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BMRB: 4969

1IEH

Backbone 1H, 13C and 15N chemical shift assignments for the Brucella D4.4 VH antibody fragment

Authors

Assembly

Bruc D4.4 VH fragment

Entity

1. Bruc D4.4 VH fragment (polymer, Thiol state: all disulfide bound), 135 monomers, 14601.87 Da Detail

DVQLQASGGG LVQPGGSLRV SCAASGFTFS SYHMAWVRQA PGKGLEWVST INPGDGSTYY ADSVKGRFTI SRDNAKNTLY LQMNSLKSED TAVYYCAKYS GGALDAWGQG TQVTVSSQSE QKLISEEDLN HHHHH

Formula weight

14601.87 Da

Entity Connection

disulfide 1 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS22:SG	1:CYS96:SG

Source organism

Exptl. method

Refine. method

simulated annealing using

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.5 %, Completeness: 83.1 %, Completeness (bb): 80.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	83.1 % (1235 of 1486)	95.7 % (729 of 762)	64.2 % (369 of 575)	91.9 % (137 of 149)
Backbone	80.5 % (647 of 804)	95.7 % (270 of 282)	65.6 % (256 of 390)	91.7 % (121 of 132)
Sidechain	87.7 % (703 of 802)	95.6 % (459 of 480)	74.8 % (228 of 305)	94.1 % (16 of 17)
Aromatic	43.8 % (64 of 146)	83.6 % (61 of 73)	0.0 % (0 of 70)	100.0 % (3 of 3)
Methyl	100.0 % (126 of 126)	100.0 % (63 of 63)	100.0 % (63 of 63)

1. VH antibody fragment

DVQLQASGGG LVQPGGSLRV SCAASGFTFS SYHMAWVRQA PGKGLEWVST INPGDGSTYY ADSVKGRFTI SRDNAKNTLY LQMNSLKSED TAVYYCAKYS GGALDAWGQG TQVTVSSQSE QKLISEEDLN HHHHH

Show sample condition

Sample

Temperature 303 (±0.2) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	VH antibody fragment	[U-13C; U-15N]		0.4 ~ 0.6 mM
2	sodium phosphate buffer			10 mM
3	NaCl			150 mM
4	EDTA			0.2 mM

LACS Plot; CA

Referencing offset: 1.66 ppm, Outliers: 1 Detail

LACS Plot; CB

Referencing offset: 1.66 ppm, Outliers: 1 Detail

LACS Plot; HA

Referencing offset: -0.05 ppm, Outliers: 6 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 1IEH, Strand ID: A Detail

Release date

2001-03-06

Citation

Solution structure of a llama single-domain antibody with hydrophobic residues typical of the VH/VL interface
Vranken, W.F., Tolkatchev, D., Xu, P., Tanha, J., Chen, Z., Narang, S., Ni, F.
Biochemistry (2002), 41, 8570-8579, PubMed 12093273 , Abstract

Related entities 1. Bruc D4.4 VH fragment, : 1 : 306 entities Detail

Experiments performed 9 experiments Detail

1 15N HSQC

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Temperature 303 (±0.2) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	VH antibody fragment	[U-13C; U-15N]		0.4 ~ 0.6 mM
2	sodium phosphate buffer			10 mM
3	NaCl			150 mM
4	EDTA			0.2 mM

2 13C HSQC

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Temperature 303 (±0.2) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	VH antibody fragment	[U-13C; U-15N]		0.4 ~ 0.6 mM
2	sodium phosphate buffer			10 mM
3	NaCl			150 mM
4	EDTA			0.2 mM

3 HNCA

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Temperature 303 (±0.2) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	VH antibody fragment	[U-13C; U-15N]		0.4 ~ 0.6 mM
2	sodium phosphate buffer			10 mM
3	NaCl			150 mM
4	EDTA			0.2 mM

4 HNcoCA

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Temperature 303 (±0.2) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	VH antibody fragment	[U-13C; U-15N]		0.4 ~ 0.6 mM
2	sodium phosphate buffer			10 mM
3	NaCl			150 mM
4	EDTA			0.2 mM

5 HNCACB

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Temperature 303 (±0.2) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	VH antibody fragment	[U-13C; U-15N]		0.4 ~ 0.6 mM
2	sodium phosphate buffer			10 mM
3	NaCl			150 mM
4	EDTA			0.2 mM

6 CBCAcoNH

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Temperature 303 (±0.2) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	VH antibody fragment	[U-13C; U-15N]		0.4 ~ 0.6 mM
2	sodium phosphate buffer			10 mM
3	NaCl			150 mM
4	EDTA			0.2 mM

7 HBHAcoNH

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Temperature 303 (±0.2) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	VH antibody fragment	[U-13C; U-15N]		0.4 ~ 0.6 mM
2	sodium phosphate buffer			10 mM
3	NaCl			150 mM
4	EDTA			0.2 mM

8 13C TOCSY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Temperature 303 (±0.2) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	VH antibody fragment	[U-13C; U-15N]		0.4 ~ 0.6 mM
2	sodium phosphate buffer			10 mM
3	NaCl			150 mM
4	EDTA			0.2 mM

9 combined 15N/13C 3D NOESY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Temperature 303 (±0.2) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	VH antibody fragment	[U-13C; U-15N]		0.4 ~ 0.6 mM
2	sodium phosphate buffer			10 mM
3	NaCl			150 mM
4	EDTA			0.2 mM

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4969_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:22:CYS:SG	1:96:CYS:SG	oxidized, CA 52.516, CB 46.165 ppm	oxidized, CA 51.706, CB 43.064 ppm	n/a

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr4969_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shifts1	Warning	1361		97.8 (chain: 1, length: 135)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: shifts1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 135, Sequence coverage: 97.8%
- Total number of assignments
  - ¹³C chemical shifts: 360
  - ¹H chemical shifts: 861
  - ¹⁵N chemical shifts: 140
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- 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: 1