1O78

Biotin carboxyl carrier domain of transcarboxylase (1.3S) [10-48] deletion mutant

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	15N-HSQC-NOESY	2.3 MM PROTEIN, N15/C13 LABELED TC 1.3S [10-48], BIOTIN (UNLABELED) COVALENTLY ATTACHED TO LYS 89		2 MM AMMONIUM ACETATE	4.5	1 atm	300
2	HNCA	2.3 MM PROTEIN, N15/C13 LABELED TC 1.3S [10-48], BIOTIN (UNLABELED) COVALENTLY ATTACHED TO LYS 89		2 MM AMMONIUM ACETATE	4.5	1 atm	300
3	HNCO	2.3 MM PROTEIN, N15/C13 LABELED TC 1.3S [10-48], BIOTIN (UNLABELED) COVALENTLY ATTACHED TO LYS 89		2 MM AMMONIUM ACETATE	4.5	1 atm	300
4	CBCANH	2.3 MM PROTEIN, N15/C13 LABELED TC 1.3S [10-48], BIOTIN (UNLABELED) COVALENTLY ATTACHED TO LYS 89		2 MM AMMONIUM ACETATE	4.5	1 atm	300
5	CBCA(CO)NH	2.3 MM PROTEIN, N15/C13 LABELED TC 1.3S [10-48], BIOTIN (UNLABELED) COVALENTLY ATTACHED TO LYS 89		2 MM AMMONIUM ACETATE	4.5	1 atm	300
6	HN(CA)CO	2.3 MM PROTEIN, N15/C13 LABELED TC 1.3S [10-48], BIOTIN (UNLABELED) COVALENTLY ATTACHED TO LYS 89		2 MM AMMONIUM ACETATE	4.5	1 atm	300
7	HCACO	2.3 MM PROTEIN, N15/C13 LABELED TC 1.3S [10-48], BIOTIN (UNLABELED) COVALENTLY ATTACHED TO LYS 89		2 MM AMMONIUM ACETATE	4.5	1 atm	300
8	HN-HSQC-TOCSY	2.3 MM PROTEIN, N15/C13 LABELED TC 1.3S [10-48], BIOTIN (UNLABELED) COVALENTLY ATTACHED TO LYS 89		2 MM AMMONIUM ACETATE	4.5	1 atm	300
9	HBHA(CBCACO)NH	2.3 MM PROTEIN, N15/C13 LABELED TC 1.3S [10-48], BIOTIN (UNLABELED) COVALENTLY ATTACHED TO LYS 89		2 MM AMMONIUM ACETATE	4.5	1 atm	300
10	(H)N(CA)NNH	2.3 MM PROTEIN, N15/C13 LABELED TC 1.3S [10-48], BIOTIN (UNLABELED) COVALENTLY ATTACHED TO LYS 89		2 MM AMMONIUM ACETATE	4.5	1 atm	300
11	HCCH-TOCSY	2.3 MM PROTEIN, N15/C13 LABELED TC 1.3S [10-48], BIOTIN (UNLABELED) COVALENTLY ATTACHED TO LYS 89		2 MM AMMONIUM ACETATE	4.5	1 atm	300
12	2D 15N-1H HSQC	2.3 MM PROTEIN, N15/C13 LABELED TC 1.3S [10-48], BIOTIN (UNLABELED) COVALENTLY ATTACHED TO LYS 89		2 MM AMMONIUM ACETATE	4.5	1 atm	300

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	DRX	600

NMR Refinement
Method	Details	Software
DISTANCE GEOMETRY/ SIMULATED ANNEALING	DGSA, REFINEMENT WITH NOES AND HYDROGEN-BOND CONSTRAINTS	X-PLOR

NMR Ensemble Information
Conformer Selection Criteria	LEAST RESTRAINT VIOLATION
Conformers Calculated Total Number	600
Conformers Submitted Total Number	20
Representative Model	3 (n/a)

Additional NMR Experimental Information
Details	THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED PROTEIN. BIOTIN WAS UNLABELED AND NOT INCLUDED IN THE STRUCTURE CALCULATION.

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	refinement	X-PLOR	3.1	BRUNGER
2	structure solution	X-PLOR
3	structure solution	PROCHECK	3.5.3
4	structure solution	AQUA	2.0

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.