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BMRB: 15032

2JMR

Chemical shift assignments of the type 1 pilus subunit FimF

Authors

Gossert, A.D., Hiller, S., Fiorito, F., Wuthrich, K.

Assembly

FimF

Entity

1. FimF (polymer, Thiol state: all disulfide bound), 179 monomers, 19170.21 Da Detail

MADSTITIRG YVRDNGCSVA AESTNFTVDL MENAAKQFNN IGATTPVVPF RILLSPCGNA VSAVKVGFTG VADSHNANLL ALENTVSAAS GLGIQLLNEQ QNQIPLNAPS SALSWTTLTP GKPNTLNFYA RLMATQVPVT AGHINATATF TLEYQDNHHH HHHKQADSTI TIRGYVRDN

Formula weight

19170.21 Da

Entity Connection

na 11, disulfide 1, metal coordination 8 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS17:SG	1:CYS57:SG
2	na	sing	1:CYS5:SG	3:ZN1:ZN
3	metal coordination	sing	1:CYS29:SG	2:ZN1:ZN
4	na	sing	1:CYS8:SG	3:ZN1:ZN
5	metal coordination	sing	1:CYS32:SG	2:ZN1:ZN
6	na	sing	1:CYS16:SG	3:ZN1:ZN
7	metal coordination	sing	1:CYS49:SG	2:ZN1:ZN
8	metal coordination	sing	1:CYS52:SG	2:ZN1:ZN
9	na	sing	1:CYS19:SG	3:ZN1:ZN
10	metal coordination	sing	1:CYS44:SG	2:ZN1:ZN
11	na	sing	1:CYS21:SG	3:ZN1:ZN
12	na	sing	1:CYS24:SG	3:ZN1:ZN
13	metal coordination	sing	1:CYS64:SG	2:ZN1:ZN
14	metal coordination	sing	1:CYS67:SG	2:ZN1:ZN
15	na	sing	1:CYS36:SG	3:ZN1:ZN
16	metal coordination	sing	1:HIS46:ND1	2:ZN1:ZN
17	na	sing	1:CYS39:SG	3:ZN1:ZN
18	na	sing	1:CYS47:SG	3:ZN1:ZN
19	na	sing	1:CYS63:SG	3:ZN1:ZN
20	na	sing	1:CYS66:SG	3:ZN1:ZN

Source organism

Escherichia coli

Exptl. method

solution NMR

Refine. method

torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 95.5 %, Completeness: 91.3 %, Completeness (bb): 92.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	91.3 % (1794 of 1966)	92.2 % (922 of 1000)	89.3 % (687 of 769)	93.9 % (185 of 197)
Backbone	92.4 % (978 of 1058)	93.1 % (336 of 361)	91.4 % (481 of 526)	94.2 % (161 of 171)
Sidechain	90.1 % (970 of 1076)	91.2 % (583 of 639)	88.3 % (363 of 411)	92.3 % (24 of 26)
Aromatic	67.6 % (92 of 136)	80.9 % (55 of 68)	53.7 % (36 of 67)	100.0 % (1 of 1)
Methyl	99.1 % (226 of 228)	98.2 % (112 of 114)	100.0 % (114 of 114)

1. FimF

MADSTITIRG YVRDNGCSVA AESTNFTVDL MENAAKQFNN IGATTPVVPF RILLSPCGNA VSAVKVGFTG VADSHNANLL ALENTVSAAS GLGIQLLNEQ QNQIPLNAPS SALSWTTLTP GKPNTLNFYA RLMATQVPVT AGHINATATF TLEYQDNHHH HHHKQADSTI TIRGYVRDN

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Temperature 310.1 K, pH 6.8

#	Name	Isotope labeling	Concentration
1	FimF	[U-99% 13C; U-99% 15N]	1.4 mM
2	sodium phosphate		25 mM
3	sodium chloride		100 mM
4	sodium azide		0.05 %
5	D2O		5 %
6	H2O		95 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.43 ppm, Outliers: 3 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.43 ppm, Outliers: 3 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.06 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 1.24 ppm, Outliers: 1 Detail

Protein Blocks Logo

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

Release date

2007-05-08

Citation

NMR assignment of the E. coli type 1 pilus protein FimF
Gossert, A.D., Hiller, S., Fiorito, F., Wuthrich, K.
J. Biomol. NMR (2007), 38, 195-195, PubMed 17417715 , DOI 10.1007/s10858-006-9123-9 , Abstract

Related entities 1. FimF, : 1 : 5 : 78 entities Detail

Interaction partners 1. FimF, : 3 interactors Detail

More details for 3 interactors identified by 2 citations

Experiments performed 8 experiments Detail

1 3D HNCACB