Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4V82

Crystal structure of cyanobacterial Photosystem II in complex with terbutryn

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
AA	0005506	molecular_function	iron ion binding
AA	0009055	molecular_function	electron transfer activity
AA	0009523	cellular_component	photosystem II
AA	0009635	biological_process	response to herbicide
AA	0009772	biological_process	photosynthetic electron transport in photosystem II
AA	0010242	molecular_function	oxygen evolving activity
AA	0015979	biological_process	photosynthesis
AA	0016168	molecular_function	chlorophyll binding
AA	0016491	molecular_function	oxidoreductase activity
AA	0016682	molecular_function	oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
AA	0019684	biological_process	photosynthesis, light reaction
AA	0031676	cellular_component	plasma membrane-derived thylakoid membrane
AA	0042651	cellular_component	thylakoid membrane
AA	0046872	molecular_function	metal ion binding
AB	0009521	cellular_component	photosystem
AB	0009523	cellular_component	photosystem II
AB	0009767	biological_process	photosynthetic electron transport chain
AB	0009772	biological_process	photosynthetic electron transport in photosystem II
AB	0015979	biological_process	photosynthesis
AB	0016020	cellular_component	membrane
AB	0016168	molecular_function	chlorophyll binding
AB	0019684	biological_process	photosynthesis, light reaction
AB	0031676	cellular_component	plasma membrane-derived thylakoid membrane
AB	0042651	cellular_component	thylakoid membrane
AC	0005737	cellular_component	cytoplasm
AC	0009521	cellular_component	photosystem
AC	0009523	cellular_component	photosystem II
AC	0009767	biological_process	photosynthetic electron transport chain
AC	0009772	biological_process	photosynthetic electron transport in photosystem II
AC	0015979	biological_process	photosynthesis
AC	0016020	cellular_component	membrane
AC	0016168	molecular_function	chlorophyll binding
AC	0019684	biological_process	photosynthesis, light reaction
AC	0031676	cellular_component	plasma membrane-derived thylakoid membrane
AC	0042651	cellular_component	thylakoid membrane
AC	0046872	molecular_function	metal ion binding
AD	0005506	molecular_function	iron ion binding
AD	0005737	cellular_component	cytoplasm
AD	0009055	molecular_function	electron transfer activity
AD	0009523	cellular_component	photosystem II
AD	0009772	biological_process	photosynthetic electron transport in photosystem II
AD	0010242	molecular_function	oxygen evolving activity
AD	0015979	biological_process	photosynthesis
AD	0016020	cellular_component	membrane
AD	0016168	molecular_function	chlorophyll binding
AD	0016491	molecular_function	oxidoreductase activity
AD	0019684	biological_process	photosynthesis, light reaction
AD	0031676	cellular_component	plasma membrane-derived thylakoid membrane
AD	0042651	cellular_component	thylakoid membrane
AD	0046872	molecular_function	metal ion binding
AE	0005506	molecular_function	iron ion binding
AE	0005737	cellular_component	cytoplasm
AE	0009055	molecular_function	electron transfer activity
AE	0009523	cellular_component	photosystem II
AE	0009539	cellular_component	photosystem II reaction center
AE	0009767	biological_process	photosynthetic electron transport chain
AE	0015979	biological_process	photosynthesis
AE	0016020	cellular_component	membrane
AE	0019684	biological_process	photosynthesis, light reaction
AE	0020037	molecular_function	heme binding
AE	0031676	cellular_component	plasma membrane-derived thylakoid membrane
AE	0042651	cellular_component	thylakoid membrane
AE	0046872	molecular_function	metal ion binding
AF	0005506	molecular_function	iron ion binding
AF	0005737	cellular_component	cytoplasm
AF	0009055	molecular_function	electron transfer activity
AF	0009523	cellular_component	photosystem II
AF	0009539	cellular_component	photosystem II reaction center
AF	0009767	biological_process	photosynthetic electron transport chain
AF	0015979	biological_process	photosynthesis
AF	0016020	cellular_component	membrane
AF	0019684	biological_process	photosynthesis, light reaction
AF	0020037	molecular_function	heme binding
AF	0031676	cellular_component	plasma membrane-derived thylakoid membrane
AF	0042651	cellular_component	thylakoid membrane
AF	0046872	molecular_function	metal ion binding
AH	0009523	cellular_component	photosystem II
AH	0015979	biological_process	photosynthesis
AH	0016020	cellular_component	membrane
AH	0031676	cellular_component	plasma membrane-derived thylakoid membrane
AH	0042301	molecular_function	phosphate ion binding
AH	0042651	cellular_component	thylakoid membrane
AH	0050821	biological_process	protein stabilization
AI	0005737	cellular_component	cytoplasm
AI	0009523	cellular_component	photosystem II
AI	0009539	cellular_component	photosystem II reaction center
AI	0015979	biological_process	photosynthesis
AI	0016020	cellular_component	membrane
AI	0031676	cellular_component	plasma membrane-derived thylakoid membrane
AI	0042651	cellular_component	thylakoid membrane
AJ	0009523	cellular_component	photosystem II
AJ	0009539	cellular_component	photosystem II reaction center
AJ	0015979	biological_process	photosynthesis
AJ	0016020	cellular_component	membrane
AJ	0031676	cellular_component	plasma membrane-derived thylakoid membrane
AJ	0042651	cellular_component	thylakoid membrane
AK	0009523	cellular_component	photosystem II
AK	0009539	cellular_component	photosystem II reaction center
AK	0015979	biological_process	photosynthesis
AL	0005737	cellular_component	cytoplasm
AL	0009523	cellular_component	photosystem II
AL	0009539	cellular_component	photosystem II reaction center
AL	0015979	biological_process	photosynthesis
AL	0016020	cellular_component	membrane
AL	0031676	cellular_component	plasma membrane-derived thylakoid membrane
AL	0042651	cellular_component	thylakoid membrane
AM	0005737	cellular_component	cytoplasm
AM	0009523	cellular_component	photosystem II
AM	0015979	biological_process	photosynthesis
AM	0016020	cellular_component	membrane
AM	0019684	biological_process	photosynthesis, light reaction
AM	0031676	cellular_component	plasma membrane-derived thylakoid membrane
AM	0042651	cellular_component	thylakoid membrane
AO	0009654	cellular_component	photosystem II oxygen evolving complex
AO	0010207	biological_process	photosystem II assembly
AO	0010242	molecular_function	oxygen evolving activity
AO	0042549	biological_process	photosystem II stabilization
AT	0009523	cellular_component	photosystem II
AT	0009539	cellular_component	photosystem II reaction center
AT	0015979	biological_process	photosynthesis
AT	0016020	cellular_component	membrane
AT	0031676	cellular_component	plasma membrane-derived thylakoid membrane
AT	0042651	cellular_component	thylakoid membrane
AU	0009523	cellular_component	photosystem II
AU	0009654	cellular_component	photosystem II oxygen evolving complex
AU	0015979	biological_process	photosynthesis
AU	0019898	cellular_component	extrinsic component of membrane
AU	0031676	cellular_component	plasma membrane-derived thylakoid membrane
AU	0042549	biological_process	photosystem II stabilization
AU	0042651	cellular_component	thylakoid membrane
AV	0005506	molecular_function	iron ion binding
AV	0009055	molecular_function	electron transfer activity
AV	0009523	cellular_component	photosystem II
AV	0015979	biological_process	photosynthesis
AV	0019684	biological_process	photosynthesis, light reaction
AV	0020037	molecular_function	heme binding
AV	0022904	biological_process	respiratory electron transport chain
AV	0031676	cellular_component	plasma membrane-derived thylakoid membrane
AV	0042651	cellular_component	thylakoid membrane
AV	0046872	molecular_function	metal ion binding
AX	0009523	cellular_component	photosystem II
AX	0015979	biological_process	photosynthesis
AX	0016020	cellular_component	membrane
AX	0031676	cellular_component	plasma membrane-derived thylakoid membrane
AX	0042651	cellular_component	thylakoid membrane
AZ	0009523	cellular_component	photosystem II
AZ	0009539	cellular_component	photosystem II reaction center
AZ	0015979	biological_process	photosynthesis
AZ	0031676	cellular_component	plasma membrane-derived thylakoid membrane
AZ	0042549	biological_process	photosystem II stabilization
AZ	0042651	cellular_component	thylakoid membrane
Ay	0009523	cellular_component	photosystem II
Ay	0015979	biological_process	photosynthesis
Ay	0016020	cellular_component	membrane
Ay	0031676	cellular_component	plasma membrane-derived thylakoid membrane
Ay	0042651	cellular_component	thylakoid membrane
BA	0005506	molecular_function	iron ion binding
BA	0009055	molecular_function	electron transfer activity
BA	0009523	cellular_component	photosystem II
BA	0009635	biological_process	response to herbicide
BA	0009772	biological_process	photosynthetic electron transport in photosystem II
BA	0010242	molecular_function	oxygen evolving activity
BA	0015979	biological_process	photosynthesis
BA	0016168	molecular_function	chlorophyll binding
BA	0016491	molecular_function	oxidoreductase activity
BA	0016682	molecular_function	oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
BA	0019684	biological_process	photosynthesis, light reaction
BA	0031676	cellular_component	plasma membrane-derived thylakoid membrane
BA	0042651	cellular_component	thylakoid membrane
BA	0046872	molecular_function	metal ion binding
BB	0009521	cellular_component	photosystem
BB	0009523	cellular_component	photosystem II
BB	0009767	biological_process	photosynthetic electron transport chain
BB	0009772	biological_process	photosynthetic electron transport in photosystem II
BB	0015979	biological_process	photosynthesis
BB	0016020	cellular_component	membrane
BB	0016168	molecular_function	chlorophyll binding
BB	0019684	biological_process	photosynthesis, light reaction
BB	0031676	cellular_component	plasma membrane-derived thylakoid membrane
BB	0042651	cellular_component	thylakoid membrane
BC	0005737	cellular_component	cytoplasm
BC	0009521	cellular_component	photosystem
BC	0009523	cellular_component	photosystem II
BC	0009767	biological_process	photosynthetic electron transport chain
BC	0009772	biological_process	photosynthetic electron transport in photosystem II
BC	0015979	biological_process	photosynthesis
BC	0016020	cellular_component	membrane
BC	0016168	molecular_function	chlorophyll binding
BC	0019684	biological_process	photosynthesis, light reaction
BC	0031676	cellular_component	plasma membrane-derived thylakoid membrane
BC	0042651	cellular_component	thylakoid membrane
BC	0046872	molecular_function	metal ion binding
BD	0005506	molecular_function	iron ion binding
BD	0005737	cellular_component	cytoplasm
BD	0009055	molecular_function	electron transfer activity
BD	0009523	cellular_component	photosystem II
BD	0009772	biological_process	photosynthetic electron transport in photosystem II
BD	0010242	molecular_function	oxygen evolving activity
BD	0015979	biological_process	photosynthesis
BD	0016020	cellular_component	membrane
BD	0016168	molecular_function	chlorophyll binding
BD	0016491	molecular_function	oxidoreductase activity
BD	0019684	biological_process	photosynthesis, light reaction
BD	0031676	cellular_component	plasma membrane-derived thylakoid membrane
BD	0042651	cellular_component	thylakoid membrane
BD	0046872	molecular_function	metal ion binding
BE	0005506	molecular_function	iron ion binding
BE	0005737	cellular_component	cytoplasm
BE	0009055	molecular_function	electron transfer activity
BE	0009523	cellular_component	photosystem II
BE	0009539	cellular_component	photosystem II reaction center
BE	0009767	biological_process	photosynthetic electron transport chain
BE	0015979	biological_process	photosynthesis
BE	0016020	cellular_component	membrane
BE	0019684	biological_process	photosynthesis, light reaction
BE	0020037	molecular_function	heme binding
BE	0031676	cellular_component	plasma membrane-derived thylakoid membrane
BE	0042651	cellular_component	thylakoid membrane
BE	0046872	molecular_function	metal ion binding
BF	0005506	molecular_function	iron ion binding
BF	0005737	cellular_component	cytoplasm
BF	0009055	molecular_function	electron transfer activity
BF	0009523	cellular_component	photosystem II
BF	0009539	cellular_component	photosystem II reaction center
BF	0009767	biological_process	photosynthetic electron transport chain
BF	0015979	biological_process	photosynthesis
BF	0016020	cellular_component	membrane
BF	0019684	biological_process	photosynthesis, light reaction
BF	0020037	molecular_function	heme binding
BF	0031676	cellular_component	plasma membrane-derived thylakoid membrane
BF	0042651	cellular_component	thylakoid membrane
BF	0046872	molecular_function	metal ion binding
BH	0009523	cellular_component	photosystem II
BH	0015979	biological_process	photosynthesis
BH	0016020	cellular_component	membrane
BH	0031676	cellular_component	plasma membrane-derived thylakoid membrane
BH	0042301	molecular_function	phosphate ion binding
BH	0042651	cellular_component	thylakoid membrane
BH	0050821	biological_process	protein stabilization
BI	0005737	cellular_component	cytoplasm
BI	0009523	cellular_component	photosystem II
BI	0009539	cellular_component	photosystem II reaction center
BI	0015979	biological_process	photosynthesis
BI	0016020	cellular_component	membrane
BI	0031676	cellular_component	plasma membrane-derived thylakoid membrane
BI	0042651	cellular_component	thylakoid membrane
BJ	0009523	cellular_component	photosystem II
BJ	0009539	cellular_component	photosystem II reaction center
BJ	0015979	biological_process	photosynthesis
BJ	0016020	cellular_component	membrane
BJ	0031676	cellular_component	plasma membrane-derived thylakoid membrane
BJ	0042651	cellular_component	thylakoid membrane
BK	0009523	cellular_component	photosystem II
BK	0009539	cellular_component	photosystem II reaction center
BK	0015979	biological_process	photosynthesis
BL	0005737	cellular_component	cytoplasm
BL	0009523	cellular_component	photosystem II
BL	0009539	cellular_component	photosystem II reaction center
BL	0015979	biological_process	photosynthesis
BL	0016020	cellular_component	membrane
BL	0031676	cellular_component	plasma membrane-derived thylakoid membrane
BL	0042651	cellular_component	thylakoid membrane
BM	0005737	cellular_component	cytoplasm
BM	0009523	cellular_component	photosystem II
BM	0015979	biological_process	photosynthesis
BM	0016020	cellular_component	membrane
BM	0019684	biological_process	photosynthesis, light reaction
BM	0031676	cellular_component	plasma membrane-derived thylakoid membrane
BM	0042651	cellular_component	thylakoid membrane
BO	0009654	cellular_component	photosystem II oxygen evolving complex
BO	0010207	biological_process	photosystem II assembly
BO	0010242	molecular_function	oxygen evolving activity
BO	0042549	biological_process	photosystem II stabilization
BT	0009523	cellular_component	photosystem II
BT	0009539	cellular_component	photosystem II reaction center
BT	0015979	biological_process	photosynthesis
BT	0016020	cellular_component	membrane
BT	0031676	cellular_component	plasma membrane-derived thylakoid membrane
BT	0042651	cellular_component	thylakoid membrane
BU	0009523	cellular_component	photosystem II
BU	0009654	cellular_component	photosystem II oxygen evolving complex
BU	0015979	biological_process	photosynthesis
BU	0019898	cellular_component	extrinsic component of membrane
BU	0031676	cellular_component	plasma membrane-derived thylakoid membrane
BU	0042549	biological_process	photosystem II stabilization
BU	0042651	cellular_component	thylakoid membrane
BV	0005506	molecular_function	iron ion binding
BV	0009055	molecular_function	electron transfer activity
BV	0009523	cellular_component	photosystem II
BV	0015979	biological_process	photosynthesis
BV	0019684	biological_process	photosynthesis, light reaction
BV	0020037	molecular_function	heme binding
BV	0022904	biological_process	respiratory electron transport chain
BV	0031676	cellular_component	plasma membrane-derived thylakoid membrane
BV	0042651	cellular_component	thylakoid membrane
BV	0046872	molecular_function	metal ion binding
BX	0009523	cellular_component	photosystem II
BX	0015979	biological_process	photosynthesis
BX	0016020	cellular_component	membrane
BX	0031676	cellular_component	plasma membrane-derived thylakoid membrane
BX	0042651	cellular_component	thylakoid membrane
BZ	0009523	cellular_component	photosystem II
BZ	0009539	cellular_component	photosystem II reaction center
BZ	0015979	biological_process	photosynthesis
BZ	0031676	cellular_component	plasma membrane-derived thylakoid membrane
BZ	0042549	biological_process	photosystem II stabilization
BZ	0042651	cellular_component	thylakoid membrane
By	0009523	cellular_component	photosystem II
By	0015979	biological_process	photosynthesis
By	0016020	cellular_component	membrane
By	0031676	cellular_component	plasma membrane-derived thylakoid membrane
By	0042651	cellular_component	thylakoid membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue FE2 AA 401

Chain	Residue
AA	HIS215
AA	HIS272
AA	BCT402
AD	HIS214
AD	HIS268

site_id	AC2
Number of Residues	7
Details	binding site for residue BCT AA 402

Chain	Residue
AA	FE2401
AD	TYR244
AD	HIS268
AA	HIS215
AA	GLU244
AA	TYR246
AA	HIS272

site_id	AC3
Number of Residues	8
Details	binding site for residue CL AA 403

Chain	Residue
AA	ASP61
AA	ILE63
AA	GLU65
AA	ASN181
AA	HIS332
AA	GLU333
AA	ARG334
AD	LYS317

site_id	AC4
Number of Residues	22
Details	binding site for residue CLA AA 404

Chain	Residue
AA	PHE119
AA	PRO150
AA	SER153
AA	ALA154
AA	VAL157
AA	MET183
AA	PHE186
AA	GLN187
AA	HIS198
AA	GLY201
AA	VAL205
AA	PHE206
AA	THR286
AA	ALA287
AA	ILE290
AA	CLA405
AA	CLA406
AD	LEU182
AD	CLA401
AD	PHO402
AD	LMG408
AT	PHE17

site_id	AC5
Number of Residues	21
Details	binding site for residue CLA AA 405

Chain	Residue
AA	THR45
AA	VAL157
AA	PHE158
AA	MET172
AA	ILE176
AA	THR179
AA	PHE180
AA	PHE182
AA	MET183
AA	CLA404
AB	LMG620
AD	MET198
AD	VAL201
AD	ALA202
AD	GLY206
AD	CLA401
AD	PHO402
AD	PL9405
AD	LMG408
AT	PHE10
AT	ILE14

site_id	AC6
Number of Residues	12
Details	binding site for residue CLA AA 406

Chain	Residue
AA	GLN199
AA	VAL202
AA	ALA203
AA	CLA404
AC	DGD519
AD	PHE157
AD	VAL175
AD	ILE178
AD	PHE179
AD	LEU182
AD	CLA401
AD	PHO403

site_id	AC7
Number of Residues	17
Details	binding site for residue CLA AA 407

Chain	Residue
AA	VAL35
AA	PRO39
AA	THR40
AA	PHE93
AA	PRO95
AA	ILE96
AA	TRP97
AA	LEU114
AA	HIS118
AA	BCR410
AA	DGD411
AC	CLA505
AI	VAL8
AI	TYR9
AI	VAL12
AI	PHE15
AI	LMG101

site_id	AC8
Number of Residues	9
Details	binding site for residue MST AA 408

Chain	Residue
AA	PHE274
AA	LEU275
AA	MET214
AA	HIS215
AA	LEU218
AA	PHE255
AA	SER264
AA	PHE265
AA	LEU271

site_id	AC9
Number of Residues	8
Details	binding site for residue OEC AA 409

Chain	Residue
AA	GLN165
AA	ASP170
AA	GLU189
AA	HIS332
AA	GLU333
AA	ASP342
AA	ALA344
AC	GLU354

site_id	AD1
Number of Residues	11
Details	binding site for residue BCR AA 410

Chain	Residue
AA	ILE38
AA	LEU42
AA	ALA43
AA	ILE50
AA	ALA51
AA	ALA55
AA	LEU102
AA	TRP105
AA	CLA407
AA	SQD416
AI	PHE15

site_id	AD2
Number of Residues	15
Details	binding site for residue DGD AA 411

Chain	Residue
AA	GLU98
AA	PHE117
AA	LEU120
AA	LEU121
AA	PHE155
AA	CLA407
AC	LEU213
AC	LYS215
AC	SER216
AC	PRO217
AC	GLU221
AC	TRP223
AC	DGD517
AI	LYS5
AI	TYR9

site_id	AD3
Number of Residues	18
Details	binding site for residue LHG AA 412

Chain	Residue
AA	ARG140
AA	TRP142
AA	VAL145
AA	PHE273
AA	PHE285
AA	SQD413
AC	TRP36
AC	PHE436
AC	TRP443
AC	ARG447
AC	CLA504
AC	CLA508
AD	GLU219
AD	ASN220
AD	ALA229
AD	SER230
AD	THR231
AD	PHE232

site_id	AD4
Number of Residues	12
Details	binding site for residue SQD AA 413

Chain	Residue
AA	ASN267
AA	SER270
AA	PHE273
AA	LHG412
AA	LHG415
AC	ALA34
AC	TRP36
AC	CLA508
AC	DGD518
AD	PHE232
AD	ARG233
AK	PHE37

site_id	AD5
Number of Residues	7
Details	binding site for residue LMG AA 414

Chain	Residue
AA	PHE260
AA	TYR262
AD	PHE27
AE	PRO9
AE	PHE10
AE	SER11
AJ	LMG102

site_id	AD6
Number of Residues	7
Details	binding site for residue LHG AA 415

Chain	Residue
AA	TYR262
AA	SER264
AA	PHE265
AA	ASN266
AA	SQD413
AC	TRP35
AK	PHE45

site_id	AD7
Number of Residues	12
Details	binding site for residue SQD AA 416

Chain	Residue
AA	TRP20
AA	ASN26
AA	ARG27
AA	LEU28
AA	ILE38
AA	BCR410
AT	PHE22
AT	BCR101
BB	TRP5113
BB	TYR5117
BB	CLA5620
BB	BCR5623

site_id	AD8
Number of Residues	12
Details	binding site for residue LMG AA 417

Chain	Residue
AA	TYR73
AA	LEU102
AA	ASP103
AO	GLY138
BB	LEU5039
BB	ALA5043
BB	TRP5075
BB	SER5076
BB	LEU5098
BB	ILE5101
BB	DGD5602
BB	LMT5603

site_id	AD9
Number of Residues	8
Details	binding site for residue CLA AB 601

Chain	Residue
AB	TRP185
AB	PRO187
AB	PHE190
AB	ILE207
AB	VAL208
AB	CLA602
AH	PHE41
AX	BCR101

site_id	AE1
Number of Residues	22
Details	binding site for residue CLA AB 602

Chain	Residue
AB	GLU184
AB	TRP185
AB	GLY189
AB	PRO192
AB	ALA200
AB	HIS201
AB	ALA204
AB	ALA205
AB	VAL208
AB	PHE246
AB	PHE247
AB	VAL251
AB	CLA601
AB	CLA603
AD	VAL154
AD	ILE159
AD	LEU162
AH	PHE38
AH	PHE41
AH	ILE45
AH	LEU46
AH	TYR49

site_id	AE2
Number of Residues	17
Details	binding site for residue CLA AB 603

Chain	Residue
AB	ARG68
AB	LEU69
AB	ALA146
AB	CYS150
AB	PHE153
AB	HIS201
AB	HIS202
AB	PHE247
AB	ALA248
AB	VAL251
AB	VAL252
AB	THR262
AB	CLA602
AB	CLA604
AB	CLA605
AB	CLA606
AH	PHE38

site_id	AE3
Number of Residues	20
Details	binding site for residue CLA AB 604

Chain	Residue
AB	TRP33
AB	PHE65
AB	ARG68
AB	LEU148
AB	VAL245
AB	ALA248
AB	ALA249
AB	VAL252
AB	PHE451
AB	HIS455
AB	PHE458
AB	ALA459
AB	PHE462
AB	CLA603
AB	CLA605
AB	CLA607
AB	CLA611
AB	CLA612
AB	CLA613
AB	CLA615

site_id	AE4
Number of Residues	18
Details	binding site for residue CLA AB 605

Chain	Residue
AB	THR27
AB	VAL30
AB	ALA31
AB	TRP33
AB	ALA34
AB	VAL62
AB	PHE65
AB	MET66
AB	ARG68
AB	LEU69
AB	HIS100
AB	LEU103
AB	GLY147
AB	CLA603
AB	CLA604
AB	CLA606
AB	CLA609
AB	CLA610

site_id	AE5
Number of Residues	20
Details	binding site for residue CLA AB 606

Chain	Residue
AB	LEU69
AB	GLY70
AB	VAL71
AB	TRP91
AB	ALA99
AB	HIS100
AB	VAL102
AB	LEU103
AB	LEU149
AB	GLY152
AB	PHE153
AB	PHE156
AB	HIS157
AB	PHE162
AB	GLY163
AB	PRO164
AB	CLA603
AB	CLA605
AB	BCR619
AB	LMT623

site_id	AE6
Number of Residues	22
Details	binding site for residue CLA AB 607

Chain	Residue
AB	TRP33
AB	MET37
AB	TYR40
AB	GLN58
AB	GLY59
AB	PHE61
AB	PHE325
AB	THR327
AB	GLY328
AB	PRO329
AB	TRP450
AB	PHE451
AB	ALA454
AB	CLA604
AB	CLA613
AB	BCR617
AB	LMG621
AD	MET199
AD	MET281
AL	PHE31
AL	PHE35
BT	BCR5101

site_id	AE7
Number of Residues	19
Details	binding site for residue CLA AB 608

Chain	Residue
AB	THR236
AB	SER239
AB	SER240
AB	ALA243
AB	PHE247
AB	HIS466
AB	ILE467
AB	CLA609
AB	CLA610
AB	SQD622
AB	LMT624
AD	PHE120
AD	ILE123
AD	MET126
AD	LEU127
AD	PHE130
AD	CLA404
AH	LEU43
AH	DGD101

site_id	AE8
Number of Residues	18
Details	binding site for residue CLA AB 609

Chain	Residue
AB	PHE139
AB	VAL208
AB	ALA212
AB	PHE215
AB	HIS216
AB	PRO221
AB	PRO222
AB	LEU225
AB	LEU229
AB	CLA605
AB	CLA608
AB	CLA610
AH	THR27
AH	THR28
AH	MET31
AH	PHE34
AH	MET35
AX	BCR101

site_id	AE9
Number of Residues	15
Details	binding site for residue CLA AB 610

Chain	Residue
AB	LEU135
AB	PHE139
AB	HIS142
AB	LEU143
AB	ALA146
AB	MET231
AB	VAL237
AB	SER240
AB	SER241
AB	VAL245
AB	CLA605
AB	CLA608
AB	CLA609
AB	CLA612
AB	CLA615

site_id	AF1
Number of Residues	19
Details	binding site for residue CLA AB 611

Chain	Residue
AB	TRP5
AB	TYR6
AB	ARG7
AB	VAL8
AB	HIS9
AB	ILE242
AB	LEU461
AB	PHE462
AB	PHE464
AB	GLY465
AB	TRP468
AB	HIS469
AB	ARG472
AB	CLA604
AB	CLA612
AB	CLA613
AB	CLA614
AB	LMG620
AD	LMG407

site_id	AF2
Number of Residues	15
Details	binding site for residue CLA AB 612

Chain	Residue
AB	HIS9
AB	LEU19
AB	HIS23
AB	HIS26
AB	THR27
AB	GLU235
AB	VAL237
AB	LEU238
AB	SER241
AB	VAL245
AB	CLA604
AB	CLA610
AB	CLA611
AB	CLA613
AB	CLA615

site_id	AF3
Number of Residues	12
Details	binding site for residue CLA AB 613

Chain	Residue
AB	HIS9
AB	HIS26
AB	VAL30
AB	TRP33
AB	PHE462
AB	CLA604
AB	CLA607
AB	CLA611
AB	CLA612
AB	CLA614
AB	BCR617
AD	LMG407

site_id	AF4
Number of Residues	16
Details	binding site for residue CLA AB 614

Chain	Residue
AB	VAL8
AB	HIS9
AB	VAL11
AB	ALA22
AB	LEU29
AB	TRP115
AB	CLA611
AB	CLA613
AB	BCR617
AB	LMG620
AB	LMG621
AB	SQD627
AL	VAL10
AM	PHE21
BM	LMG5102
BT	PHE5008

site_id	AF5
Number of Residues	14
Details	binding site for residue CLA AB 615

Chain	Residue
AB	ILE20
AB	HIS23
AB	LEU24
AB	LEU107
AB	MET138
AB	ILE141
AB	HIS142
AB	LEU145
AB	CLA604
AB	CLA610
AB	CLA612
AB	CLA616
AB	BCR619
AH	LEU14

site_id	AF6
Number of Residues	11
Details	binding site for residue CLA AB 616

Chain	Residue
AB	LEU24
AB	ALA110
AB	TRP113
AB	HIS114
AB	LEU120
AB	CLA615
AB	BCR619
AH	THR5
AH	LEU7
AH	GLY8
BA	SQD5401

site_id	AF7
Number of Residues	14
Details	binding site for residue BCR AB 617

Chain	Residue
AB	ALA21
AB	MET25
AB	LEU29
AB	CYS112
AB	TRP115
AB	CLA607
AB	CLA613
AB	CLA614
AB	BCR618
AB	LMG621
AB	SQD627
AM	ILE9
BT	PHE5019
BT	BCR5101

site_id	AF8
Number of Residues	7
Details	binding site for residue BCR AB 618

Chain	Residue
AB	LEU29
AB	TRP33
AB	VAL102
AB	GLY105
AB	LEU109
AB	BCR617
BT	BCR5101

site_id	AF9
Number of Residues	9
Details	binding site for residue BCR AB 619

Chain	Residue
AB	LEU106
AB	LEU109
AB	CYS112
AB	VAL116
AB	CLA606
AB	CLA615
AB	CLA616
BA	SQD5401
BT	PHE5023

site_id	AG1
Number of Residues	20
Details	binding site for residue LMG AB 620

Chain	Residue
AA	SER232
AA	ASN234
AA	CLA405
AB	TRP5
AB	CLA611
AB	CLA614
AD	TRP266
AD	PHE273
AD	PL9405
AD	LMG407
AD	LMG408
AL	GLU11
AL	ASN13
AL	SER16
AL	LEU19
AL	LEU22
AL	VAL26
AM	PHE21
AM	LEU22
BM	LMG5102

site_id	AG2
Number of Residues	14
Details	binding site for residue LMG AB 621

Chain	Residue
AB	THR327
AB	GLY328
AB	PRO329
AB	LYS332
AB	VAL457
AB	LEU461
AB	CLA607
AB	CLA614
AB	BCR617
AD	MET281
AD	ILE284
AL	PHE35
AM	ASN4
AM	LMT102

site_id	AG3
Number of Residues	10
Details	binding site for residue SQD AB 622

Chain	Residue
AB	LYS227
AB	ALA228
AB	ARG230
AB	LEU474
AB	CLA608
AB	LMT624
AD	LYS23
AD	TRP32
AD	ARG134
AD	LEU135

site_id	AG4
Number of Residues	2
Details	binding site for residue LMT AB 623

Chain	Residue
AB	ASP87
AB	CLA606

site_id	AG5
Number of Residues	9
Details	binding site for residue LMT AB 624

Chain	Residue
AB	ARG224
AB	LEU225
AB	CLA608
AB	SQD622
AD	PHE15
AD	ASP16
AD	ASP19
AD	LYS23
AH	MET35

site_id	AG6
Number of Residues	4
Details	binding site for residue DMS AB 625

Chain	Residue
AB	GLU387
AU	LYS134
AV	PRO76
AV	SER77

site_id	AG7
Number of Residues	5
Details	binding site for residue DMS AB 626

Chain	Residue
AB	TRP275
AB	ASP276
AB	SER278
AB	MET359
AB	PRO360

site_id	AG8
Number of Residues	13
Details	binding site for residue SQD AB 627

Chain	Residue
AB	ARG18
AB	LEU29
AB	PHE108
AB	TRP115
AB	CLA614
AB	BCR617
BL	ARG5014
BL	TYR5018
BM	TYR5026
BM	LMG5102
BT	ALA5015
BT	PHE5019
BT	PHE5023

site_id	AG9
Number of Residues	10
Details	binding site for residue DGD AB 628

Chain	Residue
AB	TRP75
AB	ASP87
AB	PRO88
AB	GLY89
AB	PHE90
AB	LMT630
BA	ILE5046
BA	ILE5050
BA	LMG5402
BI	LMG5101

site_id	AH1
Number of Residues	5
Details	binding site for residue LMT AB 629

Chain	Residue
AB	LEU39
AB	THR44
AB	THR436
BA	LMG5402
BT	ILE5004

site_id	AH2
Number of Residues	7
Details	binding site for residue LMT AB 630

Chain	Residue
AB	GLY85
AB	ASP87
AB	DGD628
BA	BCR5411
BI	MET5001
BI	LEU5004
BO	LYS5095

site_id	AH3
Number of Residues	19
Details	binding site for residue CLA AC 501

Chain	Residue
AC	LEU95
AC	LEU168
AC	GLY171
AC	ALA172
AC	LEU175
AC	VAL233
AC	HIS237
AC	ILE240
AC	ALA278
AC	MET281
AC	MET282
AC	ILE285
AC	PHE289
AC	VAL296
AC	TYR297
AC	CLA502
AC	CLA503
AC	CLA507
AC	BCR516

site_id	AH4
Number of Residues	16
Details	binding site for residue CLA AC 502

Chain	Residue
AC	TRP63
AC	HIS91
AC	LEU95
AC	LEU174
AC	PHE182
AC	LEU279
AC	MET282
AC	ALA286
AC	TYR297
AC	HIS430
AC	LEU433
AC	PHE437
AC	CLA501
AC	CLA503
AC	CLA504
AC	CLA510

site_id	AH5
Number of Residues	17
Details	binding site for residue CLA AC 503

Chain	Residue
AC	ILE60
AC	VAL61
AC	TRP63
AC	ALA64
AC	THR68
AC	LEU88
AC	HIS91
AC	LEU95
AC	VAL114
AC	HIS118
AC	LEU279
AC	MET282
AC	CLA501
AC	CLA502
AC	CLA510
AC	CLA512
AC	LMG521

site_id	AH6
Number of Residues	16
Details	binding site for residue CLA AC 504

Chain	Residue
AA	PHE197
AA	LHG412
AC	TRP63
AC	MET67
AC	PHE70
AC	GLN84
AC	GLY85
AC	SER406
AC	TRP425
AC	SER429
AC	CLA502
AC	CLA510
AC	DGD518
AC	DGD519
AC	LMG520
AK	PRO26

site_id	AH7
Number of Residues	15
Details	binding site for residue CLA AC 505

Chain	Residue
AA	PHE33
AA	MET127
AA	TRP131
AA	CLA407
AC	SER273
AC	TYR274
AC	GLY277
AC	ALA278
AC	HIS441
AC	LEU442
AC	ALA445
AC	ARG449
AC	CLA507
AI	PHE19
AI	PHE23

site_id	AH8
Number of Residues	13
Details	binding site for residue CLA AC 506

Chain	Residue
AC	LEU161
AC	LEU165
AC	LEU213
AC	ILE243
AC	CYS244
AC	GLY247
AC	TRP250
AC	HIS251
AC	THR255
AC	PHE257
AC	TRP259
AC	PHE264
AC	CLA507

site_id	AH9
Number of Residues	14
Details	binding site for residue CLA AC 507

Chain	Residue
AC	MET157
AC	LEU161
AC	HIS164
AC	LEU168
AC	PHE264
AC	TRP266
AC	TYR271
AC	TYR274
AC	SER275
AC	CLA501
AC	CLA505
AC	CLA506
AC	CLA509
AC	BCR516

site_id	AI1
Number of Residues	18
Details	binding site for residue CLA AC 508

Chain	Residue
AA	LHG412
AA	SQD413
AC	TRP36
AC	ALA37
AC	GLY38
AC	ASN39
AC	ALA40
AC	GLU269
AC	LEU276
AC	PHE436
AC	PHE437
AC	GLY440
AC	TRP443
AC	HIS444
AC	ARG447
AC	CLA509
AC	CLA510
AJ	BCR101

site_id	AI2
Number of Residues	17
Details	binding site for residue CLA AC 509

Chain	Residue
AC	ASN39
AC	LEU42
AC	LEU49
AC	ALA52
AC	HIS53
AC	HIS56
AC	TYR149
AC	TRP151
AC	GLY268
AC	TYR271
AC	LEU272
AC	SER275
AC	LEU279
AC	CLA507
AC	CLA508
AC	CLA510
AC	CLA512

site_id	AI3
Number of Residues	15
Details	binding site for residue CLA AC 510

Chain	Residue
AC	ASN39
AC	HIS56
AC	LEU59
AC	ILE60
AC	LEU279
AC	PHE437
AC	CLA502
AC	CLA503
AC	CLA504
AC	CLA508
AC	CLA509
AC	CLA511
AK	PRO29
AK	VAL30
AK	LEU33

site_id	AI4
Number of Residues	26
Details	binding site for residue CLA AC 511

Chain	Residue
AC	GLN28
AC	TRP35
AC	GLY38
AC	ASN39
AC	ARG41
AC	LEU42
AC	LEU45
AC	LYS48
AC	ALA52
AC	ALA123
AC	PHE127
AC	VAL130
AC	ALA133
AC	ILE134
AC	CLA510
AC	BCR514
AK	PHE32
AK	LEU33
AK	PHE37
AK	TRP39
AK	GLN40
AZ	VAL20
AZ	PRO24
Ay	ILE35
Ay	ASN45
Ay	LEU46

site_id	AI5
Number of Residues	11
Details	binding site for residue CLA AC 512

Chain	Residue
AC	HIS53
AC	ALA57
AC	PHE147
AC	ILE160
AC	PHE163
AC	HIS164
AC	VAL167
AC	CLA503
AC	CLA509
AC	CLA513
AC	BCR515

site_id	AI6
Number of Residues	14
Details	binding site for residue CLA AC 513

Chain	Residue
AC	LEU50
AC	VAL54
AC	VAL124
AC	LEU125
AC	GLY128
AC	TYR131
AC	HIS132
AC	PRO137
AC	LEU140
AC	TYR143
AC	PHE147
AC	CLA512
AC	BCR515
AC	LMG521

site_id	AI7
Number of Residues	16
Details	binding site for residue BCR AC 514

Chain	Residue
AC	ALA55
AC	GLY58
AC	VAL116
AC	ILE120
AC	SER122
AC	ALA123
AC	CLA511
AC	BCR515
AK	TYR15
AK	PHE32
AK	LEU35
AK	ALA36
AK	TRP39
AK	BCR102
AZ	VAL13
AZ	VAL20

site_id	AI8
Number of Residues	12
Details	binding site for residue BCR AC 515

Chain	Residue
AC	PHE109
AC	VAL116
AC	SER121
AC	VAL124
AC	PHE147
AC	CLA512
AC	CLA513
AC	BCR514
AK	TYR15
AZ	VAL54
AZ	GLY55
AZ	ASN58

site_id	AI9
Number of Residues	13
Details	binding site for residue BCR AC 516

Chain	Residue
AC	ILE209
AC	TYR212
AC	LEU213
AC	ASP232
AC	VAL233
AC	HIS237
AC	ILE240
AC	PHE264
AC	CLA501
AC	CLA507
AI	VAL20
AI	PHE23
AI	LEU24

site_id	AJ1
Number of Residues	18
Details	binding site for residue DGD AC 517

Chain	Residue
AA	PHE155
AA	ILE160
AA	DGD411
AC	PRO217
AC	PHE218
AC	GLY219
AC	GLY220
AC	GLY222
AC	TRP223
AC	VAL225
AC	SER226
AC	ASN228
AC	PHE284
AC	CYS288
AC	PHE292
AC	ASN294
AC	THR295
AC	LEU438

site_id	AJ2
Number of Residues	19
Details	binding site for residue DGD AC 518

Chain	Residue
AA	LEU288
AA	THR292
AA	SQD413
AC	TYR82
AC	GLU83
AC	GLN84
AC	GLY85
AC	ASN418
AC	PHE419
AC	VAL420
AC	TRP425
AC	THR428
AC	VAL432
AC	CLA504
AC	DGD519
AC	LMG520
AJ	PHE29
AJ	TYR33
AJ	BCR101

site_id	AJ3
Number of Residues	23
Details	binding site for residue DGD AC 519

Chain	Residue
AA	LEU200
AA	TRP278
AA	VAL281
AA	PHE300
AA	PHE302
AA	SER305
AA	CLA406
AC	LEU404
AC	ASN405
AC	SER406
AC	VAL407
AC	ASN415
AC	SER416
AC	VAL417
AC	ASN418
AC	CLA504
AC	DGD518
AJ	ALA32
AJ	TYR33
AJ	GLY37
AJ	SER38
AJ	LEU40
AV	GLN60

site_id	AJ4
Number of Residues	5
Details	binding site for residue LMG AC 520

Chain	Residue
AC	HIS74
AC	CLA504
AC	DGD518
AJ	BCR101
AK	VAL30

site_id	AJ5
Number of Residues	9
Details	binding site for residue LMG AC 521

Chain	Residue
AC	TRP97
AC	PHE109
AC	PRO110
AC	VAL113
AC	VAL114
AC	VAL117
AC	HIS118
AC	CLA503
AC	CLA513

site_id	AJ6
Number of Residues	23
Details	binding site for residue CLA AD 401

Chain	Residue
AA	PHE206
AA	CLA404
AA	CLA405
AA	CLA406
AD	LEU45
AD	LEU122
AD	PRO149
AD	VAL152
AD	PHE153
AD	SER155
AD	VAL156
AD	LEU182
AD	PHE185
AD	GLN186
AD	TRP191
AD	THR192
AD	HIS197
AD	VAL201
AD	VAL204
AD	LEU279
AD	SER282
AD	ALA283
AD	PHO403

site_id	AJ7
Number of Residues	18
Details	binding site for residue PHO AD 402

Chain	Residue
AA	LEU41
AA	ALA44
AA	PHE119
AA	TYR126
AA	GLN130
AA	ALA146
AA	TYR147
AA	GLY175
AA	VAL283
AA	CLA404
AA	CLA405
AD	ALA208
AD	LEU209
AD	ALA212
AD	ILE213
AD	TRP253
AD	PHE257
AD	LMG408

site_id	AJ8
Number of Residues	20
Details	binding site for residue PHO AD 403

Chain	Residue
AA	PHE206
AA	ALA209
AA	LEU210
AA	MET214
AA	CLA406
AD	ALA41
AD	TRP48
AD	GLY118
AD	PHE125
AD	GLN129
AD	ASN142
AD	ALA145
AD	PHE146
AD	ALA148
AD	PRO149
AD	PHE153
AD	GLY174
AD	VAL175
AD	PRO275
AD	CLA401

site_id	AJ9
Number of Residues	16
Details	binding site for residue CLA AD 404

Chain	Residue
AX	LEU30
AX	BCR101
AB	CLA608
AD	ILE35
AD	PRO39
AD	LEU43
AD	LEU89
AD	LEU90
AD	LEU91
AD	LEU92
AD	TRP93
AD	PHE113
AD	HIS117
AD	PHE120
AH	GLU47
AX	LEU23

site_id	AK1
Number of Residues	22
Details	binding site for residue PL9 AD 405

Chain	Residue
AA	PHE48
AA	ILE53
AA	ILE77
AA	CLA405
AB	LMG620
AD	MET199
AD	ALA202
AD	LEU209
AD	LEU210
AD	ILE213
AD	HIS214
AD	THR217
AD	TRP253
AD	ALA260
AD	PHE261
AD	LEU267
AD	VAL274
AD	THR277
AD	GLY278
AD	LMG408
AL	LEU27
AL	LEU29

site_id	AK2
Number of Residues	10
Details	binding site for residue BCR AD 406

Chain	Residue
AD	GLY46
AD	LEU49
AD	PHE101
AD	PHE113
AE	DGD101
AF	PHE33
AF	LEU34
AJ	VAL21
AJ	VAL25
AJ	LMG102

site_id	AK3
Number of Residues	18
Details	binding site for residue LMG AD 407

Chain	Residue
AA	ASN234
AB	TYR6
AB	ARG7
AB	PHE464
AB	TRP468
AB	PHE479
AB	CLA611
AB	CLA613
AB	LMG620
AD	ARG139
AD	TYR141
AD	PHE269
AD	PHE273
AD	VAL276
AD	TRP280
AM	PHE14
AM	VAL17
AM	PRO18

site_id	AK4
Number of Residues	20
Details	binding site for residue LMG AD 408

Chain	Residue
AA	CLA404
AA	CLA405
AB	LMG620
AD	PHE257
AD	ILE259
AD	ALA260
AD	PHE261
AD	SER262
AD	ASN263
AD	TRP266
AD	PHO402
AD	PL9405
AL	ASN13
AL	THR15
AL	LEU19
AL	LEU22
AT	PHE10
AT	PHE17
AT	ILE21
AT	BCR101

site_id	AK5
Number of Residues	7
Details	binding site for residue LMT AD 409

Chain	Residue
AD	TRP93
AD	GLY99
AD	ASP100
AD	PHE101
AE	DGD101
AX	ILE21
AX	SER25

site_id	AK6
Number of Residues	7
Details	binding site for residue DGD AE 101

Chain	Residue
AD	PHE101
AD	BCR406
AD	LMT409
AE	ASP45
AE	VAL46
AF	VAL28
AF	PHE32

site_id	AK7
Number of Residues	14
Details	binding site for residue HEM AF 101

Chain	Residue
AE	ARG8
AE	PHE10
AE	ILE13
AE	TYR19
AE	HIS23
AE	THR26
AE	ILE27
AE	LEU30
AF	ILE15
AF	ARG19
AF	TRP20
AF	HIS24
AF	ALA27
AF	ILE31

site_id	AK8
Number of Residues	11
Details	binding site for residue SQD AF 102

Chain	Residue
AD	TRP21
AD	ARG24
AD	ARG26
AE	GLU7
AF	PRO14
AF	PHE16
AF	THR17
AF	VAL18
AF	VAL21
AX	THR33
AX	ILE40

site_id	AK9
Number of Residues	2
Details	binding site for residue CA AF 103

Chain	Residue
AF	ARG45
AV	GLU49

site_id	AL1
Number of Residues	16
Details	binding site for residue DGD AH 101

Chain	Residue
AB	TYR193
AB	PHE250
AB	TYR258
AB	THR271
AB	TYR273
AB	PHE463
AB	CLA608
AD	GLY86
AD	HIS87
AD	LEU162
AD	SER165
AH	TYR49
AH	ASN50
AH	VAL60
AH	SER61
AH	TRP62

site_id	AL2
Number of Residues	7
Details	binding site for residue LMG AI 101

Chain	Residue
AA	CLA407
AI	MET1
AI	GLU2
AI	THR3
AI	LEU4
AI	LMT102
BB	DGD5602

site_id	AL3
Number of Residues	6
Details	binding site for residue LMT AI 102

Chain	Residue
AI	THR3
AI	ILE6
AI	ILE10
AI	VAL11
AI	PHE14
AI	LMG101

site_id	AL4
Number of Residues	6
Details	binding site for residue LMT AI 103

Chain	Residue
AA	GLU15
AC	ARG262
AI	PHE21
AI	LEU24
AI	SER25
AI	GLY26

site_id	AL5
Number of Residues	6
Details	binding site for residue BCR AJ 101

Chain	Residue
AC	CLA508
AC	DGD518
AC	LMG520
AJ	ILE22
AJ	PHE29
AJ	TYR33

site_id	AL6
Number of Residues	12
Details	binding site for residue LMG AJ 102

Chain	Residue
AA	LMG414
AD	TYR67
AD	CYS71
AD	PHE73
AD	BCR406
AF	THR30
AF	MET40
AF	GLN41
AJ	PHE28
AJ	GLY31
AJ	ALA32
AJ	GLY37

site_id	AL7
Number of Residues	2
Details	binding site for residue CA AK 101

Chain	Residue
AK	ASP19
AK	ASP23

site_id	AL8
Number of Residues	12
Details	binding site for residue BCR AK 102

Chain	Residue
AC	BCR514
AJ	GLY18
AJ	MET19
AK	LEU31
AK	PHE32
AK	PHE37
AK	VAL38
AZ	VAL13
AZ	SER16
AZ	PHE17
Ay	ILE28
Ay	GLY32

site_id	AL9
Number of Residues	12
Details	binding site for residue LMG AM 101

Chain	Residue
AM	ILE23
AM	GLU30
AM	SER31
AM	GLN32
AM	GLN33
BB	SQD5601
BB	CLA5618
BL	PRO5009
BL	VAL5010
BL	LMG5101
BM	ILE5024
BM	GLN5028

site_id	AM1
Number of Residues	6
Details	binding site for residue LMT AM 102

Chain	Residue
AB	LMG621
AM	GLN5
BM	MET5001
BM	GLU5002
BT	GLU5002
BT	THR5005

site_id	AM2
Number of Residues	1
Details	binding site for residue CA AO 301

Chain	Residue
AO	GLU140

site_id	AM3
Number of Residues	14
Details	binding site for residue BCR AT 101

Chain	Residue
AA	SQD416
AD	LMG408
AT	ILE4
AT	PHE8
AT	PHE17
AT	PHE18
AT	ILE21
AT	PHE22
BB	SER5036
BB	MET5037
BB	TYR5040
BB	CLA5611
BB	BCR5621
BB	BCR5622

site_id	AM4
Number of Residues	2
Details	binding site for residue DMS AU 201

Chain	Residue
AU	LYS134
AV	LYS160

site_id	AM5
Number of Residues	17
Details	binding site for residue HEM AV 201

Chain	Residue
AC	ALA393
AV	ALA62
AV	CYS63
AV	CYS66
AV	HIS67
AV	THR72
AV	THR74
AV	ASN75
AV	LEU78
AV	ASP79
AV	LEU80
AV	THR84
AV	TYR101
AV	MET102
AV	TYR108
AV	HIS118
AV	MET130

site_id	AM6
Number of Residues	2
Details	binding site for residue DMS AV 202

Chain	Residue
AC	THR397
AV	LYS73

site_id	AM7
Number of Residues	10
Details	binding site for residue BCR AX 101

Chain	Residue
AB	CLA601
AB	CLA609
AD	CLA404
AH	MET35
AH	PHE38
AH	PHE41
AX	THR11
AX	ILE12
AX	LEU16
AX	PHE20

site_id	AM8
Number of Residues	12
Details	binding site for residue SQD BA 5401

Chain	Residue
AB	TRP113
AB	TYR117
AB	CLA616
AB	BCR619
BA	TRP5020
BA	ASN5026
BA	ARG5027
BA	LEU5028
BA	ILE5038
BA	LEU5042
BI	LMG5101
BT	BCR5101

site_id	AM9
Number of Residues	13
Details	binding site for residue LMG BA 5402

Chain	Residue
AB	LEU39
AB	ALA43
AB	TRP75
AB	SER76
AB	LEU98
AB	ILE101
AB	DGD628
AB	LMT629
BA	TYR5073
BA	LEU5102
BA	ASP5103
BO	GLY5138
BO	GLY5139

site_id	AN1
Number of Residues	8
Details	binding site for residue BCT BA 5403

Chain	Residue
BA	HIS5215
BA	GLU5244
BA	TYR5246
BA	HIS5272
BD	HIS5214
BD	TYR5244
BD	HIS5268
BD	FE25401

site_id	AN2
Number of Residues	8
Details	binding site for residue CL BA 5404

Chain	Residue
BA	ASP5061
BA	ILE5063
BA	GLU5065
BA	ASN5181
BA	HIS5332
BA	GLU5333
BA	ARG5334
BD	LYS5317

site_id	AN3
Number of Residues	23
Details	binding site for residue CLA BA 5405

Chain	Residue
BA	PHE5119
BA	PRO5150
BA	SER5153
BA	ALA5154
BA	VAL5157
BA	MET5183
BA	PHE5186
BA	GLN5187
BA	LEU5193
BA	HIS5198
BA	GLY5201
BA	VAL5205
BA	PHE5206
BA	THR5286
BA	ALA5287
BA	ILE5290
BA	CLA5406
BA	CLA5407
BD	LEU5182
BD	CLA5402
BD	PHO5403
BD	LMG5410
BT	PHE5017

site_id	AN4
Number of Residues	21
Details	binding site for residue CLA BA 5406

Chain	Residue
BA	THR5045
BA	VAL5157
BA	PHE5158
BA	MET5172
BA	ILE5176
BA	THR5179
BA	PHE5180
BA	PHE5182
BA	MET5183
BA	CLA5405
BD	MET5198
BD	VAL5201
BD	ALA5202
BD	GLY5206
BD	CLA5402
BD	PHO5403
BD	PL95406
BD	LMG5410
BL	LMG5101
BT	PHE5010
BT	ILE5014

site_id	AN5
Number of Residues	14
Details	binding site for residue CLA BA 5407

Chain	Residue
BA	GLN5199
BA	VAL5202
BA	ALA5203
BA	PHE5206
BA	CLA5405
BC	DGD5519
BD	PHE5157
BD	VAL5175
BD	ILE5178
BD	PHE5179
BD	PHE5181
BD	LEU5182
BD	CLA5402
BD	PHO5404

site_id	AN6
Number of Residues	19
Details	binding site for residue CLA BA 5408

Chain	Residue
BA	VAL5035
BA	ILE5036
BA	PRO5039
BA	THR5040
BA	PHE5093
BA	TYR5094
BA	PRO5095
BA	ILE5096
BA	TRP5097
BA	LEU5114
BA	HIS5118
BA	BCR5411
BA	DGD5412
BC	CLA5505
BI	VAL5008
BI	TYR5009
BI	VAL5012
BI	PHE5015
BI	LMG5101

site_id	AN7
Number of Residues	8
Details	binding site for residue MST BA 5409

Chain	Residue
BA	HIS5215
BA	LEU5218
BA	PHE5255
BA	SER5264
BA	PHE5265
BA	LEU5271
BA	PHE5274
BA	LEU5275

site_id	AN8
Number of Residues	8
Details	binding site for residue OEC BA 5410

Chain	Residue
BA	GLN5165
BA	ASP5170
BA	GLU5189
BA	HIS5332
BA	GLU5333
BA	ASP5342
BA	ALA5344
BC	GLU5354

site_id	AN9
Number of Residues	11
Details	binding site for residue BCR BA 5411

Chain	Residue
AB	LMT630
BA	ILE5038
BA	LEU5042
BA	ALA5043
BA	ILE5050
BA	ALA5051
BA	ALA5055
BA	LEU5102
BA	TRP5105
BA	CLA5408
BI	PHE5015

site_id	AO1
Number of Residues	14
Details	binding site for residue DGD BA 5412

Chain	Residue
BA	GLU5098
BA	PHE5117
BA	LEU5120
BA	LEU5121
BA	PHE5155
BA	CLA5408
BC	LEU5213
BC	SER5216
BC	PRO5217
BC	GLU5221
BC	TRP5223
BC	DGD5517
BI	LYS5005
BI	TYR5009

site_id	AO2
Number of Residues	17
Details	binding site for residue LHG BA 5413

Chain	Residue
BA	ARG5140
BA	TRP5142
BA	VAL5145
BA	PHE5273
BA	PHE5285
BA	SQD5414
BC	TRP5036
BC	PHE5436
BC	TRP5443
BC	ARG5447
BC	CLA5504
BC	CLA5508
BD	GLU5219
BD	ASN5220
BD	ALA5229
BD	THR5231
BD	PHE5232

site_id	AO3
Number of Residues	12
Details	binding site for residue SQD BA 5414

Chain	Residue
BA	ASN5267
BA	SER5270
BA	PHE5273
BA	LHG5413
BA	LHG5415
BC	ALA5034
BC	TRP5036
BC	CLA5508
BC	DGD5518
BD	PHE5232
BD	ARG5233
BK	PHE5037

site_id	AO4
Number of Residues	7
Details	binding site for residue LHG BA 5415

Chain	Residue
BA	TYR5262
BA	SER5264
BA	PHE5265
BA	ASN5266
BA	SQD5414
BC	TRP5035
BK	PHE5045

site_id	AO5
Number of Residues	13
Details	binding site for residue SQD BB 5601

Chain	Residue
AL	ARG14
AL	TYR18
AM	TYR26
AM	LMG101
AT	ALA15
AT	PHE19
AT	PHE23
BB	ARG5018
BB	LEU5029
BB	SER5104
BB	TRP5115
BB	CLA5618
BB	BCR5621

site_id	AO6
Number of Residues	11
Details	binding site for residue DGD BB 5602

Chain	Residue
AA	ILE46
AA	ILE50
AA	LMG417
AI	LMG101
BB	TRP5075
BB	ASP5087
BB	PRO5088
BB	GLY5089
BB	PHE5090
BB	LMT5604
BB	LMT5626

site_id	AO7
Number of Residues	5
Details	binding site for residue LMT BB 5603

Chain	Residue
AA	LMG417
AT	ILE4
BB	LEU5039
BB	THR5044
BB	THR5436

site_id	AO8
Number of Residues	6
Details	binding site for residue LMT BB 5604

Chain	Residue
AI	MET1
AI	LEU4
AO	LYS95
BB	GLY5085
BB	ASP5087
BB	DGD5602

site_id	AO9
Number of Residues	8
Details	binding site for residue CLA BB 5605

Chain	Residue
BB	TRP5185
BB	PRO5187
BB	PHE5190
BB	ILE5207
BB	VAL5208
BB	CLA5606
BH	PHE5041
BX	BCR5101

site_id	AP1
Number of Residues	22
Details	binding site for residue CLA BB 5606

Chain	Residue
BB	GLU5184
BB	TRP5185
BB	GLY5189
BB	PRO5192
BB	ALA5200
BB	HIS5201
BB	ALA5204
BB	ALA5205
BB	VAL5208
BB	PHE5246
BB	PHE5247
BB	VAL5251
BB	CLA5605
BB	CLA5607
BD	VAL5154
BD	ILE5159
BD	LEU5162
BH	PHE5038
BH	PHE5041
BH	ILE5045
BH	LEU5046
BH	TYR5049

site_id	AP2
Number of Residues	19
Details	binding site for residue CLA BB 5607

Chain	Residue
BB	ARG5068
BB	LEU5069
BB	ALA5146
BB	CYS5150
BB	PHE5153
BB	VAL5198
BB	HIS5201
BB	HIS5202
BB	PHE5247
BB	ALA5248
BB	VAL5251
BB	VAL5252
BB	THR5262
BB	CLA5606
BB	CLA5608
BB	CLA5609
BB	CLA5610
BB	CLA5614
BH	PHE5038

site_id	AP3
Number of Residues	20
Details	binding site for residue CLA BB 5608

Chain	Residue
BB	TRP5033
BB	PHE5065
BB	ARG5068
BB	LEU5148
BB	VAL5245
BB	ALA5248
BB	ALA5249
BB	VAL5252
BB	PHE5451
BB	HIS5455
BB	PHE5458
BB	ALA5459
BB	PHE5462
BB	CLA5607
BB	CLA5609
BB	CLA5611
BB	CLA5615
BB	CLA5616
BB	CLA5617
BB	CLA5619

site_id	AP4
Number of Residues	19
Details	binding site for residue CLA BB 5609

Chain	Residue
BB	THR5027
BB	VAL5030
BB	ALA5031
BB	TRP5033
BB	ALA5034
BB	VAL5062
BB	PHE5065
BB	MET5066
BB	ARG5068
BB	LEU5069
BB	HIS5100
BB	LEU5103
BB	GLY5147
BB	CLA5607
BB	CLA5608
BB	CLA5610
BB	CLA5613
BB	CLA5614
BB	BCR5623

site_id	AP5
Number of Residues	19
Details	binding site for residue CLA BB 5610

Chain	Residue
BB	GLY5070
BB	VAL5071
BB	TRP5091
BB	ALA5099
BB	HIS5100
BB	VAL5102
BB	LEU5103
BB	LEU5149
BB	GLY5152
BB	PHE5153
BB	PHE5156
BB	HIS5157
BB	PHE5162
BB	GLY5163
BB	PRO5164
BB	CLA5607
BB	CLA5609
BB	BCR5623
BB	LMT5626

site_id	AP6
Number of Residues	22
Details	binding site for residue CLA BB 5611

Chain	Residue
AT	BCR101
BB	TRP5033
BB	MET5037
BB	TYR5040
BB	GLN5058
BB	GLY5059
BB	PHE5061
BB	PHE5325
BB	THR5327
BB	GLY5328
BB	PRO5329
BB	TRP5450
BB	PHE5451
BB	ALA5454
BB	CLA5608
BB	CLA5617
BB	LMG5624
BD	MET5199
BD	MET5281
BL	PHE5031
BL	PHE5035
BM	PHE5014

site_id	AP7
Number of Residues	19
Details	binding site for residue CLA BB 5612

Chain	Residue
BB	THR5236
BB	SER5239
BB	SER5240
BB	ALA5243
BB	PHE5247
BB	HIS5466
BB	ILE5467
BB	CLA5613
BB	CLA5614
BB	SQD5625
BB	LMT5627
BD	PHE5120
BD	ILE5123
BD	MET5126
BD	LEU5127
BD	PHE5130
BD	CLA5405
BH	LEU5043
BH	DGD5101

site_id	AP8
Number of Residues	19
Details	binding site for residue CLA BB 5613

Chain	Residue
BB	PHE5139
BB	VAL5208
BB	ALA5212
BB	PHE5215
BB	HIS5216
BB	ARG5220
BB	PRO5221
BB	PRO5222
BB	LEU5225
BB	LEU5229
BB	CLA5609
BB	CLA5612
BB	CLA5614
BH	THR5027
BH	THR5028
BH	MET5031
BH	PHE5034
BH	MET5035
BX	BCR5101

site_id	AP9
Number of Residues	16
Details	binding site for residue CLA BB 5614

Chain	Residue
BB	LEU5135
BB	PHE5139
BB	HIS5142
BB	LEU5143
BB	ALA5146
BB	MET5231
BB	VAL5237
BB	SER5240
BB	SER5241
BB	VAL5245
BB	CLA5607
BB	CLA5609
BB	CLA5612
BB	CLA5613
BB	CLA5616
BB	CLA5619

site_id	AQ1
Number of Residues	19
Details	binding site for residue CLA BB 5615

Chain	Residue
BB	TRP5005
BB	TYR5006
BB	ARG5007
BB	VAL5008
BB	HIS5009
BB	ILE5242
BB	LEU5461
BB	PHE5462
BB	PHE5464
BB	GLY5465
BB	TRP5468
BB	HIS5469
BB	ARG5472
BB	CLA5608
BB	CLA5616
BB	CLA5617
BB	CLA5618
BD	LMG5409
BL	LMG5101

site_id	AQ2
Number of Residues	15
Details	binding site for residue CLA BB 5616

Chain	Residue
BB	HIS5009
BB	LEU5019
BB	HIS5023
BB	HIS5026
BB	THR5027
BB	GLU5235
BB	VAL5237
BB	LEU5238
BB	SER5241
BB	VAL5245
BB	CLA5608
BB	CLA5614
BB	CLA5615
BB	CLA5617
BB	CLA5619

site_id	AQ3
Number of Residues	12
Details	binding site for residue CLA BB 5617

Chain	Residue
BB	HIS5009
BB	HIS5026
BB	VAL5030
BB	TRP5033
BB	PHE5462
BB	CLA5608
BB	CLA5611
BB	CLA5615
BB	CLA5616
BB	CLA5618
BB	BCR5621
BD	LMG5409

site_id	AQ4
Number of Residues	16
Details	binding site for residue CLA BB 5618

Chain	Residue
AM	LMG101
AT	PHE8
BB	VAL5008
BB	HIS5009
BB	VAL5011
BB	ALA5022
BB	LEU5029
BB	TRP5115
BB	SQD5601
BB	CLA5615
BB	CLA5617
BB	BCR5621
BB	LMG5624
BL	VAL5010
BL	LMG5101
BM	PHE5021

site_id	AQ5
Number of Residues	14
Details	binding site for residue CLA BB 5619

Chain	Residue
BB	ILE5020
BB	HIS5023
BB	LEU5024
BB	LEU5107
BB	MET5138
BB	ILE5141
BB	HIS5142
BB	LEU5145
BB	CLA5608
BB	CLA5614
BB	CLA5616
BB	CLA5620
BB	BCR5623
BH	LEU5014

site_id	AQ6
Number of Residues	11
Details	binding site for residue CLA BB 5620

Chain	Residue
AA	SQD416
BB	LEU5024
BB	ALA5110
BB	TRP5113
BB	HIS5114
BB	LEU5120
BB	CLA5619
BB	BCR5623
BH	THR5005
BH	LEU5007
BH	GLY5008

site_id	AQ7
Number of Residues	13
Details	binding site for residue BCR BB 5621

Chain	Residue
AT	PHE19
AT	BCR101
BB	ALA5021
BB	MET5025
BB	LEU5029
BB	CYS5112
BB	TRP5115
BB	SQD5601
BB	CLA5617
BB	CLA5618
BB	BCR5622
BB	LMG5624
BM	ILE5009

site_id	AQ8
Number of Residues	7
Details	binding site for residue BCR BB 5622

Chain	Residue
AT	BCR101
BB	LEU5029
BB	TRP5033
BB	VAL5102
BB	GLY5105
BB	LEU5109
BB	BCR5621

site_id	AQ9
Number of Residues	11
Details	binding site for residue BCR BB 5623

Chain	Residue
AA	SQD416
AT	PHE22
AT	PHE23
BB	LEU5106
BB	LEU5109
BB	CYS5112
BB	VAL5116
BB	CLA5609
BB	CLA5610
BB	CLA5619
BB	CLA5620

site_id	AR1
Number of Residues	13
Details	binding site for residue LMG BB 5624

Chain	Residue
BB	THR5327
BB	GLY5328
BB	PRO5329
BB	LYS5332
BB	VAL5457
BB	LEU5461
BB	CLA5611
BB	CLA5618
BB	BCR5621
BD	MET5281
BD	ILE5284
BL	PHE5035
BM	LMT5101

site_id	AR2
Number of Residues	10
Details	binding site for residue SQD BB 5625

Chain	Residue
BB	LYS5227
BB	ALA5228
BB	ARG5230
BB	LEU5474
BB	CLA5612
BB	LMT5627
BD	LYS5023
BD	TRP5032
BD	ARG5134
BD	LEU5135

site_id	AR3
Number of Residues	3
Details	binding site for residue LMT BB 5626

Chain	Residue
BB	ASP5087
BB	DGD5602
BB	CLA5610

site_id	AR4
Number of Residues	9
Details	binding site for residue LMT BB 5627

Chain	Residue
BB	ARG5224
BB	LEU5225
BB	CLA5612
BB	SQD5625
BD	PHE5015
BD	ASP5016
BD	ASP5019
BD	LYS5023
BH	MET5035

site_id	AR5
Number of Residues	4
Details	binding site for residue DMS BB 5628

Chain	Residue
BB	GLU5387
BU	LYS5134
BV	PRO5076
BV	SER5077

site_id	AR6
Number of Residues	5
Details	binding site for residue DMS BB 5629

Chain	Residue
BB	TRP5275
BB	ASP5276
BB	SER5278
BB	MET5359
BB	PRO5360

site_id	AR7
Number of Residues	19
Details	binding site for residue CLA BC 5501

Chain	Residue
BC	LEU5095
BC	LEU5168
BC	GLY5171
BC	ALA5172
BC	LEU5175
BC	VAL5233
BC	HIS5237
BC	ILE5240
BC	ALA5278
BC	MET5281
BC	MET5282
BC	ILE5285
BC	PHE5289
BC	VAL5296
BC	TYR5297
BC	CLA5502
BC	CLA5503
BC	CLA5507
BC	BCR5516

site_id	AR8
Number of Residues	16
Details	binding site for residue CLA BC 5502

Chain	Residue
BC	TRP5063
BC	HIS5091
BC	LEU5095
BC	LEU5174
BC	PHE5182
BC	LEU5279
BC	MET5282
BC	ALA5286
BC	TYR5297
BC	HIS5430
BC	LEU5433
BC	PHE5437
BC	CLA5501
BC	CLA5503
BC	CLA5504
BC	CLA5510

site_id	AR9
Number of Residues	18
Details	binding site for residue CLA BC 5503

Chain	Residue
BC	ILE5060
BC	VAL5061
BC	TRP5063
BC	ALA5064
BC	THR5068
BC	LEU5088
BC	HIS5091
BC	LEU5095
BC	VAL5114
BC	HIS5118
BC	LEU5279
BC	MET5282
BC	CLA5501
BC	CLA5502
BC	CLA5509
BC	CLA5510
BC	CLA5512
BC	LMG5521

site_id	AS1
Number of Residues	16
Details	binding site for residue CLA BC 5504

Chain	Residue
BA	PHE5197
BA	LHG5413
BC	TRP5063
BC	MET5067
BC	PHE5070
BC	GLN5084
BC	GLY5085
BC	SER5406
BC	TRP5425
BC	SER5429
BC	CLA5502
BC	CLA5510
BC	DGD5518
BC	DGD5519
BC	LMG5520
BK	PRO5026

site_id	AS2
Number of Residues	15
Details	binding site for residue CLA BC 5505

Chain	Residue
BA	PHE5033
BA	MET5127
BA	TRP5131
BA	CLA5408
BC	SER5273
BC	TYR5274
BC	GLY5277
BC	ALA5278
BC	HIS5441
BC	LEU5442
BC	ALA5445
BC	ARG5449
BC	CLA5507
BI	PHE5019
BI	PHE5023

site_id	AS3
Number of Residues	14
Details	binding site for residue CLA BC 5506

Chain	Residue
BC	LEU5161
BC	LEU5165
BC	LEU5213
BC	ILE5243
BC	CYS5244
BC	GLY5247
BC	TRP5250
BC	HIS5251
BC	THR5255
BC	PHE5257
BC	TRP5259
BC	ALA5260
BC	PHE5264
BC	CLA5507

site_id	AS4
Number of Residues	14
Details	binding site for residue CLA BC 5507

Chain	Residue
BC	MET5157
BC	LEU5161
BC	HIS5164
BC	LEU5168
BC	PHE5264
BC	TRP5266
BC	TYR5271
BC	TYR5274
BC	SER5275
BC	CLA5501
BC	CLA5505
BC	CLA5506
BC	CLA5509
BC	BCR5516

site_id	AS5
Number of Residues	17
Details	binding site for residue CLA BC 5508

Chain	Residue
BA	LHG5413
BA	SQD5414
BC	TRP5036
BC	ALA5037
BC	GLY5038
BC	ASN5039
BC	ALA5040
BC	GLU5269
BC	LEU5276
BC	PHE5436
BC	PHE5437
BC	GLY5440
BC	TRP5443
BC	HIS5444
BC	ARG5447
BC	CLA5509
BC	CLA5510

site_id	AS6
Number of Residues	18
Details	binding site for residue CLA BC 5509

Chain	Residue
BC	ASN5039
BC	LEU5049
BC	ALA5052
BC	HIS5053
BC	HIS5056
BC	ILE5060
BC	TYR5149
BC	TRP5151
BC	GLY5268
BC	TYR5271
BC	LEU5272
BC	SER5275
BC	LEU5279
BC	CLA5503
BC	CLA5507
BC	CLA5508
BC	CLA5510
BC	CLA5512

site_id	AS7
Number of Residues	15
Details	binding site for residue CLA BC 5510

Chain	Residue
BC	ASN5039
BC	HIS5056
BC	LEU5059
BC	ILE5060
BC	LEU5279
BC	PHE5437
BC	CLA5502
BC	CLA5503
BC	CLA5504
BC	CLA5508
BC	CLA5509
BC	CLA5511
BK	PRO5029
BK	VAL5030
BK	LEU5033

site_id	AS8
Number of Residues	25
Details	binding site for residue CLA BC 5511

Chain	Residue
BC	GLN5028
BC	TRP5035
BC	GLY5038
BC	ASN5039
BC	ARG5041
BC	LEU5042
BC	LEU5045
BC	LYS5048
BC	ALA5052
BC	ALA5123
BC	PHE5127
BC	VAL5130
BC	ALA5133
BC	ILE5134
BC	CLA5510
BC	BCR5514
BK	PHE5032
BK	LEU5033
BK	PHE5037
BK	TRP5039
BK	GLN5040
BZ	VAL5020
BZ	VAL5023
BZ	PRO5024
By	ILE5035

site_id	AS9
Number of Residues	12
Details	binding site for residue CLA BC 5512

Chain	Residue
BC	HIS5053
BC	ALA5057
BC	PHE5147
BC	ILE5160
BC	PHE5163
BC	HIS5164
BC	VAL5167
BC	CLA5503
BC	CLA5509
BC	CLA5513
BC	BCR5515
BC	LMG5521

site_id	AT1
Number of Residues	13
Details	binding site for residue CLA BC 5513

Chain	Residue
BC	LEU5050
BC	VAL5054
BC	VAL5124
BC	LEU5125
BC	GLY5128
BC	TYR5131
BC	HIS5132
BC	PRO5137
BC	LEU5140
BC	TYR5143
BC	PHE5147
BC	CLA5512
BC	BCR5515

site_id	AT2
Number of Residues	17
Details	binding site for residue BCR BC 5514

Chain	Residue
BC	ALA5055
BC	GLY5058
BC	VAL5116
BC	ILE5120
BC	SER5122
BC	ALA5123
BC	CLA5511
BC	BCR5515
BK	TYR5015
BK	PHE5018
BK	PHE5032
BK	LEU5035
BK	ALA5036
BK	TRP5039
BK	BCR5102
BZ	VAL5013
BZ	VAL5020

site_id	AT3
Number of Residues	12
Details	binding site for residue BCR BC 5515

Chain	Residue
BC	PHE5109
BC	VAL5116
BC	SER5121
BC	VAL5124
BC	PHE5147
BC	CLA5512
BC	CLA5513
BC	BCR5514
BK	TYR5015
BZ	VAL5054
BZ	GLY5055
BZ	ASN5058

site_id	AT4
Number of Residues	14
Details	binding site for residue BCR BC 5516

Chain	Residue
BC	ILE5209
BC	TYR5212
BC	LEU5213
BC	VAL5227
BC	ASP5232
BC	VAL5233
BC	HIS5237
BC	ILE5240
BC	PHE5264
BC	CLA5501
BC	CLA5507
BI	VAL5020
BI	PHE5023
BI	LEU5024

site_id	AT5
Number of Residues	19
Details	binding site for residue DGD BC 5517

Chain	Residue
BA	PHE5155
BA	ILE5160
BA	ILE5163
BA	DGD5412
BC	PRO5217
BC	PHE5218
BC	GLY5219
BC	GLY5220
BC	GLY5222
BC	TRP5223
BC	VAL5225
BC	SER5226
BC	ASN5228
BC	PHE5284
BC	CYS5288
BC	PHE5292
BC	ASN5294
BC	THR5295
BC	LEU5438

site_id	AT6
Number of Residues	19
Details	binding site for residue DGD BC 5518

Chain	Residue
BA	LEU5288
BA	THR5292
BA	SQD5414
BC	TYR5082
BC	GLU5083
BC	GLN5084
BC	GLY5085
BC	ASN5418
BC	PHE5419
BC	VAL5420
BC	TRP5425
BC	THR5428
BC	VAL5432
BC	CLA5504
BC	DGD5519
BC	LMG5520
BJ	PHE5029
BJ	TYR5033
BJ	BCR5101

site_id	AT7
Number of Residues	24
Details	binding site for residue DGD BC 5519

Chain	Residue
BA	LEU5200
BA	TRP5278
BA	VAL5281
BA	PHE5300
BA	PHE5302
BA	SER5305
BA	CLA5407
BC	LEU5404
BC	ASN5405
BC	SER5406
BC	VAL5407
BC	ASN5415
BC	SER5416
BC	VAL5417
BC	ASN5418
BC	CLA5504
BC	DGD5518
BJ	PHE5029
BJ	ALA5032
BJ	TYR5033
BJ	GLY5037
BJ	SER5038
BJ	LEU5040
BV	GLN5060

site_id	AT8
Number of Residues	5
Details	binding site for residue LMG BC 5520

Chain	Residue
BC	HIS5074
BC	CLA5504
BC	DGD5518
BJ	BCR5101
BK	VAL5030

site_id	AT9
Number of Residues	9
Details	binding site for residue LMG BC 5521

Chain	Residue
BC	TRP5097
BC	PHE5109
BC	PRO5110
BC	VAL5113
BC	VAL5114
BC	VAL5117
BC	HIS5118
BC	CLA5503
BC	CLA5512

site_id	AU1
Number of Residues	6
Details	binding site for residue LMT BC 5522

Chain	Residue
BA	GLU5015
BC	ARG5262
BI	PHE5021
BI	LEU5024
BI	SER5025
BI	GLY5026

site_id	AU2
Number of Residues	5
Details	binding site for residue FE2 BD 5401

Chain	Residue
BA	HIS5215
BA	HIS5272
BA	BCT5403
BD	HIS5214
BD	HIS5268

site_id	AU3
Number of Residues	23
Details	binding site for residue CLA BD 5402

Chain	Residue
BA	PHE5206
BA	CLA5405
BA	CLA5406
BA	CLA5407
BD	LEU5045
BD	LEU5122
BD	PRO5149
BD	VAL5152
BD	PHE5153
BD	SER5155
BD	VAL5156
BD	LEU5182
BD	PHE5185
BD	GLN5186
BD	TRP5191
BD	THR5192
BD	HIS5197
BD	VAL5201
BD	VAL5204
BD	LEU5279
BD	SER5282
BD	ALA5283
BD	PHO5404

site_id	AU4
Number of Residues	19
Details	binding site for residue PHO BD 5403

Chain	Residue
BA	LEU5041
BA	ALA5044
BA	PHE5119
BA	TYR5126
BA	GLN5130
BA	ALA5146
BA	TYR5147
BA	PHE5158
BA	GLY5175
BA	VAL5283
BA	CLA5405
BA	CLA5406
BD	ALA5208
BD	LEU5209
BD	ALA5212
BD	ILE5213
BD	TRP5253
BD	PHE5257
BD	LMG5410

site_id	AU5
Number of Residues	20
Details	binding site for residue PHO BD 5404

Chain	Residue
BA	PHE5206
BA	ALA5209
BA	LEU5210
BA	MET5214
BA	CLA5407
BD	ALA5041
BD	TRP5048
BD	GLY5118
BD	PHE5125
BD	GLN5129
BD	ASN5142
BD	ALA5145
BD	PHE5146
BD	ALA5148
BD	PRO5149
BD	PHE5153
BD	GLY5174
BD	VAL5175
BD	PRO5275
BD	CLA5402

site_id	AU6
Number of Residues	18
Details	binding site for residue CLA BD 5405

Chain	Residue
BB	CLA5612
BD	ILE5035
BD	PRO5039
BD	CYS5040
BD	LEU5043
BD	LEU5089
BD	LEU5090
BD	LEU5091
BD	LEU5092
BD	TRP5093
BD	PHE5113
BD	HIS5117
BD	PHE5120
BD	LMT5411
BH	GLU5047
BX	LEU5023
BX	LEU5030
BX	BCR5101

site_id	AU7
Number of Residues	23
Details	binding site for residue PL9 BD 5406

Chain	Residue
BA	PHE5048
BA	PHE5052
BA	ILE5053
BA	CLA5406
BD	MET5199
BD	ALA5202
BD	LEU5209
BD	LEU5210
BD	ILE5213
BD	HIS5214
BD	THR5217
BD	TRP5253
BD	ALA5260
BD	PHE5261
BD	LEU5267
BD	VAL5274
BD	THR5277
BD	GLY5278
BD	LMG5410
BL	LEU5027
BL	LEU5029
BL	LMG5101
BT	PHE5010

site_id	AU8
Number of Residues	11
Details	binding site for residue BCR BD 5407

Chain	Residue
BD	TYR5042
BD	GLY5046
BD	LEU5049
BD	PHE5101
BD	PHE5113
BD	LMG5408
BE	DGD5102
BF	PHE5033
BF	LEU5034
BJ	VAL5021
BJ	VAL5025

site_id	AU9
Number of Residues	12
Details	binding site for residue LMG BD 5408

Chain	Residue
BD	TYR5067
BD	CYS5071
BD	ASN5072
BD	PHE5073
BD	BCR5407
BE	LMG5101
BF	THR5030
BF	MET5040
BF	GLN5041
BJ	GLY5031
BJ	ALA5032
BJ	GLY5037

site_id	AV1
Number of Residues	18
Details	binding site for residue LMG BD 5409

Chain	Residue
BA	ASN5234
BB	TYR5006
BB	ARG5007
BB	PHE5464
BB	TRP5468
BB	PHE5479
BB	CLA5615
BB	CLA5617
BD	ARG5139
BD	TYR5141
BD	PHE5269
BD	PHE5273
BD	VAL5276
BD	TRP5280
BL	LMG5101
BM	PHE5014
BM	VAL5017
BM	PRO5018

site_id	AV2
Number of Residues	19
Details	binding site for residue LMG BD 5410

Chain	Residue
BA	CLA5405
BA	CLA5406
BD	PHE5257
BD	ALA5260
BD	PHE5261
BD	SER5262
BD	ASN5263
BD	TRP5266
BD	PHO5403
BD	PL95406
BL	ASN5013
BL	THR5015
BL	LEU5019
BL	LEU5022
BL	LMG5101
BT	PHE5010
BT	PHE5017
BT	ALA5020
BT	ILE5021

site_id	AV3
Number of Residues	7
Details	binding site for residue LMT BD 5411

Chain	Residue
BD	GLY5099
BD	ASP5100
BD	PHE5101
BD	CLA5405
BE	DGD5102
BX	ILE5021
BX	SER5025

site_id	AV4
Number of Residues	7
Details	binding site for residue LMG BE 5101

Chain	Residue
BA	PHE5260
BA	TYR5262
BD	PHE5027
BD	LMG5408
BE	PRO5009
BE	PHE5010
BE	SER5011

site_id	AV5
Number of Residues	7
Details	binding site for residue DGD BE 5102

Chain	Residue
BD	PHE5101
BD	BCR5407
BD	LMT5411
BE	ASP5045
BE	VAL5046
BF	VAL5028
BF	PHE5032

site_id	AV6
Number of Residues	14
Details	binding site for residue HEM BF 5101

Chain	Residue
BE	ARG5008
BE	PHE5010
BE	ILE5013
BE	TYR5019
BE	HIS5023
BE	THR5026
BE	ILE5027
BE	LEU5030
BF	ILE5015
BF	ARG5019
BF	TRP5020
BF	HIS5024
BF	ALA5027
BF	ILE5031

site_id	AV7
Number of Residues	11
Details	binding site for residue SQD BF 5102

Chain	Residue
BD	TRP5021
BD	ARG5024
BD	ARG5026
BE	GLU5007
BF	PRO5014
BF	PHE5016
BF	THR5017
BF	VAL5018
BF	VAL5021
BX	THR5033
BX	ILE5040

site_id	AV8
Number of Residues	2
Details	binding site for residue CA BF 5103

Chain	Residue
BF	ARG5045
BV	GLU5049

site_id	AV9
Number of Residues	16
Details	binding site for residue DGD BH 5101

Chain	Residue
BB	TYR5193
BB	PHE5250
BB	TYR5258
BB	THR5271
BB	TYR5273
BB	PHE5463
BB	CLA5612
BD	GLY5086
BD	HIS5087
BD	LEU5162
BD	SER5165
BH	TYR5049
BH	ASN5050
BH	VAL5060
BH	SER5061
BH	TRP5062

site_id	AW1
Number of Residues	8
Details	binding site for residue LMG BI 5101

Chain	Residue
AB	DGD628
BA	SQD5401
BA	CLA5408
BI	MET5001
BI	GLU5002
BI	THR5003
BI	LEU5004
BI	LMT5102

site_id	AW2
Number of Residues	6
Details	binding site for residue LMT BI 5102

Chain	Residue
BI	THR5003
BI	ILE5006
BI	ILE5010
BI	VAL5011
BI	PHE5014
BI	LMG5101

site_id	AW3
Number of Residues	5
Details	binding site for residue BCR BJ 5101

Chain	Residue
BC	DGD5518
BC	LMG5520
BJ	ILE5022
BJ	PHE5029
BJ	TYR5033

site_id	AW4
Number of Residues	2
Details	binding site for residue CA BK 5101

Chain	Residue
BK	ASP5019
BK	ASP5023

site_id	AW5
Number of Residues	12
Details	binding site for residue BCR BK 5102

Chain	Residue
BC	BCR5514
BJ	GLY5018
BJ	MET5019
BK	LEU5021
BK	LEU5031
BK	PHE5032
BK	PHE5037
BK	VAL5038
BZ	VAL5013
BZ	SER5016
BZ	PHE5017
By	ILE5028

site_id	AW6
Number of Residues	20
Details	binding site for residue LMG BL 5101

Chain	Residue
AM	LMG101
BA	SER5232
BA	ASN5234
BA	CLA5406
BB	TRP5005
BB	CLA5615
BB	CLA5618
BD	TRP5266
BD	PHE5273
BD	PL95406
BD	LMG5409
BD	LMG5410
BL	GLU5011
BL	ASN5013
BL	SER5016
BL	LEU5019
BL	LEU5022
BL	VAL5026
BM	PHE5021
BM	LEU5022

site_id	AW7
Number of Residues	7
Details	binding site for residue LMT BM 5101

Chain	Residue
AM	MET1
AM	GLU2
AT	GLU2
AT	THR5
AT	PHE8
BB	LMG5624
BM	GLN5005

site_id	AW8
Number of Residues	11
Details	binding site for residue LMG BM 5102

Chain	Residue
AB	CLA614
AB	LMG620
AB	SQD627
AL	PRO9
AL	VAL10
AM	ILE24
AM	GLN28
BM	GLU5030
BM	SER5031
BM	GLN5032
BM	GLN5033

site_id	AW9
Number of Residues	2
Details	binding site for residue CA BO 5301

Chain	Residue
BO	GLU5140
BO	HIS5257

site_id	AX1
Number of Residues	8
Details	binding site for residue BCR BT 5101

Chain	Residue
AB	SER36
AB	TYR40
AB	CLA607
AB	BCR617
AB	BCR618
BA	SQD5401
BT	ILE5004
BT	PHE5018

site_id	AX2
Number of Residues	18
Details	binding site for residue HEM BV 5201

Chain	Residue
BC	ALA5393
BV	ALA5062
BV	CYS5063
BV	CYS5066
BV	HIS5067
BV	THR5072
BV	THR5074
BV	ASN5075
BV	LEU5078
BV	ASP5079
BV	LEU5080
BV	THR5084
BV	LEU5085
BV	TYR5101
BV	MET5102
BV	TYR5108
BV	HIS5118
BV	MET5130

site_id	AX3
Number of Residues	3
Details	binding site for residue DMS BV 5202

Chain	Residue
BA	LEU5343
BC	THR5397
BV	LYS5073

site_id	AX4
Number of Residues	4
Details	binding site for residue DMS BV 5203

Chain	Residue
BU	LYS5134
BV	GLY5159
BV	LYS5160
BV	TYR5163

site_id	AX5
Number of Residues	10
Details	binding site for residue BCR BX 5101

Chain	Residue
BB	CLA5605
BB	CLA5613
BD	CLA5405
BH	MET5035
BH	PHE5038
BH	PHE5041
BX	THR5011
BX	ILE5012
BX	LEU5016
BX	PHE5020

Functional Information from PROSITE/UniProt

site_id	PS00244
Number of Residues	27
Details	REACTION_CENTER Photosynthetic reaction center proteins signature. NilmhPfHqlGvagvfggalfcAmHGS

Chain	Residue	Details
AA	ASN191-SER217
AD	ASN190-ALA216

site_id	PS00537
Number of Residues	15
Details	CYTOCHROME_B559 Cytochrome b559 subunits heme-binding site signature. ItSVRYwvIHSITIP

Chain	Residue	Details
AE	ILE14-PRO28
AF	ILE15-PRO29

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	470
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	840
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	216
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Site: {"description":"Tyrosine radical intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11217865","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Site: {"description":"Stabilizes free radical intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	258
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	452
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	92
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01496","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	664
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	474
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	246
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_00642","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_00643","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16172937","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	8
Details	Modified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	28
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	26
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	40
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00808","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"12881497","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgangb K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/b406989g"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	6
Details	Topological domain: {"description":"Lumenal"}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)