eF-site ID 1bfr-ABCDEFGHIJKLMNOPQRSTUVWX
PDB Code 1bfr
Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Title IRON STORAGE AND ELECTRON TRANSPORT
Classification ELECTRON TRANSPORT
Compound BACTERIOFERRITIN
Source ORGANISM_SCIENTIFIC: Escherichia coli;
Sequence A:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
B:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
C:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
D:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
E:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
F:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
G:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
H:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
I:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
J:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
K:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
L:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
M:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
N:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
O:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
P:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
Q:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
R:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
S:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
T:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
U:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
V:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
W:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
X:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL
NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG
EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM
IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
Description


Functional site

1) chain A
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MA

2) chain A
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MA

3) chain A
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MA

4) chain A
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MA

5) chain A
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MA

6) chain A
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MA

7) chain B
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MB

8) chain B
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MB

9) chain B
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MB

10) chain B
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MB

11) chain B
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MB

12) chain B
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MB

13) chain C
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MC

14) chain C
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MC

15) chain C
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MC

16) chain C
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MC

17) chain C
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MC

18) chain C
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MC

19) chain D
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MD

20) chain D
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MD

21) chain D
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MD

22) chain D
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MD

23) chain D
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MD

24) chain D
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MD

25) chain E
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : ME

26) chain E
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : ME

27) chain E
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : ME

28) chain E
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : ME

29) chain E
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : ME

30) chain E
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : ME

31) chain F
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MF

32) chain F
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MF

33) chain F
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MF

34) chain F
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MF

35) chain F
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MF

36) chain F
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MF

37) chain G
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MG

38) chain G
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MG

39) chain G
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MG

40) chain G
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MG

41) chain G
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MG

42) chain G
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MG

43) chain H
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MH

44) chain H
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MH

45) chain H
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MH

46) chain H
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MH

47) chain H
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MH

48) chain H
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MH

49) chain I
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MI

50) chain I
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MI

51) chain I
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MI

52) chain I
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MI

53) chain I
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MI

54) chain I
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MI

55) chain J
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MJ

56) chain J
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MJ

57) chain J
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MJ

58) chain J
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MJ

59) chain J
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MJ

60) chain J
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MJ

61) chain K
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MK

62) chain K
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MK

63) chain K
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MK

64) chain K
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MK

65) chain K
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MK

66) chain K
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MK

67) chain L
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : ML

68) chain L
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : ML

69) chain L
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : ML

70) chain L
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : ML

71) chain L
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : ML

72) chain L
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : ML

73) chain M
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MM

74) chain M
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MM

75) chain M
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MM

76) chain M
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MM

77) chain M
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MM

78) chain M
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MM

79) chain N
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MN

80) chain N
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MN

81) chain N
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MN

82) chain N
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MN

83) chain N
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MN

84) chain N
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MN

85) chain O
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MO

86) chain O
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MO

87) chain O
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MO

88) chain O
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MO

89) chain O
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MO

90) chain O
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MO

91) chain P
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MP

92) chain P
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MP

93) chain P
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MP

94) chain P
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MP

95) chain P
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MP

96) chain P
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MP

97) chain Q
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MQ

98) chain Q
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MQ

99) chain Q
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MQ

100) chain Q
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MQ

101) chain Q
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MQ

102) chain Q
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MQ

103) chain R
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MR

104) chain R
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MR

105) chain R
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MR

106) chain R
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MR

107) chain R
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MR

108) chain R
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MR

109) chain S
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MS

110) chain S
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MS

111) chain S
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MS

112) chain S
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MS

113) chain S
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MS

114) chain S
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MS

115) chain T
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MT

116) chain T
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MT

117) chain T
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MT

118) chain T
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MT

119) chain T
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MT

120) chain T
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MT

121) chain U
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MU

122) chain U
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MU

123) chain U
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MU

124) chain U
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MU

125) chain U
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MU

126) chain U
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MU

127) chain V
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MV

128) chain V
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MV

129) chain V
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MV

130) chain V
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MV

131) chain V
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MV

132) chain V
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MV

133) chain W
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MW

134) chain W
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MW

135) chain W
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MW

136) chain W
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MW

137) chain W
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MW

138) chain W
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MW

139) chain X
residue 18
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MX

140) chain X
residue 51
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MX

141) chain X
residue 54
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MX

142) chain X
residue 94
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MX

143) chain X
residue 127
type
sequence E
description BINUCLEAR METAL-BINDING SITE
source : MX

144) chain X
residue 130
type
sequence H
description BINUCLEAR METAL-BINDING SITE
source : MX

145) chain A
residue 25
type
sequence Y
description BINDING SITE FOR RESIDUE MN A 201
source : AC1

146) chain A
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN A 201
source : AC1

147) chain A
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN A 201
source : AC1

148) chain A
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN A 201
source : AC1

149) chain A
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN A 201
source : AC1

150) chain A
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN A 202
source : AC2

151) chain A
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN A 202
source : AC2

152) chain A
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN A 202
source : AC2

153) chain A
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN A 202
source : AC2

154) chain B
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN B 201
source : AC3

155) chain B
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN B 201
source : AC3

156) chain B
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN B 201
source : AC3

157) chain B
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN B 201
source : AC3

158) chain B
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN B 202
source : AC4

159) chain B
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN B 202
source : AC4

160) chain B
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN B 202
source : AC4

161) chain B
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN B 202
source : AC4

162) chain C
residue 25
type
sequence Y
description BINDING SITE FOR RESIDUE MN C 201
source : AC5

163) chain C
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN C 201
source : AC5

164) chain C
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN C 201
source : AC5

165) chain C
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN C 201
source : AC5

166) chain C
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN C 201
source : AC5

167) chain C
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN C 202
source : AC6

168) chain C
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN C 202
source : AC6

169) chain C
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN C 202
source : AC6

170) chain C
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN C 202
source : AC6

171) chain D
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN D 201
source : AC7

172) chain D
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN D 201
source : AC7

173) chain D
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN D 201
source : AC7

174) chain D
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN D 201
source : AC7

175) chain D
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN D 202
source : AC8

176) chain D
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN D 202
source : AC8

177) chain D
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN D 202
source : AC8

178) chain D
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN D 202
source : AC8

179) chain E
residue 25
type
sequence Y
description BINDING SITE FOR RESIDUE MN E 201
source : AC9

180) chain E
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN E 201
source : AC9

181) chain E
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN E 201
source : AC9

182) chain E
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN E 201
source : AC9

183) chain E
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN E 201
source : AC9

184) chain E
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN E 202
source : BC1

185) chain E
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN E 202
source : BC1

186) chain E
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN E 202
source : BC1

187) chain E
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN E 202
source : BC1

188) chain F
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN F 201
source : BC2

189) chain F
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN F 201
source : BC2

190) chain F
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN F 201
source : BC2

191) chain F
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN F 201
source : BC2

192) chain F
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN F 202
source : BC3

193) chain F
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN F 202
source : BC3

194) chain F
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN F 202
source : BC3

195) chain F
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN F 202
source : BC3

196) chain G
residue 25
type
sequence Y
description BINDING SITE FOR RESIDUE MN G 201
source : BC4

197) chain G
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN G 201
source : BC4

198) chain G
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN G 201
source : BC4

199) chain G
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN G 201
source : BC4

200) chain G
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN G 201
source : BC4

201) chain G
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN G 202
source : BC5

202) chain G
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN G 202
source : BC5

203) chain G
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN G 202
source : BC5

204) chain G
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN G 202
source : BC5

205) chain H
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN H 201
source : BC6

206) chain H
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN H 201
source : BC6

207) chain H
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN H 201
source : BC6

208) chain H
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN H 201
source : BC6

209) chain H
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN H 202
source : BC7

210) chain H
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN H 202
source : BC7

211) chain H
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN H 202
source : BC7

212) chain H
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN H 202
source : BC7

213) chain I
residue 25
type
sequence Y
description BINDING SITE FOR RESIDUE MN I 201
source : BC8

214) chain I
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN I 201
source : BC8

215) chain I
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN I 201
source : BC8

216) chain I
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN I 201
source : BC8

217) chain I
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN I 201
source : BC8

218) chain I
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN I 202
source : BC9

219) chain I
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN I 202
source : BC9

220) chain I
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN I 202
source : BC9

221) chain I
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN I 202
source : BC9

222) chain J
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN J 201
source : CC1

223) chain J
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN J 201
source : CC1

224) chain J
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN J 201
source : CC1

225) chain J
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN J 201
source : CC1

226) chain J
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN J 202
source : CC2

227) chain J
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN J 202
source : CC2

228) chain J
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN J 202
source : CC2

229) chain J
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN J 202
source : CC2

230) chain K
residue 25
type
sequence Y
description BINDING SITE FOR RESIDUE MN K 201
source : CC3

231) chain K
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN K 201
source : CC3

232) chain K
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN K 201
source : CC3

233) chain K
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN K 201
source : CC3

234) chain K
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN K 201
source : CC3

235) chain K
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN K 202
source : CC4

236) chain K
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN K 202
source : CC4

237) chain K
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN K 202
source : CC4

238) chain K
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN K 202
source : CC4

239) chain L
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN L 201
source : CC5

240) chain L
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN L 201
source : CC5

241) chain L
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN L 201
source : CC5

242) chain L
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN L 201
source : CC5

243) chain L
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN L 202
source : CC6

244) chain L
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN L 202
source : CC6

245) chain L
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN L 202
source : CC6

246) chain L
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN L 202
source : CC6

247) chain M
residue 25
type
sequence Y
description BINDING SITE FOR RESIDUE MN M 201
source : CC7

248) chain M
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN M 201
source : CC7

249) chain M
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN M 201
source : CC7

250) chain M
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN M 201
source : CC7

251) chain M
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN M 201
source : CC7

252) chain M
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN M 202
source : CC8

253) chain M
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN M 202
source : CC8

254) chain M
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN M 202
source : CC8

255) chain M
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN M 202
source : CC8

256) chain N
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN N 201
source : CC9

257) chain N
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN N 201
source : CC9

258) chain N
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN N 201
source : CC9

259) chain N
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN N 201
source : CC9

260) chain N
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN N 202
source : DC1

261) chain N
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN N 202
source : DC1

262) chain N
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN N 202
source : DC1

263) chain N
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN N 202
source : DC1

264) chain O
residue 25
type
sequence Y
description BINDING SITE FOR RESIDUE MN O 201
source : DC2

265) chain O
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN O 201
source : DC2

266) chain O
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN O 201
source : DC2

267) chain O
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN O 201
source : DC2

268) chain O
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN O 201
source : DC2

269) chain O
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN O 202
source : DC3

270) chain O
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN O 202
source : DC3

271) chain O
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN O 202
source : DC3

272) chain O
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN O 202
source : DC3

273) chain P
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN P 201
source : DC4

274) chain P
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN P 201
source : DC4

275) chain P
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN P 201
source : DC4

276) chain P
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN P 201
source : DC4

277) chain P
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN P 202
source : DC5

278) chain P
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN P 202
source : DC5

279) chain P
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN P 202
source : DC5

280) chain P
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN P 202
source : DC5

281) chain Q
residue 25
type
sequence Y
description BINDING SITE FOR RESIDUE MN Q 201
source : DC6

282) chain Q
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN Q 201
source : DC6

283) chain Q
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN Q 201
source : DC6

284) chain Q
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN Q 201
source : DC6

285) chain Q
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN Q 201
source : DC6

286) chain Q
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN Q 202
source : DC7

287) chain Q
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN Q 202
source : DC7

288) chain Q
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN Q 202
source : DC7

289) chain Q
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN Q 202
source : DC7

290) chain R
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN R 201
source : DC8

291) chain R
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN R 201
source : DC8

292) chain R
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN R 201
source : DC8

293) chain R
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN R 201
source : DC8

294) chain R
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN R 202
source : DC9

295) chain R
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN R 202
source : DC9

296) chain R
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN R 202
source : DC9

297) chain R
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN R 202
source : DC9

298) chain S
residue 25
type
sequence Y
description BINDING SITE FOR RESIDUE MN S 201
source : EC1

299) chain S
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN S 201
source : EC1

300) chain S
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN S 201
source : EC1

301) chain S
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN S 201
source : EC1

302) chain S
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN S 201
source : EC1

303) chain S
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN S 202
source : EC2

304) chain S
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN S 202
source : EC2

305) chain S
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN S 202
source : EC2

306) chain S
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN S 202
source : EC2

307) chain T
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN T 201
source : EC3

308) chain T
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN T 201
source : EC3

309) chain T
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN T 201
source : EC3

310) chain T
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN T 201
source : EC3

311) chain T
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN T 202
source : EC4

312) chain T
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN T 202
source : EC4

313) chain T
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN T 202
source : EC4

314) chain T
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN T 202
source : EC4

315) chain U
residue 25
type
sequence Y
description BINDING SITE FOR RESIDUE MN U 201
source : EC5

316) chain U
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN U 201
source : EC5

317) chain U
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN U 201
source : EC5

318) chain U
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN U 201
source : EC5

319) chain U
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN U 201
source : EC5

320) chain U
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN U 202
source : EC6

321) chain U
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN U 202
source : EC6

322) chain U
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN U 202
source : EC6

323) chain U
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN U 202
source : EC6

324) chain V
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN V 201
source : EC7

325) chain V
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN V 201
source : EC7

326) chain V
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN V 201
source : EC7

327) chain V
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN V 201
source : EC7

328) chain V
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN V 202
source : EC8

329) chain V
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN V 202
source : EC8

330) chain V
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN V 202
source : EC8

331) chain V
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN V 202
source : EC8

332) chain W
residue 25
type
sequence Y
description BINDING SITE FOR RESIDUE MN W 201
source : EC9

333) chain W
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN W 201
source : EC9

334) chain W
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN W 201
source : EC9

335) chain W
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN W 201
source : EC9

336) chain W
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN W 201
source : EC9

337) chain W
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN W 202
source : FC1

338) chain W
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN W 202
source : FC1

339) chain W
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN W 202
source : FC1

340) chain W
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN W 202
source : FC1

341) chain X
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN X 201
source : FC2

342) chain X
residue 94
type
sequence E
description BINDING SITE FOR RESIDUE MN X 201
source : FC2

343) chain X
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN X 201
source : FC2

344) chain X
residue 130
type
sequence H
description BINDING SITE FOR RESIDUE MN X 201
source : FC2

345) chain X
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE MN X 202
source : FC3

346) chain X
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE MN X 202
source : FC3

347) chain X
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE MN X 202
source : FC3

348) chain X
residue 127
type
sequence E
description BINDING SITE FOR RESIDUE MN X 202
source : FC3

349) chain A
residue 23
type
sequence N
description BINDING SITE FOR RESIDUE HEM B 200
source : FC4

350) chain A
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM B 200
source : FC4

351) chain A
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM B 200
source : FC4

352) chain A
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM B 200
source : FC4

353) chain A
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM B 200
source : FC4

354) chain A
residue 55
type
sequence A
description BINDING SITE FOR RESIDUE HEM B 200
source : FC4

355) chain A
residue 56
type
sequence D
description BINDING SITE FOR RESIDUE HEM B 200
source : FC4

356) chain B
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM B 200
source : FC4

357) chain B
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM B 200
source : FC4

358) chain B
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM B 200
source : FC4

359) chain B
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM B 200
source : FC4

360) chain C
residue 23
type
sequence N
description BINDING SITE FOR RESIDUE HEM D 200
source : FC5

361) chain C
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM D 200
source : FC5

362) chain C
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM D 200
source : FC5

363) chain C
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM D 200
source : FC5

364) chain C
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM D 200
source : FC5

365) chain C
residue 55
type
sequence A
description BINDING SITE FOR RESIDUE HEM D 200
source : FC5

366) chain C
residue 56
type
sequence D
description BINDING SITE FOR RESIDUE HEM D 200
source : FC5

367) chain D
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM D 200
source : FC5

368) chain D
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM D 200
source : FC5

369) chain D
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM D 200
source : FC5

370) chain D
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM D 200
source : FC5

371) chain E
residue 23
type
sequence N
description BINDING SITE FOR RESIDUE HEM F 200
source : FC6

372) chain E
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM F 200
source : FC6

373) chain E
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM F 200
source : FC6

374) chain E
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM F 200
source : FC6

375) chain E
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM F 200
source : FC6

376) chain E
residue 55
type
sequence A
description BINDING SITE FOR RESIDUE HEM F 200
source : FC6

377) chain E
residue 56
type
sequence D
description BINDING SITE FOR RESIDUE HEM F 200
source : FC6

378) chain F
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM F 200
source : FC6

379) chain F
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM F 200
source : FC6

380) chain F
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM F 200
source : FC6

381) chain F
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM F 200
source : FC6

382) chain G
residue 23
type
sequence N
description BINDING SITE FOR RESIDUE HEM H 200
source : FC7

383) chain G
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM H 200
source : FC7

384) chain G
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM H 200
source : FC7

385) chain G
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM H 200
source : FC7

386) chain G
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM H 200
source : FC7

387) chain G
residue 55
type
sequence A
description BINDING SITE FOR RESIDUE HEM H 200
source : FC7

388) chain G
residue 56
type
sequence D
description BINDING SITE FOR RESIDUE HEM H 200
source : FC7

389) chain H
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM H 200
source : FC7

390) chain H
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM H 200
source : FC7

391) chain H
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM H 200
source : FC7

392) chain H
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM H 200
source : FC7

393) chain I
residue 23
type
sequence N
description BINDING SITE FOR RESIDUE HEM J 200
source : FC8

394) chain I
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM J 200
source : FC8

395) chain I
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM J 200
source : FC8

396) chain I
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM J 200
source : FC8

397) chain I
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM J 200
source : FC8

398) chain I
residue 55
type
sequence A
description BINDING SITE FOR RESIDUE HEM J 200
source : FC8

399) chain I
residue 56
type
sequence D
description BINDING SITE FOR RESIDUE HEM J 200
source : FC8

400) chain J
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM J 200
source : FC8

401) chain J
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM J 200
source : FC8

402) chain J
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM J 200
source : FC8

403) chain J
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM J 200
source : FC8

404) chain K
residue 23
type
sequence N
description BINDING SITE FOR RESIDUE HEM L 200
source : FC9

405) chain K
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM L 200
source : FC9

406) chain K
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM L 200
source : FC9

407) chain K
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM L 200
source : FC9

408) chain K
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM L 200
source : FC9

409) chain K
residue 55
type
sequence A
description BINDING SITE FOR RESIDUE HEM L 200
source : FC9

410) chain K
residue 56
type
sequence D
description BINDING SITE FOR RESIDUE HEM L 200
source : FC9

411) chain L
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM L 200
source : FC9

412) chain L
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM L 200
source : FC9

413) chain L
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM L 200
source : FC9

414) chain L
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM L 200
source : FC9

415) chain M
residue 23
type
sequence N
description BINDING SITE FOR RESIDUE HEM N 200
source : GC1

416) chain M
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM N 200
source : GC1

417) chain M
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM N 200
source : GC1

418) chain M
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM N 200
source : GC1

419) chain M
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM N 200
source : GC1

420) chain M
residue 55
type
sequence A
description BINDING SITE FOR RESIDUE HEM N 200
source : GC1

421) chain M
residue 56
type
sequence D
description BINDING SITE FOR RESIDUE HEM N 200
source : GC1

422) chain N
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM N 200
source : GC1

423) chain N
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM N 200
source : GC1

424) chain N
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM N 200
source : GC1

425) chain N
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM N 200
source : GC1

426) chain O
residue 23
type
sequence N
description BINDING SITE FOR RESIDUE HEM P 200
source : GC2

427) chain O
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM P 200
source : GC2

428) chain O
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM P 200
source : GC2

429) chain O
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM P 200
source : GC2

430) chain O
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM P 200
source : GC2

431) chain O
residue 55
type
sequence A
description BINDING SITE FOR RESIDUE HEM P 200
source : GC2

432) chain O
residue 56
type
sequence D
description BINDING SITE FOR RESIDUE HEM P 200
source : GC2

433) chain P
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM P 200
source : GC2

434) chain P
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM P 200
source : GC2

435) chain P
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM P 200
source : GC2

436) chain P
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM P 200
source : GC2

437) chain Q
residue 23
type
sequence N
description BINDING SITE FOR RESIDUE HEM R 200
source : GC3

438) chain Q
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM R 200
source : GC3

439) chain Q
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM R 200
source : GC3

440) chain Q
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM R 200
source : GC3

441) chain Q
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM R 200
source : GC3

442) chain Q
residue 55
type
sequence A
description BINDING SITE FOR RESIDUE HEM R 200
source : GC3

443) chain Q
residue 56
type
sequence D
description BINDING SITE FOR RESIDUE HEM R 200
source : GC3

444) chain R
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM R 200
source : GC3

445) chain R
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM R 200
source : GC3

446) chain R
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM R 200
source : GC3

447) chain R
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM R 200
source : GC3

448) chain S
residue 23
type
sequence N
description BINDING SITE FOR RESIDUE HEM T 200
source : GC4

449) chain S
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM T 200
source : GC4

450) chain S
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM T 200
source : GC4

451) chain S
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM T 200
source : GC4

452) chain S
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM T 200
source : GC4

453) chain S
residue 55
type
sequence A
description BINDING SITE FOR RESIDUE HEM T 200
source : GC4

454) chain S
residue 56
type
sequence D
description BINDING SITE FOR RESIDUE HEM T 200
source : GC4

455) chain T
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM T 200
source : GC4

456) chain T
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM T 200
source : GC4

457) chain T
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM T 200
source : GC4

458) chain T
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM T 200
source : GC4

459) chain U
residue 23
type
sequence N
description BINDING SITE FOR RESIDUE HEM V 200
source : GC5

460) chain U
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM V 200
source : GC5

461) chain U
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM V 200
source : GC5

462) chain U
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM V 200
source : GC5

463) chain U
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM V 200
source : GC5

464) chain U
residue 55
type
sequence A
description BINDING SITE FOR RESIDUE HEM V 200
source : GC5

465) chain U
residue 56
type
sequence D
description BINDING SITE FOR RESIDUE HEM V 200
source : GC5

466) chain V
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM V 200
source : GC5

467) chain V
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM V 200
source : GC5

468) chain V
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM V 200
source : GC5

469) chain V
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM V 200
source : GC5

470) chain W
residue 23
type
sequence N
description BINDING SITE FOR RESIDUE HEM X 200
source : GC6

471) chain W
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM X 200
source : GC6

472) chain W
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM X 200
source : GC6

473) chain W
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM X 200
source : GC6

474) chain W
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM X 200
source : GC6

475) chain W
residue 55
type
sequence A
description BINDING SITE FOR RESIDUE HEM X 200
source : GC6

476) chain W
residue 56
type
sequence D
description BINDING SITE FOR RESIDUE HEM X 200
source : GC6

477) chain X
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE HEM X 200
source : GC6

478) chain X
residue 45
type
sequence Y
description BINDING SITE FOR RESIDUE HEM X 200
source : GC6

479) chain X
residue 52
type
sequence M
description BINDING SITE FOR RESIDUE HEM X 200
source : GC6

480) chain X
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE HEM X 200
source : GC6

481) chain A
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

482) chain B
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

483) chain M
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

484) chain M
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

485) chain M
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

486) chain M
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

487) chain M
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

488) chain N
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

489) chain N
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

490) chain N
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

491) chain N
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

492) chain N
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

493) chain B
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

494) chain N
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

495) chain N
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

496) chain N
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

497) chain O
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

498) chain O
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

499) chain O
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

500) chain O
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

501) chain O
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

502) chain O
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

503) chain O
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

504) chain B
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

505) chain O
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

506) chain P
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

507) chain P
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

508) chain P
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

509) chain P
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

510) chain P
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

511) chain P
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

512) chain P
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

513) chain P
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

514) chain Q
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

515) chain B
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

516) chain Q
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

517) chain Q
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

518) chain Q
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

519) chain Q
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

520) chain Q
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

521) chain Q
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

522) chain Q
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

523) chain R
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

524) chain R
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

525) chain R
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

526) chain B
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

527) chain R
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

528) chain R
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

529) chain R
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

530) chain R
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

531) chain R
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

532) chain S
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

533) chain S
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

534) chain S
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

535) chain S
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

536) chain S
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

537) chain B
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

538) chain S
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

539) chain S
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

540) chain S
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

541) chain T
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

542) chain T
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

543) chain T
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

544) chain T
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

545) chain T
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

546) chain T
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

547) chain T
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

548) chain B
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

549) chain T
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

550) chain U
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

551) chain U
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

552) chain U
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

553) chain U
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

554) chain U
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

555) chain U
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

556) chain U
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

557) chain U
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

558) chain V
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

559) chain C
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

560) chain V
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

561) chain V
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

562) chain V
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

563) chain V
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

564) chain V
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

565) chain V
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

566) chain V
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

567) chain W
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

568) chain W
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

569) chain W
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

570) chain C
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

571) chain W
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

572) chain W
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

573) chain W
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

574) chain W
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

575) chain W
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

576) chain X
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

577) chain X
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

578) chain X
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

579) chain X
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

580) chain X
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

581) chain C
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

582) chain X
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

583) chain X
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

584) chain X
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

585) chain A
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

586) chain C
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

587) chain C
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

588) chain C
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

589) chain C
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

590) chain C
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

591) chain D
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

592) chain D
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

593) chain D
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

594) chain D
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

595) chain D
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

596) chain A
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

597) chain D
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

598) chain D
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

599) chain D
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

600) chain E
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

601) chain E
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

602) chain E
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

603) chain E
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

604) chain E
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

605) chain E
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

606) chain E
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

607) chain A
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

608) chain E
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

609) chain F
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

610) chain F
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

611) chain F
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

612) chain F
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

613) chain F
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

614) chain F
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

615) chain F
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

616) chain F
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

617) chain G
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

618) chain A
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

619) chain G
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

620) chain G
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

621) chain G
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

622) chain G
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

623) chain G
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

624) chain G
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

625) chain G
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

626) chain H
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

627) chain H
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

628) chain H
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

629) chain A
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

630) chain H
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

631) chain H
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

632) chain H
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

633) chain H
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

634) chain H
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

635) chain I
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

636) chain I
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

637) chain I
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

638) chain I
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

639) chain I
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

640) chain A
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

641) chain I
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

642) chain I
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

643) chain I
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

644) chain J
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

645) chain J
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

646) chain J
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

647) chain J
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

648) chain J
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

649) chain J
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

650) chain J
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

651) chain A
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

652) chain J
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

653) chain K
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

654) chain K
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

655) chain K
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

656) chain K
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

657) chain K
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

658) chain K
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

659) chain K
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

660) chain K
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

661) chain L
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

662) chain B
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

663) chain L
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

664) chain L
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

665) chain L
residue 51
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

666) chain L
residue 54
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

667) chain L
residue 94
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

668) chain L
residue 127
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

669) chain L
residue 130
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

670) chain M
residue 18
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

671) chain M
residue 46
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

672) chain M
residue 50
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI1

673) chain A
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

674) chain J
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

675) chain K
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

676) chain L
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

677) chain M
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

678) chain N
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

679) chain O
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

680) chain P
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

681) chain Q
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

682) chain R
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

683) chain S
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

684) chain B
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

685) chain T
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

686) chain U
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

687) chain V
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

688) chain W
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

689) chain X
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

690) chain C
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

691) chain D
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

692) chain E
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

693) chain F
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

694) chain G
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

695) chain H
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

696) chain I
residue 52
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480
source Swiss-Prot : SWS_FT_FI2

697) chain A
residue 1-19
type prosite
sequence MKGDTKVINYLNKLLGNEL
description BACTERIOFERRITIN Bacterioferritin signature. MkGdtkVInyLnklLgneL
source prosite : PS00549


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