BMRBj - BMREntryMaster

Found 1 Document (0.957 seconds)

BMRB: 4349

43C9

Backbone Resonance Assignments for the Fv Fragment of the Catalytic Antibody NPN43C9 with Bound p-nitrophenol

Authors

Kroon, G.J. A., Martinez-Yamout, M.A., Krebs, J.F., Chung, J., Dyson, H.JANE., Wright, P.E.

Assembly

Fv fragment of the catalytic antibody NPN43C9

Entity

1. Variable light chain (polymer), 113 monomers, 12422.84 Da Detail

DVVMTQTPSS LAMSVGQKVT MSCKSSQSLL NISNQKNYLA WYQQKPGQSP KLLVYFASTR ESGVPDRFIG SGSGTDFTLT ISSVQAEDQA DYFCQQHYRA PRTFGGGTKL EIK

2. Variable heavy chain (polymer), 117 monomers, 12779.30 Da Detail

QVQLVESGPG LVAPSQSLSI TCTVSGISLS RYNVHWVRQS PGKGLEWLGM IWGGGSIEYN PALKSRLSIS KDNSKSQIFL KMNSLQTDDS AMYYCVSYGY GGDRFSYWGQ GTLVTVS

3. NPO (non-polymer), 139.109 Da

Total weight

25341.25 Da

Max. entity weight

12779.3 Da

Entity Connection

disulfide 2 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS23:SG	1:CYS94:SG
2	disulfide	sing	2:CYS22:SG	2:CYS95:SG

Source organism

Mus musculus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 52.6 %, Completeness: 27.2 %, Completeness (bb): 48.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	27.2 % (717 of 2632)	19.9 % (271 of 1363)	32.8 % (334 of 1018)	44.6 % (112 of 251)
Backbone	48.6 % (662 of 1362)	47.7 % (226 of 474)	48.6 % (324 of 667)	50.7 % (112 of 221)
Sidechain	11.1 % (164 of 1477)	5.1 % (45 of 889)	21.3 % (119 of 558)	0.0 % (0 of 30)
Aromatic	0.0 % (0 of 234)	0.0 % (0 of 117)	0.0 % (0 of 112)	0.0 % (0 of 5)
Methyl	13.7 % (31 of 226)	12.4 % (14 of 113)	15.0 % (17 of 113)

1. Variable light chain

DVVMTQTPSS LAMSVGQKVT MSCKSSQSLL NISNQKNYLA WYQQKPGQSP KLLVYFASTR ESGVPDRFIG SGSGTDFTLT ISSVQAEDQA DYFCQQHYRA PRTFGGGTKL EIK

2. Variable heavy chain

QVQLVESGPG LVAPSQSLSI TCTVSGISLS RYNVHWVRQS PGKGLEWLGM IWGGGSIEYN PALKSRLSIS KDNSKSQIFL KMNSLQTDDS AMYYCVSYGY GGDRFSYWGQ GTLVTVS

Show sample condition

Sample

Temperature 298 (±1) K, pH 6.8 (±0.2), Details All samples contained the same concentration of protein and were made using the same buffer conditions.

#	Name	Isotope labeling	Concentration
1	Variable heavy chain	[U-90% 15N; U-90% 13C, U-70% 2H]	0.5 mM
2	Variable light chain	[U-90% 15N; U-90% 13C, U-70% 2H]	0.5 mM
3	d11Tris		10 mM
4	NaCl		100 mM
5	p-nitrophenol		80 uM

Chem. Shift Complete2

Sequence coverage: 50.0 %, Completeness: 26.1 %, Completeness (bb): 46.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	26.1 % (1372 of 5264)	18.4 % (501 of 2726)	32.2 % (655 of 2036)	43.0 % (216 of 502)
Backbone	46.7 % (1271 of 2724)	44.4 % (421 of 948)	47.6 % (635 of 1334)	48.6 % (215 of 442)
Sidechain	10.6 % (313 of 2954)	4.5 % (80 of 1778)	20.8 % (232 of 1116)	1.7 % (1 of 60)
Aromatic	1.7 % (8 of 468)	1.7 % (4 of 234)	1.8 % (4 of 224)	0.0 % (0 of 10)
Methyl	9.5 % (43 of 452)	8.4 % (19 of 226)	10.6 % (24 of 226)

1. Variable light chain

DVVMTQTPSS LAMSVGQKVT MSCKSSQSLL NISNQKNYLA WYQQKPGQSP KLLVYFASTR ESGVPDRFIG SGSGTDFTLT ISSVQAEDQA DYFCQQHYRA PRTFGGGTKL EIK

2. Variable heavy chain

QVQLVESGPG LVAPSQSLSI TCTVSGISLS RYNVHWVRQS PGKGLEWLGM IWGGGSIEYN PALKSRLSIS KDNSKSQIFL KMNSLQTDDS AMYYCVSYGY GGDRFSYWGQ GTLVTVS

Show sample condition

Sample

Temperature 298 (±1) K, pH 6.8 (±0.2), Details All samples contained the same concentration of protein and were made using the same buffer conditions.

#	Name	Isotope labeling	Concentration
1	Variable heavy chain	[U-90% 15N; U-90% 13C, U-70% 2H]	0.5 mM
2	Variable light chain	[U-90% 15N; U-90% 13C, U-70% 2H]	0.5 mM
3	d11Tris		10 mM
4	NaCl		100 mM
5	p-nitrophenol		80 uM

Release date

2007-07-12

Citation 1

Backbone resonance assignments for the Fv fragment of the catalytic antibody NPN43C9 with bound p-nitrophenol
Kroon, G.J. A., Martinez-Yamout, M.A., Krebs, J.F., Chung, J., Dyson, H.JANE., Wright, P.E.
J. Biomol. NMR (1999), 15, 83-84, PubMed 10549136 , Abstract

Show more 3 citaions

Citation 2

NMRPipe: a multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., Bax, A.
J. Biomol. NMR (1995), 6, 277-293, PubMed 8520220 , DOI 10.1007/bf00197809 , Abstract

Citation 3

NMR View: A computer program for the visualization and analysis of NMR data
Johson
J. Biomol. NMR (1994), 4, 603-614

Citation 4

Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins
Grzesiek, S., Bax, A.
J. Biomol. NMR (1993), 3, 185-204, PubMed 8477186 , DOI 10.1007/bf00178261 , Abstract

Hide non-primary 3 citaions

Related entities 1. Variable light chain, : 1 : 1 : 359 entities Detail

Related entities 2. Variable heavy chain, : 1 : 1 : 466 entities Detail

Experiments performed 8 experiments Detail

1 2D 1H-15N HSQC