eF-site/Summary 6bky-ABCDEF

eF-site ID	6bky-ABCDEF
PDB Code	6bky
Chain	A, B, C, D, E, F

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Title	Novel Binding Modes of Inhibition of Wild-Type IDH1: Allosteric Inhibition with Cmpd2
Classification	OXIDOREDUCTASE/OXIDOREDUCTASE inhibitor
Compound	Isocitrate dehydrogenase [NADP] cytoplasmic
Source	(IDHC_HUMAN)

Sequence	A:	KKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSY DLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKR VEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVS GWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGT QKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALS KGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQ KIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVA QGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKG QETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEV SIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLG ENLKIKLAQAKLSLEH
	B:	KKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSY DLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKR VEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVS GWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGT QKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALS KGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQ KIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVA QGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKG QETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEV SIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLG ENLKIKLAQAKLS
	C:	KKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSY DLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKR VEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVS GWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGT QKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALS KGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQ KIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVA QGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKG QETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEV SIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLG ENLKIKLAQAKLSL
	D:	KKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSY DLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKR VEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVS GWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGT QKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALS KGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQ KIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVA QGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKG QETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEV SIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLG ENLKIKLAQAKLSLEH
	E:	KKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSY DLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKR VEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVS GWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGT QKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALS KGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQ KIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVA QGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKG QETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEV SIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLG ENLKIKLAQAKLSLEH
	F:	KKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSY DLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKR VEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVS GWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGT QKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALS KGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQ KIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVA QGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKG QETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEV SIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLG ENLKIKLAQAKLS

Description

Functional site


1)	chain	C
	residue	252
	type
	sequence	D
	description	binding site for residue LMR D 501
	source	: AC1

2)	chain	D
	residue	77
	type
	sequence	T
	description	binding site for residue LMR D 501
	source	: AC1

3)	chain	D
	residue	94
	type
	sequence	S
	description	binding site for residue LMR D 501
	source	: AC1

4)	chain	D
	residue	96
	type
	sequence	N
	description	binding site for residue LMR D 501
	source	: AC1

5)	chain	D
	residue	100
	type
	sequence	R
	description	binding site for residue LMR D 501
	source	: AC1

6)	chain	D
	residue	109
	type
	sequence	R
	description	binding site for residue LMR D 501
	source	: AC1

7)	chain	D
	residue	132
	type
	sequence	R
	description	binding site for residue LMR D 501
	source	: AC1

8)	chain	D
	residue	139
	type
	sequence	Y
	description	binding site for residue LMR D 501
	source	: AC1

9)	chain	D
	residue	275
	type
	sequence	D
	description	binding site for residue LMR D 501
	source	: AC1

10)	chain	C
	residue	252
	type
	sequence	D
	description	binding site for residue MG D 502
	source	: AC2

11)	chain	D
	residue	275
	type
	sequence	D
	description	binding site for residue MG D 502
	source	: AC2

12)	chain	D
	residue	279
	type
	sequence	D
	description	binding site for residue MG D 502
	source	: AC2

13)	chain	C
	residue	121
	type
	sequence	V
	description	binding site for residue K32 D 503
	source	: AC3

14)	chain	C
	residue	255
	type
	sequence	V
	description	binding site for residue K32 D 503
	source	: AC3

15)	chain	C
	residue	259
	type
	sequence	M
	description	binding site for residue K32 D 503
	source	: AC3

16)	chain	C
	residue	277
	type
	sequence	Q
	description	binding site for residue K32 D 503
	source	: AC3

17)	chain	C
	residue	280
	type
	sequence	S
	description	binding site for residue K32 D 503
	source	: AC3

18)	chain	D
	residue	255
	type
	sequence	V
	description	binding site for residue K32 D 503
	source	: AC3

19)	chain	D
	residue	259
	type
	sequence	M
	description	binding site for residue K32 D 503
	source	: AC3

20)	chain	D
	residue	277
	type
	sequence	Q
	description	binding site for residue K32 D 503
	source	: AC3

21)	chain	D
	residue	280
	type
	sequence	S
	description	binding site for residue K32 D 503
	source	: AC3

22)	chain	C
	residue	275
	type
	sequence	D
	description	binding site for residue MG D 504
	source	: AC4

23)	chain	C
	residue	279
	type
	sequence	D
	description	binding site for residue MG D 504
	source	: AC4

24)	chain	D
	residue	252
	type
	sequence	D
	description	binding site for residue MG D 504
	source	: AC4

25)	chain	E
	residue	77
	type
	sequence	T
	description	binding site for residue LMR F 501
	source	: AC5

26)	chain	E
	residue	94
	type
	sequence	S
	description	binding site for residue LMR F 501
	source	: AC5

27)	chain	E
	residue	96
	type
	sequence	N
	description	binding site for residue LMR F 501
	source	: AC5

28)	chain	E
	residue	100
	type
	sequence	R
	description	binding site for residue LMR F 501
	source	: AC5

29)	chain	E
	residue	109
	type
	sequence	R
	description	binding site for residue LMR F 501
	source	: AC5

30)	chain	E
	residue	132
	type
	sequence	R
	description	binding site for residue LMR F 501
	source	: AC5

31)	chain	E
	residue	139
	type
	sequence	Y
	description	binding site for residue LMR F 501
	source	: AC5

32)	chain	E
	residue	275
	type
	sequence	D
	description	binding site for residue LMR F 501
	source	: AC5

33)	chain	F
	residue	252
	type
	sequence	D
	description	binding site for residue LMR F 501
	source	: AC5

34)	chain	E
	residue	275
	type
	sequence	D
	description	binding site for residue MG F 502
	source	: AC6

35)	chain	E
	residue	279
	type
	sequence	D
	description	binding site for residue MG F 502
	source	: AC6

36)	chain	F
	residue	252
	type
	sequence	D
	description	binding site for residue MG F 502
	source	: AC6

37)	chain	A
	residue	252
	type
	sequence	D
	description	binding site for residue MG A 501
	source	: AC7

38)	chain	B
	residue	275
	type
	sequence	D
	description	binding site for residue MG A 501
	source	: AC7

39)	chain	B
	residue	279
	type
	sequence	D
	description	binding site for residue MG A 501
	source	: AC7

40)	chain	A
	residue	121
	type
	sequence	V
	description	binding site for residue K32 A 502
	source	: AC8

41)	chain	A
	residue	255
	type
	sequence	V
	description	binding site for residue K32 A 502
	source	: AC8

42)	chain	A
	residue	259
	type
	sequence	M
	description	binding site for residue K32 A 502
	source	: AC8

43)	chain	A
	residue	277
	type
	sequence	Q
	description	binding site for residue K32 A 502
	source	: AC8

44)	chain	A
	residue	280
	type
	sequence	S
	description	binding site for residue K32 A 502
	source	: AC8

45)	chain	B
	residue	121
	type
	sequence	V
	description	binding site for residue K32 A 502
	source	: AC8

46)	chain	B
	residue	255
	type
	sequence	V
	description	binding site for residue K32 A 502
	source	: AC8

47)	chain	B
	residue	259
	type
	sequence	M
	description	binding site for residue K32 A 502
	source	: AC8

48)	chain	B
	residue	277
	type
	sequence	Q
	description	binding site for residue K32 A 502
	source	: AC8

49)	chain	B
	residue	280
	type
	sequence	S
	description	binding site for residue K32 A 502
	source	: AC8

50)	chain	A
	residue	252
	type
	sequence	D
	description	binding site for residue LMR A 503
	source	: AC9

51)	chain	B
	residue	77
	type
	sequence	T
	description	binding site for residue LMR A 503
	source	: AC9

52)	chain	B
	residue	94
	type
	sequence	S
	description	binding site for residue LMR A 503
	source	: AC9

53)	chain	B
	residue	96
	type
	sequence	N
	description	binding site for residue LMR A 503
	source	: AC9

54)	chain	B
	residue	100
	type
	sequence	R
	description	binding site for residue LMR A 503
	source	: AC9

55)	chain	B
	residue	109
	type
	sequence	R
	description	binding site for residue LMR A 503
	source	: AC9

56)	chain	B
	residue	132
	type
	sequence	R
	description	binding site for residue LMR A 503
	source	: AC9

57)	chain	B
	residue	139
	type
	sequence	Y
	description	binding site for residue LMR A 503
	source	: AC9

58)	chain	B
	residue	275
	type
	sequence	D
	description	binding site for residue LMR A 503
	source	: AC9

59)	chain	E
	residue	121
	type
	sequence	V
	description	binding site for residue K32 E 501
	source	: AD1

60)	chain	E
	residue	255
	type
	sequence	V
	description	binding site for residue K32 E 501
	source	: AD1

61)	chain	E
	residue	259
	type
	sequence	M
	description	binding site for residue K32 E 501
	source	: AD1

62)	chain	E
	residue	277
	type
	sequence	Q
	description	binding site for residue K32 E 501
	source	: AD1

63)	chain	E
	residue	280
	type
	sequence	S
	description	binding site for residue K32 E 501
	source	: AD1

64)	chain	F
	residue	121
	type
	sequence	V
	description	binding site for residue K32 E 501
	source	: AD1

65)	chain	F
	residue	255
	type
	sequence	V
	description	binding site for residue K32 E 501
	source	: AD1

66)	chain	F
	residue	259
	type
	sequence	M
	description	binding site for residue K32 E 501
	source	: AD1

67)	chain	F
	residue	277
	type
	sequence	Q
	description	binding site for residue K32 E 501
	source	: AD1

68)	chain	F
	residue	280
	type
	sequence	S
	description	binding site for residue K32 E 501
	source	: AD1

69)	chain	D
	residue	271-290
	type	prosite
	sequence	NYDGDVQSDSVAQGYGSLGM
	description	IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NYDGDVqSDsvAqgy.GSLGM
	source	prosite : PS00470

70)	chain	D
	residue	75
	type	BINDING
	sequence	T
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI1

71)	chain	A
	residue	75
	type	BINDING
	sequence	T
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI1

72)	chain	A
	residue	310
	type	BINDING
	sequence	G
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI1

73)	chain	A
	residue	328
	type	BINDING
	sequence	N
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI1

74)	chain	E
	residue	75
	type	BINDING
	sequence	T
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI1

75)	chain	E
	residue	310
	type	BINDING
	sequence	G
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI1

76)	chain	E
	residue	328
	type	BINDING
	sequence	N
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI1

77)	chain	B
	residue	75
	type	BINDING
	sequence	T
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI1

78)	chain	B
	residue	310
	type	BINDING
	sequence	G
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI1

79)	chain	B
	residue	328
	type	BINDING
	sequence	N
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI1

80)	chain	D
	residue	310
	type	BINDING
	sequence	G
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI1

81)	chain	D
	residue	328
	type	BINDING
	sequence	N
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI1

82)	chain	C
	residue	75
	type	BINDING
	sequence	T
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI1

83)	chain	C
	residue	310
	type	BINDING
	sequence	G
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI1

84)	chain	C
	residue	328
	type	BINDING
	sequence	N
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI1

85)	chain	F
	residue	75
	type	BINDING
	sequence	T
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI1

86)	chain	F
	residue	310
	type	BINDING
	sequence	G
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI1

87)	chain	F
	residue	328
	type	BINDING
	sequence	N
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5L58, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI1

88)	chain	D
	residue	42
	type	MOD_RES
	sequence	Y
	description	Phosphotyrosine => ECO:0007744\|PubMed:24275569
	source	Swiss-Prot : SWS_FT_FI10

89)	chain	C
	residue	42
	type	MOD_RES
	sequence	Y
	description	Phosphotyrosine => ECO:0007744\|PubMed:24275569
	source	Swiss-Prot : SWS_FT_FI10

90)	chain	F
	residue	42
	type	MOD_RES
	sequence	Y
	description	Phosphotyrosine => ECO:0007744\|PubMed:24275569
	source	Swiss-Prot : SWS_FT_FI10

91)	chain	A
	residue	42
	type	MOD_RES
	sequence	Y
	description	Phosphotyrosine => ECO:0007744\|PubMed:24275569
	source	Swiss-Prot : SWS_FT_FI10

92)	chain	E
	residue	42
	type	MOD_RES
	sequence	Y
	description	Phosphotyrosine => ECO:0007744\|PubMed:24275569
	source	Swiss-Prot : SWS_FT_FI10

93)	chain	B
	residue	42
	type	MOD_RES
	sequence	Y
	description	Phosphotyrosine => ECO:0007744\|PubMed:24275569
	source	Swiss-Prot : SWS_FT_FI10

94)	chain	D
	residue	81
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

95)	chain	F
	residue	224
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

96)	chain	F
	residue	233
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

97)	chain	F
	residue	243
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

98)	chain	A
	residue	81
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

99)	chain	A
	residue	224
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

100)	chain	A
	residue	233
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

101)	chain	A
	residue	243
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

102)	chain	E
	residue	81
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

103)	chain	E
	residue	224
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

104)	chain	E
	residue	233
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

105)	chain	D
	residue	224
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

106)	chain	E
	residue	243
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

107)	chain	B
	residue	81
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

108)	chain	B
	residue	224
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

109)	chain	B
	residue	233
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

110)	chain	B
	residue	243
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

111)	chain	D
	residue	233
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

112)	chain	D
	residue	243
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

113)	chain	C
	residue	81
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

114)	chain	C
	residue	224
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

115)	chain	C
	residue	233
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

116)	chain	C
	residue	243
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

117)	chain	F
	residue	81
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI11

118)	chain	D
	residue	126
	type	MOD_RES
	sequence	K
	description	N6-succinyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI12

119)	chain	E
	residue	400
	type	MOD_RES
	sequence	K
	description	N6-succinyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI12

120)	chain	B
	residue	126
	type	MOD_RES
	sequence	K
	description	N6-succinyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI12

121)	chain	B
	residue	400
	type	MOD_RES
	sequence	K
	description	N6-succinyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI12

122)	chain	D
	residue	400
	type	MOD_RES
	sequence	K
	description	N6-succinyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI12

123)	chain	C
	residue	126
	type	MOD_RES
	sequence	K
	description	N6-succinyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI12

124)	chain	C
	residue	400
	type	MOD_RES
	sequence	K
	description	N6-succinyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI12

125)	chain	F
	residue	126
	type	MOD_RES
	sequence	K
	description	N6-succinyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI12

126)	chain	F
	residue	400
	type	MOD_RES
	sequence	K
	description	N6-succinyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI12

127)	chain	A
	residue	126
	type	MOD_RES
	sequence	K
	description	N6-succinyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI12

128)	chain	A
	residue	400
	type	MOD_RES
	sequence	K
	description	N6-succinyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI12

129)	chain	E
	residue	126
	type	MOD_RES
	sequence	K
	description	N6-succinyllysine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI12

130)	chain	D
	residue	321
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0007744\|PubMed:19608861
	source	Swiss-Prot : SWS_FT_FI13

131)	chain	C
	residue	321
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0007744\|PubMed:19608861
	source	Swiss-Prot : SWS_FT_FI13

132)	chain	F
	residue	321
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0007744\|PubMed:19608861
	source	Swiss-Prot : SWS_FT_FI13

133)	chain	A
	residue	321
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0007744\|PubMed:19608861
	source	Swiss-Prot : SWS_FT_FI13

134)	chain	E
	residue	321
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0007744\|PubMed:19608861
	source	Swiss-Prot : SWS_FT_FI13

135)	chain	B
	residue	321
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0007744\|PubMed:19608861
	source	Swiss-Prot : SWS_FT_FI13

136)	chain	D
	residue	389
	type	MOD_RES
	sequence	S
	description	Phosphoserine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI14

137)	chain	C
	residue	389
	type	MOD_RES
	sequence	S
	description	Phosphoserine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI14

138)	chain	F
	residue	389
	type	MOD_RES
	sequence	S
	description	Phosphoserine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI14

139)	chain	A
	residue	389
	type	MOD_RES
	sequence	S
	description	Phosphoserine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI14

140)	chain	E
	residue	389
	type	MOD_RES
	sequence	S
	description	Phosphoserine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI14

141)	chain	B
	residue	389
	type	MOD_RES
	sequence	S
	description	Phosphoserine => ECO:0000250\|UniProtKB:O88844
	source	Swiss-Prot : SWS_FT_FI14

142)	chain	D
	residue	77
	type	BINDING
	sequence	T
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

143)	chain	F
	residue	94
	type	BINDING
	sequence	S
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

144)	chain	F
	residue	109
	type	BINDING
	sequence	R
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

145)	chain	F
	residue	132
	type	BINDING
	sequence	R
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

146)	chain	A
	residue	77
	type	BINDING
	sequence	T
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

147)	chain	A
	residue	94
	type	BINDING
	sequence	S
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

148)	chain	A
	residue	109
	type	BINDING
	sequence	R
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

149)	chain	A
	residue	132
	type	BINDING
	sequence	R
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

150)	chain	E
	residue	77
	type	BINDING
	sequence	T
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

151)	chain	E
	residue	94
	type	BINDING
	sequence	S
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

152)	chain	E
	residue	109
	type	BINDING
	sequence	R
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

153)	chain	D
	residue	94
	type	BINDING
	sequence	S
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

154)	chain	E
	residue	132
	type	BINDING
	sequence	R
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

155)	chain	B
	residue	77
	type	BINDING
	sequence	T
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

156)	chain	B
	residue	94
	type	BINDING
	sequence	S
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

157)	chain	B
	residue	109
	type	BINDING
	sequence	R
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

158)	chain	B
	residue	132
	type	BINDING
	sequence	R
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

159)	chain	D
	residue	109
	type	BINDING
	sequence	R
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

160)	chain	D
	residue	132
	type	BINDING
	sequence	R
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

161)	chain	C
	residue	77
	type	BINDING
	sequence	T
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

162)	chain	C
	residue	94
	type	BINDING
	sequence	S
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

163)	chain	C
	residue	109
	type	BINDING
	sequence	R
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

164)	chain	C
	residue	132
	type	BINDING
	sequence	R
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

165)	chain	F
	residue	77
	type	BINDING
	sequence	T
	description	in other chain => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI2

166)	chain	D
	residue	82
	type	BINDING
	sequence	R
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI3

167)	chain	C
	residue	82
	type	BINDING
	sequence	R
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI3

168)	chain	F
	residue	82
	type	BINDING
	sequence	R
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI3

169)	chain	A
	residue	82
	type	BINDING
	sequence	R
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI3

170)	chain	E
	residue	82
	type	BINDING
	sequence	R
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI3

171)	chain	B
	residue	82
	type	BINDING
	sequence	R
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T09, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM, ECO:0007744\|PDB:3MAP, ECO:0007744\|PDB:3MAR, ECO:0007744\|PDB:3MAS, ECO:0007744\|PDB:4I3K, ECO:0007744\|PDB:4I3L, ECO:0007744\|PDB:4KZO, ECO:0007744\|PDB:4L03, ECO:0007744\|PDB:4L04, ECO:0007744\|PDB:4L06, ECO:0007744\|PDB:4UMX, ECO:0007744\|PDB:4UMY, ECO:0007744\|PDB:4XRX, ECO:0007744\|PDB:4XS3, ECO:0007744\|PDB:5DE1, ECO:0007744\|PDB:5L57, ECO:0007744\|PDB:5LGE, ECO:0007744\|PDB:5SUN, ECO:0007744\|PDB:5SVF, ECO:0007744\|PDB:5TQH
	source	Swiss-Prot : SWS_FT_FI3

172)	chain	D
	residue	212
	type	BINDING
	sequence	K
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI4

173)	chain	C
	residue	212
	type	BINDING
	sequence	K
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI4

174)	chain	F
	residue	212
	type	BINDING
	sequence	K
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI4

175)	chain	A
	residue	212
	type	BINDING
	sequence	K
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI4

176)	chain	E
	residue	212
	type	BINDING
	sequence	K
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI4

177)	chain	B
	residue	212
	type	BINDING
	sequence	K
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0007744\|PDB:1T0L
	source	Swiss-Prot : SWS_FT_FI4

178)	chain	D
	residue	252
	type	BINDING
	sequence	D
	description	BINDING => ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI5

179)	chain	C
	residue	252
	type	BINDING
	sequence	D
	description	BINDING => ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI5

180)	chain	F
	residue	252
	type	BINDING
	sequence	D
	description	BINDING => ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI5

181)	chain	A
	residue	252
	type	BINDING
	sequence	D
	description	BINDING => ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI5

182)	chain	E
	residue	252
	type	BINDING
	sequence	D
	description	BINDING => ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI5

183)	chain	B
	residue	252
	type	BINDING
	sequence	D
	description	BINDING => ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI5

184)	chain	D
	residue	260
	type	BINDING
	sequence	K
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI6

185)	chain	C
	residue	260
	type	BINDING
	sequence	K
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI6

186)	chain	F
	residue	260
	type	BINDING
	sequence	K
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI6

187)	chain	A
	residue	260
	type	BINDING
	sequence	K
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI6

188)	chain	E
	residue	260
	type	BINDING
	sequence	K
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI6

189)	chain	B
	residue	260
	type	BINDING
	sequence	K
	description	BINDING => ECO:0000269\|PubMed:15173171, ECO:0000269\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI6

190)	chain	D
	residue	275
	type	BINDING
	sequence	D
	description	in other chain => ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI7

191)	chain	E
	residue	279
	type	BINDING
	sequence	D
	description	in other chain => ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI7

192)	chain	B
	residue	275
	type	BINDING
	sequence	D
	description	in other chain => ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI7

193)	chain	B
	residue	279
	type	BINDING
	sequence	D
	description	in other chain => ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI7

194)	chain	D
	residue	279
	type	BINDING
	sequence	D
	description	in other chain => ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI7

195)	chain	C
	residue	275
	type	BINDING
	sequence	D
	description	in other chain => ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI7

196)	chain	C
	residue	279
	type	BINDING
	sequence	D
	description	in other chain => ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI7

197)	chain	F
	residue	275
	type	BINDING
	sequence	D
	description	in other chain => ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI7

198)	chain	F
	residue	279
	type	BINDING
	sequence	D
	description	in other chain => ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI7

199)	chain	A
	residue	275
	type	BINDING
	sequence	D
	description	in other chain => ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI7

200)	chain	A
	residue	279
	type	BINDING
	sequence	D
	description	in other chain => ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI7

201)	chain	E
	residue	275
	type	BINDING
	sequence	D
	description	in other chain => ECO:0000305\|PubMed:15173171, ECO:0000305\|PubMed:19935646, ECO:0007744\|PDB:1T0L, ECO:0007744\|PDB:3INM
	source	Swiss-Prot : SWS_FT_FI7

202)	chain	D
	residue	139
	type	SITE
	sequence	Y
	description	Critical for catalysis
	source	Swiss-Prot : SWS_FT_FI8

203)	chain	E
	residue	212
	type	SITE
	sequence	K
	description	Critical for catalysis
	source	Swiss-Prot : SWS_FT_FI8

204)	chain	B
	residue	139
	type	SITE
	sequence	Y
	description	Critical for catalysis
	source	Swiss-Prot : SWS_FT_FI8

205)	chain	B
	residue	212
	type	SITE
	sequence	K
	description	Critical for catalysis
	source	Swiss-Prot : SWS_FT_FI8

206)	chain	D
	residue	212
	type	SITE
	sequence	K
	description	Critical for catalysis
	source	Swiss-Prot : SWS_FT_FI8

207)	chain	C
	residue	139
	type	SITE
	sequence	Y
	description	Critical for catalysis
	source	Swiss-Prot : SWS_FT_FI8

208)	chain	C
	residue	212
	type	SITE
	sequence	K
	description	Critical for catalysis
	source	Swiss-Prot : SWS_FT_FI8

209)	chain	F
	residue	139
	type	SITE
	sequence	Y
	description	Critical for catalysis
	source	Swiss-Prot : SWS_FT_FI8

210)	chain	F
	residue	212
	type	SITE
	sequence	K
	description	Critical for catalysis
	source	Swiss-Prot : SWS_FT_FI8

211)	chain	A
	residue	139
	type	SITE
	sequence	Y
	description	Critical for catalysis
	source	Swiss-Prot : SWS_FT_FI8

212)	chain	A
	residue	212
	type	SITE
	sequence	K
	description	Critical for catalysis
	source	Swiss-Prot : SWS_FT_FI8

213)	chain	E
	residue	139
	type	SITE
	sequence	Y
	description	Critical for catalysis
	source	Swiss-Prot : SWS_FT_FI8