HEADER MEMBRANE PROTEIN 24-MAY-18 6DJB
TITLE STRUCTURE OF HUMAN VOLUME REGULATED ANION CHANNEL COMPOSED OF SWELL1
TITLE 2 (LRRC8A)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VOLUME-REGULATED ANION CHANNEL SUBUNIT LRRC8A;
COMPND 3 CHAIN: A, B, E, F, C, D;
COMPND 4 SYNONYM: LEUCINE-RICH REPEAT-CONTAINING PROTEIN 8A,SWELLING PROTEIN
COMPND 5 1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: LRRC8A, KIAA1437, LRRC8, SWELL1, UNQ221/PRO247;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK 293F LRRC8(B,C,D,E)-/-
KEYWDS ANION CHANNEL, LRRC8A, SWELL1, MEMBRANE PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR J.M.KEFAUVER,K.SAOTOME,J.PALLESEN,C.A.COTTRELL,A.B.WARD,A.PATAPOUTIAN
REVDAT 4 18-DEC-19 6DJB 1 CRYST1 SCALE
REVDAT 3 20-NOV-19 6DJB 1 REMARK
REVDAT 2 22-AUG-18 6DJB 1 JRNL
REVDAT 1 15-AUG-18 6DJB 0
JRNL AUTH J.M.KEFAUVER,K.SAOTOME,A.E.DUBIN,J.PALLESEN,C.A.COTTRELL,
JRNL AUTH 2 S.M.CAHALAN,Z.QIU,G.HONG,C.S.CROWLEY,T.WHITWAM,W.H.LEE,
JRNL AUTH 3 A.B.WARD,A.PATAPOUTIAN
JRNL TITL STRUCTURE OF THE HUMAN VOLUME REGULATED ANION CHANNEL.
JRNL REF ELIFE V. 7 2018
JRNL REFN ESSN 2050-084X
JRNL PMID 30095067
JRNL DOI 10.7554/ELIFE.38461
REMARK 2
REMARK 2 RESOLUTION. 4.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : GCTF, RELION
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 4.400
REMARK 3 NUMBER OF PARTICLES : 25719
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 6DJB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1000234736.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : HOMOMERIC VOLUME REGULATED
REMARK 245 ANION CHANNEL COMPOSED OF SWELL1
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 8.00
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 8.00
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 4627
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TALOS ARCTICA
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 800.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 1500.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 55.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 36000
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 200
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ILE A 2
REMARK 465 PRO A 3
REMARK 465 VAL A 4
REMARK 465 THR A 5
REMARK 465 GLU A 6
REMARK 465 LEU A 7
REMARK 465 ARG A 8
REMARK 465 TYR A 9
REMARK 465 PHE A 10
REMARK 465 ALA A 11
REMARK 465 ASP A 12
REMARK 465 THR A 13
REMARK 465 GLN A 14
REMARK 465 PHE A 69
REMARK 465 ARG A 70
REMARK 465 GLY A 71
REMARK 465 TRP A 72
REMARK 465 ALA A 73
REMARK 465 ALA A 74
REMARK 465 PRO A 75
REMARK 465 GLY A 76
REMARK 465 PRO A 77
REMARK 465 GLU A 78
REMARK 465 PRO A 79
REMARK 465 THR A 80
REMARK 465 TYR A 81
REMARK 465 PRO A 82
REMARK 465 ASN A 83
REMARK 465 SER A 84
REMARK 465 THR A 85
REMARK 465 ILE A 86
REMARK 465 LEU A 87
REMARK 465 PRO A 88
REMARK 465 THR A 89
REMARK 465 PRO A 90
REMARK 465 ASP A 91
REMARK 465 THR A 92
REMARK 465 GLY A 93
REMARK 465 GLU A 175
REMARK 465 THR A 176
REMARK 465 VAL A 177
REMARK 465 VAL A 178
REMARK 465 GLU A 179
REMARK 465 GLU A 180
REMARK 465 SER A 181
REMARK 465 ASP A 182
REMARK 465 PRO A 183
REMARK 465 LYS A 184
REMARK 465 PRO A 185
REMARK 465 ALA A 186
REMARK 465 PHE A 187
REMARK 465 SER A 188
REMARK 465 LYS A 189
REMARK 465 MET A 190
REMARK 465 ASN A 191
REMARK 465 GLY A 192
REMARK 465 SER A 193
REMARK 465 MET A 194
REMARK 465 ASP A 195
REMARK 465 LYS A 196
REMARK 465 LYS A 197
REMARK 465 SER A 198
REMARK 465 SER A 199
REMARK 465 THR A 200
REMARK 465 VAL A 201
REMARK 465 SER A 202
REMARK 465 GLU A 203
REMARK 465 ASP A 204
REMARK 465 VAL A 205
REMARK 465 GLU A 206
REMARK 465 ALA A 207
REMARK 465 THR A 208
REMARK 465 VAL A 209
REMARK 465 PRO A 210
REMARK 465 MET A 211
REMARK 465 LEU A 212
REMARK 465 GLN A 213
REMARK 465 ARG A 214
REMARK 465 THR A 215
REMARK 465 LYS A 216
REMARK 465 SER A 217
REMARK 465 ARG A 218
REMARK 465 ILE A 219
REMARK 465 GLU A 220
REMARK 465 GLN A 221
REMARK 465 GLY A 222
REMARK 465 ILE A 223
REMARK 465 VAL A 224
REMARK 465 ASP A 225
REMARK 465 ARG A 226
REMARK 465 SER A 227
REMARK 465 GLU A 228
REMARK 465 THR A 229
REMARK 465 GLY A 230
REMARK 465 VAL A 231
REMARK 465 TRP A 803
REMARK 465 ARG A 804
REMARK 465 ALA A 805
REMARK 465 ASP A 806
REMARK 465 LYS A 807
REMARK 465 GLU A 808
REMARK 465 GLN A 809
REMARK 465 ALA A 810
REMARK 465 MET B 1
REMARK 465 ILE B 2
REMARK 465 PRO B 3
REMARK 465 VAL B 4
REMARK 465 THR B 5
REMARK 465 GLU B 6
REMARK 465 LEU B 7
REMARK 465 ARG B 8
REMARK 465 TYR B 9
REMARK 465 PHE B 10
REMARK 465 ALA B 11
REMARK 465 ASP B 12
REMARK 465 THR B 13
REMARK 465 GLN B 14
REMARK 465 PHE B 69
REMARK 465 ARG B 70
REMARK 465 GLY B 71
REMARK 465 TRP B 72
REMARK 465 ALA B 73
REMARK 465 ALA B 74
REMARK 465 PRO B 75
REMARK 465 GLY B 76
REMARK 465 PRO B 77
REMARK 465 GLU B 78
REMARK 465 PRO B 79
REMARK 465 THR B 80
REMARK 465 TYR B 81
REMARK 465 PRO B 82
REMARK 465 ASN B 83
REMARK 465 SER B 84
REMARK 465 THR B 85
REMARK 465 ILE B 86
REMARK 465 LEU B 87
REMARK 465 PRO B 88
REMARK 465 THR B 89
REMARK 465 PRO B 90
REMARK 465 ASP B 91
REMARK 465 THR B 92
REMARK 465 GLY B 93
REMARK 465 THR B 176
REMARK 465 VAL B 177
REMARK 465 VAL B 178
REMARK 465 GLU B 179
REMARK 465 GLU B 180
REMARK 465 SER B 181
REMARK 465 ASP B 182
REMARK 465 PRO B 183
REMARK 465 LYS B 184
REMARK 465 PRO B 185
REMARK 465 ALA B 186
REMARK 465 PHE B 187
REMARK 465 SER B 188
REMARK 465 LYS B 189
REMARK 465 MET B 190
REMARK 465 ASN B 191
REMARK 465 GLY B 192
REMARK 465 SER B 193
REMARK 465 MET B 194
REMARK 465 ASP B 195
REMARK 465 LYS B 196
REMARK 465 LYS B 197
REMARK 465 SER B 198
REMARK 465 SER B 199
REMARK 465 THR B 200
REMARK 465 VAL B 201
REMARK 465 SER B 202
REMARK 465 GLU B 203
REMARK 465 ASP B 204
REMARK 465 VAL B 205
REMARK 465 GLU B 206
REMARK 465 ALA B 207
REMARK 465 THR B 208
REMARK 465 VAL B 209
REMARK 465 PRO B 210
REMARK 465 MET B 211
REMARK 465 LEU B 212
REMARK 465 GLN B 213
REMARK 465 TRP B 803
REMARK 465 ARG B 804
REMARK 465 ALA B 805
REMARK 465 ASP B 806
REMARK 465 LYS B 807
REMARK 465 GLU B 808
REMARK 465 GLN B 809
REMARK 465 ALA B 810
REMARK 465 MET E 1
REMARK 465 ILE E 2
REMARK 465 PRO E 3
REMARK 465 VAL E 4
REMARK 465 THR E 5
REMARK 465 GLU E 6
REMARK 465 LEU E 7
REMARK 465 ARG E 8
REMARK 465 TYR E 9
REMARK 465 PHE E 10
REMARK 465 ALA E 11
REMARK 465 ASP E 12
REMARK 465 THR E 13
REMARK 465 GLN E 14
REMARK 465 PHE E 69
REMARK 465 ARG E 70
REMARK 465 GLY E 71
REMARK 465 TRP E 72
REMARK 465 ALA E 73
REMARK 465 ALA E 74
REMARK 465 PRO E 75
REMARK 465 GLY E 76
REMARK 465 PRO E 77
REMARK 465 GLU E 78
REMARK 465 PRO E 79
REMARK 465 THR E 80
REMARK 465 TYR E 81
REMARK 465 PRO E 82
REMARK 465 ASN E 83
REMARK 465 SER E 84
REMARK 465 THR E 85
REMARK 465 ILE E 86
REMARK 465 LEU E 87
REMARK 465 PRO E 88
REMARK 465 THR E 89
REMARK 465 PRO E 90
REMARK 465 ASP E 91
REMARK 465 THR E 92
REMARK 465 GLY E 93
REMARK 465 GLU E 175
REMARK 465 THR E 176
REMARK 465 VAL E 177
REMARK 465 VAL E 178
REMARK 465 GLU E 179
REMARK 465 GLU E 180
REMARK 465 SER E 181
REMARK 465 ASP E 182
REMARK 465 PRO E 183
REMARK 465 LYS E 184
REMARK 465 PRO E 185
REMARK 465 ALA E 186
REMARK 465 PHE E 187
REMARK 465 SER E 188
REMARK 465 LYS E 189
REMARK 465 MET E 190
REMARK 465 ASN E 191
REMARK 465 GLY E 192
REMARK 465 SER E 193
REMARK 465 MET E 194
REMARK 465 ASP E 195
REMARK 465 LYS E 196
REMARK 465 LYS E 197
REMARK 465 SER E 198
REMARK 465 SER E 199
REMARK 465 THR E 200
REMARK 465 VAL E 201
REMARK 465 SER E 202
REMARK 465 GLU E 203
REMARK 465 ASP E 204
REMARK 465 VAL E 205
REMARK 465 GLU E 206
REMARK 465 ALA E 207
REMARK 465 THR E 208
REMARK 465 VAL E 209
REMARK 465 PRO E 210
REMARK 465 MET E 211
REMARK 465 LEU E 212
REMARK 465 GLN E 213
REMARK 465 ARG E 214
REMARK 465 THR E 215
REMARK 465 LYS E 216
REMARK 465 SER E 217
REMARK 465 ARG E 218
REMARK 465 ILE E 219
REMARK 465 GLU E 220
REMARK 465 GLN E 221
REMARK 465 GLY E 222
REMARK 465 ILE E 223
REMARK 465 VAL E 224
REMARK 465 ASP E 225
REMARK 465 ARG E 226
REMARK 465 SER E 227
REMARK 465 GLU E 228
REMARK 465 THR E 229
REMARK 465 GLY E 230
REMARK 465 VAL E 231
REMARK 465 TRP E 803
REMARK 465 ARG E 804
REMARK 465 ALA E 805
REMARK 465 ASP E 806
REMARK 465 LYS E 807
REMARK 465 GLU E 808
REMARK 465 GLN E 809
REMARK 465 ALA E 810
REMARK 465 MET F 1
REMARK 465 ILE F 2
REMARK 465 PRO F 3
REMARK 465 VAL F 4
REMARK 465 THR F 5
REMARK 465 GLU F 6
REMARK 465 LEU F 7
REMARK 465 ARG F 8
REMARK 465 TYR F 9
REMARK 465 PHE F 10
REMARK 465 ALA F 11
REMARK 465 ASP F 12
REMARK 465 THR F 13
REMARK 465 GLN F 14
REMARK 465 PHE F 69
REMARK 465 ARG F 70
REMARK 465 GLY F 71
REMARK 465 TRP F 72
REMARK 465 ALA F 73
REMARK 465 ALA F 74
REMARK 465 PRO F 75
REMARK 465 GLY F 76
REMARK 465 PRO F 77
REMARK 465 GLU F 78
REMARK 465 PRO F 79
REMARK 465 THR F 80
REMARK 465 TYR F 81
REMARK 465 PRO F 82
REMARK 465 ASN F 83
REMARK 465 SER F 84
REMARK 465 THR F 85
REMARK 465 ILE F 86
REMARK 465 LEU F 87
REMARK 465 PRO F 88
REMARK 465 THR F 89
REMARK 465 PRO F 90
REMARK 465 ASP F 91
REMARK 465 THR F 92
REMARK 465 GLY F 93
REMARK 465 THR F 176
REMARK 465 VAL F 177
REMARK 465 VAL F 178
REMARK 465 GLU F 179
REMARK 465 GLU F 180
REMARK 465 SER F 181
REMARK 465 ASP F 182
REMARK 465 PRO F 183
REMARK 465 LYS F 184
REMARK 465 PRO F 185
REMARK 465 ALA F 186
REMARK 465 PHE F 187
REMARK 465 SER F 188
REMARK 465 LYS F 189
REMARK 465 MET F 190
REMARK 465 ASN F 191
REMARK 465 GLY F 192
REMARK 465 SER F 193
REMARK 465 MET F 194
REMARK 465 ASP F 195
REMARK 465 LYS F 196
REMARK 465 LYS F 197
REMARK 465 SER F 198
REMARK 465 SER F 199
REMARK 465 THR F 200
REMARK 465 VAL F 201
REMARK 465 SER F 202
REMARK 465 GLU F 203
REMARK 465 ASP F 204
REMARK 465 VAL F 205
REMARK 465 GLU F 206
REMARK 465 ALA F 207
REMARK 465 THR F 208
REMARK 465 VAL F 209
REMARK 465 PRO F 210
REMARK 465 MET F 211
REMARK 465 LEU F 212
REMARK 465 GLN F 213
REMARK 465 TRP F 803
REMARK 465 ARG F 804
REMARK 465 ALA F 805
REMARK 465 ASP F 806
REMARK 465 LYS F 807
REMARK 465 GLU F 808
REMARK 465 GLN F 809
REMARK 465 ALA F 810
REMARK 465 MET C 1
REMARK 465 ILE C 2
REMARK 465 PRO C 3
REMARK 465 VAL C 4
REMARK 465 THR C 5
REMARK 465 GLU C 6
REMARK 465 LEU C 7
REMARK 465 ARG C 8
REMARK 465 TYR C 9
REMARK 465 PHE C 10
REMARK 465 ALA C 11
REMARK 465 ASP C 12
REMARK 465 THR C 13
REMARK 465 GLN C 14
REMARK 465 PHE C 69
REMARK 465 ARG C 70
REMARK 465 GLY C 71
REMARK 465 TRP C 72
REMARK 465 ALA C 73
REMARK 465 ALA C 74
REMARK 465 PRO C 75
REMARK 465 GLY C 76
REMARK 465 PRO C 77
REMARK 465 GLU C 78
REMARK 465 PRO C 79
REMARK 465 THR C 80
REMARK 465 TYR C 81
REMARK 465 PRO C 82
REMARK 465 ASN C 83
REMARK 465 SER C 84
REMARK 465 THR C 85
REMARK 465 ILE C 86
REMARK 465 LEU C 87
REMARK 465 PRO C 88
REMARK 465 THR C 89
REMARK 465 PRO C 90
REMARK 465 ASP C 91
REMARK 465 THR C 92
REMARK 465 GLY C 93
REMARK 465 GLU C 175
REMARK 465 THR C 176
REMARK 465 VAL C 177
REMARK 465 VAL C 178
REMARK 465 GLU C 179
REMARK 465 GLU C 180
REMARK 465 SER C 181
REMARK 465 ASP C 182
REMARK 465 PRO C 183
REMARK 465 LYS C 184
REMARK 465 PRO C 185
REMARK 465 ALA C 186
REMARK 465 PHE C 187
REMARK 465 SER C 188
REMARK 465 LYS C 189
REMARK 465 MET C 190
REMARK 465 ASN C 191
REMARK 465 GLY C 192
REMARK 465 SER C 193
REMARK 465 MET C 194
REMARK 465 ASP C 195
REMARK 465 LYS C 196
REMARK 465 LYS C 197
REMARK 465 SER C 198
REMARK 465 SER C 199
REMARK 465 THR C 200
REMARK 465 VAL C 201
REMARK 465 SER C 202
REMARK 465 GLU C 203
REMARK 465 ASP C 204
REMARK 465 VAL C 205
REMARK 465 GLU C 206
REMARK 465 ALA C 207
REMARK 465 THR C 208
REMARK 465 VAL C 209
REMARK 465 PRO C 210
REMARK 465 MET C 211
REMARK 465 LEU C 212
REMARK 465 GLN C 213
REMARK 465 ARG C 214
REMARK 465 THR C 215
REMARK 465 LYS C 216
REMARK 465 SER C 217
REMARK 465 ARG C 218
REMARK 465 ILE C 219
REMARK 465 GLU C 220
REMARK 465 GLN C 221
REMARK 465 GLY C 222
REMARK 465 ILE C 223
REMARK 465 VAL C 224
REMARK 465 ASP C 225
REMARK 465 ARG C 226
REMARK 465 SER C 227
REMARK 465 GLU C 228
REMARK 465 THR C 229
REMARK 465 GLY C 230
REMARK 465 VAL C 231
REMARK 465 TRP C 803
REMARK 465 ARG C 804
REMARK 465 ALA C 805
REMARK 465 ASP C 806
REMARK 465 LYS C 807
REMARK 465 GLU C 808
REMARK 465 GLN C 809
REMARK 465 ALA C 810
REMARK 465 MET D 1
REMARK 465 ILE D 2
REMARK 465 PRO D 3
REMARK 465 VAL D 4
REMARK 465 THR D 5
REMARK 465 GLU D 6
REMARK 465 LEU D 7
REMARK 465 ARG D 8
REMARK 465 TYR D 9
REMARK 465 PHE D 10
REMARK 465 ALA D 11
REMARK 465 ASP D 12
REMARK 465 THR D 13
REMARK 465 GLN D 14
REMARK 465 PHE D 69
REMARK 465 ARG D 70
REMARK 465 GLY D 71
REMARK 465 TRP D 72
REMARK 465 ALA D 73
REMARK 465 ALA D 74
REMARK 465 PRO D 75
REMARK 465 GLY D 76
REMARK 465 PRO D 77
REMARK 465 GLU D 78
REMARK 465 PRO D 79
REMARK 465 THR D 80
REMARK 465 TYR D 81
REMARK 465 PRO D 82
REMARK 465 ASN D 83
REMARK 465 SER D 84
REMARK 465 THR D 85
REMARK 465 ILE D 86
REMARK 465 LEU D 87
REMARK 465 PRO D 88
REMARK 465 THR D 89
REMARK 465 PRO D 90
REMARK 465 ASP D 91
REMARK 465 THR D 92
REMARK 465 GLY D 93
REMARK 465 THR D 176
REMARK 465 VAL D 177
REMARK 465 VAL D 178
REMARK 465 GLU D 179
REMARK 465 GLU D 180
REMARK 465 SER D 181
REMARK 465 ASP D 182
REMARK 465 PRO D 183
REMARK 465 LYS D 184
REMARK 465 PRO D 185
REMARK 465 ALA D 186
REMARK 465 PHE D 187
REMARK 465 SER D 188
REMARK 465 LYS D 189
REMARK 465 MET D 190
REMARK 465 ASN D 191
REMARK 465 GLY D 192
REMARK 465 SER D 193
REMARK 465 MET D 194
REMARK 465 ASP D 195
REMARK 465 LYS D 196
REMARK 465 LYS D 197
REMARK 465 SER D 198
REMARK 465 SER D 199
REMARK 465 THR D 200
REMARK 465 VAL D 201
REMARK 465 SER D 202
REMARK 465 GLU D 203
REMARK 465 ASP D 204
REMARK 465 VAL D 205
REMARK 465 GLU D 206
REMARK 465 ALA D 207
REMARK 465 THR D 208
REMARK 465 VAL D 209
REMARK 465 PRO D 210
REMARK 465 MET D 211
REMARK 465 LEU D 212
REMARK 465 GLN D 213
REMARK 465 TRP D 803
REMARK 465 ARG D 804
REMARK 465 ALA D 805
REMARK 465 ASP D 806
REMARK 465 LYS D 807
REMARK 465 GLU D 808
REMARK 465 GLN D 809
REMARK 465 ALA D 810
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 TYR A 17 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 18 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 19 CG1 CG2 CD1
REMARK 470 LEU A 20 CG CD1 CD2
REMARK 470 LYS A 21 CG CD CE NZ
REMARK 470 GLU A 359 CG CD OE1 OE2
REMARK 470 SER A 360 OG
REMARK 470 SER A 361 OG
REMARK 470 TYR A 362 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER A 363 OG
REMARK 470 ASP A 364 CG OD1 OD2
REMARK 470 GLU A 787 CG CD OE1 OE2
REMARK 470 GLU A 788 CG CD OE1 OE2
REMARK 470 ASP A 789 CG OD1 OD2
REMARK 470 LEU A 790 CG CD1 CD2
REMARK 470 PHE A 791 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN A 792 CG OD1 ND2
REMARK 470 THR A 793 OG1 CG2
REMARK 470 LEU A 794 CG CD1 CD2
REMARK 470 PRO A 795 CG CD
REMARK 470 PRO A 796 CG CD
REMARK 470 GLU A 797 CG CD OE1 OE2
REMARK 470 VAL A 798 CG1 CG2
REMARK 470 LYS A 799 CG CD CE NZ
REMARK 470 GLU A 800 CG CD OE1 OE2
REMARK 470 ARG A 801 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 802 CG CD1 CD2
REMARK 470 TYR B 17 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 18 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 19 CG1 CG2 CD1
REMARK 470 LEU B 20 CG CD1 CD2
REMARK 470 LYS B 21 CG CD CE NZ
REMARK 470 ARG B 214 CG CD NE CZ NH1 NH2
REMARK 470 THR B 215 OG1 CG2
REMARK 470 LYS B 216 CG CD CE NZ
REMARK 470 SER B 217 OG
REMARK 470 ARG B 218 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 219 CG1 CG2 CD1
REMARK 470 GLU B 220 CG CD OE1 OE2
REMARK 470 GLN B 221 CG CD OE1 NE2
REMARK 470 ILE B 223 CG1 CG2 CD1
REMARK 470 VAL B 224 CG1 CG2
REMARK 470 ASP B 225 CG OD1 OD2
REMARK 470 ARG B 226 CG CD NE CZ NH1 NH2
REMARK 470 SER B 227 OG
REMARK 470 GLU B 228 CG CD OE1 OE2
REMARK 470 THR B 229 OG1 CG2
REMARK 470 VAL B 231 CG1 CG2
REMARK 470 LEU B 232 CG CD1 CD2
REMARK 470 ASP B 233 CG OD1 OD2
REMARK 470 GLU B 359 CG CD OE1 OE2
REMARK 470 SER B 360 OG
REMARK 470 SER B 361 OG
REMARK 470 TYR B 362 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER B 363 OG
REMARK 470 ASP B 364 CG OD1 OD2
REMARK 470 GLU B 787 CG CD OE1 OE2
REMARK 470 GLU B 788 CG CD OE1 OE2
REMARK 470 ASP B 789 CG OD1 OD2
REMARK 470 LEU B 790 CG CD1 CD2
REMARK 470 PHE B 791 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN B 792 CG OD1 ND2
REMARK 470 THR B 793 OG1 CG2
REMARK 470 LEU B 794 CG CD1 CD2
REMARK 470 PRO B 795 CG CD
REMARK 470 PRO B 796 CG CD
REMARK 470 GLU B 797 CG CD OE1 OE2
REMARK 470 VAL B 798 CG1 CG2
REMARK 470 LYS B 799 CG CD CE NZ
REMARK 470 GLU B 800 CG CD OE1 OE2
REMARK 470 ARG B 801 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 802 CG CD1 CD2
REMARK 470 TYR E 17 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG E 18 CG CD NE CZ NH1 NH2
REMARK 470 ILE E 19 CG1 CG2 CD1
REMARK 470 LEU E 20 CG CD1 CD2
REMARK 470 LYS E 21 CG CD CE NZ
REMARK 470 GLU E 359 CG CD OE1 OE2
REMARK 470 SER E 360 OG
REMARK 470 SER E 361 OG
REMARK 470 TYR E 362 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER E 363 OG
REMARK 470 ASP E 364 CG OD1 OD2
REMARK 470 GLU E 787 CG CD OE1 OE2
REMARK 470 GLU E 788 CG CD OE1 OE2
REMARK 470 ASP E 789 CG OD1 OD2
REMARK 470 LEU E 790 CG CD1 CD2
REMARK 470 PHE E 791 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN E 792 CG OD1 ND2
REMARK 470 THR E 793 OG1 CG2
REMARK 470 LEU E 794 CG CD1 CD2
REMARK 470 PRO E 795 CG CD
REMARK 470 PRO E 796 CG CD
REMARK 470 GLU E 797 CG CD OE1 OE2
REMARK 470 VAL E 798 CG1 CG2
REMARK 470 LYS E 799 CG CD CE NZ
REMARK 470 GLU E 800 CG CD OE1 OE2
REMARK 470 ARG E 801 CG CD NE CZ NH1 NH2
REMARK 470 LEU E 802 CG CD1 CD2
REMARK 470 TYR F 17 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG F 18 CG CD NE CZ NH1 NH2
REMARK 470 ILE F 19 CG1 CG2 CD1
REMARK 470 LEU F 20 CG CD1 CD2
REMARK 470 LYS F 21 CG CD CE NZ
REMARK 470 ARG F 214 CG CD NE CZ NH1 NH2
REMARK 470 THR F 215 OG1 CG2
REMARK 470 LYS F 216 CG CD CE NZ
REMARK 470 SER F 217 OG
REMARK 470 ARG F 218 CG CD NE CZ NH1 NH2
REMARK 470 ILE F 219 CG1 CG2 CD1
REMARK 470 GLU F 220 CG CD OE1 OE2
REMARK 470 GLN F 221 CG CD OE1 NE2
REMARK 470 ILE F 223 CG1 CG2 CD1
REMARK 470 VAL F 224 CG1 CG2
REMARK 470 ASP F 225 CG OD1 OD2
REMARK 470 ARG F 226 CG CD NE CZ NH1 NH2
REMARK 470 SER F 227 OG
REMARK 470 GLU F 228 CG CD OE1 OE2
REMARK 470 THR F 229 OG1 CG2
REMARK 470 VAL F 231 CG1 CG2
REMARK 470 LEU F 232 CG CD1 CD2
REMARK 470 ASP F 233 CG OD1 OD2
REMARK 470 GLU F 359 CG CD OE1 OE2
REMARK 470 SER F 360 OG
REMARK 470 SER F 361 OG
REMARK 470 TYR F 362 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER F 363 OG
REMARK 470 ASP F 364 CG OD1 OD2
REMARK 470 GLU F 787 CG CD OE1 OE2
REMARK 470 GLU F 788 CG CD OE1 OE2
REMARK 470 ASP F 789 CG OD1 OD2
REMARK 470 LEU F 790 CG CD1 CD2
REMARK 470 PHE F 791 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN F 792 CG OD1 ND2
REMARK 470 THR F 793 OG1 CG2
REMARK 470 LEU F 794 CG CD1 CD2
REMARK 470 PRO F 795 CG CD
REMARK 470 PRO F 796 CG CD
REMARK 470 GLU F 797 CG CD OE1 OE2
REMARK 470 VAL F 798 CG1 CG2
REMARK 470 LYS F 799 CG CD CE NZ
REMARK 470 GLU F 800 CG CD OE1 OE2
REMARK 470 ARG F 801 CG CD NE CZ NH1 NH2
REMARK 470 LEU F 802 CG CD1 CD2
REMARK 470 TYR C 17 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG C 18 CG CD NE CZ NH1 NH2
REMARK 470 ILE C 19 CG1 CG2 CD1
REMARK 470 LEU C 20 CG CD1 CD2
REMARK 470 LYS C 21 CG CD CE NZ
REMARK 470 GLU C 359 CG CD OE1 OE2
REMARK 470 SER C 360 OG
REMARK 470 SER C 361 OG
REMARK 470 TYR C 362 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER C 363 OG
REMARK 470 ASP C 364 CG OD1 OD2
REMARK 470 GLU C 787 CG CD OE1 OE2
REMARK 470 GLU C 788 CG CD OE1 OE2
REMARK 470 ASP C 789 CG OD1 OD2
REMARK 470 LEU C 790 CG CD1 CD2
REMARK 470 PHE C 791 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN C 792 CG OD1 ND2
REMARK 470 THR C 793 OG1 CG2
REMARK 470 LEU C 794 CG CD1 CD2
REMARK 470 PRO C 795 CG CD
REMARK 470 PRO C 796 CG CD
REMARK 470 GLU C 797 CG CD OE1 OE2
REMARK 470 VAL C 798 CG1 CG2
REMARK 470 LYS C 799 CG CD CE NZ
REMARK 470 GLU C 800 CG CD OE1 OE2
REMARK 470 ARG C 801 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 802 CG CD1 CD2
REMARK 470 TYR D 17 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG D 18 CG CD NE CZ NH1 NH2
REMARK 470 ILE D 19 CG1 CG2 CD1
REMARK 470 LEU D 20 CG CD1 CD2
REMARK 470 LYS D 21 CG CD CE NZ
REMARK 470 ARG D 214 CG CD NE CZ NH1 NH2
REMARK 470 THR D 215 OG1 CG2
REMARK 470 LYS D 216 CG CD CE NZ
REMARK 470 SER D 217 OG
REMARK 470 ARG D 218 CG CD NE CZ NH1 NH2
REMARK 470 ILE D 219 CG1 CG2 CD1
REMARK 470 GLU D 220 CG CD OE1 OE2
REMARK 470 GLN D 221 CG CD OE1 NE2
REMARK 470 ILE D 223 CG1 CG2 CD1
REMARK 470 VAL D 224 CG1 CG2
REMARK 470 ASP D 225 CG OD1 OD2
REMARK 470 ARG D 226 CG CD NE CZ NH1 NH2
REMARK 470 SER D 227 OG
REMARK 470 GLU D 228 CG CD OE1 OE2
REMARK 470 THR D 229 OG1 CG2
REMARK 470 VAL D 231 CG1 CG2
REMARK 470 LEU D 232 CG CD1 CD2
REMARK 470 ASP D 233 CG OD1 OD2
REMARK 470 GLU D 359 CG CD OE1 OE2
REMARK 470 SER D 360 OG
REMARK 470 SER D 361 OG
REMARK 470 TYR D 362 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER D 363 OG
REMARK 470 ASP D 364 CG OD1 OD2
REMARK 470 GLU D 787 CG CD OE1 OE2
REMARK 470 GLU D 788 CG CD OE1 OE2
REMARK 470 ASP D 789 CG OD1 OD2
REMARK 470 LEU D 790 CG CD1 CD2
REMARK 470 PHE D 791 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN D 792 CG OD1 ND2
REMARK 470 THR D 793 OG1 CG2
REMARK 470 LEU D 794 CG CD1 CD2
REMARK 470 PRO D 795 CG CD
REMARK 470 PRO D 796 CG CD
REMARK 470 GLU D 797 CG CD OE1 OE2
REMARK 470 VAL D 798 CG1 CG2
REMARK 470 LYS D 799 CG CD CE NZ
REMARK 470 GLU D 800 CG CD OE1 OE2
REMARK 470 ARG D 801 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 802 CG CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS B 310 CB CYS B 310 SG -0.128
REMARK 500 CYS F 310 CB CYS F 310 SG -0.128
REMARK 500 CYS D 310 CB CYS D 310 SG -0.128
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TYR A 106 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 PHE A 502 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 TYR E 106 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 PHE E 502 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 TYR C 106 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 PHE C 502 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TRP A 24 -54.67 -131.36
REMARK 500 ASN A 66 -169.08 -76.09
REMARK 500 THR A 95 -77.09 -123.07
REMARK 500 LYS A 98 -47.68 72.08
REMARK 500 TYR A 99 72.72 42.62
REMARK 500 ASP A 100 77.81 -67.77
REMARK 500 ARG A 117 -155.89 -127.17
REMARK 500 LEU A 118 177.55 -59.66
REMARK 500 HIS A 119 31.90 75.58
REMARK 500 ASP A 258 26.13 -143.75
REMARK 500 LEU A 348 -10.27 62.21
REMARK 500 ASN A 370 -168.25 -174.49
REMARK 500 THR A 421 -166.65 -126.38
REMARK 500 ASP A 426 -71.94 -33.42
REMARK 500 LEU A 428 73.06 55.41
REMARK 500 ILE A 461 80.34 49.75
REMARK 500 PRO A 463 87.85 -66.33
REMARK 500 THR A 469 -67.87 -108.99
REMARK 500 LEU A 471 48.69 -146.63
REMARK 500 THR A 479 -87.21 -117.44
REMARK 500 ALA A 481 59.80 -143.15
REMARK 500 ALA A 487 48.29 -146.15
REMARK 500 ASN A 494 -156.29 -128.75
REMARK 500 ASP A 504 -154.36 -124.55
REMARK 500 SER A 556 -15.21 70.74
REMARK 500 ALA A 591 -18.39 56.14
REMARK 500 GLU A 595 108.68 -161.56
REMARK 500 GLN A 617 10.13 55.91
REMARK 500 GLU A 618 122.95 -178.90
REMARK 500 ILE A 633 -60.88 -128.23
REMARK 500 THR A 642 -15.18 63.26
REMARK 500 TRP A 647 170.65 -56.55
REMARK 500 ASN A 649 -162.35 -123.06
REMARK 500 ARG A 688 -29.45 60.85
REMARK 500 THR A 698 -13.46 68.96
REMARK 500 ASN A 741 -162.15 -128.34
REMARK 500 THR A 754 -3.78 73.20
REMARK 500 MET B 52 71.81 53.55
REMARK 500 THR B 61 -77.76 -110.35
REMARK 500 SER B 64 -7.75 71.51
REMARK 500 ASN B 66 -152.72 -131.58
REMARK 500 LYS B 98 71.73 62.77
REMARK 500 LEU B 118 -158.48 -76.17
REMARK 500 SER B 166 74.72 57.17
REMARK 500 PRO B 167 -18.94 -37.25
REMARK 500 GLU B 228 16.13 56.20
REMARK 500 ASP B 258 29.95 -142.11
REMARK 500 ASN B 370 -168.52 -170.12
REMARK 500 LYS B 427 17.56 56.11
REMARK 500 LEU B 428 79.93 53.53
REMARK 500
REMARK 500 THIS ENTRY HAS 196 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-7935 RELATED DB: EMDB
REMARK 900 STRUCTURE OF HUMAN VOLUME REGULATED ANION CHANNEL COMPOSED OF
REMARK 900 SWELL1 (LRRC8A)
DBREF 6DJB A 1 810 UNP Q8IWT6 LRC8A_HUMAN 1 810
DBREF 6DJB B 1 810 UNP Q8IWT6 LRC8A_HUMAN 1 810
DBREF 6DJB E 1 810 UNP Q8IWT6 LRC8A_HUMAN 1 810
DBREF 6DJB F 1 810 UNP Q8IWT6 LRC8A_HUMAN 1 810
DBREF 6DJB C 1 810 UNP Q8IWT6 LRC8A_HUMAN 1 810
DBREF 6DJB D 1 810 UNP Q8IWT6 LRC8A_HUMAN 1 810
SEQRES 1 A 810 MET ILE PRO VAL THR GLU LEU ARG TYR PHE ALA ASP THR
SEQRES 2 A 810 GLN PRO ALA TYR ARG ILE LEU LYS PRO TRP TRP ASP VAL
SEQRES 3 A 810 PHE THR ASP TYR ILE SER ILE VAL MET LEU MET ILE ALA
SEQRES 4 A 810 VAL PHE GLY GLY THR LEU GLN VAL THR GLN ASP LYS MET
SEQRES 5 A 810 ILE CYS LEU PRO CYS LYS TRP VAL THR LYS ASP SER CYS
SEQRES 6 A 810 ASN ASP SER PHE ARG GLY TRP ALA ALA PRO GLY PRO GLU
SEQRES 7 A 810 PRO THR TYR PRO ASN SER THR ILE LEU PRO THR PRO ASP
SEQRES 8 A 810 THR GLY PRO THR GLY ILE LYS TYR ASP LEU ASP ARG HIS
SEQRES 9 A 810 GLN TYR ASN TYR VAL ASP ALA VAL CYS TYR GLU ASN ARG
SEQRES 10 A 810 LEU HIS TRP PHE ALA LYS TYR PHE PRO TYR LEU VAL LEU
SEQRES 11 A 810 LEU HIS THR LEU ILE PHE LEU ALA CYS SER ASN PHE TRP
SEQRES 12 A 810 PHE LYS PHE PRO ARG THR SER SER LYS LEU GLU HIS PHE
SEQRES 13 A 810 VAL SER ILE LEU LEU LYS CYS PHE ASP SER PRO TRP THR
SEQRES 14 A 810 THR ARG ALA LEU SER GLU THR VAL VAL GLU GLU SER ASP
SEQRES 15 A 810 PRO LYS PRO ALA PHE SER LYS MET ASN GLY SER MET ASP
SEQRES 16 A 810 LYS LYS SER SER THR VAL SER GLU ASP VAL GLU ALA THR
SEQRES 17 A 810 VAL PRO MET LEU GLN ARG THR LYS SER ARG ILE GLU GLN
SEQRES 18 A 810 GLY ILE VAL ASP ARG SER GLU THR GLY VAL LEU ASP LYS
SEQRES 19 A 810 LYS GLU GLY GLU GLN ALA LYS ALA LEU PHE GLU LYS VAL
SEQRES 20 A 810 LYS LYS PHE ARG THR HIS VAL GLU GLU GLY ASP ILE VAL
SEQRES 21 A 810 TYR ARG LEU TYR MET ARG GLN THR ILE ILE LYS VAL ILE
SEQRES 22 A 810 LYS PHE ILE LEU ILE ILE CYS TYR THR VAL TYR TYR VAL
SEQRES 23 A 810 HIS ASN ILE LYS PHE ASP VAL ASP CYS THR VAL ASP ILE
SEQRES 24 A 810 GLU SER LEU THR GLY TYR ARG THR TYR ARG CYS ALA HIS
SEQRES 25 A 810 PRO LEU ALA THR LEU PHE LYS ILE LEU ALA SER PHE TYR
SEQRES 26 A 810 ILE SER LEU VAL ILE PHE TYR GLY LEU ILE CYS MET TYR
SEQRES 27 A 810 THR LEU TRP TRP MET LEU ARG ARG SER LEU LYS LYS TYR
SEQRES 28 A 810 SER PHE GLU SER ILE ARG GLU GLU SER SER TYR SER ASP
SEQRES 29 A 810 ILE PRO ASP VAL LYS ASN ASP PHE ALA PHE MET LEU HIS
SEQRES 30 A 810 LEU ILE ASP GLN TYR ASP PRO LEU TYR SER LYS ARG PHE
SEQRES 31 A 810 ALA VAL PHE LEU SER GLU VAL SER GLU ASN LYS LEU ARG
SEQRES 32 A 810 GLN LEU ASN LEU ASN ASN GLU TRP THR LEU ASP LYS LEU
SEQRES 33 A 810 ARG GLN ARG LEU THR LYS ASN ALA GLN ASP LYS LEU GLU
SEQRES 34 A 810 LEU HIS LEU PHE MET LEU SER GLY ILE PRO ASP THR VAL
SEQRES 35 A 810 PHE ASP LEU VAL GLU LEU GLU VAL LEU LYS LEU GLU LEU
SEQRES 36 A 810 ILE PRO ASP VAL THR ILE PRO PRO SER ILE ALA GLN LEU
SEQRES 37 A 810 THR GLY LEU LYS GLU LEU TRP LEU TYR HIS THR ALA ALA
SEQRES 38 A 810 LYS ILE GLU ALA PRO ALA LEU ALA PHE LEU ARG GLU ASN
SEQRES 39 A 810 LEU ARG ALA LEU HIS ILE LYS PHE THR ASP ILE LYS GLU
SEQRES 40 A 810 ILE PRO LEU TRP ILE TYR SER LEU LYS THR LEU GLU GLU
SEQRES 41 A 810 LEU HIS LEU THR GLY ASN LEU SER ALA GLU ASN ASN ARG
SEQRES 42 A 810 TYR ILE VAL ILE ASP GLY LEU ARG GLU LEU LYS ARG LEU
SEQRES 43 A 810 LYS VAL LEU ARG LEU LYS SER ASN LEU SER LYS LEU PRO
SEQRES 44 A 810 GLN VAL VAL THR ASP VAL GLY VAL HIS LEU GLN LYS LEU
SEQRES 45 A 810 SER ILE ASN ASN GLU GLY THR LYS LEU ILE VAL LEU ASN
SEQRES 46 A 810 SER LEU LYS LYS MET ALA ASN LEU THR GLU LEU GLU LEU
SEQRES 47 A 810 ILE ARG CYS ASP LEU GLU ARG ILE PRO HIS SER ILE PHE
SEQRES 48 A 810 SER LEU HIS ASN LEU GLN GLU ILE ASP LEU LYS ASP ASN
SEQRES 49 A 810 ASN LEU LYS THR ILE GLU GLU ILE ILE SER PHE GLN HIS
SEQRES 50 A 810 LEU HIS ARG LEU THR CYS LEU LYS LEU TRP TYR ASN HIS
SEQRES 51 A 810 ILE ALA TYR ILE PRO ILE GLN ILE GLY ASN LEU THR ASN
SEQRES 52 A 810 LEU GLU ARG LEU TYR LEU ASN ARG ASN LYS ILE GLU LYS
SEQRES 53 A 810 ILE PRO THR GLN LEU PHE TYR CYS ARG LYS LEU ARG TYR
SEQRES 54 A 810 LEU ASP LEU SER HIS ASN ASN LEU THR PHE LEU PRO ALA
SEQRES 55 A 810 ASP ILE GLY LEU LEU GLN ASN LEU GLN ASN LEU ALA ILE
SEQRES 56 A 810 THR ALA ASN ARG ILE GLU THR LEU PRO PRO GLU LEU PHE
SEQRES 57 A 810 GLN CYS ARG LYS LEU ARG ALA LEU HIS LEU GLY ASN ASN
SEQRES 58 A 810 VAL LEU GLN SER LEU PRO SER ARG VAL GLY GLU LEU THR
SEQRES 59 A 810 ASN LEU THR GLN ILE GLU LEU ARG GLY ASN ARG LEU GLU
SEQRES 60 A 810 CYS LEU PRO VAL GLU LEU GLY GLU CYS PRO LEU LEU LYS
SEQRES 61 A 810 ARG SER GLY LEU VAL VAL GLU GLU ASP LEU PHE ASN THR
SEQRES 62 A 810 LEU PRO PRO GLU VAL LYS GLU ARG LEU TRP ARG ALA ASP
SEQRES 63 A 810 LYS GLU GLN ALA
SEQRES 1 B 810 MET ILE PRO VAL THR GLU LEU ARG TYR PHE ALA ASP THR
SEQRES 2 B 810 GLN PRO ALA TYR ARG ILE LEU LYS PRO TRP TRP ASP VAL
SEQRES 3 B 810 PHE THR ASP TYR ILE SER ILE VAL MET LEU MET ILE ALA
SEQRES 4 B 810 VAL PHE GLY GLY THR LEU GLN VAL THR GLN ASP LYS MET
SEQRES 5 B 810 ILE CYS LEU PRO CYS LYS TRP VAL THR LYS ASP SER CYS
SEQRES 6 B 810 ASN ASP SER PHE ARG GLY TRP ALA ALA PRO GLY PRO GLU
SEQRES 7 B 810 PRO THR TYR PRO ASN SER THR ILE LEU PRO THR PRO ASP
SEQRES 8 B 810 THR GLY PRO THR GLY ILE LYS TYR ASP LEU ASP ARG HIS
SEQRES 9 B 810 GLN TYR ASN TYR VAL ASP ALA VAL CYS TYR GLU ASN ARG
SEQRES 10 B 810 LEU HIS TRP PHE ALA LYS TYR PHE PRO TYR LEU VAL LEU
SEQRES 11 B 810 LEU HIS THR LEU ILE PHE LEU ALA CYS SER ASN PHE TRP
SEQRES 12 B 810 PHE LYS PHE PRO ARG THR SER SER LYS LEU GLU HIS PHE
SEQRES 13 B 810 VAL SER ILE LEU LEU LYS CYS PHE ASP SER PRO TRP THR
SEQRES 14 B 810 THR ARG ALA LEU SER GLU THR VAL VAL GLU GLU SER ASP
SEQRES 15 B 810 PRO LYS PRO ALA PHE SER LYS MET ASN GLY SER MET ASP
SEQRES 16 B 810 LYS LYS SER SER THR VAL SER GLU ASP VAL GLU ALA THR
SEQRES 17 B 810 VAL PRO MET LEU GLN ARG THR LYS SER ARG ILE GLU GLN
SEQRES 18 B 810 GLY ILE VAL ASP ARG SER GLU THR GLY VAL LEU ASP LYS
SEQRES 19 B 810 LYS GLU GLY GLU GLN ALA LYS ALA LEU PHE GLU LYS VAL
SEQRES 20 B 810 LYS LYS PHE ARG THR HIS VAL GLU GLU GLY ASP ILE VAL
SEQRES 21 B 810 TYR ARG LEU TYR MET ARG GLN THR ILE ILE LYS VAL ILE
SEQRES 22 B 810 LYS PHE ILE LEU ILE ILE CYS TYR THR VAL TYR TYR VAL
SEQRES 23 B 810 HIS ASN ILE LYS PHE ASP VAL ASP CYS THR VAL ASP ILE
SEQRES 24 B 810 GLU SER LEU THR GLY TYR ARG THR TYR ARG CYS ALA HIS
SEQRES 25 B 810 PRO LEU ALA THR LEU PHE LYS ILE LEU ALA SER PHE TYR
SEQRES 26 B 810 ILE SER LEU VAL ILE PHE TYR GLY LEU ILE CYS MET TYR
SEQRES 27 B 810 THR LEU TRP TRP MET LEU ARG ARG SER LEU LYS LYS TYR
SEQRES 28 B 810 SER PHE GLU SER ILE ARG GLU GLU SER SER TYR SER ASP
SEQRES 29 B 810 ILE PRO ASP VAL LYS ASN ASP PHE ALA PHE MET LEU HIS
SEQRES 30 B 810 LEU ILE ASP GLN TYR ASP PRO LEU TYR SER LYS ARG PHE
SEQRES 31 B 810 ALA VAL PHE LEU SER GLU VAL SER GLU ASN LYS LEU ARG
SEQRES 32 B 810 GLN LEU ASN LEU ASN ASN GLU TRP THR LEU ASP LYS LEU
SEQRES 33 B 810 ARG GLN ARG LEU THR LYS ASN ALA GLN ASP LYS LEU GLU
SEQRES 34 B 810 LEU HIS LEU PHE MET LEU SER GLY ILE PRO ASP THR VAL
SEQRES 35 B 810 PHE ASP LEU VAL GLU LEU GLU VAL LEU LYS LEU GLU LEU
SEQRES 36 B 810 ILE PRO ASP VAL THR ILE PRO PRO SER ILE ALA GLN LEU
SEQRES 37 B 810 THR GLY LEU LYS GLU LEU TRP LEU TYR HIS THR ALA ALA
SEQRES 38 B 810 LYS ILE GLU ALA PRO ALA LEU ALA PHE LEU ARG GLU ASN
SEQRES 39 B 810 LEU ARG ALA LEU HIS ILE LYS PHE THR ASP ILE LYS GLU
SEQRES 40 B 810 ILE PRO LEU TRP ILE TYR SER LEU LYS THR LEU GLU GLU
SEQRES 41 B 810 LEU HIS LEU THR GLY ASN LEU SER ALA GLU ASN ASN ARG
SEQRES 42 B 810 TYR ILE VAL ILE ASP GLY LEU ARG GLU LEU LYS ARG LEU
SEQRES 43 B 810 LYS VAL LEU ARG LEU LYS SER ASN LEU SER LYS LEU PRO
SEQRES 44 B 810 GLN VAL VAL THR ASP VAL GLY VAL HIS LEU GLN LYS LEU
SEQRES 45 B 810 SER ILE ASN ASN GLU GLY THR LYS LEU ILE VAL LEU ASN
SEQRES 46 B 810 SER LEU LYS LYS MET ALA ASN LEU THR GLU LEU GLU LEU
SEQRES 47 B 810 ILE ARG CYS ASP LEU GLU ARG ILE PRO HIS SER ILE PHE
SEQRES 48 B 810 SER LEU HIS ASN LEU GLN GLU ILE ASP LEU LYS ASP ASN
SEQRES 49 B 810 ASN LEU LYS THR ILE GLU GLU ILE ILE SER PHE GLN HIS
SEQRES 50 B 810 LEU HIS ARG LEU THR CYS LEU LYS LEU TRP TYR ASN HIS
SEQRES 51 B 810 ILE ALA TYR ILE PRO ILE GLN ILE GLY ASN LEU THR ASN
SEQRES 52 B 810 LEU GLU ARG LEU TYR LEU ASN ARG ASN LYS ILE GLU LYS
SEQRES 53 B 810 ILE PRO THR GLN LEU PHE TYR CYS ARG LYS LEU ARG TYR
SEQRES 54 B 810 LEU ASP LEU SER HIS ASN ASN LEU THR PHE LEU PRO ALA
SEQRES 55 B 810 ASP ILE GLY LEU LEU GLN ASN LEU GLN ASN LEU ALA ILE
SEQRES 56 B 810 THR ALA ASN ARG ILE GLU THR LEU PRO PRO GLU LEU PHE
SEQRES 57 B 810 GLN CYS ARG LYS LEU ARG ALA LEU HIS LEU GLY ASN ASN
SEQRES 58 B 810 VAL LEU GLN SER LEU PRO SER ARG VAL GLY GLU LEU THR
SEQRES 59 B 810 ASN LEU THR GLN ILE GLU LEU ARG GLY ASN ARG LEU GLU
SEQRES 60 B 810 CYS LEU PRO VAL GLU LEU GLY GLU CYS PRO LEU LEU LYS
SEQRES 61 B 810 ARG SER GLY LEU VAL VAL GLU GLU ASP LEU PHE ASN THR
SEQRES 62 B 810 LEU PRO PRO GLU VAL LYS GLU ARG LEU TRP ARG ALA ASP
SEQRES 63 B 810 LYS GLU GLN ALA
SEQRES 1 E 810 MET ILE PRO VAL THR GLU LEU ARG TYR PHE ALA ASP THR
SEQRES 2 E 810 GLN PRO ALA TYR ARG ILE LEU LYS PRO TRP TRP ASP VAL
SEQRES 3 E 810 PHE THR ASP TYR ILE SER ILE VAL MET LEU MET ILE ALA
SEQRES 4 E 810 VAL PHE GLY GLY THR LEU GLN VAL THR GLN ASP LYS MET
SEQRES 5 E 810 ILE CYS LEU PRO CYS LYS TRP VAL THR LYS ASP SER CYS
SEQRES 6 E 810 ASN ASP SER PHE ARG GLY TRP ALA ALA PRO GLY PRO GLU
SEQRES 7 E 810 PRO THR TYR PRO ASN SER THR ILE LEU PRO THR PRO ASP
SEQRES 8 E 810 THR GLY PRO THR GLY ILE LYS TYR ASP LEU ASP ARG HIS
SEQRES 9 E 810 GLN TYR ASN TYR VAL ASP ALA VAL CYS TYR GLU ASN ARG
SEQRES 10 E 810 LEU HIS TRP PHE ALA LYS TYR PHE PRO TYR LEU VAL LEU
SEQRES 11 E 810 LEU HIS THR LEU ILE PHE LEU ALA CYS SER ASN PHE TRP
SEQRES 12 E 810 PHE LYS PHE PRO ARG THR SER SER LYS LEU GLU HIS PHE
SEQRES 13 E 810 VAL SER ILE LEU LEU LYS CYS PHE ASP SER PRO TRP THR
SEQRES 14 E 810 THR ARG ALA LEU SER GLU THR VAL VAL GLU GLU SER ASP
SEQRES 15 E 810 PRO LYS PRO ALA PHE SER LYS MET ASN GLY SER MET ASP
SEQRES 16 E 810 LYS LYS SER SER THR VAL SER GLU ASP VAL GLU ALA THR
SEQRES 17 E 810 VAL PRO MET LEU GLN ARG THR LYS SER ARG ILE GLU GLN
SEQRES 18 E 810 GLY ILE VAL ASP ARG SER GLU THR GLY VAL LEU ASP LYS
SEQRES 19 E 810 LYS GLU GLY GLU GLN ALA LYS ALA LEU PHE GLU LYS VAL
SEQRES 20 E 810 LYS LYS PHE ARG THR HIS VAL GLU GLU GLY ASP ILE VAL
SEQRES 21 E 810 TYR ARG LEU TYR MET ARG GLN THR ILE ILE LYS VAL ILE
SEQRES 22 E 810 LYS PHE ILE LEU ILE ILE CYS TYR THR VAL TYR TYR VAL
SEQRES 23 E 810 HIS ASN ILE LYS PHE ASP VAL ASP CYS THR VAL ASP ILE
SEQRES 24 E 810 GLU SER LEU THR GLY TYR ARG THR TYR ARG CYS ALA HIS
SEQRES 25 E 810 PRO LEU ALA THR LEU PHE LYS ILE LEU ALA SER PHE TYR
SEQRES 26 E 810 ILE SER LEU VAL ILE PHE TYR GLY LEU ILE CYS MET TYR
SEQRES 27 E 810 THR LEU TRP TRP MET LEU ARG ARG SER LEU LYS LYS TYR
SEQRES 28 E 810 SER PHE GLU SER ILE ARG GLU GLU SER SER TYR SER ASP
SEQRES 29 E 810 ILE PRO ASP VAL LYS ASN ASP PHE ALA PHE MET LEU HIS
SEQRES 30 E 810 LEU ILE ASP GLN TYR ASP PRO LEU TYR SER LYS ARG PHE
SEQRES 31 E 810 ALA VAL PHE LEU SER GLU VAL SER GLU ASN LYS LEU ARG
SEQRES 32 E 810 GLN LEU ASN LEU ASN ASN GLU TRP THR LEU ASP LYS LEU
SEQRES 33 E 810 ARG GLN ARG LEU THR LYS ASN ALA GLN ASP LYS LEU GLU
SEQRES 34 E 810 LEU HIS LEU PHE MET LEU SER GLY ILE PRO ASP THR VAL
SEQRES 35 E 810 PHE ASP LEU VAL GLU LEU GLU VAL LEU LYS LEU GLU LEU
SEQRES 36 E 810 ILE PRO ASP VAL THR ILE PRO PRO SER ILE ALA GLN LEU
SEQRES 37 E 810 THR GLY LEU LYS GLU LEU TRP LEU TYR HIS THR ALA ALA
SEQRES 38 E 810 LYS ILE GLU ALA PRO ALA LEU ALA PHE LEU ARG GLU ASN
SEQRES 39 E 810 LEU ARG ALA LEU HIS ILE LYS PHE THR ASP ILE LYS GLU
SEQRES 40 E 810 ILE PRO LEU TRP ILE TYR SER LEU LYS THR LEU GLU GLU
SEQRES 41 E 810 LEU HIS LEU THR GLY ASN LEU SER ALA GLU ASN ASN ARG
SEQRES 42 E 810 TYR ILE VAL ILE ASP GLY LEU ARG GLU LEU LYS ARG LEU
SEQRES 43 E 810 LYS VAL LEU ARG LEU LYS SER ASN LEU SER LYS LEU PRO
SEQRES 44 E 810 GLN VAL VAL THR ASP VAL GLY VAL HIS LEU GLN LYS LEU
SEQRES 45 E 810 SER ILE ASN ASN GLU GLY THR LYS LEU ILE VAL LEU ASN
SEQRES 46 E 810 SER LEU LYS LYS MET ALA ASN LEU THR GLU LEU GLU LEU
SEQRES 47 E 810 ILE ARG CYS ASP LEU GLU ARG ILE PRO HIS SER ILE PHE
SEQRES 48 E 810 SER LEU HIS ASN LEU GLN GLU ILE ASP LEU LYS ASP ASN
SEQRES 49 E 810 ASN LEU LYS THR ILE GLU GLU ILE ILE SER PHE GLN HIS
SEQRES 50 E 810 LEU HIS ARG LEU THR CYS LEU LYS LEU TRP TYR ASN HIS
SEQRES 51 E 810 ILE ALA TYR ILE PRO ILE GLN ILE GLY ASN LEU THR ASN
SEQRES 52 E 810 LEU GLU ARG LEU TYR LEU ASN ARG ASN LYS ILE GLU LYS
SEQRES 53 E 810 ILE PRO THR GLN LEU PHE TYR CYS ARG LYS LEU ARG TYR
SEQRES 54 E 810 LEU ASP LEU SER HIS ASN ASN LEU THR PHE LEU PRO ALA
SEQRES 55 E 810 ASP ILE GLY LEU LEU GLN ASN LEU GLN ASN LEU ALA ILE
SEQRES 56 E 810 THR ALA ASN ARG ILE GLU THR LEU PRO PRO GLU LEU PHE
SEQRES 57 E 810 GLN CYS ARG LYS LEU ARG ALA LEU HIS LEU GLY ASN ASN
SEQRES 58 E 810 VAL LEU GLN SER LEU PRO SER ARG VAL GLY GLU LEU THR
SEQRES 59 E 810 ASN LEU THR GLN ILE GLU LEU ARG GLY ASN ARG LEU GLU
SEQRES 60 E 810 CYS LEU PRO VAL GLU LEU GLY GLU CYS PRO LEU LEU LYS
SEQRES 61 E 810 ARG SER GLY LEU VAL VAL GLU GLU ASP LEU PHE ASN THR
SEQRES 62 E 810 LEU PRO PRO GLU VAL LYS GLU ARG LEU TRP ARG ALA ASP
SEQRES 63 E 810 LYS GLU GLN ALA
SEQRES 1 F 810 MET ILE PRO VAL THR GLU LEU ARG TYR PHE ALA ASP THR
SEQRES 2 F 810 GLN PRO ALA TYR ARG ILE LEU LYS PRO TRP TRP ASP VAL
SEQRES 3 F 810 PHE THR ASP TYR ILE SER ILE VAL MET LEU MET ILE ALA
SEQRES 4 F 810 VAL PHE GLY GLY THR LEU GLN VAL THR GLN ASP LYS MET
SEQRES 5 F 810 ILE CYS LEU PRO CYS LYS TRP VAL THR LYS ASP SER CYS
SEQRES 6 F 810 ASN ASP SER PHE ARG GLY TRP ALA ALA PRO GLY PRO GLU
SEQRES 7 F 810 PRO THR TYR PRO ASN SER THR ILE LEU PRO THR PRO ASP
SEQRES 8 F 810 THR GLY PRO THR GLY ILE LYS TYR ASP LEU ASP ARG HIS
SEQRES 9 F 810 GLN TYR ASN TYR VAL ASP ALA VAL CYS TYR GLU ASN ARG
SEQRES 10 F 810 LEU HIS TRP PHE ALA LYS TYR PHE PRO TYR LEU VAL LEU
SEQRES 11 F 810 LEU HIS THR LEU ILE PHE LEU ALA CYS SER ASN PHE TRP
SEQRES 12 F 810 PHE LYS PHE PRO ARG THR SER SER LYS LEU GLU HIS PHE
SEQRES 13 F 810 VAL SER ILE LEU LEU LYS CYS PHE ASP SER PRO TRP THR
SEQRES 14 F 810 THR ARG ALA LEU SER GLU THR VAL VAL GLU GLU SER ASP
SEQRES 15 F 810 PRO LYS PRO ALA PHE SER LYS MET ASN GLY SER MET ASP
SEQRES 16 F 810 LYS LYS SER SER THR VAL SER GLU ASP VAL GLU ALA THR
SEQRES 17 F 810 VAL PRO MET LEU GLN ARG THR LYS SER ARG ILE GLU GLN
SEQRES 18 F 810 GLY ILE VAL ASP ARG SER GLU THR GLY VAL LEU ASP LYS
SEQRES 19 F 810 LYS GLU GLY GLU GLN ALA LYS ALA LEU PHE GLU LYS VAL
SEQRES 20 F 810 LYS LYS PHE ARG THR HIS VAL GLU GLU GLY ASP ILE VAL
SEQRES 21 F 810 TYR ARG LEU TYR MET ARG GLN THR ILE ILE LYS VAL ILE
SEQRES 22 F 810 LYS PHE ILE LEU ILE ILE CYS TYR THR VAL TYR TYR VAL
SEQRES 23 F 810 HIS ASN ILE LYS PHE ASP VAL ASP CYS THR VAL ASP ILE
SEQRES 24 F 810 GLU SER LEU THR GLY TYR ARG THR TYR ARG CYS ALA HIS
SEQRES 25 F 810 PRO LEU ALA THR LEU PHE LYS ILE LEU ALA SER PHE TYR
SEQRES 26 F 810 ILE SER LEU VAL ILE PHE TYR GLY LEU ILE CYS MET TYR
SEQRES 27 F 810 THR LEU TRP TRP MET LEU ARG ARG SER LEU LYS LYS TYR
SEQRES 28 F 810 SER PHE GLU SER ILE ARG GLU GLU SER SER TYR SER ASP
SEQRES 29 F 810 ILE PRO ASP VAL LYS ASN ASP PHE ALA PHE MET LEU HIS
SEQRES 30 F 810 LEU ILE ASP GLN TYR ASP PRO LEU TYR SER LYS ARG PHE
SEQRES 31 F 810 ALA VAL PHE LEU SER GLU VAL SER GLU ASN LYS LEU ARG
SEQRES 32 F 810 GLN LEU ASN LEU ASN ASN GLU TRP THR LEU ASP LYS LEU
SEQRES 33 F 810 ARG GLN ARG LEU THR LYS ASN ALA GLN ASP LYS LEU GLU
SEQRES 34 F 810 LEU HIS LEU PHE MET LEU SER GLY ILE PRO ASP THR VAL
SEQRES 35 F 810 PHE ASP LEU VAL GLU LEU GLU VAL LEU LYS LEU GLU LEU
SEQRES 36 F 810 ILE PRO ASP VAL THR ILE PRO PRO SER ILE ALA GLN LEU
SEQRES 37 F 810 THR GLY LEU LYS GLU LEU TRP LEU TYR HIS THR ALA ALA
SEQRES 38 F 810 LYS ILE GLU ALA PRO ALA LEU ALA PHE LEU ARG GLU ASN
SEQRES 39 F 810 LEU ARG ALA LEU HIS ILE LYS PHE THR ASP ILE LYS GLU
SEQRES 40 F 810 ILE PRO LEU TRP ILE TYR SER LEU LYS THR LEU GLU GLU
SEQRES 41 F 810 LEU HIS LEU THR GLY ASN LEU SER ALA GLU ASN ASN ARG
SEQRES 42 F 810 TYR ILE VAL ILE ASP GLY LEU ARG GLU LEU LYS ARG LEU
SEQRES 43 F 810 LYS VAL LEU ARG LEU LYS SER ASN LEU SER LYS LEU PRO
SEQRES 44 F 810 GLN VAL VAL THR ASP VAL GLY VAL HIS LEU GLN LYS LEU
SEQRES 45 F 810 SER ILE ASN ASN GLU GLY THR LYS LEU ILE VAL LEU ASN
SEQRES 46 F 810 SER LEU LYS LYS MET ALA ASN LEU THR GLU LEU GLU LEU
SEQRES 47 F 810 ILE ARG CYS ASP LEU GLU ARG ILE PRO HIS SER ILE PHE
SEQRES 48 F 810 SER LEU HIS ASN LEU GLN GLU ILE ASP LEU LYS ASP ASN
SEQRES 49 F 810 ASN LEU LYS THR ILE GLU GLU ILE ILE SER PHE GLN HIS
SEQRES 50 F 810 LEU HIS ARG LEU THR CYS LEU LYS LEU TRP TYR ASN HIS
SEQRES 51 F 810 ILE ALA TYR ILE PRO ILE GLN ILE GLY ASN LEU THR ASN
SEQRES 52 F 810 LEU GLU ARG LEU TYR LEU ASN ARG ASN LYS ILE GLU LYS
SEQRES 53 F 810 ILE PRO THR GLN LEU PHE TYR CYS ARG LYS LEU ARG TYR
SEQRES 54 F 810 LEU ASP LEU SER HIS ASN ASN LEU THR PHE LEU PRO ALA
SEQRES 55 F 810 ASP ILE GLY LEU LEU GLN ASN LEU GLN ASN LEU ALA ILE
SEQRES 56 F 810 THR ALA ASN ARG ILE GLU THR LEU PRO PRO GLU LEU PHE
SEQRES 57 F 810 GLN CYS ARG LYS LEU ARG ALA LEU HIS LEU GLY ASN ASN
SEQRES 58 F 810 VAL LEU GLN SER LEU PRO SER ARG VAL GLY GLU LEU THR
SEQRES 59 F 810 ASN LEU THR GLN ILE GLU LEU ARG GLY ASN ARG LEU GLU
SEQRES 60 F 810 CYS LEU PRO VAL GLU LEU GLY GLU CYS PRO LEU LEU LYS
SEQRES 61 F 810 ARG SER GLY LEU VAL VAL GLU GLU ASP LEU PHE ASN THR
SEQRES 62 F 810 LEU PRO PRO GLU VAL LYS GLU ARG LEU TRP ARG ALA ASP
SEQRES 63 F 810 LYS GLU GLN ALA
SEQRES 1 C 810 MET ILE PRO VAL THR GLU LEU ARG TYR PHE ALA ASP THR
SEQRES 2 C 810 GLN PRO ALA TYR ARG ILE LEU LYS PRO TRP TRP ASP VAL
SEQRES 3 C 810 PHE THR ASP TYR ILE SER ILE VAL MET LEU MET ILE ALA
SEQRES 4 C 810 VAL PHE GLY GLY THR LEU GLN VAL THR GLN ASP LYS MET
SEQRES 5 C 810 ILE CYS LEU PRO CYS LYS TRP VAL THR LYS ASP SER CYS
SEQRES 6 C 810 ASN ASP SER PHE ARG GLY TRP ALA ALA PRO GLY PRO GLU
SEQRES 7 C 810 PRO THR TYR PRO ASN SER THR ILE LEU PRO THR PRO ASP
SEQRES 8 C 810 THR GLY PRO THR GLY ILE LYS TYR ASP LEU ASP ARG HIS
SEQRES 9 C 810 GLN TYR ASN TYR VAL ASP ALA VAL CYS TYR GLU ASN ARG
SEQRES 10 C 810 LEU HIS TRP PHE ALA LYS TYR PHE PRO TYR LEU VAL LEU
SEQRES 11 C 810 LEU HIS THR LEU ILE PHE LEU ALA CYS SER ASN PHE TRP
SEQRES 12 C 810 PHE LYS PHE PRO ARG THR SER SER LYS LEU GLU HIS PHE
SEQRES 13 C 810 VAL SER ILE LEU LEU LYS CYS PHE ASP SER PRO TRP THR
SEQRES 14 C 810 THR ARG ALA LEU SER GLU THR VAL VAL GLU GLU SER ASP
SEQRES 15 C 810 PRO LYS PRO ALA PHE SER LYS MET ASN GLY SER MET ASP
SEQRES 16 C 810 LYS LYS SER SER THR VAL SER GLU ASP VAL GLU ALA THR
SEQRES 17 C 810 VAL PRO MET LEU GLN ARG THR LYS SER ARG ILE GLU GLN
SEQRES 18 C 810 GLY ILE VAL ASP ARG SER GLU THR GLY VAL LEU ASP LYS
SEQRES 19 C 810 LYS GLU GLY GLU GLN ALA LYS ALA LEU PHE GLU LYS VAL
SEQRES 20 C 810 LYS LYS PHE ARG THR HIS VAL GLU GLU GLY ASP ILE VAL
SEQRES 21 C 810 TYR ARG LEU TYR MET ARG GLN THR ILE ILE LYS VAL ILE
SEQRES 22 C 810 LYS PHE ILE LEU ILE ILE CYS TYR THR VAL TYR TYR VAL
SEQRES 23 C 810 HIS ASN ILE LYS PHE ASP VAL ASP CYS THR VAL ASP ILE
SEQRES 24 C 810 GLU SER LEU THR GLY TYR ARG THR TYR ARG CYS ALA HIS
SEQRES 25 C 810 PRO LEU ALA THR LEU PHE LYS ILE LEU ALA SER PHE TYR
SEQRES 26 C 810 ILE SER LEU VAL ILE PHE TYR GLY LEU ILE CYS MET TYR
SEQRES 27 C 810 THR LEU TRP TRP MET LEU ARG ARG SER LEU LYS LYS TYR
SEQRES 28 C 810 SER PHE GLU SER ILE ARG GLU GLU SER SER TYR SER ASP
SEQRES 29 C 810 ILE PRO ASP VAL LYS ASN ASP PHE ALA PHE MET LEU HIS
SEQRES 30 C 810 LEU ILE ASP GLN TYR ASP PRO LEU TYR SER LYS ARG PHE
SEQRES 31 C 810 ALA VAL PHE LEU SER GLU VAL SER GLU ASN LYS LEU ARG
SEQRES 32 C 810 GLN LEU ASN LEU ASN ASN GLU TRP THR LEU ASP LYS LEU
SEQRES 33 C 810 ARG GLN ARG LEU THR LYS ASN ALA GLN ASP LYS LEU GLU
SEQRES 34 C 810 LEU HIS LEU PHE MET LEU SER GLY ILE PRO ASP THR VAL
SEQRES 35 C 810 PHE ASP LEU VAL GLU LEU GLU VAL LEU LYS LEU GLU LEU
SEQRES 36 C 810 ILE PRO ASP VAL THR ILE PRO PRO SER ILE ALA GLN LEU
SEQRES 37 C 810 THR GLY LEU LYS GLU LEU TRP LEU TYR HIS THR ALA ALA
SEQRES 38 C 810 LYS ILE GLU ALA PRO ALA LEU ALA PHE LEU ARG GLU ASN
SEQRES 39 C 810 LEU ARG ALA LEU HIS ILE LYS PHE THR ASP ILE LYS GLU
SEQRES 40 C 810 ILE PRO LEU TRP ILE TYR SER LEU LYS THR LEU GLU GLU
SEQRES 41 C 810 LEU HIS LEU THR GLY ASN LEU SER ALA GLU ASN ASN ARG
SEQRES 42 C 810 TYR ILE VAL ILE ASP GLY LEU ARG GLU LEU LYS ARG LEU
SEQRES 43 C 810 LYS VAL LEU ARG LEU LYS SER ASN LEU SER LYS LEU PRO
SEQRES 44 C 810 GLN VAL VAL THR ASP VAL GLY VAL HIS LEU GLN LYS LEU
SEQRES 45 C 810 SER ILE ASN ASN GLU GLY THR LYS LEU ILE VAL LEU ASN
SEQRES 46 C 810 SER LEU LYS LYS MET ALA ASN LEU THR GLU LEU GLU LEU
SEQRES 47 C 810 ILE ARG CYS ASP LEU GLU ARG ILE PRO HIS SER ILE PHE
SEQRES 48 C 810 SER LEU HIS ASN LEU GLN GLU ILE ASP LEU LYS ASP ASN
SEQRES 49 C 810 ASN LEU LYS THR ILE GLU GLU ILE ILE SER PHE GLN HIS
SEQRES 50 C 810 LEU HIS ARG LEU THR CYS LEU LYS LEU TRP TYR ASN HIS
SEQRES 51 C 810 ILE ALA TYR ILE PRO ILE GLN ILE GLY ASN LEU THR ASN
SEQRES 52 C 810 LEU GLU ARG LEU TYR LEU ASN ARG ASN LYS ILE GLU LYS
SEQRES 53 C 810 ILE PRO THR GLN LEU PHE TYR CYS ARG LYS LEU ARG TYR
SEQRES 54 C 810 LEU ASP LEU SER HIS ASN ASN LEU THR PHE LEU PRO ALA
SEQRES 55 C 810 ASP ILE GLY LEU LEU GLN ASN LEU GLN ASN LEU ALA ILE
SEQRES 56 C 810 THR ALA ASN ARG ILE GLU THR LEU PRO PRO GLU LEU PHE
SEQRES 57 C 810 GLN CYS ARG LYS LEU ARG ALA LEU HIS LEU GLY ASN ASN
SEQRES 58 C 810 VAL LEU GLN SER LEU PRO SER ARG VAL GLY GLU LEU THR
SEQRES 59 C 810 ASN LEU THR GLN ILE GLU LEU ARG GLY ASN ARG LEU GLU
SEQRES 60 C 810 CYS LEU PRO VAL GLU LEU GLY GLU CYS PRO LEU LEU LYS
SEQRES 61 C 810 ARG SER GLY LEU VAL VAL GLU GLU ASP LEU PHE ASN THR
SEQRES 62 C 810 LEU PRO PRO GLU VAL LYS GLU ARG LEU TRP ARG ALA ASP
SEQRES 63 C 810 LYS GLU GLN ALA
SEQRES 1 D 810 MET ILE PRO VAL THR GLU LEU ARG TYR PHE ALA ASP THR
SEQRES 2 D 810 GLN PRO ALA TYR ARG ILE LEU LYS PRO TRP TRP ASP VAL
SEQRES 3 D 810 PHE THR ASP TYR ILE SER ILE VAL MET LEU MET ILE ALA
SEQRES 4 D 810 VAL PHE GLY GLY THR LEU GLN VAL THR GLN ASP LYS MET
SEQRES 5 D 810 ILE CYS LEU PRO CYS LYS TRP VAL THR LYS ASP SER CYS
SEQRES 6 D 810 ASN ASP SER PHE ARG GLY TRP ALA ALA PRO GLY PRO GLU
SEQRES 7 D 810 PRO THR TYR PRO ASN SER THR ILE LEU PRO THR PRO ASP
SEQRES 8 D 810 THR GLY PRO THR GLY ILE LYS TYR ASP LEU ASP ARG HIS
SEQRES 9 D 810 GLN TYR ASN TYR VAL ASP ALA VAL CYS TYR GLU ASN ARG
SEQRES 10 D 810 LEU HIS TRP PHE ALA LYS TYR PHE PRO TYR LEU VAL LEU
SEQRES 11 D 810 LEU HIS THR LEU ILE PHE LEU ALA CYS SER ASN PHE TRP
SEQRES 12 D 810 PHE LYS PHE PRO ARG THR SER SER LYS LEU GLU HIS PHE
SEQRES 13 D 810 VAL SER ILE LEU LEU LYS CYS PHE ASP SER PRO TRP THR
SEQRES 14 D 810 THR ARG ALA LEU SER GLU THR VAL VAL GLU GLU SER ASP
SEQRES 15 D 810 PRO LYS PRO ALA PHE SER LYS MET ASN GLY SER MET ASP
SEQRES 16 D 810 LYS LYS SER SER THR VAL SER GLU ASP VAL GLU ALA THR
SEQRES 17 D 810 VAL PRO MET LEU GLN ARG THR LYS SER ARG ILE GLU GLN
SEQRES 18 D 810 GLY ILE VAL ASP ARG SER GLU THR GLY VAL LEU ASP LYS
SEQRES 19 D 810 LYS GLU GLY GLU GLN ALA LYS ALA LEU PHE GLU LYS VAL
SEQRES 20 D 810 LYS LYS PHE ARG THR HIS VAL GLU GLU GLY ASP ILE VAL
SEQRES 21 D 810 TYR ARG LEU TYR MET ARG GLN THR ILE ILE LYS VAL ILE
SEQRES 22 D 810 LYS PHE ILE LEU ILE ILE CYS TYR THR VAL TYR TYR VAL
SEQRES 23 D 810 HIS ASN ILE LYS PHE ASP VAL ASP CYS THR VAL ASP ILE
SEQRES 24 D 810 GLU SER LEU THR GLY TYR ARG THR TYR ARG CYS ALA HIS
SEQRES 25 D 810 PRO LEU ALA THR LEU PHE LYS ILE LEU ALA SER PHE TYR
SEQRES 26 D 810 ILE SER LEU VAL ILE PHE TYR GLY LEU ILE CYS MET TYR
SEQRES 27 D 810 THR LEU TRP TRP MET LEU ARG ARG SER LEU LYS LYS TYR
SEQRES 28 D 810 SER PHE GLU SER ILE ARG GLU GLU SER SER TYR SER ASP
SEQRES 29 D 810 ILE PRO ASP VAL LYS ASN ASP PHE ALA PHE MET LEU HIS
SEQRES 30 D 810 LEU ILE ASP GLN TYR ASP PRO LEU TYR SER LYS ARG PHE
SEQRES 31 D 810 ALA VAL PHE LEU SER GLU VAL SER GLU ASN LYS LEU ARG
SEQRES 32 D 810 GLN LEU ASN LEU ASN ASN GLU TRP THR LEU ASP LYS LEU
SEQRES 33 D 810 ARG GLN ARG LEU THR LYS ASN ALA GLN ASP LYS LEU GLU
SEQRES 34 D 810 LEU HIS LEU PHE MET LEU SER GLY ILE PRO ASP THR VAL
SEQRES 35 D 810 PHE ASP LEU VAL GLU LEU GLU VAL LEU LYS LEU GLU LEU
SEQRES 36 D 810 ILE PRO ASP VAL THR ILE PRO PRO SER ILE ALA GLN LEU
SEQRES 37 D 810 THR GLY LEU LYS GLU LEU TRP LEU TYR HIS THR ALA ALA
SEQRES 38 D 810 LYS ILE GLU ALA PRO ALA LEU ALA PHE LEU ARG GLU ASN
SEQRES 39 D 810 LEU ARG ALA LEU HIS ILE LYS PHE THR ASP ILE LYS GLU
SEQRES 40 D 810 ILE PRO LEU TRP ILE TYR SER LEU LYS THR LEU GLU GLU
SEQRES 41 D 810 LEU HIS LEU THR GLY ASN LEU SER ALA GLU ASN ASN ARG
SEQRES 42 D 810 TYR ILE VAL ILE ASP GLY LEU ARG GLU LEU LYS ARG LEU
SEQRES 43 D 810 LYS VAL LEU ARG LEU LYS SER ASN LEU SER LYS LEU PRO
SEQRES 44 D 810 GLN VAL VAL THR ASP VAL GLY VAL HIS LEU GLN LYS LEU
SEQRES 45 D 810 SER ILE ASN ASN GLU GLY THR LYS LEU ILE VAL LEU ASN
SEQRES 46 D 810 SER LEU LYS LYS MET ALA ASN LEU THR GLU LEU GLU LEU
SEQRES 47 D 810 ILE ARG CYS ASP LEU GLU ARG ILE PRO HIS SER ILE PHE
SEQRES 48 D 810 SER LEU HIS ASN LEU GLN GLU ILE ASP LEU LYS ASP ASN
SEQRES 49 D 810 ASN LEU LYS THR ILE GLU GLU ILE ILE SER PHE GLN HIS
SEQRES 50 D 810 LEU HIS ARG LEU THR CYS LEU LYS LEU TRP TYR ASN HIS
SEQRES 51 D 810 ILE ALA TYR ILE PRO ILE GLN ILE GLY ASN LEU THR ASN
SEQRES 52 D 810 LEU GLU ARG LEU TYR LEU ASN ARG ASN LYS ILE GLU LYS
SEQRES 53 D 810 ILE PRO THR GLN LEU PHE TYR CYS ARG LYS LEU ARG TYR
SEQRES 54 D 810 LEU ASP LEU SER HIS ASN ASN LEU THR PHE LEU PRO ALA
SEQRES 55 D 810 ASP ILE GLY LEU LEU GLN ASN LEU GLN ASN LEU ALA ILE
SEQRES 56 D 810 THR ALA ASN ARG ILE GLU THR LEU PRO PRO GLU LEU PHE
SEQRES 57 D 810 GLN CYS ARG LYS LEU ARG ALA LEU HIS LEU GLY ASN ASN
SEQRES 58 D 810 VAL LEU GLN SER LEU PRO SER ARG VAL GLY GLU LEU THR
SEQRES 59 D 810 ASN LEU THR GLN ILE GLU LEU ARG GLY ASN ARG LEU GLU
SEQRES 60 D 810 CYS LEU PRO VAL GLU LEU GLY GLU CYS PRO LEU LEU LYS
SEQRES 61 D 810 ARG SER GLY LEU VAL VAL GLU GLU ASP LEU PHE ASN THR
SEQRES 62 D 810 LEU PRO PRO GLU VAL LYS GLU ARG LEU TRP ARG ALA ASP
SEQRES 63 D 810 LYS GLU GLN ALA
HELIX 1 AA1 PRO A 15 LEU A 20 5 6
HELIX 2 AA2 TRP A 24 ASP A 50 1 27
HELIX 3 AA3 ASP A 102 ARG A 117 1 16
HELIX 4 AA4 HIS A 119 ASN A 141 1 23
HELIX 5 AA5 THR A 149 ASP A 165 1 17
HELIX 6 AA6 SER A 166 LEU A 173 1 8
HELIX 7 AA7 LYS A 235 GLU A 256 1 22
HELIX 8 AA8 ASP A 258 TYR A 285 1 28
HELIX 9 AA9 ILE A 299 GLY A 304 1 6
HELIX 10 AB1 LEU A 314 ARG A 345 1 32
HELIX 11 AB2 PHE A 353 GLU A 358 1 6
HELIX 12 AB3 ASN A 370 ASP A 383 1 14
HELIX 13 AB4 ASP A 383 LEU A 394 1 12
HELIX 14 AB5 SER A 395 TRP A 411 1 17
HELIX 15 AB6 THR A 412 ARG A 419 1 8
HELIX 16 AB7 PRO A 439 LEU A 445 5 7
HELIX 17 AB8 SER A 464 LEU A 468 5 5
HELIX 18 AB9 ALA A 487 ASN A 494 1 8
HELIX 19 AC1 SER A 528 ARG A 541 1 14
HELIX 20 AC2 PRO A 559 GLY A 566 1 8
HELIX 21 AC3 VAL A 567 LEU A 569 5 3
HELIX 22 AC4 SER A 586 ALA A 591 1 6
HELIX 23 AC5 SER A 634 LEU A 638 5 5
HELIX 24 AC6 ILE A 656 LEU A 661 5 6
HELIX 25 AC7 ASP A 703 LEU A 707 5 5
HELIX 26 AC8 PRO A 724 GLN A 729 5 6
HELIX 27 AC9 PRO A 747 LEU A 753 5 7
HELIX 28 AD1 PRO A 770 GLU A 775 5 6
HELIX 29 AD2 LEU A 794 LEU A 802 1 9
HELIX 30 AD3 PRO B 15 LEU B 20 5 6
HELIX 31 AD4 ASP B 25 GLN B 49 1 25
HELIX 32 AD5 ASP B 102 ASN B 116 1 15
HELIX 33 AD6 HIS B 119 TYR B 124 1 6
HELIX 34 AD7 TYR B 124 SER B 140 1 17
HELIX 35 AD8 PHE B 146 PHE B 164 1 19
HELIX 36 AD9 PRO B 167 LEU B 173 1 7
HELIX 37 AE1 GLU B 220 SER B 227 1 8
HELIX 38 AE2 LYS B 235 GLU B 255 1 21
HELIX 39 AE3 ASP B 258 TYR B 285 1 28
HELIX 40 AE4 ILE B 299 GLY B 304 1 6
HELIX 41 AE5 PRO B 313 ARG B 346 1 34
HELIX 42 AE6 PHE B 353 SER B 360 1 8
HELIX 43 AE7 ASN B 370 GLN B 381 1 12
HELIX 44 AE8 ASP B 383 LEU B 394 1 12
HELIX 45 AE9 SER B 395 TRP B 411 1 17
HELIX 46 AF1 THR B 412 ARG B 417 1 6
HELIX 47 AF2 GLN B 418 LEU B 420 5 3
HELIX 48 AF3 ASP B 440 LEU B 445 5 6
HELIX 49 AF4 ALA B 487 ARG B 492 1 6
HELIX 50 AF5 TRP B 511 LEU B 515 5 5
HELIX 51 AF6 SER B 528 LEU B 540 1 13
HELIX 52 AF7 PRO B 559 GLY B 566 1 8
HELIX 53 AF8 VAL B 583 ALA B 591 1 9
HELIX 54 AF9 PRO B 607 LEU B 613 5 7
HELIX 55 AG1 SER B 634 LEU B 638 5 5
HELIX 56 AG2 GLN B 657 LEU B 661 5 5
HELIX 57 AG3 GLN B 680 CYS B 684 5 5
HELIX 58 AG4 PRO B 701 LEU B 706 5 6
HELIX 59 AG5 PRO B 724 GLN B 729 5 6
HELIX 60 AG6 PRO B 747 THR B 754 5 8
HELIX 61 AG7 GLU B 772 CYS B 776 5 5
HELIX 62 AG8 LEU B 794 LEU B 802 1 9
HELIX 63 AG9 PRO E 15 LEU E 20 5 6
HELIX 64 AH1 TRP E 24 ASP E 50 1 27
HELIX 65 AH2 ASP E 102 ARG E 117 1 16
HELIX 66 AH3 HIS E 119 ASN E 141 1 23
HELIX 67 AH4 THR E 149 ASP E 165 1 17
HELIX 68 AH5 SER E 166 LEU E 173 1 8
HELIX 69 AH6 LYS E 235 GLU E 256 1 22
HELIX 70 AH7 ASP E 258 TYR E 285 1 28
HELIX 71 AH8 ILE E 299 GLY E 304 1 6
HELIX 72 AH9 LEU E 314 ARG E 345 1 32
HELIX 73 AI1 PHE E 353 GLU E 358 1 6
HELIX 74 AI2 ASN E 370 ASP E 383 1 14
HELIX 75 AI3 ASP E 383 LEU E 394 1 12
HELIX 76 AI4 SER E 395 TRP E 411 1 17
HELIX 77 AI5 THR E 412 ARG E 419 1 8
HELIX 78 AI6 PRO E 439 LEU E 445 5 7
HELIX 79 AI7 SER E 464 LEU E 468 5 5
HELIX 80 AI8 ALA E 487 ASN E 494 1 8
HELIX 81 AI9 SER E 528 ARG E 541 1 14
HELIX 82 AJ1 PRO E 559 GLY E 566 1 8
HELIX 83 AJ2 VAL E 567 LEU E 569 5 3
HELIX 84 AJ3 SER E 586 ALA E 591 1 6
HELIX 85 AJ4 SER E 634 LEU E 638 5 5
HELIX 86 AJ5 ILE E 656 LEU E 661 5 6
HELIX 87 AJ6 ASP E 703 LEU E 707 5 5
HELIX 88 AJ7 PRO E 724 GLN E 729 5 6
HELIX 89 AJ8 PRO E 747 LEU E 753 5 7
HELIX 90 AJ9 PRO E 770 GLU E 775 5 6
HELIX 91 AK1 LEU E 794 LEU E 802 1 9
HELIX 92 AK2 PRO F 15 LEU F 20 5 6
HELIX 93 AK3 ASP F 25 GLN F 49 1 25
HELIX 94 AK4 ASP F 102 ASN F 116 1 15
HELIX 95 AK5 HIS F 119 TYR F 124 1 6
HELIX 96 AK6 TYR F 124 SER F 140 1 17
HELIX 97 AK7 PHE F 146 PHE F 164 1 19
HELIX 98 AK8 PRO F 167 LEU F 173 1 7
HELIX 99 AK9 GLU F 220 SER F 227 1 8
HELIX 100 AL1 LYS F 235 GLU F 255 1 21
HELIX 101 AL2 ASP F 258 TYR F 285 1 28
HELIX 102 AL3 ILE F 299 GLY F 304 1 6
HELIX 103 AL4 PRO F 313 ARG F 346 1 34
HELIX 104 AL5 PHE F 353 SER F 360 1 8
HELIX 105 AL6 ASN F 370 GLN F 381 1 12
HELIX 106 AL7 ASP F 383 LEU F 394 1 12
HELIX 107 AL8 SER F 395 TRP F 411 1 17
HELIX 108 AL9 THR F 412 ARG F 417 1 6
HELIX 109 AM1 GLN F 418 LEU F 420 5 3
HELIX 110 AM2 ASP F 440 LEU F 445 5 6
HELIX 111 AM3 ALA F 487 ARG F 492 1 6
HELIX 112 AM4 TRP F 511 LEU F 515 5 5
HELIX 113 AM5 SER F 528 LEU F 540 1 13
HELIX 114 AM6 PRO F 559 GLY F 566 1 8
HELIX 115 AM7 VAL F 583 ALA F 591 1 9
HELIX 116 AM8 PRO F 607 LEU F 613 5 7
HELIX 117 AM9 SER F 634 LEU F 638 5 5
HELIX 118 AN1 GLN F 657 LEU F 661 5 5
HELIX 119 AN2 GLN F 680 CYS F 684 5 5
HELIX 120 AN3 PRO F 701 LEU F 706 5 6
HELIX 121 AN4 PRO F 724 GLN F 729 5 6
HELIX 122 AN5 PRO F 747 THR F 754 5 8
HELIX 123 AN6 GLU F 772 CYS F 776 5 5
HELIX 124 AN7 LEU F 794 LEU F 802 1 9
HELIX 125 AN8 PRO C 15 LEU C 20 5 6
HELIX 126 AN9 TRP C 24 ASP C 50 1 27
HELIX 127 AO1 ASP C 102 ARG C 117 1 16
HELIX 128 AO2 HIS C 119 ASN C 141 1 23
HELIX 129 AO3 THR C 149 ASP C 165 1 17
HELIX 130 AO4 SER C 166 LEU C 173 1 8
HELIX 131 AO5 LYS C 235 GLU C 256 1 22
HELIX 132 AO6 ASP C 258 TYR C 285 1 28
HELIX 133 AO7 ILE C 299 GLY C 304 1 6
HELIX 134 AO8 LEU C 314 ARG C 345 1 32
HELIX 135 AO9 PHE C 353 GLU C 358 1 6
HELIX 136 AP1 ASN C 370 ASP C 383 1 14
HELIX 137 AP2 ASP C 383 LEU C 394 1 12
HELIX 138 AP3 SER C 395 TRP C 411 1 17
HELIX 139 AP4 THR C 412 ARG C 419 1 8
HELIX 140 AP5 PRO C 439 LEU C 445 5 7
HELIX 141 AP6 SER C 464 LEU C 468 5 5
HELIX 142 AP7 ALA C 487 ASN C 494 1 8
HELIX 143 AP8 SER C 528 ARG C 541 1 14
HELIX 144 AP9 PRO C 559 GLY C 566 1 8
HELIX 145 AQ1 VAL C 567 LEU C 569 5 3
HELIX 146 AQ2 SER C 586 ALA C 591 1 6
HELIX 147 AQ3 SER C 634 LEU C 638 5 5
HELIX 148 AQ4 ILE C 656 LEU C 661 5 6
HELIX 149 AQ5 ASP C 703 LEU C 707 5 5
HELIX 150 AQ6 PRO C 724 GLN C 729 5 6
HELIX 151 AQ7 PRO C 747 LEU C 753 5 7
HELIX 152 AQ8 PRO C 770 GLU C 775 5 6
HELIX 153 AQ9 LEU C 794 LEU C 802 1 9
HELIX 154 AR1 PRO D 15 LEU D 20 5 6
HELIX 155 AR2 ASP D 25 GLN D 49 1 25
HELIX 156 AR3 ASP D 102 ASN D 116 1 15
HELIX 157 AR4 HIS D 119 TYR D 124 1 6
HELIX 158 AR5 TYR D 124 SER D 140 1 17
HELIX 159 AR6 PHE D 146 PHE D 164 1 19
HELIX 160 AR7 PRO D 167 LEU D 173 1 7
HELIX 161 AR8 GLU D 220 SER D 227 1 8
HELIX 162 AR9 LYS D 235 GLU D 255 1 21
HELIX 163 AS1 ASP D 258 TYR D 285 1 28
HELIX 164 AS2 ILE D 299 GLY D 304 1 6
HELIX 165 AS3 PRO D 313 ARG D 346 1 34
HELIX 166 AS4 PHE D 353 SER D 360 1 8
HELIX 167 AS5 ASN D 370 GLN D 381 1 12
HELIX 168 AS6 ASP D 383 LEU D 394 1 12
HELIX 169 AS7 SER D 395 TRP D 411 1 17
HELIX 170 AS8 THR D 412 ARG D 417 1 6
HELIX 171 AS9 GLN D 418 LEU D 420 5 3
HELIX 172 AT1 ASP D 440 LEU D 445 5 6
HELIX 173 AT2 ALA D 487 ARG D 492 1 6
HELIX 174 AT3 TRP D 511 LEU D 515 5 5
HELIX 175 AT4 SER D 528 LEU D 540 1 13
HELIX 176 AT5 PRO D 559 GLY D 566 1 8
HELIX 177 AT6 VAL D 583 ALA D 591 1 9
HELIX 178 AT7 PRO D 607 LEU D 613 5 7
HELIX 179 AT8 SER D 634 LEU D 638 5 5
HELIX 180 AT9 GLN D 657 LEU D 661 5 5
HELIX 181 AU1 GLN D 680 CYS D 684 5 5
HELIX 182 AU2 PRO D 701 LEU D 706 5 6
HELIX 183 AU3 PRO D 724 GLN D 729 5 6
HELIX 184 AU4 PRO D 747 THR D 754 5 8
HELIX 185 AU5 GLU D 772 CYS D 776 5 5
HELIX 186 AU6 LEU D 794 LEU D 802 1 9
SHEET 1 AA1 3 ILE A 53 PRO A 56 0
SHEET 2 AA1 3 TYR A 308 ALA A 311 -1 O ARG A 309 N LEU A 55
SHEET 3 AA1 3 ASP A 292 CYS A 295 -1 N CYS A 295 O TYR A 308
SHEET 1 AA216 LEU A 420 THR A 421 0
SHEET 2 AA216 GLU A 429 LEU A 432 -1 O GLU A 429 N THR A 421
SHEET 3 AA216 VAL A 450 GLU A 454 1 O LYS A 452 N LEU A 430
SHEET 4 AA216 GLU A 473 TYR A 477 1 O TRP A 475 N LEU A 453
SHEET 5 AA216 ALA A 497 LYS A 501 1 O HIS A 499 N LEU A 476
SHEET 6 AA216 GLU A 520 THR A 524 1 O HIS A 522 N ILE A 500
SHEET 7 AA216 VAL A 548 LYS A 552 1 O VAL A 548 N LEU A 521
SHEET 8 AA216 LYS A 571 ASN A 575 1 O LYS A 571 N LEU A 549
SHEET 9 AA216 GLU A 595 ILE A 599 1 O GLU A 595 N LEU A 572
SHEET 10 AA216 ILE A 619 LYS A 622 1 O ASP A 620 N LEU A 598
SHEET 11 AA216 THR A 642 LYS A 645 1 O LYS A 645 N LEU A 621
SHEET 12 AA216 LEU A 664 ASN A 670 1 O GLU A 665 N THR A 642
SHEET 13 AA216 TYR A 689 SER A 693 1 O ASP A 691 N LEU A 669
SHEET 14 AA216 ASN A 712 THR A 716 1 O ASN A 712 N LEU A 690
SHEET 15 AA216 ALA A 735 GLY A 739 1 O HIS A 737 N ILE A 715
SHEET 16 AA216 GLN A 758 ARG A 762 1 O GLN A 758 N LEU A 736
SHEET 1 AA3 3 ILE B 53 PRO B 56 0
SHEET 2 AA3 3 TYR B 308 ALA B 311 -1 O ARG B 309 N LEU B 55
SHEET 3 AA3 3 ASP B 292 CYS B 295 -1 N CYS B 295 O TYR B 308
SHEET 1 AA4 2 LYS B 350 SER B 352 0
SHEET 2 AA4 2 ASP B 367 LYS B 369 -1 O VAL B 368 N TYR B 351
SHEET 1 AA516 HIS B 431 LEU B 432 0
SHEET 2 AA516 VAL B 450 GLU B 454 1 O LYS B 452 N LEU B 432
SHEET 3 AA516 GLU B 473 TYR B 477 1 O TRP B 475 N LEU B 453
SHEET 4 AA516 ALA B 497 LYS B 501 1 O HIS B 499 N LEU B 476
SHEET 5 AA516 GLU B 520 THR B 524 1 O HIS B 522 N ILE B 500
SHEET 6 AA516 VAL B 548 LYS B 552 1 O VAL B 548 N LEU B 521
SHEET 7 AA516 LYS B 571 ILE B 574 1 O SER B 573 N LEU B 551
SHEET 8 AA516 GLU B 595 ILE B 599 1 O GLU B 597 N ILE B 574
SHEET 9 AA516 ILE B 619 LYS B 622 1 O ASP B 620 N LEU B 598
SHEET 10 AA516 THR B 642 LYS B 645 1 O LYS B 645 N LEU B 621
SHEET 11 AA516 LEU B 664 ASN B 670 1 O GLU B 665 N THR B 642
SHEET 12 AA516 TYR B 689 SER B 693 1 O ASP B 691 N LEU B 669
SHEET 13 AA516 ASN B 712 THR B 716 1 O ASN B 712 N LEU B 690
SHEET 14 AA516 ALA B 735 GLY B 739 1 O HIS B 737 N ILE B 715
SHEET 15 AA516 GLN B 758 ARG B 762 1 O GLU B 760 N LEU B 736
SHEET 16 AA516 LEU B 784 VAL B 785 1 O VAL B 785 N LEU B 761
SHEET 1 AA6 3 ILE E 53 PRO E 56 0
SHEET 2 AA6 3 TYR E 308 ALA E 311 -1 O ARG E 309 N LEU E 55
SHEET 3 AA6 3 ASP E 292 CYS E 295 -1 N CYS E 295 O TYR E 308
SHEET 1 AA716 LEU E 420 THR E 421 0
SHEET 2 AA716 GLU E 429 LEU E 432 -1 O GLU E 429 N THR E 421
SHEET 3 AA716 VAL E 450 GLU E 454 1 O LYS E 452 N LEU E 430
SHEET 4 AA716 GLU E 473 TYR E 477 1 O TRP E 475 N LEU E 453
SHEET 5 AA716 ALA E 497 LYS E 501 1 O HIS E 499 N LEU E 476
SHEET 6 AA716 GLU E 520 THR E 524 1 O HIS E 522 N ILE E 500
SHEET 7 AA716 VAL E 548 LYS E 552 1 O VAL E 548 N LEU E 521
SHEET 8 AA716 LYS E 571 ASN E 575 1 O LYS E 571 N LEU E 549
SHEET 9 AA716 GLU E 595 ILE E 599 1 O GLU E 595 N LEU E 572
SHEET 10 AA716 ILE E 619 LYS E 622 1 O ASP E 620 N LEU E 598
SHEET 11 AA716 THR E 642 LYS E 645 1 O LYS E 645 N LEU E 621
SHEET 12 AA716 LEU E 664 ASN E 670 1 O GLU E 665 N THR E 642
SHEET 13 AA716 TYR E 689 SER E 693 1 O ASP E 691 N LEU E 669
SHEET 14 AA716 ASN E 712 THR E 716 1 O ASN E 712 N LEU E 690
SHEET 15 AA716 ALA E 735 GLY E 739 1 O HIS E 737 N ILE E 715
SHEET 16 AA716 GLN E 758 ARG E 762 1 O GLN E 758 N LEU E 736
SHEET 1 AA8 3 ILE F 53 PRO F 56 0
SHEET 2 AA8 3 TYR F 308 ALA F 311 -1 O ARG F 309 N LEU F 55
SHEET 3 AA8 3 ASP F 292 CYS F 295 -1 N CYS F 295 O TYR F 308
SHEET 1 AA9 2 LYS F 350 SER F 352 0
SHEET 2 AA9 2 ASP F 367 LYS F 369 -1 O VAL F 368 N TYR F 351
SHEET 1 AB116 HIS F 431 LEU F 432 0
SHEET 2 AB116 VAL F 450 GLU F 454 1 O LYS F 452 N LEU F 432
SHEET 3 AB116 GLU F 473 TYR F 477 1 O TRP F 475 N LEU F 453
SHEET 4 AB116 ALA F 497 LYS F 501 1 O HIS F 499 N LEU F 476
SHEET 5 AB116 GLU F 520 THR F 524 1 O HIS F 522 N ILE F 500
SHEET 6 AB116 VAL F 548 LYS F 552 1 O VAL F 548 N LEU F 521
SHEET 7 AB116 LYS F 571 ILE F 574 1 O SER F 573 N LEU F 551
SHEET 8 AB116 GLU F 595 ILE F 599 1 O GLU F 597 N ILE F 574
SHEET 9 AB116 ILE F 619 LYS F 622 1 O ASP F 620 N LEU F 598
SHEET 10 AB116 THR F 642 LYS F 645 1 O LYS F 645 N LEU F 621
SHEET 11 AB116 LEU F 664 ASN F 670 1 O GLU F 665 N THR F 642
SHEET 12 AB116 TYR F 689 SER F 693 1 O ASP F 691 N LEU F 669
SHEET 13 AB116 ASN F 712 THR F 716 1 O ASN F 712 N LEU F 690
SHEET 14 AB116 ALA F 735 GLY F 739 1 O HIS F 737 N ILE F 715
SHEET 15 AB116 GLN F 758 ARG F 762 1 O GLU F 760 N LEU F 736
SHEET 16 AB116 LEU F 784 VAL F 785 1 O VAL F 785 N LEU F 761
SHEET 1 AB2 3 ILE C 53 PRO C 56 0
SHEET 2 AB2 3 TYR C 308 ALA C 311 -1 O ARG C 309 N LEU C 55
SHEET 3 AB2 3 ASP C 292 CYS C 295 -1 N CYS C 295 O TYR C 308
SHEET 1 AB316 LEU C 420 THR C 421 0
SHEET 2 AB316 GLU C 429 LEU C 432 -1 O GLU C 429 N THR C 421
SHEET 3 AB316 VAL C 450 GLU C 454 1 O LYS C 452 N LEU C 430
SHEET 4 AB316 GLU C 473 TYR C 477 1 O TRP C 475 N LEU C 453
SHEET 5 AB316 ALA C 497 LYS C 501 1 O HIS C 499 N LEU C 476
SHEET 6 AB316 GLU C 520 THR C 524 1 O HIS C 522 N ILE C 500
SHEET 7 AB316 VAL C 548 LYS C 552 1 O VAL C 548 N LEU C 521
SHEET 8 AB316 LYS C 571 ASN C 575 1 O LYS C 571 N LEU C 549
SHEET 9 AB316 GLU C 595 ILE C 599 1 O GLU C 595 N LEU C 572
SHEET 10 AB316 ILE C 619 LYS C 622 1 O ASP C 620 N LEU C 598
SHEET 11 AB316 THR C 642 LYS C 645 1 O LYS C 645 N LEU C 621
SHEET 12 AB316 LEU C 664 ASN C 670 1 O GLU C 665 N THR C 642
SHEET 13 AB316 TYR C 689 SER C 693 1 O ASP C 691 N LEU C 669
SHEET 14 AB316 ASN C 712 THR C 716 1 O ASN C 712 N LEU C 690
SHEET 15 AB316 ALA C 735 GLY C 739 1 O HIS C 737 N ILE C 715
SHEET 16 AB316 GLN C 758 ARG C 762 1 O GLN C 758 N LEU C 736
SHEET 1 AB4 3 ILE D 53 PRO D 56 0
SHEET 2 AB4 3 TYR D 308 ALA D 311 -1 O ARG D 309 N LEU D 55
SHEET 3 AB4 3 ASP D 292 CYS D 295 -1 N CYS D 295 O TYR D 308
SHEET 1 AB5 2 LYS D 350 SER D 352 0
SHEET 2 AB5 2 ASP D 367 LYS D 369 -1 O VAL D 368 N TYR D 351
SHEET 1 AB616 HIS D 431 LEU D 432 0
SHEET 2 AB616 VAL D 450 GLU D 454 1 O LYS D 452 N LEU D 432
SHEET 3 AB616 GLU D 473 TYR D 477 1 O TRP D 475 N LEU D 453
SHEET 4 AB616 ALA D 497 LYS D 501 1 O HIS D 499 N LEU D 476
SHEET 5 AB616 GLU D 520 THR D 524 1 O HIS D 522 N ILE D 500
SHEET 6 AB616 VAL D 548 LYS D 552 1 O VAL D 548 N LEU D 521
SHEET 7 AB616 LYS D 571 ILE D 574 1 O SER D 573 N LEU D 551
SHEET 8 AB616 GLU D 595 ILE D 599 1 O GLU D 597 N ILE D 574
SHEET 9 AB616 ILE D 619 LYS D 622 1 O ASP D 620 N LEU D 598
SHEET 10 AB616 THR D 642 LYS D 645 1 O LYS D 645 N LEU D 621
SHEET 11 AB616 LEU D 664 ASN D 670 1 O GLU D 665 N THR D 642
SHEET 12 AB616 TYR D 689 SER D 693 1 O ASP D 691 N LEU D 669
SHEET 13 AB616 ASN D 712 THR D 716 1 O ASN D 712 N LEU D 690
SHEET 14 AB616 ALA D 735 GLY D 739 1 O HIS D 737 N ILE D 715
SHEET 15 AB616 GLN D 758 ARG D 762 1 O GLU D 760 N LEU D 736
SHEET 16 AB616 LEU D 784 VAL D 785 1 O VAL D 785 N LEU D 761
SSBOND 1 CYS A 54 CYS A 310 1555 1555 2.03
SSBOND 2 CYS A 57 CYS A 65 1555 1555 2.02
SSBOND 3 CYS A 113 CYS A 295 1555 1555 2.03
SSBOND 4 CYS B 54 CYS B 310 1555 1555 2.02
SSBOND 5 CYS B 57 CYS B 65 1555 1555 2.01
SSBOND 6 CYS B 113 CYS B 295 1555 1555 2.03
SSBOND 7 CYS E 54 CYS E 310 1555 1555 2.03
SSBOND 8 CYS E 57 CYS E 65 1555 1555 2.02
SSBOND 9 CYS E 113 CYS E 295 1555 1555 2.03
SSBOND 10 CYS F 54 CYS F 310 1555 1555 2.02
SSBOND 11 CYS F 57 CYS F 65 1555 1555 2.01
SSBOND 12 CYS F 113 CYS F 295 1555 1555 2.03
SSBOND 13 CYS C 54 CYS C 310 1555 1555 2.03
SSBOND 14 CYS C 57 CYS C 65 1555 1555 2.02
SSBOND 15 CYS C 113 CYS C 295 1555 1555 2.03
SSBOND 16 CYS D 54 CYS D 310 1555 1555 2.02
SSBOND 17 CYS D 57 CYS D 65 1555 1555 2.01
SSBOND 18 CYS D 113 CYS D 295 1555 1555 2.03
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
