8OVP

X-ray structure of the iAspSnFR in complex with L-aspartate

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A, B (A, B)	Putative periplasmic binding transport protein,Green fluorescent protein	polymer	520	58137.7	2	UniProt (A0A0H2UXX1) UniProt (P42212) Pfam (PF00497) Pfam (PF01353) UniProt (by SIFTS) (P37902)	Escherichia coli
2	C, G (A, B)	ASPARTIC ACID	non-polymer		133.1	2	Chemie (ASP)
3	D, H (A, B)	ACETATE ION	non-polymer		59.0	2	Chemie (ACT)
4	E, F, I (A, B)	MAGNESIUM ION	non-polymer		24.3	3	Chemie (MG)
5	J, K (A, B)	water	water		18.0	684	Chemie (HOH)

Sequence modifications

A, B: 2 - 250 (UniProt: A0A0H2UXX1)

PDB	External Database	Details
Gly 1	-	expression tag
Phe 39	Tyr 65	engineered mutation
Ala 69	Ser 95	engineered mutation
Asp 89	Thr 115	engineered mutation
Thr 108	Gly 134	engineered mutation
Asn 124	Asp 150	engineered mutation
Asp 127	Gly 153	engineered mutation
Val 181	Ala 207	engineered mutation
Arg 189	Lys 215	engineered mutation
Glu 197	Asp 223	engineered mutation
Trp 208	Tyr 234	engineered mutation
Arg 231	Gln 257	engineered mutation
Leu 249	Pro 275	engineered mutation
Val 250	Pro 276	engineered mutation

A, B: 251 - 342 (UniProt: P42212)

PDB	External Database	Details
Thr 257	Met 153	engineered mutation
Ala 267	Val 163	engineered mutation
Val 275	Ile 171	engineered mutation
Val 310	Ala 206	engineered mutation
Leu 335	His 231	engineered mutation

A, B: 349 - 496 (UniProt: P42212)

PDB	External Database	Details
Gly 343	-	linker
Gly 344	-	linker
Thr 345	-	linker
Gly 346	-	linker
Gly 347	-	linker
Ser 348	-	linker
Arg 378	Ser 30	engineered mutation
Asn 387	Tyr 39	engineered mutation
Leu 412	Phe 64	engineered mutation
Cro 413	Ser 65	chromophore
Cro 413	Tyr 66	chromophore
Cro 413	Gly 67	chromophore
Ser 447	Phe 99	engineered mutation
Thr 453	Asn 105	engineered mutation
Phe 493	Tyr 145	engineered mutation
Asn 495	Ser 147	engineered mutation
Pro 496	His 148	engineered mutation

A, B: 497 - 520 (UniProt: A0A0H2UXX1)

PDB	External Database	Details
Lys 520	Asn 302	engineered mutation

Contents of the asymmetric unit

Polymers	Number of chains	2
	Total formula weight	116275.4
Non-Polymers*	Number of molecules	7
	Total formula weight	457.2
All*	Total formula weight	116732.6

*Water molecules are not included.