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BMRB: 17807

2LGF

Solution structure of Ca2+/calmodulin complexed with a peptide representing the calmodulin-binding domain of L-selectin

Authors

Gifford, J.L., Ishida, H., Vogel, H.J.

Assembly

Ca2+/CaM L-selectin peptide complex

Entity

1. Calmodulin (polymer, Thiol state: not present), 147 monomers, 16635.14 Da Detail

DQLTEEQIAE FKEAFSLFDK DGDGTITTKE LGTVMRSLGQ NPTEAELQDM INEVDADGNG TIDFPEFLTM MARKMKDTDS EEEIREAFRV FDKDGNGYIS AAELRHVMTN LGEKLTDEEV DEMIREADID GDGQVNYEEF VQMMTAK

2. L-selectin binding domain peptide (polymer, Thiol state: not present), 15 monomers, 1828.295 Da Detail

AFIIWLARRL KKGKK

3. CA (non-polymer), 40.078 × 4 Da

Total weight

18623.748 Da

Max. entity weight

16635.14 Da

Source organism

Escherichia coli

Exptl. method

solution NMR

Refine. method

torsion angle dynamics, simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 47.7 %, Completeness (bb): 79.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	47.7 % (895 of 1875)	30.7 % (300 of 978)	62.2 % (450 of 724)	83.8 % (145 of 173)
Backbone	79.9 % (773 of 968)	59.0 % (197 of 334)	90.9 % (431 of 474)	90.6 % (145 of 160)
Sidechain	24.5 % (259 of 1057)	16.0 % (103 of 644)	39.0 % (156 of 400)	0.0 % (0 of 13)
Aromatic	7.4 % (9 of 122)	14.8 % (9 of 61)	0.0 % (0 of 60)	0.0 % (0 of 1)
Methyl	19.4 % (31 of 160)	20.0 % (16 of 80)	18.8 % (15 of 80)

1. Calmodulin

DQLTEEQIAE FKEAFSLFDK DGDGTITTKE LGTVMRSLGQ NPTEAELQDM INEVDADGNG TIDFPEFLTM MARKMKDTDS EEEIREAFRV FDKDGNGYIS AAELRHVMTN LGEKLTDEEV DEMIREADID GDGQVNYEEF VQMMTAK

2. L-selectin binding domain peptide

AFIIWLARRL KKGKK

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.8, Details Sample for backbone and side chain assignment of CaM in the complex

#	Name	Isotope labeling	Concentration
1	Calmodulin	[U-13C; U-15N]	0.5 ~ 0.8 mM
2	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
3	CALCIUM ION	natural abundance	4 mM
4	DSS	natural abundance	0.5 mM
5	potassium chloride	natural abundance	100 mM
6	sodium azide	natural abundance	0.03 %
7	Bis-Tris	natural abundance	20 mM
8	H2O	natural abundance	90 %
9	D2O	natural abundance	10 %

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.8, Details Sample for collecting intrapeptide NOEs to determine the structure of the bound LSEL15

#	Name	Isotope labeling	Concentration
10	Calmodulin	[U-2H; U-15N]	0.5 ~ 0.8 mM
11	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
12	CALCIUM ION	natural abundance	4 mM
13	DSS	natural abundance	0.5 mM
14	potassium chloride	natural abundance	100 mM
15	sodium azide	natural abundance	0.03 %
16	Bis-Tris	natural abundance	20 mM
17	H2O	natural abundance	90 %
18	D2O	natural abundance	10 %

Sample #3

Solvent system 100% D2O, Pressure 1 atm, Temperature 303 K, pH 6.8, Details Methionine methyl-labeled CaM sample for the collection of intermolecular NOEs between CaM and the bound peptide

#	Name	Isotope labeling	Concentration
19	Calmodulin	[1H/13C-methyl Met; U-2H; U-15N]	0.5 ~ 0.8 mM
20	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
21	CALCIUM ION	natural abundance	4 mM
22	DSS	natural abundance	0.5 mM
23	potassium chloride	natural abundance	100 mM
24	sodium azide	natural abundance	0.03 %
25	Bis-Tris	natural abundance	20 mM
26	D2O	natural abundance	100 %

Sample #4

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.8, Details Isotropic U-13;U-15 sample for collection of CaM RDCs

#	Name	Isotope labeling	Concentration
27	Calmodulin	[U-13C; U-15N]	0.5 ~ 0.8 mM
28	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
29	CALCIUM ION	natural abundance	4 mM
30	DSS	natural abundance	0.5 mM
31	potassium chloride	natural abundance	300 mM
32	sodium azide	natural abundance	0.03 %
33	Bis-Tris	natural abundance	20 mM
34	H2O	natural abundance	90 %
35	D2O	natural abundance	10 %

Sample #5

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.8, Details Anisotropic U13;U15 sample for the collection of CaM RDCs

#	Name	Isotope labeling	Concentration
36	Calmodulin	[U-13C; U-15N]	0.5 ~ 0.8 mM
37	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
38	CALCIUM ION	natural abundance	4 mM
39	DSS	natural abundance	0.5 mM
40	potassium chloride	natural abundance	300 mM
41	sodium azide	natural abundance	0.03 %
42	Bis-Tris	natural abundance	20 mM
43	Pf1 phage	natural abundance	16 w/v
44	D2O	natural abundance	10 %
45	H2O	natural abundance	90 %

Protein Blocks Logo

Calculated from 1 models in PDB: 2LGF, Strand ID: A, B Detail

Release date

2012-06-10

Citation

Structural insights into calmodulin-regulated L-selectin ectodomain shedding
Gifford, J.L., Ishida, H., Vogel, H.J.
J. Biol. Chem. (2012), 287, 26513-26527, PubMed 22711531 , DOI 10.1074/jbc.M112.373373 , Abstract

Related entities 1. Calmodulin, : 11 : 88 entities Detail

Related entities 2. L-selectin binding domain peptide, : 1 : 8 : 2 : 1 entities Detail

Experiments performed 16 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.8, Details Sample for backbone and side chain assignment of CaM in the complex

#	Name	Isotope labeling	Concentration
1	Calmodulin	[U-13C; U-15N]	0.5 ~ 0.8 mM
2	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
3	CALCIUM ION	natural abundance	4 mM
4	DSS	natural abundance	0.5 mM
5	potassium chloride	natural abundance	100 mM
6	sodium azide	natural abundance	0.03 %
7	Bis-Tris	natural abundance	20 mM
8	H2O	natural abundance	90 %
9	D2O	natural abundance	10 %

2 2D 1H-13C HSQC

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 303 K, pH 6.8, Details Methionine methyl-labeled CaM sample for the collection of intermolecular NOEs between CaM and the bound peptide

#	Name	Isotope labeling	Concentration
19	Calmodulin	[1H/13C-methyl Met; U-2H; U-15N]	0.5 ~ 0.8 mM
20	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
21	CALCIUM ION	natural abundance	4 mM
22	DSS	natural abundance	0.5 mM
23	potassium chloride	natural abundance	100 mM
24	sodium azide	natural abundance	0.03 %
25	Bis-Tris	natural abundance	20 mM
26	D2O	natural abundance	100 %

3 2D 1H-1H COSY

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.8, Details Sample for collecting intrapeptide NOEs to determine the structure of the bound LSEL15

#	Name	Isotope labeling	Concentration
10	Calmodulin	[U-2H; U-15N]	0.5 ~ 0.8 mM
11	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
12	CALCIUM ION	natural abundance	4 mM
13	DSS	natural abundance	0.5 mM
14	potassium chloride	natural abundance	100 mM
15	sodium azide	natural abundance	0.03 %
16	Bis-Tris	natural abundance	20 mM
17	H2O	natural abundance	90 %
18	D2O	natural abundance	10 %

4 3D CBCA(CO)NH

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.8, Details Sample for backbone and side chain assignment of CaM in the complex

#	Name	Isotope labeling	Concentration
1	Calmodulin	[U-13C; U-15N]	0.5 ~ 0.8 mM
2	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
3	CALCIUM ION	natural abundance	4 mM
4	DSS	natural abundance	0.5 mM
5	potassium chloride	natural abundance	100 mM
6	sodium azide	natural abundance	0.03 %
7	Bis-Tris	natural abundance	20 mM
8	H2O	natural abundance	90 %
9	D2O	natural abundance	10 %

5 3D C(CO)NH

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.8, Details Sample for backbone and side chain assignment of CaM in the complex

#	Name	Isotope labeling	Concentration
1	Calmodulin	[U-13C; U-15N]	0.5 ~ 0.8 mM
2	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
3	CALCIUM ION	natural abundance	4 mM
4	DSS	natural abundance	0.5 mM
5	potassium chloride	natural abundance	100 mM
6	sodium azide	natural abundance	0.03 %
7	Bis-Tris	natural abundance	20 mM
8	H2O	natural abundance	90 %
9	D2O	natural abundance	10 %

6 3D HNCO

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.8, Details Sample for backbone and side chain assignment of CaM in the complex

#	Name	Isotope labeling	Concentration
1	Calmodulin	[U-13C; U-15N]	0.5 ~ 0.8 mM
2	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
3	CALCIUM ION	natural abundance	4 mM
4	DSS	natural abundance	0.5 mM
5	potassium chloride	natural abundance	100 mM
6	sodium azide	natural abundance	0.03 %
7	Bis-Tris	natural abundance	20 mM
8	H2O	natural abundance	90 %
9	D2O	natural abundance	10 %

7 3D HNCACB

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.8, Details Sample for backbone and side chain assignment of CaM in the complex

#	Name	Isotope labeling	Concentration
1	Calmodulin	[U-13C; U-15N]	0.5 ~ 0.8 mM
2	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
3	CALCIUM ION	natural abundance	4 mM
4	DSS	natural abundance	0.5 mM
5	potassium chloride	natural abundance	100 mM
6	sodium azide	natural abundance	0.03 %
7	Bis-Tris	natural abundance	20 mM
8	H2O	natural abundance	90 %
9	D2O	natural abundance	10 %

8 3D HBHA(CO)NH

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.8, Details Sample for backbone and side chain assignment of CaM in the complex

#	Name	Isotope labeling	Concentration
1	Calmodulin	[U-13C; U-15N]	0.5 ~ 0.8 mM
2	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
3	CALCIUM ION	natural abundance	4 mM
4	DSS	natural abundance	0.5 mM
5	potassium chloride	natural abundance	100 mM
6	sodium azide	natural abundance	0.03 %
7	Bis-Tris	natural abundance	20 mM
8	H2O	natural abundance	90 %
9	D2O	natural abundance	10 %

9 3D H(CCO)NH

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.8, Details Sample for backbone and side chain assignment of CaM in the complex

#	Name	Isotope labeling	Concentration
1	Calmodulin	[U-13C; U-15N]	0.5 ~ 0.8 mM
2	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
3	CALCIUM ION	natural abundance	4 mM
4	DSS	natural abundance	0.5 mM
5	potassium chloride	natural abundance	100 mM
6	sodium azide	natural abundance	0.03 %
7	Bis-Tris	natural abundance	20 mM
8	H2O	natural abundance	90 %
9	D2O	natural abundance	10 %

10 3D 1H-13C NOESY

Instrument

Bruker Avance - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
19	Calmodulin	[1H/13C-methyl Met; U-2H; U-15N]	0.5 ~ 0.8 mM
20	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
21	CALCIUM ION	natural abundance	4 mM
22	DSS	natural abundance	0.5 mM
23	potassium chloride	natural abundance	100 mM
24	sodium azide	natural abundance	0.03 %
25	Bis-Tris	natural abundance	20 mM
26	D2O	natural abundance	100 %

11 3D HN(CA)CO

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.8, Details Sample for backbone and side chain assignment of CaM in the complex

#	Name	Isotope labeling	Concentration
1	Calmodulin	[U-13C; U-15N]	0.5 ~ 0.8 mM
2	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
3	CALCIUM ION	natural abundance	4 mM
4	DSS	natural abundance	0.5 mM
5	potassium chloride	natural abundance	100 mM
6	sodium azide	natural abundance	0.03 %
7	Bis-Tris	natural abundance	20 mM
8	H2O	natural abundance	90 %
9	D2O	natural abundance	10 %

12 2D HMBC

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.8, Details Sample for backbone and side chain assignment of CaM in the complex

#	Name	Isotope labeling	Concentration
1	Calmodulin	[U-13C; U-15N]	0.5 ~ 0.8 mM
2	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
3	CALCIUM ION	natural abundance	4 mM
4	DSS	natural abundance	0.5 mM
5	potassium chloride	natural abundance	100 mM
6	sodium azide	natural abundance	0.03 %
7	Bis-Tris	natural abundance	20 mM
8	H2O	natural abundance	90 %
9	D2O	natural abundance	10 %

13 3D LRCH

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.8, Details Sample for backbone and side chain assignment of CaM in the complex

#	Name	Isotope labeling	Concentration
1	Calmodulin	[U-13C; U-15N]	0.5 ~ 0.8 mM
2	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
3	CALCIUM ION	natural abundance	4 mM
4	DSS	natural abundance	0.5 mM
5	potassium chloride	natural abundance	100 mM
6	sodium azide	natural abundance	0.03 %
7	Bis-Tris	natural abundance	20 mM
8	H2O	natural abundance	90 %
9	D2O	natural abundance	10 %

14 F2-filtered 2D 1H-1H NOESY

Instrument

Bruker Avance - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
10	Calmodulin	[U-2H; U-15N]	0.5 ~ 0.8 mM
11	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
12	CALCIUM ION	natural abundance	4 mM
13	DSS	natural abundance	0.5 mM
14	potassium chloride	natural abundance	100 mM
15	sodium azide	natural abundance	0.03 %
16	Bis-Tris	natural abundance	20 mM
17	H2O	natural abundance	90 %
18	D2O	natural abundance	10 %

15 2D 1H-15N IPAP HSQC

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.8, Details Isotropic U-13;U-15 sample for collection of CaM RDCs

#	Name	Isotope labeling	Concentration
27	Calmodulin	[U-13C; U-15N]	0.5 ~ 0.8 mM
28	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
29	CALCIUM ION	natural abundance	4 mM
30	DSS	natural abundance	0.5 mM
31	potassium chloride	natural abundance	300 mM
32	sodium azide	natural abundance	0.03 %
33	Bis-Tris	natural abundance	20 mM
34	H2O	natural abundance	90 %
35	D2O	natural abundance	10 %

16 2D 1H-15N IPAP HSQC

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.8, Details Anisotropic U13;U15 sample for the collection of CaM RDCs

#	Name	Isotope labeling	Concentration
36	Calmodulin	[U-13C; U-15N]	0.5 ~ 0.8 mM
37	L-selectin binding domain peptide	natural abundance	0.5 ~ 0.8 mM
38	CALCIUM ION	natural abundance	4 mM
39	DSS	natural abundance	0.5 mM
40	potassium chloride	natural abundance	300 mM
41	sodium azide	natural abundance	0.03 %
42	Bis-Tris	natural abundance	20 mM
43	Pf1 phage	natural abundance	16 w/v
44	D2O	natural abundance	10 %
45	H2O	natural abundance	90 %

NMR combined restraints 7 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints, RDC restraints	combined_17807_2lgf.nef
Input source #2: Coordindates	2lgf.cif
Diamagnetism of the molecular assembly	False (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	Error

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)
1:98:TYR:O	3:3:CA:CA	unknown	unknown	n/a
1:61:THR:O	3:2:CA:CA	unknown	unknown	n/a
1:103:GLU:OE1	3:3:CA:CA	unknown	unknown	n/a
1:94:ASP:OD1	3:3:CA:CA	unknown	unknown	n/a
1:66:GLU:OE2	3:2:CA:CA	unknown	unknown	n/a
1:57:ASP:OD2	3:2:CA:CA	unknown	unknown	n/a
1:59:ASN:OD1	3:2:CA:CA	unknown	unknown	n/a
1:139:GLU:OE2	3:4:CA:CA	unknown	unknown	n/a
1:96:ASN:OD1	3:3:CA:CA	unknown	unknown	n/a
1:55:ASP:OD1	3:2:CA:CA	unknown	unknown	n/a
1:128:ASP:OD1	3:4:CA:CA	unknown	unknown	n/a
1:57:ASP:OD1	3:2:CA:CA	unknown	unknown	n/a
1:103:GLU:OE2	3:3:CA:CA	unknown	unknown	n/a
1:132:ASP:OD2	3:4:CA:CA	unknown	unknown	n/a
1:25:THR:O	3:1:CA:CA	unknown	unknown	n/a
1:66:GLU:OE1	3:2:CA:CA	unknown	unknown	n/a
1:94:ASP:OD2	3:3:CA:CA	unknown	unknown	n/a
1:30:GLU:OE2	3:1:CA:CA	unknown	unknown	n/a
1:21:ASP:OD1	3:1:CA:CA	unknown	unknown	n/a
1:139:GLU:OE1	3:4:CA:CA	unknown	unknown	n/a
1:134:GLN:O	3:4:CA:CA	unknown	unknown	n/a
1:92:ASP:OD2	3:3:CA:CA	unknown	unknown	n/a
1:130:ASP:OD2	3:4:CA:CA	unknown	unknown	n/a
1:30:GLU:OE1	3:1:CA:CA	unknown	unknown	n/a
1:19:ASP:OD2	3:1:CA:CA	unknown	unknown	n/a
1:23:ASP:OD2	3:1:CA:CA	unknown	unknown	n/a
1:19:ASP:OD1	3:1:CA:CA	unknown	unknown	n/a
1:55:ASP:OD2	3:2:CA:CA	unknown	unknown	n/a
1:130:ASP:OD1	3:4:CA:CA	unknown	unknown	n/a
1:132:ASP:OD1	3:4:CA:CA	unknown	unknown	n/a
1:23:ASP:OD1	3:1:CA:CA	unknown	unknown	n/a
1:21:ASP:OD2	3:1:CA:CA	unknown	unknown	n/a
1:92:ASP:OD1	3:3:CA:CA	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
C	1	CA	CALCIUM ION	Distance restraints
C	2	CA	CALCIUM ION	None
C	3	CA	CALCIUM ION	None
C	4	CA	CALCIUM ION	None

Sequence alignments

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

-------10--------20--------30--------40--------50--------60--------70--------80--------90-------100-
DQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYIS
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
DQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYIS
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

------110-------120-------130-------140--------
AAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK
|||||||||||||||||||||||||||||||||||||||||||||||
AAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK
-------110-------120-------130-------140-------

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

-350-----360---
AFIIWLARRLKKGKK
|||||||||||||||
AFIIWLARRLKKGKK
--------10-----

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	147	0	0	100.0
B	B	15	0	0	100.0

Content subtype: combined_17807_2lgf.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	33		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	833		100.0 (chain: A, length: 147), 100.0 (chain: B, length: 15)
1	Distance restraints	CNS/XPLOR_distance_constraints_5	Warning	312 (1)	noe	6.1 (chain: A, length: 147), 100.0 (chain: B, length: 15)
2	Distance restraints	CNS/XPLOR_distance_constraints_6	Error	24 (1)	undefined	13.6 (chain: A, length: 147), 25.0 (chain: C, length: 4)
3	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	122 (1)	hbond	61.2 (chain: A, length: 147), 40.0 (chain: B, length: 15)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	316 (316)	.	99.3 (chain: A, length: 147), 100.0 (chain: B, length: 15)
1	RDC restraints	CNS/XPLOR_dipolar_coupling_2	OK	109 (109)	.	74.1 (chain: A, length: 147)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 147, Sequence coverage: 100.0%
  - Entity_assembly_ID: B, Chain length: 15, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 438
  - ¹H chemical shifts: 251
  - ¹⁵N chemical shifts: 144
- Completeness of assignments
  - Entity_assemble_ID: A
  - Entity_assemble_ID: B
- Peptide bond of PRO
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A
  - Chain_ID: B

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	642	438	68.2
¹H chemical shifts	864	162	18.8
¹⁵N chemical shifts	163	144	88.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	294	293	99.7
¹H chemical shifts	303	153	50.5
¹⁵N chemical shifts	145	144	99.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	348	145	41.7
¹H chemical shifts	561	9	1.6
¹⁵N chemical shifts	18	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	79	19	24.1
¹H chemical shifts	79	9	11.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	50	0	0.0
¹H chemical shifts	50	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	82	0	0.0
¹H chemical shifts	114	88	77.2
¹⁵N chemical shifts	18	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	30	0	0.0
¹H chemical shifts	31	29	93.5
¹⁵N chemical shifts	15	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	52	0	0.0
¹H chemical shifts	83	59	71.1
¹⁵N chemical shifts	3	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	10	0	0.0
¹H chemical shifts	10	9	90.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	10	0	0.0
¹H chemical shifts	11	9	81.8
¹⁵N chemical shifts	1	0	0.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_5
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 147, Sequence coverage: 6.1%
  - Entity_assembly_ID: B, Chain length: 15, Sequence coverage: 100.0%
- Total number of restraints: 312
- Weight of restraints: 1.0 (312)
- Potential type of restraints: square-well-parabolic (312)
- Range of distance target values: 1.43, 3.9 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
  - Chain_ID: C
    None
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_6
  - Status: Error
  - Experiment type: undefined
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 147, Sequence coverage: 13.6%
    - Entity_assembly_ID: C, Chain length: 4, Sequence coverage: 25.0%
  - Total number of restraints: 24
  - Weight of restraints: 1.0 (24)
  - Potential type of restraints: square-well-parabolic (24)
  - Range of distance target values: 1.25, 1.25 (Å)
  - Distance restraints per residue
    - Chain_ID: A
    - Chain_ID: B
      None
    - Chain_ID: C
  - 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: 147, Sequence coverage: 61.2%
      - Entity_assembly_ID: B, Chain length: 15, Sequence coverage: 40.0%
    - Total number of restraints: 122
    - Weight of restraints: 1.0 (122)
    - Potential type of restraints: square-well-parabolic (122)
    - Range of distance target values: 1.05, 1.55 (Å)
    - Histogram of distance target values
    - Distance restraints per residue
      - Chain_ID: A
      - Chain_ID: B
      - Chain_ID: C
        None
    - 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: 147, Sequence coverage: 99.3%
  - Entity_assembly_ID: B, Chain length: 15, Sequence coverage: 100.0%
- Total number of restraints: 316
- Total number of restraints per polymer type: 316
- Weight of restraints: 1.0 (316)
- Potential type of restraints: square-well-parabolic (316)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
  - Chain_ID: B

RDC restraints

Saveframe: CNS/XPLOR_dipolar_coupling_2

Status: OK
Experiment type: .

Sequence coverage of experimental data

Entity_assembly_ID: A, Chain length: 147, Sequence coverage: 74.1%

-------10--------20--------30--------40--------50--------60--------70--------80--------90-------100-
DQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYIS
  ||| |||  ||| || |||||||||| ||| | |||||| ||| |||  |  |||| |||||  |    || || ||||||| |   | |||||||||
..LTE.QIA..KEA.SL.DKDGDGTITT.ELG.V.RSLGQN.TEA.LQD..N..DADG.GTIDF..F....AR.MK.TDSEEEI.E...V.DKDGNGYIS

------110-------120-------130-------140--------
AAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK
||  || |||||||||| |||| |||||||||||||| |||| | ||
AA..RH.MTNLGEKLTD.EVDE.IREADIDGDGQVNY.EFVQ.M.AK

Total number of restraints: 109
Potential type of restraints: undefined (109)
Range of observed RDC values: 100.0, -100.0 (Hz)
RDC restraints per residue
- Chain_ID: A
  None

Keywords calcium-calmodulin, L-selectin, peptide complex

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BMRB: 17807

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Related entities 1. Calmodulin, : 11 : 88 entities Detail

Related entities 2. L-selectin binding domain peptide, : 1 : 8 : 2 : 1 entities Detail

Experiments performed 16 experiments Detail

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NMR combined restraints 7 contents Detail