eF-site/Summary 2xwj-ABCDEFGHIJKL

eF-site ID	2xwj-ABCDEFGHIJKL
PDB Code	2xwj
Chain	A, B, C, D, E, F, G, H, I, J, K, L

Title	Crystal Structure of Complement C3b in Complex with Factor B
Classification	HYDROLASE
Compound	COMPLEMENT C3 BETA CHAIN
Source	ORGANISM_COMMON: HUMAN; ORGANISM_SCIENTIFIC: HOMO SAPIENS;

Sequence	A:	SPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDF PGKKLVLSSEKTVLTPATNHMGNVTFTIPANREFKKGRNK FVTVQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPGST VLYRIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSSQN QLGVLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEFEV KEYVLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYGKK VEGTAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVLSR KVLLDGVQNPRAEDLVGKSLYVSATVILHSGSDMVQAERS GIPIVTSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGSPA YRVPVAVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSITV RTKKQELSEAEQATRTMQALPYSTVGNSNNYLHLSVLRTE LRPGETLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLKAG RQVREPGQDLVVLPLSITTDFIPSFRLVAYYTLIGASGQR EVVADSVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMTLK IEGDHGARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEKAD IGCTPGSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQCPQ
	B:	DEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKLM NIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFFI DLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNPA FCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEVE VKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPER LGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQMT EDAVDAERLKHLIVTPSGCGEENMIGMTPTVIAVHYLDET EQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVK RAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEK QKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISL QEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAI AGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVE ATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQA TFMVFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRI HWESASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAK AKDQLTCNKFDLKVTIKPAPKNTMILEICTRYRGDQDATM SILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSD RNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVY AYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFI QKDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEYI MAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHY LMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEEN QKQCQDLGAFTESMVVFGCPN
	C:	SPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDF PGKKLVLSSEKTVLTPATNHMGNVTFTIPANREFKKGRNK FVTVQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPGST VLYRIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSSQN QLGVLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEFEV KEYVLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYGKK VEGTAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVLSR KVLLDGVQNPRAEDLVGKSLYVSATVILHSGSDMVQAERS GIPIVTSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGSPA YRVPVAVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSITV RTKKQELSEAEQATRTMQALPYSTVGNSNNYLHLSVLRTE LRPGETLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLKAG RQVREPGQDLVVLPLSITTDFIPSFRLVAYYTLIGASGQR EVVADSVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMTLK IEGDHGARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEKAD IGCTPGSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQCPQ
	D:	DEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKLM NIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFFI DLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNPA FCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEVE VKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPER LGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQMT EDAVDAERLKHLIVTPSGCGEENMIGMTPTVIAVHYLDET EQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVK RAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEK QKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISL QEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAI AGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVE ATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQA TFMVFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRI HWESASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAK AKDQLTCNKFDLKVTIKPAPKNTMILEICTRYRGDQDATM SILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSD RNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVY AYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFI QKDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEYI MAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHY LMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEEN QKQCQDLGAFTESMVVFGCPN
	E:	SPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDF PGKKLVLSSEKTVLTPATNHMGNVTFTIPANREFKKGRNK FVTVQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPGST VLYRIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSSQN QLGVLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEFEV KEYVLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYGKK VEGTAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVLSR KVLLDGVQNPRAEDLVGKSLYVSATVILHSGSDMVQAERS GIPIVTSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGSPA YRVPVAVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSITV RTKKQELSEAEQATRTMQALPYSTVGNSNNYLHLSVLRTE LRPGETLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLKAG RQVREPGQDLVVLPLSITTDFIPSFRLVAYYTLIGASGQR EVVADSVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMTLK IEGDHGARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEKAD IGCTPGSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQCPQ
	F:	DEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKLM NIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFFI DLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNPA FCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEVE VKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPER LGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQMT EDAVDAERLKHLIVTPSGCGEENMIGMTPTVIAVHYLDET EQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVK RAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEK QKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISL QEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAI AGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVE ATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQA TFMVFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRI HWESASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAK AKDQLTCNKFDLKVTIKPAPKNTMILEICTRYRGDQDATM SILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSD RNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVY AYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFI QKDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEYI MAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHY LMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEEN QKQCQDLGAFTESMVVFGCPN
	G:	SPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDF PGKKLVLSSEKTVLTPATNHMGNVTFTIPANREFKKGRNK FVTVQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPGST VLYRIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSSQN QLGVLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEFEV KEYVLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYGKK VEGTAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVLSR KVLLDGVQNPRAEDLVGKSLYVSATVILHSGSDMVQAERS GIPIVTSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGSPA YRVPVAVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSITV RTKKQELSEAEQATRTMQALPYSTVGNSNNYLHLSVLRTE LRPGETLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLKAG RQVREPGQDLVVLPLSITTDFIPSFRLVAYYTLIGASGQR EVVADSVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMTLK IEGDHGARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEKAD IGCTPGSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQCPQ
	H:	DEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKLM NIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFFI DLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNPA FCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEVE VKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPER LGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQMT EDAVDAERLKHLIVTPSGCGEENMIGMTPTVIAVHYLDET EQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVK RAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEK QKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISL QEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAI AGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVE ATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQA TFMVFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRI HWESASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAK AKDQLTCNKFDLKVTIKPAPKNTMILEICTRYRGDQDATM SILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSD RNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVY AYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFI QKDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEYI MAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHY LMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEEN QKQCQDLGAFTESMVVFGCPN
	I:	GSCSLEGVEIKGGSFRLLQEGQALEYVCPSGFYPYPVQTR TCRSTGSWSTLKTQDQKTVRKAECRAIHCPRPHDFENGEY WPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQ TAICDNGAGYCSNPGIPIGTRKVGSQYRLEDSVTYHCSRG LTLRGSQRRTCQEGGSWSGTEPSCQDSFMYDTPQEVAEAF LSSLTETIEGVDAEPSGSMNIYLVLDGSGSIGASDFTGAK KCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSS NADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMSWPD DVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLY IGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKDNEQ HVFKVKDMENLEDVFYQMIDESQSLSLCGMVWEHDYHKQP WQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKE HSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYD YDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTT CQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKG SCERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNT CRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQV PAHARDFHINLFQVLPWLKEKLQDEDLGFLAA
	J:	GSCSLEGVEIKGGSFRLLQEGQALEYVCPSGFYPYPVQTR TCRSTGSWSTLKTQDQKTVRKAECRAIHCPRPHDFENGEY WPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQ TAICDNGAGYCSNPGIPIGTRKVGSQYRLEDSVTYHCSRG LTLRGSQRRTCQEGGSWSGTEPSCQDSFMYDTPQEVAEAF LSSLTETIEGVDAEPSGSMNIYLVLDGSGSIGASDFTGAK KCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSS NADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMSWPD DVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLY IGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKDNEQ HVFKVKDMENLEDVFYQMIDESQSLSLCGMVWEGTDYHKQ PWQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDK EHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFY DYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTT TCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKK GSCERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPN TCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQ VPAHARDFHINLFQVLPWLKEKLQDEDLGFLAA
	K:	GSCSLEGVEIKGGSFRLLQEGQALEYVCPSGFYPYPVQTR TCRSTGSWSTLKTQDQKTVRKAECRAIHCPRPHDFENGEY WPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQ TAICDNGAGYCSNPGIPIGTRKVGSQYRLEDSVTYHCSRG LTLRGSQRRTCQEGGSWSGTEPSCQDSFMYDTPQEVAEAF LSSLTETIEGVDAEPSGSMNIYLVLDGSGSIGASDFTGAK KCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSS NADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMSWPD DVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLY IGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKDNEQ HVFKVKDMENLEDVFYQMIDESQSLSLCGMVWEGTDYHKQ PWQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDK EHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFY DYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTT TCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKK GSCERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPN TCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQ VPAHARDFHINLFQVLPWLKEKLQDEDLGFLAA
	L:	GSCSLEGVEIKGGSFRLLQEGQALEYVCPSGFYPYPVQTR TCRSTGSWSTLKTQDQKTVRKAECRAIHCPRPHDFENGEY WPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQ TAICDNGAGYCSNPGIPIGTRKVGSQYRLEDSVTYHCSRG LTLRGSQRRTCQEGGSWSGTEPSCQDSFMYDTPQEVAEAF LSSLTETIEGVDAEPSGSMNIYLVLDGSGSIGASDFTGAK KCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSS NADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMSWPD DVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLY IGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKDNEQ HVFKVKDMENLEDVFYQMIDESQSLSLCGMVWEDYHKQPW QAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEH SIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDY DVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTC QQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGS CERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTC RGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVP AHARDFHINLFQVLPWLKEKLQDEDLGFLAA

Description

Functional site


1)	chain	I
	residue	501
	type	ACT_SITE
	sequence	H
	description	Charge relay system
	source	Swiss-Prot : SWS_FT_FI1

2)	chain	L
	residue	501
	type	ACT_SITE
	sequence	H
	description	Charge relay system
	source	Swiss-Prot : SWS_FT_FI1

3)	chain	L
	residue	551
	type	ACT_SITE
	sequence	D
	description	Charge relay system
	source	Swiss-Prot : SWS_FT_FI1

4)	chain	L
	residue	674
	type	ACT_SITE
	sequence	S
	description	Charge relay system
	source	Swiss-Prot : SWS_FT_FI1

5)	chain	I
	residue	551
	type	ACT_SITE
	sequence	D
	description	Charge relay system
	source	Swiss-Prot : SWS_FT_FI1

6)	chain	I
	residue	674
	type	ACT_SITE
	sequence	S
	description	Charge relay system
	source	Swiss-Prot : SWS_FT_FI1

7)	chain	J
	residue	501
	type	ACT_SITE
	sequence	H
	description	Charge relay system
	source	Swiss-Prot : SWS_FT_FI1

8)	chain	J
	residue	551
	type	ACT_SITE
	sequence	D
	description	Charge relay system
	source	Swiss-Prot : SWS_FT_FI1

9)	chain	J
	residue	674
	type	ACT_SITE
	sequence	S
	description	Charge relay system
	source	Swiss-Prot : SWS_FT_FI1

10)	chain	K
	residue	501
	type	ACT_SITE
	sequence	H
	description	Charge relay system
	source	Swiss-Prot : SWS_FT_FI1

11)	chain	K
	residue	551
	type	ACT_SITE
	sequence	D
	description	Charge relay system
	source	Swiss-Prot : SWS_FT_FI1

12)	chain	K
	residue	674
	type	ACT_SITE
	sequence	S
	description	Charge relay system
	source	Swiss-Prot : SWS_FT_FI1

13)	chain	I
	residue	97
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI2

14)	chain	E
	residue	48
	type	CARBOHYD
	sequence	S
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI2

15)	chain	E
	residue	275
	type	CARBOHYD
	sequence	S
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI2

16)	chain	E
	residue	281
	type	CARBOHYD
	sequence	S
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI2

17)	chain	G
	residue	16
	type	CARBOHYD
	sequence	S
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI2

18)	chain	G
	residue	48
	type	CARBOHYD
	sequence	S
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI2

19)	chain	G
	residue	275
	type	CARBOHYD
	sequence	S
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI2

20)	chain	G
	residue	281
	type	CARBOHYD
	sequence	S
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI2

21)	chain	I
	residue	260
	type	CARBOHYD
	sequence	D
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI2

22)	chain	J
	residue	97
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI2

23)	chain	J
	residue	260
	type	CARBOHYD
	sequence	D
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI2

24)	chain	K
	residue	97
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI2

25)	chain	K
	residue	260
	type	CARBOHYD
	sequence	D
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI2

26)	chain	L
	residue	97
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI2

27)	chain	L
	residue	260
	type	CARBOHYD
	sequence	D
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI2

28)	chain	E
	residue	16
	type	CARBOHYD
	sequence	S
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI2

29)	chain	B
	residue	1595
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952
	source	Swiss-Prot : SWS_FT_FI6

30)	chain	D
	residue	1595
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952
	source	Swiss-Prot : SWS_FT_FI6

31)	chain	F
	residue	1595
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952
	source	Swiss-Prot : SWS_FT_FI6

32)	chain	H
	residue	1595
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952
	source	Swiss-Prot : SWS_FT_FI6

33)	chain	B
	residue	988
	type	CROSSLNK
	sequence	C
	description	Isoglutamyl cysteine thioester (Cys-Gln)
	source	Swiss-Prot : SWS_FT_FI7

34)	chain	B
	residue	991
	type	CROSSLNK
	sequence	E
	description	Isoglutamyl cysteine thioester (Cys-Gln)
	source	Swiss-Prot : SWS_FT_FI7

35)	chain	D
	residue	988
	type	CROSSLNK
	sequence	C
	description	Isoglutamyl cysteine thioester (Cys-Gln)
	source	Swiss-Prot : SWS_FT_FI7

36)	chain	D
	residue	991
	type	CROSSLNK
	sequence	E
	description	Isoglutamyl cysteine thioester (Cys-Gln)
	source	Swiss-Prot : SWS_FT_FI7

37)	chain	F
	residue	988
	type	CROSSLNK
	sequence	C
	description	Isoglutamyl cysteine thioester (Cys-Gln)
	source	Swiss-Prot : SWS_FT_FI7

38)	chain	F
	residue	991
	type	CROSSLNK
	sequence	E
	description	Isoglutamyl cysteine thioester (Cys-Gln)
	source	Swiss-Prot : SWS_FT_FI7

39)	chain	H
	residue	988
	type	CROSSLNK
	sequence	C
	description	Isoglutamyl cysteine thioester (Cys-Gln)
	source	Swiss-Prot : SWS_FT_FI7

40)	chain	H
	residue	991
	type	CROSSLNK
	sequence	E
	description	Isoglutamyl cysteine thioester (Cys-Gln)
	source	Swiss-Prot : SWS_FT_FI7

41)	chain	I
	residue	117
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19574954, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI3

42)	chain	J
	residue	117
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19574954, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI3

43)	chain	K
	residue	117
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19574954, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI3

44)	chain	L
	residue	117
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19574954, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI3

45)	chain	B
	residue	985-993
	type	prosite
	sequence	PSGCGEENM
	description	ALPHA_2_MACROGLOBULIN Alpha-2-macroglobulin family thiolester region signature. PsGCGEEnM
	source	prosite : PS00477

46)	chain	I
	residue	497-502
	type	prosite
	sequence	LTAAHC
	description	TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
	source	prosite : PS00134

47)	chain	I
	residue	668-679
	type	prosite
	sequence	NTCRGDSGGPLI
	description	TRYPSIN_SER Serine proteases, trypsin family, serine active site. NTcrGDSGGPLI
	source	prosite : PS00135

48)	chain	I
	residue	266
	type	CARBOHYD
	sequence	K
	description	N-linked (Glc) (glycation) lysine => ECO:0000269\|PubMed:2006911
	source	Swiss-Prot : SWS_FT_FI4

49)	chain	H
	residue	946
	type	CARBOHYD
	sequence	S
	description	N-linked (Glc) (glycation) lysine => ECO:0000269\|PubMed:2006911
	source	Swiss-Prot : SWS_FT_FI4

50)	chain	H
	residue	1299
	type	CARBOHYD
	sequence	S
	description	N-linked (Glc) (glycation) lysine => ECO:0000269\|PubMed:2006911
	source	Swiss-Prot : SWS_FT_FI4

51)	chain	H
	residue	1551
	type	CARBOHYD
	sequence	S
	description	N-linked (Glc) (glycation) lysine => ECO:0000269\|PubMed:2006911
	source	Swiss-Prot : SWS_FT_FI4

52)	chain	J
	residue	266
	type	CARBOHYD
	sequence	K
	description	N-linked (Glc) (glycation) lysine => ECO:0000269\|PubMed:2006911
	source	Swiss-Prot : SWS_FT_FI4

53)	chain	K
	residue	266
	type	CARBOHYD
	sequence	K
	description	N-linked (Glc) (glycation) lysine => ECO:0000269\|PubMed:2006911
	source	Swiss-Prot : SWS_FT_FI4

54)	chain	L
	residue	266
	type	CARBOHYD
	sequence	K
	description	N-linked (Glc) (glycation) lysine => ECO:0000269\|PubMed:2006911
	source	Swiss-Prot : SWS_FT_FI4

55)	chain	D
	residue	1299
	type	CARBOHYD
	sequence	S
	description	N-linked (Glc) (glycation) lysine => ECO:0000269\|PubMed:2006911
	source	Swiss-Prot : SWS_FT_FI4

56)	chain	D
	residue	1551
	type	CARBOHYD
	sequence	S
	description	N-linked (Glc) (glycation) lysine => ECO:0000269\|PubMed:2006911
	source	Swiss-Prot : SWS_FT_FI4

57)	chain	F
	residue	946
	type	CARBOHYD
	sequence	S
	description	N-linked (Glc) (glycation) lysine => ECO:0000269\|PubMed:2006911
	source	Swiss-Prot : SWS_FT_FI4

58)	chain	F
	residue	1299
	type	CARBOHYD
	sequence	S
	description	N-linked (Glc) (glycation) lysine => ECO:0000269\|PubMed:2006911
	source	Swiss-Prot : SWS_FT_FI4

59)	chain	F
	residue	1551
	type	CARBOHYD
	sequence	S
	description	N-linked (Glc) (glycation) lysine => ECO:0000269\|PubMed:2006911
	source	Swiss-Prot : SWS_FT_FI4

60)	chain	I
	residue	353
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19574954, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI5

61)	chain	J
	residue	353
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19574954, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI5

62)	chain	K
	residue	353
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19574954, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI5

63)	chain	L
	residue	353
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:17310251, ECO:0000269\|PubMed:19574954, ECO:0000269\|PubMed:6546754
	source	Swiss-Prot : SWS_FT_FI5