1MG2

MUTATION OF ALPHA PHE55 OF METHYLAMINE DEHYDROGENASE ALTERS THE REORGANIZATION ENERGY AND ELECTRONIC COUPLING FOR ITS ELECTRON TRANSFER REACTION WITH AMICYANIN

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A, E, I, M (A, E, I, M)	Methylamine dehydrogenase, heavy chain	polymer	390	42673.5	4	UniProt (P29894) Pfam (PF06433)	Paracoccus denitrificans	MADH
2	B, F, J, N (B, F, J, N)	Methylamine dehydrogenase, light chain	polymer	131	14210.7	4	UniProt (P22619) Pfam (PF02975)	Paracoccus denitrificans	MADH
3	C, G, K, O (C, G, K, O)	Amicyanin	polymer	105	11505.2	4	UniProt (P22364) Pfam (PF00127)	Paracoccus denitrificans
4	D, H, L, P (D, H, L, P)	CYTOCHROME C-L	polymer	155	17094.7	4	UniProt (P29889) UniProt (by SIFTS) (P29899)	Paracoccus denitrificans	CYTOCHROME C551I
5	AA, BA, FA, GA, Q... (I, J, M, N, A...)	PHOSPHATE ION	non-polymer		95.0	8	Chemie (PO4)
6	CA, HA, S, X (K, O, C, G)	COPPER (II) ION	non-polymer		63.5	4	Chemie (CU)
7	DA, IA, T, Y (L, P, D, H)	SODIUM ION	non-polymer		23.0	4	Chemie (NA)
8	EA, JA, U, Z (L, P, D, H)	HEME C	non-polymer		618.5	4	Chemie (HEC)
9	KA, LA, MA, NA, OA... (A, B, C, D, E...)	water	water		18.0	1685	Chemie (HOH)

Sequence modifications

A, E, I, M: -3 - 386 (UniProt: P29894)

PDB	External Database	Details
Ala 55	Phe 86	engineered mutation
Phe 312	Leu 343	SEE REMARK 999
Val 313	Leu 344	SEE REMARK 999

B, F, J, N: 1 - 131 (UniProt: P22619)

PDB	External Database	Details
Trq 57	Trp 114	modified residue

Contents of the asymmetric unit

Polymers	Number of chains	16
	Total formula weight	341936.0
Non-Polymers*	Number of molecules	20
	Total formula weight	3579.9
All*	Total formula weight	345516.0

*Water molecules are not included.