-28S). pH of the sample is buffered at pH 6.5.

#	Name	Isotope labeling	Concentration
1	entity_1	[U-99% 15N]	0.5 mM
2	entity_2	natural abundance	0.5 mM
3	sodium phosphate	natural abundance	20 mM
4	sodium azide	natural abundance	0.1 %
5	H2O	natural abundance	90 %
6	D2O	natural abundance	10 %

2 2D 1H-15N HSQC

Instrument

Varian INOVA - 500 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
1	entity_1	[U-99% 15N]	0.5 mM
2	entity_2	natural abundance	0.5 mM
3	sodium phosphate	natural abundance	20 mM
4	sodium azide	natural abundance	0.1 %
5	H2O	natural abundance	90 %
6	D2O	natural abundance	10 %

3 2D 1H-15N HSQC

Instrument

Bruker Avance - 900 MHz triple [1H,13C,15N] cryogenic probe

Sample

#	Name	Isotope labeling	Concentration
1	entity_1	[U-99% 15N]	0.5 mM
2	entity_2	natural abundance	0.5 mM
3	sodium phosphate	natural abundance	20 mM
4	sodium azide	natural abundance	0.1 %
5	H2O	natural abundance	90 %
6	D2O	natural abundance	10 %

4 2D 1H-13C HSQC

Instrument

Varian INOVA - 600 MHz triple [1H,13C,15N] probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 6.5 (±0.1), Details Titrated 1:1 complex of uniformly labelled [13C,15N] CHIPS and unlabelled C5aR(P7-28S) peptide. pH of the sample is buffered at 6.5.

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

5 2D 1H-13C HSQC

Instrument

Varian INOVA - 500 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

6 2D 1H-13C HSQC

Instrument

Bruker Avance - 900 MHz triple [1H,13C,15N] cryogenic probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

7 3D CBCA(CO)NH

Instrument

Varian INOVA - 600 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

8 3D HNCACB

Instrument

Varian INOVA - 600 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

9 3D HNCO

Instrument

Varian INOVA - 600 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

10 3D HBHACBCA(CO)NH

Instrument

Varian INOVA - 600 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

11 3D HCCH-TOCSY

Instrument

Varian INOVA - 600 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

12 3D HCCH-TOCSY

Instrument

Varian INOVA - 500 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

13 3D 1H-15N NOESY

Instrument

Varian INOVA - 500 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
1	entity_1	[U-99% 15N]	0.5 mM
2	entity_2	natural abundance	0.5 mM
3	sodium phosphate	natural abundance	20 mM
4	sodium azide	natural abundance	0.1 %
5	H2O	natural abundance	90 %
6	D2O	natural abundance	10 %

14 3D 1H-15N NOESY

Instrument

Varian INOVA - 600 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

15 3D 1H-15N TOCSY

Instrument

Varian INOVA - 500 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
1	entity_1	[U-99% 15N]	0.5 mM
2	entity_2	natural abundance	0.5 mM
3	sodium phosphate	natural abundance	20 mM
4	sodium azide	natural abundance	0.1 %
5	H2O	natural abundance	90 %
6	D2O	natural abundance	10 %

16 3D 1H-13C NOESY

Instrument

Varian INOVA - 600 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

17 3D 1H-13C NOESY

Instrument

Bruker Avance - 900 MHz triple [1H,13C,15N] cryogenic probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

18 2D 1H-1H NOESY

Instrument

Bruker Avance - 900 MHz triple [1H,13C,15N] cryogenic probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

19 2D 1H-1H TOCSY

Instrument

Bruker Avance - 900 MHz triple [1H,13C,15N] cryogenic probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

20 3D COCA(HN)

Instrument

Varian INOVA - 600 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

21 3D-CNH-NOESY

Instrument

Varian INOVA - 500 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

22 2D-HBHD aromatic

Instrument

Varian INOVA - 600 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

23 2D-HBHE aromatic

Instrument

Varian INOVA - 600 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

24 2D-CBHD aromatic

Instrument

Varian INOVA - 600 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

25 2D-CBHE aromatic

Instrument

Varian INOVA - 600 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

26 3D HNHA

Instrument

Varian INOVA - 500 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

27 3D HNHB

Instrument

Varian INOVA - 500 MHz triple [1H,13C,15N] probe

Sample

#	Name	Isotope labeling	Concentration
7	entity_1	[U-99% 13C; U-99% 15N]	1.0 mM
8	entity_2	natural abundance	1.0 mM
9	sodium phosphate	natural abundance	20 mM
10	sodium azide	natural abundance	0.1 %
11	H2O	natural abundance	90 %
12	D2O	natural abundance	10 %

NMR combined restraints 6 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_15778_2k3u.nef
Input source #2: Coordindates	2k3u.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	True (see coodinates for details)
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)

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
2:1:ACE:C	2:2:THR:N	unknown	unknown	n/a
2:5:ASP:C	2:6:TYS:N	unknown	unknown	n/a
2:6:TYS:C	2:7:GLY:N	unknown	unknown	n/a
2:8:HIS:C	2:9:TYS:N	unknown	unknown	n/a
2:9:TYS:C	2:10:ASP:N	unknown	unknown	n/a
2:23:LYS:C	2:24:NH2:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
B	6	ACE	ACETYL GROUP	Coordinates
B	11	TYS	O-SULFO-L-TYROSINE	Assigned chemical shifts, Distance restraints, Coordinates
B	14	TYS	O-SULFO-L-TYROSINE	Assigned chemical shifts, Distance restraints, Coordinates
B	29	NH2	AMINO GROUP	Coordinates

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------40--------50--------60--------70--------80--------90-------100-------110-------120-
NSGLPTTLGKLDERLRNYLKKGTKNSAQFEKMVILTENKGYYTVYLNTPLAEDRKNVELLGKMYKTYFFKKGESKSSYVINGPGKTNEYAY
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NSGLPTTLGKLDERLRNYLKKGTKNSAQFEKMVILTENKGYYTVYLNTPLAEDRKNVELLGKMYKTYFFKKGESKSSYVINGPGKTNEYAY
--------10--------20--------30--------40--------50--------60--------70--------80--------90-

Entity_assembly_ID (NMR): B vs Auth_asym_ID (model): B

---10--------20---------
XTTPDXGHXDDKDTLDLNTPVDKX
||||||||||||||||||||||||
XTTPDXGHXDDKDTLDLNTPVDKX
--------10--------20----

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	91	0	0	100.0
B	B	24	0	0	100.0

Content subtype: combined_15778_2k3u.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	6		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1229		100.0 (chain: A, length: 91), 75.0 (chain: B, length: 24)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	3708 (1)	noe	98.9 (chain: A, length: 91), 91.7 (chain: B, length: 24)
2	Distance restraints	CNS/XPLOR_distance_constraints_5	Warning	887 (1)	noe	36.3 (chain: A, length: 91), 66.7 (chain: B, length: 24)
3	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	32 (1)	hbond	20.9 (chain: A, length: 91), 12.5 (chain: B, length: 24)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	Warning	123 (123)	.	83.5 (chain: A, length: 91), 16.7 (chain: B, length: 24)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1

Status: Warning

Sequence coverage of experimental data

Entity_assembly_ID: A, Chain length: 91, Sequence coverage: 100.0%

--------40--------50--------60--------70--------80--------90-------100-------110-------120-
NSGLPTTLGKLDERLRNYLKKGTKNSAQFEKMVILTENKGYYTVYLNTPLAEDRKNVELLGKMYKTYFFKKGESKSSYVINGPGKTNEYAY
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NSGLPTTLGKLDERLRNYLKKGTKNSAQFEKMVILTENKGYYTVYLNTPLAEDRKNVELLGKMYKTYFFKKGESKSSYVINGPGKTNEYAY

Entity_assembly_ID: B, Chain length: 24, Sequence coverage: 75.0%

Total number of assignments
- ¹H chemical shifts: 711
- ¹³C chemical shifts: 416
- ¹⁵N chemical shifts: 102

Completeness of assignments

Entity_assemble_ID: A

Excluded Atom_ID in statistics

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
31	ASN	CG	176.954
44	ARG	HH21	6.742
44	ARG	NH2	71.802
46	ARG	HH11	6.587
46	ARG	HH21	6.229
46	ARG	NH2	71.535
46	ARG	NH1	70.2
47	ASN	CG	176.045
53	THR	HG1	3.62
55	ASN	CG	177.634
58	GLN	CD	179.597
68	ASN	CG	178.146
77	ASN	CG	177.423
84	ARG	HH21	6.681
84	ARG	NH2	69.95
86	ASN	CG	177.287
96	THR	HG1	3.306
111	ASN	CG	176.534
117	ASN	CG	176.931

All atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	586	584	99.7
¹³C chemical shifts	431	407	94.4
¹⁵N chemical shifts	100	98	98.0

Backbone atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	187	185	98.9
¹³C chemical shifts	182	182	100.0
¹⁵N chemical shifts	88	86	97.7

Side chain atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	399	399	100.0
¹³C chemical shifts	249	225	90.4
¹⁵N chemical shifts	12	12	100.0

Methyl group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	45	45	100.0
¹³C chemical shifts	45	45	100.0

Aromatic group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	51	51	100.0
¹³C chemical shifts	51	27	52.9

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
- Chain_ID: B

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 91, Sequence coverage: 98.9%
  - Entity_assembly_ID: B, Chain length: 24, Sequence coverage: 91.7%
- Total number of restraints: 3705
- Weight of restraints: 1.0 (3705)
- Potential type of restraints: square-well-parabolic (3705)
- Range of distance target values: 1.7, 4.0 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_5
  - Status: Warning
  - Experiment type: noe
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 91, Sequence coverage: 36.3%
    - Entity_assembly_ID: B, Chain length: 24, Sequence coverage: 66.7%
  - Total number of restraints: 887
  - Weight of restraints: 1.0 (887)
  - Potential type of restraints: square-well-parabolic (887)
  - Range of distance target values: 1.1, 4.51 (Å)
  - Histogram of distance target values
  - Histogram of discrepancy in distance target values
  - Distance restraints per residue
    - Chain_ID: A
    - Chain_ID: B
  - Distance restraints on contact map
  - Saveframe: CNS/XPLOR_distance_constraints_3
    - Status: Warning
    - Experiment type: hbond
    - Sequence coverage of experimental data
      - Entity_assembly_ID: A, Chain length: 91, Sequence coverage: 20.9%
      - Entity_assembly_ID: B, Chain length: 24, Sequence coverage: 12.5%
    - Total number of restraints: 32
    - Weight of restraints: 1.0 (32)
    - Potential type of restraints: square-well-parabolic (32)
    - Range of distance target values: 2.0, 2.9 (Å)
    - Histogram of distance target values
    - Distance restraints per residue
      - Chain_ID: A
      - Chain_ID: B
    - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_4
- Status: Warning
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 91, Sequence coverage: 83.5%
  - Entity_assembly_ID: B, Chain length: 24, Sequence coverage: 16.7%
- Total number of restraints: 123
- Total number of restraints per polymer type: 123
- Weight of restraints: 1.0 (123)
- Potential type of restraints: square-well-parabolic (123)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords anaphylotoxin C5a, Chemotaxis Inhibitory Protein (CHIPS), complement cascade, GPCR membrane protein C5aR, O-sulfated tyrosine, Staphylococcus Aureus

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 (1.081 seconds)

BMRB: 15778

Sample #1

Sample #2

Related entities 1. CHIPS protein, : 3 : 1 entities Detail

Related entities 2. C5aR(P7-28S) peptide, : 1 entities Detail

Experiments performed 27 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample