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7kjr.pdb
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4829 lines (4829 loc) · 382 KB
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HEADER TRANSPORT PROTEIN, VIRAL PROTEIN 26-OCT-20 7KJR
TITLE CRYO-EM STRUCTURE OF SARS-COV-2 ORF3A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ORF3A PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACCESSORY PROTEIN 3A,PROTEIN U274,PROTEIN X1,ORF3A,PROTEIN
COMPND 5 3A;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: APOLIPOPROTEIN A-I;
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: UNP RESIDUES 79-267;
COMPND 11 SYNONYM: APOA-I,APOLIPOPROTEIN A1,MSPE3D1;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS
SOURCE 3 2;
SOURCE 4 ORGANISM_COMMON: 2019-NCOV;
SOURCE 5 ORGANISM_TAXID: 2697049;
SOURCE 6 GENE: 3A;
SOURCE 7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 8 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: APOA1;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SARS-COV-2, CORONAVIRUS, TRANSPORT PROTEIN, VIRAL PROTEIN, VIROPORIN,
KEYWDS 2 MEMBRANE PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR D.M.KERN,C.M.HOEL,A.KOTECHA,S.G.BROHAWN
REVDAT 4 31-AUG-22 7KJR 1 COMPND JRNL REMARK HETNAM
REVDAT 4 2 1 FORMUL ATOM
REVDAT 3 18-AUG-21 7KJR 1 JRNL
REVDAT 2 27-JAN-21 7KJR 1 COMPND
REVDAT 1 18-NOV-20 7KJR 0
JRNL AUTH D.M.KERN,B.SORUM,S.S.MALI,C.M.HOEL,S.SRIDHARAN,J.P.REMIS,
JRNL AUTH 2 D.B.TOSO,A.KOTECHA,D.M.BAUTISTA,S.G.BROHAWN
JRNL TITL CRYO-EM STRUCTURE OF SARS-COV-2 ORF3A IN LIPID NANODISCS.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 28 573 2021
JRNL REFN ESSN 1545-9985
JRNL PMID 34158638
JRNL DOI 10.1038/S41594-021-00619-0
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.M.KERN,B.SORUM,S.S.MALI,C.M.HOEL,S.SRIDHARAN,J.P.REMIS,
REMARK 1 AUTH 2 D.B.TOSO,A.KOTECHA,D.M.BAUTISTA,S.G.BROHAWN
REMARK 1 TITL CRYO-EM STRUCTURE OF THE SARS-COV-2 3A ION CHANNEL IN LIPID
REMARK 1 TITL 2 NANODISCS.
REMARK 1 REF BIORXIV 2021
REMARK 1 REFN
REMARK 1 PMID 32587976
REMARK 1 DOI 10.1101/2020.06.17.156554
REMARK 2
REMARK 2 RESOLUTION. 2.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : PHENIX
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : REAL
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) : 2.080
REMARK 3 NUMBER OF PARTICLES : 91218
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 7KJR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-20.
REMARK 100 THE DEPOSITION ID IS D_1000252579.
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 : SARS-COV-2 PROTEIN 3A IN LIPID
REMARK 245 NANODISCS
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.10
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : 1 BLOT FORCE 5 SECOND WAIT TIME
REMARK 245 3 SECOND BLOT TIME
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.40
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 ASP A 2
REMARK 465 LEU A 3
REMARK 465 PHE A 4
REMARK 465 MET A 5
REMARK 465 ARG A 6
REMARK 465 ILE A 7
REMARK 465 PHE A 8
REMARK 465 THR A 9
REMARK 465 ILE A 10
REMARK 465 GLY A 11
REMARK 465 THR A 12
REMARK 465 VAL A 13
REMARK 465 THR A 14
REMARK 465 LEU A 15
REMARK 465 LYS A 16
REMARK 465 GLN A 17
REMARK 465 GLY A 18
REMARK 465 GLU A 19
REMARK 465 ILE A 20
REMARK 465 LYS A 21
REMARK 465 ASP A 22
REMARK 465 ALA A 23
REMARK 465 THR A 24
REMARK 465 PRO A 25
REMARK 465 SER A 26
REMARK 465 ASP A 27
REMARK 465 PHE A 28
REMARK 465 VAL A 29
REMARK 465 ARG A 30
REMARK 465 ALA A 31
REMARK 465 THR A 32
REMARK 465 ALA A 33
REMARK 465 THR A 34
REMARK 465 ILE A 35
REMARK 465 PRO A 36
REMARK 465 ILE A 37
REMARK 465 GLN A 38
REMARK 465 ALA A 39
REMARK 465 THR A 175
REMARK 465 THR A 176
REMARK 465 SER A 177
REMARK 465 PRO A 178
REMARK 465 ILE A 179
REMARK 465 SER A 180
REMARK 465 GLU A 239
REMARK 465 PRO A 240
REMARK 465 GLU A 241
REMARK 465 GLU A 242
REMARK 465 HIS A 243
REMARK 465 VAL A 244
REMARK 465 GLN A 245
REMARK 465 ILE A 246
REMARK 465 HIS A 247
REMARK 465 THR A 248
REMARK 465 ILE A 249
REMARK 465 ASP A 250
REMARK 465 GLY A 251
REMARK 465 SER A 252
REMARK 465 SER A 253
REMARK 465 GLY A 254
REMARK 465 VAL A 255
REMARK 465 VAL A 256
REMARK 465 ASN A 257
REMARK 465 PRO A 258
REMARK 465 VAL A 259
REMARK 465 MET A 260
REMARK 465 GLU A 261
REMARK 465 PRO A 262
REMARK 465 ILE A 263
REMARK 465 TYR A 264
REMARK 465 ASP A 265
REMARK 465 GLU A 266
REMARK 465 PRO A 267
REMARK 465 THR A 268
REMARK 465 THR A 269
REMARK 465 THR A 270
REMARK 465 THR A 271
REMARK 465 SER A 272
REMARK 465 VAL A 273
REMARK 465 PRO A 274
REMARK 465 LEU A 275
REMARK 465 SER A 276
REMARK 465 ASN A 277
REMARK 465 SER A 278
REMARK 465 LEU A 279
REMARK 465 GLU A 280
REMARK 465 VAL A 281
REMARK 465 LEU A 282
REMARK 465 PHE A 283
REMARK 465 GLN A 284
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 LEU B 3
REMARK 465 PHE B 4
REMARK 465 MET B 5
REMARK 465 ARG B 6
REMARK 465 ILE B 7
REMARK 465 PHE B 8
REMARK 465 THR B 9
REMARK 465 ILE B 10
REMARK 465 GLY B 11
REMARK 465 THR B 12
REMARK 465 VAL B 13
REMARK 465 THR B 14
REMARK 465 LEU B 15
REMARK 465 LYS B 16
REMARK 465 GLN B 17
REMARK 465 GLY B 18
REMARK 465 GLU B 19
REMARK 465 ILE B 20
REMARK 465 LYS B 21
REMARK 465 ASP B 22
REMARK 465 ALA B 23
REMARK 465 THR B 24
REMARK 465 PRO B 25
REMARK 465 SER B 26
REMARK 465 ASP B 27
REMARK 465 PHE B 28
REMARK 465 VAL B 29
REMARK 465 ARG B 30
REMARK 465 ALA B 31
REMARK 465 THR B 32
REMARK 465 ALA B 33
REMARK 465 THR B 34
REMARK 465 ILE B 35
REMARK 465 PRO B 36
REMARK 465 ILE B 37
REMARK 465 GLN B 38
REMARK 465 ALA B 39
REMARK 465 THR B 175
REMARK 465 THR B 176
REMARK 465 SER B 177
REMARK 465 PRO B 178
REMARK 465 ILE B 179
REMARK 465 SER B 180
REMARK 465 GLU B 239
REMARK 465 PRO B 240
REMARK 465 GLU B 241
REMARK 465 GLU B 242
REMARK 465 HIS B 243
REMARK 465 VAL B 244
REMARK 465 GLN B 245
REMARK 465 ILE B 246
REMARK 465 HIS B 247
REMARK 465 THR B 248
REMARK 465 ILE B 249
REMARK 465 ASP B 250
REMARK 465 GLY B 251
REMARK 465 SER B 252
REMARK 465 SER B 253
REMARK 465 GLY B 254
REMARK 465 VAL B 255
REMARK 465 VAL B 256
REMARK 465 ASN B 257
REMARK 465 PRO B 258
REMARK 465 VAL B 259
REMARK 465 MET B 260
REMARK 465 GLU B 261
REMARK 465 PRO B 262
REMARK 465 ILE B 263
REMARK 465 TYR B 264
REMARK 465 ASP B 265
REMARK 465 GLU B 266
REMARK 465 PRO B 267
REMARK 465 THR B 268
REMARK 465 THR B 269
REMARK 465 THR B 270
REMARK 465 THR B 271
REMARK 465 SER B 272
REMARK 465 VAL B 273
REMARK 465 PRO B 274
REMARK 465 LEU B 275
REMARK 465 SER B 276
REMARK 465 ASN B 277
REMARK 465 SER B 278
REMARK 465 LEU B 279
REMARK 465 GLU B 280
REMARK 465 VAL B 281
REMARK 465 LEU B 282
REMARK 465 PHE B 283
REMARK 465 GLN B 284
REMARK 465 HIS C 2
REMARK 465 HIS C 3
REMARK 465 HIS C 4
REMARK 465 HIS C 5
REMARK 465 HIS C 6
REMARK 465 HIS C 7
REMARK 465 HIS C 8
REMARK 465 ASP C 9
REMARK 465 TYR C 10
REMARK 465 ASP C 11
REMARK 465 ILE C 12
REMARK 465 PRO C 13
REMARK 465 THR C 14
REMARK 465 THR C 15
REMARK 465 GLU C 16
REMARK 465 ASN C 17
REMARK 465 LEU C 18
REMARK 465 TYR C 19
REMARK 465 PHE C 20
REMARK 465 GLN C 21
REMARK 465 GLY C 22
REMARK 465 SER C 23
REMARK 465 THR C 24
REMARK 465 LYS C 56
REMARK 465 ASP C 57
REMARK 465 LEU C 58
REMARK 465 GLU C 59
REMARK 465 GLU C 60
REMARK 465 VAL C 61
REMARK 465 LYS C 62
REMARK 465 ALA C 63
REMARK 465 LYS C 64
REMARK 465 VAL C 65
REMARK 465 GLN C 66
REMARK 465 PRO C 67
REMARK 465 TYR C 68
REMARK 465 LEU C 69
REMARK 465 ASP C 70
REMARK 465 ASP C 71
REMARK 465 PHE C 72
REMARK 465 GLN C 73
REMARK 465 LYS C 74
REMARK 465 LYS C 75
REMARK 465 TRP C 76
REMARK 465 GLN C 77
REMARK 465 GLU C 78
REMARK 465 GLU C 79
REMARK 465 MET C 80
REMARK 465 GLU C 81
REMARK 465 LEU C 82
REMARK 465 TYR C 83
REMARK 465 ARG C 84
REMARK 465 GLN C 85
REMARK 465 LYS C 86
REMARK 465 VAL C 87
REMARK 465 GLU C 88
REMARK 465 PRO C 89
REMARK 465 LEU C 90
REMARK 465 ARG C 91
REMARK 465 ALA C 92
REMARK 465 GLU C 93
REMARK 465 LEU C 94
REMARK 465 GLN C 95
REMARK 465 GLU C 96
REMARK 465 GLY C 97
REMARK 465 ALA C 98
REMARK 465 ARG C 99
REMARK 465 GLN C 100
REMARK 465 LYS C 101
REMARK 465 LEU C 102
REMARK 465 HIS C 103
REMARK 465 GLU C 104
REMARK 465 LEU C 105
REMARK 465 GLN C 106
REMARK 465 GLU C 107
REMARK 465 LYS C 108
REMARK 465 LEU C 109
REMARK 465 SER C 110
REMARK 465 PRO C 111
REMARK 465 LEU C 112
REMARK 465 GLY C 113
REMARK 465 GLU C 114
REMARK 465 GLU C 115
REMARK 465 MET C 116
REMARK 465 ARG C 117
REMARK 465 ASP C 118
REMARK 465 ARG C 119
REMARK 465 ALA C 120
REMARK 465 ARG C 121
REMARK 465 ALA C 122
REMARK 465 HIS C 123
REMARK 465 VAL C 124
REMARK 465 ASP C 125
REMARK 465 ALA C 126
REMARK 465 LEU C 127
REMARK 465 ARG C 128
REMARK 465 THR C 129
REMARK 465 HIS C 130
REMARK 465 LEU C 131
REMARK 465 ALA C 132
REMARK 465 PRO C 133
REMARK 465 TYR C 134
REMARK 465 SER C 135
REMARK 465 ASP C 136
REMARK 465 GLU C 137
REMARK 465 LEU C 138
REMARK 465 ARG C 139
REMARK 465 GLN C 140
REMARK 465 ARG C 141
REMARK 465 LEU C 142
REMARK 465 ALA C 143
REMARK 465 ALA C 144
REMARK 465 ARG C 145
REMARK 465 LEU C 146
REMARK 465 GLU C 147
REMARK 465 ALA C 148
REMARK 465 LEU C 149
REMARK 465 LYS C 150
REMARK 465 GLU C 151
REMARK 465 ASN C 152
REMARK 465 GLY C 153
REMARK 465 GLY C 154
REMARK 465 ALA C 155
REMARK 465 ARG C 156
REMARK 465 LEU C 157
REMARK 465 ALA C 158
REMARK 465 GLU C 159
REMARK 465 TYR C 160
REMARK 465 HIS C 161
REMARK 465 ALA C 162
REMARK 465 LYS C 163
REMARK 465 ALA C 164
REMARK 465 THR C 165
REMARK 465 GLU C 166
REMARK 465 HIS C 167
REMARK 465 LEU C 168
REMARK 465 SER C 169
REMARK 465 THR C 170
REMARK 465 LEU C 171
REMARK 465 SER C 172
REMARK 465 GLU C 173
REMARK 465 LYS C 174
REMARK 465 ALA C 175
REMARK 465 LYS C 176
REMARK 465 PRO C 177
REMARK 465 ALA C 178
REMARK 465 LEU C 179
REMARK 465 GLU C 180
REMARK 465 ASP C 181
REMARK 465 LEU C 182
REMARK 465 ARG C 183
REMARK 465 GLN C 184
REMARK 465 GLY C 185
REMARK 465 LEU C 186
REMARK 465 LEU C 187
REMARK 465 PRO C 188
REMARK 465 VAL C 189
REMARK 465 LEU C 190
REMARK 465 GLU C 191
REMARK 465 SER C 192
REMARK 465 PHE C 193
REMARK 465 LYS C 194
REMARK 465 VAL C 195
REMARK 465 SER C 196
REMARK 465 PHE C 197
REMARK 465 LEU C 198
REMARK 465 SER C 199
REMARK 465 ALA C 200
REMARK 465 LEU C 201
REMARK 465 GLU C 202
REMARK 465 GLU C 203
REMARK 465 TYR C 204
REMARK 465 THR C 205
REMARK 465 LYS C 206
REMARK 465 LYS C 207
REMARK 465 LEU C 208
REMARK 465 ASN C 209
REMARK 465 THR C 210
REMARK 465 GLN C 211
REMARK 465 HIS D 2
REMARK 465 HIS D 3
REMARK 465 HIS D 4
REMARK 465 HIS D 5
REMARK 465 HIS D 6
REMARK 465 HIS D 7
REMARK 465 HIS D 8
REMARK 465 ASP D 9
REMARK 465 TYR D 10
REMARK 465 ASP D 11
REMARK 465 ILE D 12
REMARK 465 PRO D 13
REMARK 465 THR D 14
REMARK 465 THR D 15
REMARK 465 GLU D 16
REMARK 465 ASN D 17
REMARK 465 LEU D 18
REMARK 465 TYR D 19
REMARK 465 PHE D 20
REMARK 465 GLN D 21
REMARK 465 GLY D 22
REMARK 465 SER D 23
REMARK 465 THR D 24
REMARK 465 LYS D 56
REMARK 465 ASP D 57
REMARK 465 LEU D 58
REMARK 465 GLU D 59
REMARK 465 GLU D 60
REMARK 465 VAL D 61
REMARK 465 LYS D 62
REMARK 465 ALA D 63
REMARK 465 LYS D 64
REMARK 465 VAL D 65
REMARK 465 GLN D 66
REMARK 465 PRO D 67
REMARK 465 TYR D 68
REMARK 465 LEU D 69
REMARK 465 ASP D 70
REMARK 465 ASP D 71
REMARK 465 PHE D 72
REMARK 465 GLN D 73
REMARK 465 LYS D 74
REMARK 465 LYS D 75
REMARK 465 TRP D 76
REMARK 465 GLN D 77
REMARK 465 GLU D 78
REMARK 465 GLU D 79
REMARK 465 MET D 80
REMARK 465 GLU D 81
REMARK 465 LEU D 82
REMARK 465 TYR D 83
REMARK 465 ARG D 84
REMARK 465 GLN D 85
REMARK 465 LYS D 86
REMARK 465 VAL D 87
REMARK 465 GLU D 88
REMARK 465 PRO D 89
REMARK 465 LEU D 90
REMARK 465 ARG D 91
REMARK 465 ALA D 92
REMARK 465 GLU D 93
REMARK 465 LEU D 94
REMARK 465 GLN D 95
REMARK 465 GLU D 96
REMARK 465 GLY D 97
REMARK 465 ALA D 98
REMARK 465 ARG D 99
REMARK 465 GLN D 100
REMARK 465 LYS D 101
REMARK 465 LEU D 102
REMARK 465 HIS D 103
REMARK 465 GLU D 104
REMARK 465 LEU D 105
REMARK 465 GLN D 106
REMARK 465 GLU D 107
REMARK 465 LYS D 108
REMARK 465 LEU D 109
REMARK 465 SER D 110
REMARK 465 PRO D 111
REMARK 465 LEU D 112
REMARK 465 GLY D 113
REMARK 465 GLU D 114
REMARK 465 GLU D 115
REMARK 465 MET D 116
REMARK 465 ARG D 117
REMARK 465 ASP D 118
REMARK 465 ARG D 119
REMARK 465 ALA D 120
REMARK 465 ARG D 121
REMARK 465 ALA D 122
REMARK 465 HIS D 123
REMARK 465 VAL D 124
REMARK 465 ASP D 125
REMARK 465 ALA D 126
REMARK 465 LEU D 127
REMARK 465 ARG D 128
REMARK 465 THR D 129
REMARK 465 HIS D 130
REMARK 465 LEU D 131
REMARK 465 ALA D 132
REMARK 465 PRO D 133
REMARK 465 TYR D 134
REMARK 465 SER D 135
REMARK 465 ASP D 136
REMARK 465 GLU D 137
REMARK 465 LEU D 138
REMARK 465 ARG D 139
REMARK 465 GLN D 140
REMARK 465 ARG D 141
REMARK 465 LEU D 142
REMARK 465 ALA D 143
REMARK 465 ALA D 144
REMARK 465 ARG D 145
REMARK 465 LEU D 146
REMARK 465 GLU D 147
REMARK 465 ALA D 148
REMARK 465 LEU D 149
REMARK 465 LYS D 150
REMARK 465 GLU D 151
REMARK 465 ASN D 152
REMARK 465 GLY D 153
REMARK 465 GLY D 154
REMARK 465 ALA D 155
REMARK 465 ARG D 156
REMARK 465 LEU D 157
REMARK 465 ALA D 158
REMARK 465 GLU D 159
REMARK 465 TYR D 160
REMARK 465 HIS D 161
REMARK 465 ALA D 162
REMARK 465 LYS D 163
REMARK 465 ALA D 164
REMARK 465 THR D 165
REMARK 465 GLU D 166
REMARK 465 HIS D 167
REMARK 465 LEU D 168
REMARK 465 SER D 169
REMARK 465 THR D 170
REMARK 465 LEU D 171
REMARK 465 SER D 172
REMARK 465 GLU D 173
REMARK 465 LYS D 174
REMARK 465 ALA D 175
REMARK 465 LYS D 176
REMARK 465 PRO D 177
REMARK 465 ALA D 178
REMARK 465 LEU D 179
REMARK 465 GLU D 180
REMARK 465 ASP D 181
REMARK 465 LEU D 182
REMARK 465 ARG D 183
REMARK 465 GLN D 184
REMARK 465 GLY D 185
REMARK 465 LEU D 186
REMARK 465 LEU D 187
REMARK 465 PRO D 188
REMARK 465 VAL D 189
REMARK 465 LEU D 190
REMARK 465 GLU D 191
REMARK 465 SER D 192
REMARK 465 PHE D 193
REMARK 465 LYS D 194
REMARK 465 VAL D 195
REMARK 465 SER D 196
REMARK 465 PHE D 197
REMARK 465 LEU D 198
REMARK 465 SER D 199
REMARK 465 ALA D 200
REMARK 465 LEU D 201
REMARK 465 GLU D 202
REMARK 465 GLU D 203
REMARK 465 TYR D 204
REMARK 465 THR D 205
REMARK 465 LYS D 206
REMARK 465 LYS D 207
REMARK 465 LEU D 208
REMARK 465 ASN D 209
REMARK 465 THR D 210
REMARK 465 GLN D 211
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 LEU A 65 74.51 -103.90
REMARK 500 SER A 205 -168.47 -126.86
REMARK 500 LEU B 65 63.72 -100.74
REMARK 500 PRO B 104 5.42 -68.05
REMARK 500 SER B 205 -167.57 -126.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PEE A 301
REMARK 610 PEE B 301
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEE A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEE B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6XDC RELATED DB: PDB
REMARK 900 CRYO-EM STRUCTURE OF SARS-COV-2 ORF3A
REMARK 900 RELATED ID: EMD-22898 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF SARS-COV-2 ORF3A
REMARK 900 RELATED ID: EMD-22136 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF SARS-COV-2 ORF3A
DBREF 7KJR A 1 275 UNP P0DTC3 AP3A_SARS2 1 275
DBREF 7KJR B 1 275 UNP P0DTC3 AP3A_SARS2 1 275
DBREF 7KJR C 23 211 UNP P02647 APOA1_HUMAN 79 267
DBREF 7KJR D 23 211 UNP P02647 APOA1_HUMAN 79 267
SEQADV 7KJR SER A 276 UNP P0DTC3 EXPRESSION TAG
SEQADV 7KJR ASN A 277 UNP P0DTC3 EXPRESSION TAG
SEQADV 7KJR SER A 278 UNP P0DTC3 EXPRESSION TAG
SEQADV 7KJR LEU A 279 UNP P0DTC3 EXPRESSION TAG
SEQADV 7KJR GLU A 280 UNP P0DTC3 EXPRESSION TAG
SEQADV 7KJR VAL A 281 UNP P0DTC3 EXPRESSION TAG
SEQADV 7KJR LEU A 282 UNP P0DTC3 EXPRESSION TAG
SEQADV 7KJR PHE A 283 UNP P0DTC3 EXPRESSION TAG
SEQADV 7KJR GLN A 284 UNP P0DTC3 EXPRESSION TAG
SEQADV 7KJR SER B 276 UNP P0DTC3 EXPRESSION TAG
SEQADV 7KJR ASN B 277 UNP P0DTC3 EXPRESSION TAG
SEQADV 7KJR SER B 278 UNP P0DTC3 EXPRESSION TAG
SEQADV 7KJR LEU B 279 UNP P0DTC3 EXPRESSION TAG
SEQADV 7KJR GLU B 280 UNP P0DTC3 EXPRESSION TAG
SEQADV 7KJR VAL B 281 UNP P0DTC3 EXPRESSION TAG
SEQADV 7KJR LEU B 282 UNP P0DTC3 EXPRESSION TAG
SEQADV 7KJR PHE B 283 UNP P0DTC3 EXPRESSION TAG
SEQADV 7KJR GLN B 284 UNP P0DTC3 EXPRESSION TAG
SEQADV 7KJR HIS C 2 UNP P02647 EXPRESSION TAG
SEQADV 7KJR HIS C 3 UNP P02647 EXPRESSION TAG
SEQADV 7KJR HIS C 4 UNP P02647 EXPRESSION TAG
SEQADV 7KJR HIS C 5 UNP P02647 EXPRESSION TAG
SEQADV 7KJR HIS C 6 UNP P02647 EXPRESSION TAG
SEQADV 7KJR HIS C 7 UNP P02647 EXPRESSION TAG
SEQADV 7KJR HIS C 8 UNP P02647 EXPRESSION TAG
SEQADV 7KJR ASP C 9 UNP P02647 EXPRESSION TAG
SEQADV 7KJR TYR C 10 UNP P02647 EXPRESSION TAG
SEQADV 7KJR ASP C 11 UNP P02647 EXPRESSION TAG
SEQADV 7KJR ILE C 12 UNP P02647 EXPRESSION TAG
SEQADV 7KJR PRO C 13 UNP P02647 EXPRESSION TAG
SEQADV 7KJR THR C 14 UNP P02647 EXPRESSION TAG
SEQADV 7KJR THR C 15 UNP P02647 EXPRESSION TAG
SEQADV 7KJR GLU C 16 UNP P02647 EXPRESSION TAG
SEQADV 7KJR ASN C 17 UNP P02647 EXPRESSION TAG
SEQADV 7KJR LEU C 18 UNP P02647 EXPRESSION TAG
SEQADV 7KJR TYR C 19 UNP P02647 EXPRESSION TAG
SEQADV 7KJR PHE C 20 UNP P02647 EXPRESSION TAG
SEQADV 7KJR GLN C 21 UNP P02647 EXPRESSION TAG
SEQADV 7KJR GLY C 22 UNP P02647 EXPRESSION TAG
SEQADV 7KJR HIS D 2 UNP P02647 EXPRESSION TAG
SEQADV 7KJR HIS D 3 UNP P02647 EXPRESSION TAG
SEQADV 7KJR HIS D 4 UNP P02647 EXPRESSION TAG
SEQADV 7KJR HIS D 5 UNP P02647 EXPRESSION TAG
SEQADV 7KJR HIS D 6 UNP P02647 EXPRESSION TAG
SEQADV 7KJR HIS D 7 UNP P02647 EXPRESSION TAG
SEQADV 7KJR HIS D 8 UNP P02647 EXPRESSION TAG
SEQADV 7KJR ASP D 9 UNP P02647 EXPRESSION TAG
SEQADV 7KJR TYR D 10 UNP P02647 EXPRESSION TAG
SEQADV 7KJR ASP D 11 UNP P02647 EXPRESSION TAG
SEQADV 7KJR ILE D 12 UNP P02647 EXPRESSION TAG
SEQADV 7KJR PRO D 13 UNP P02647 EXPRESSION TAG
SEQADV 7KJR THR D 14 UNP P02647 EXPRESSION TAG
SEQADV 7KJR THR D 15 UNP P02647 EXPRESSION TAG
SEQADV 7KJR GLU D 16 UNP P02647 EXPRESSION TAG
SEQADV 7KJR ASN D 17 UNP P02647 EXPRESSION TAG
SEQADV 7KJR LEU D 18 UNP P02647 EXPRESSION TAG
SEQADV 7KJR TYR D 19 UNP P02647 EXPRESSION TAG
SEQADV 7KJR PHE D 20 UNP P02647 EXPRESSION TAG
SEQADV 7KJR GLN D 21 UNP P02647 EXPRESSION TAG
SEQADV 7KJR GLY D 22 UNP P02647 EXPRESSION TAG
SEQRES 1 A 284 MET ASP LEU PHE MET ARG ILE PHE THR ILE GLY THR VAL
SEQRES 2 A 284 THR LEU LYS GLN GLY GLU ILE LYS ASP ALA THR PRO SER
SEQRES 3 A 284 ASP PHE VAL ARG ALA THR ALA THR ILE PRO ILE GLN ALA
SEQRES 4 A 284 SER LEU PRO PHE GLY TRP LEU ILE VAL GLY VAL ALA LEU
SEQRES 5 A 284 LEU ALA VAL PHE GLN SER ALA SER LYS ILE ILE THR LEU
SEQRES 6 A 284 LYS LYS ARG TRP GLN LEU ALA LEU SER LYS GLY VAL HIS
SEQRES 7 A 284 PHE VAL CYS ASN LEU LEU LEU LEU PHE VAL THR VAL TYR
SEQRES 8 A 284 SER HIS LEU LEU LEU VAL ALA ALA GLY LEU GLU ALA PRO
SEQRES 9 A 284 PHE LEU TYR LEU TYR ALA LEU VAL TYR PHE LEU GLN SER
SEQRES 10 A 284 ILE ASN PHE VAL ARG ILE ILE MET ARG LEU TRP LEU CYS
SEQRES 11 A 284 TRP LYS CYS ARG SER LYS ASN PRO LEU LEU TYR ASP ALA
SEQRES 12 A 284 ASN TYR PHE LEU CYS TRP HIS THR ASN CYS TYR ASP TYR
SEQRES 13 A 284 CYS ILE PRO TYR ASN SER VAL THR SER SER ILE VAL ILE
SEQRES 14 A 284 THR SER GLY ASP GLY THR THR SER PRO ILE SER GLU HIS
SEQRES 15 A 284 ASP TYR GLN ILE GLY GLY TYR THR GLU LYS TRP GLU SER
SEQRES 16 A 284 GLY VAL LYS ASP CYS VAL VAL LEU HIS SER TYR PHE THR
SEQRES 17 A 284 SER ASP TYR TYR GLN LEU TYR SER THR GLN LEU SER THR
SEQRES 18 A 284 ASP THR GLY VAL GLU HIS VAL THR PHE PHE ILE TYR ASN
SEQRES 19 A 284 LYS ILE VAL ASP GLU PRO GLU GLU HIS VAL GLN ILE HIS
SEQRES 20 A 284 THR ILE ASP GLY SER SER GLY VAL VAL ASN PRO VAL MET
SEQRES 21 A 284 GLU PRO ILE TYR ASP GLU PRO THR THR THR THR SER VAL
SEQRES 22 A 284 PRO LEU SER ASN SER LEU GLU VAL LEU PHE GLN
SEQRES 1 B 284 MET ASP LEU PHE MET ARG ILE PHE THR ILE GLY THR VAL
SEQRES 2 B 284 THR LEU LYS GLN GLY GLU ILE LYS ASP ALA THR PRO SER
SEQRES 3 B 284 ASP PHE VAL ARG ALA THR ALA THR ILE PRO ILE GLN ALA
SEQRES 4 B 284 SER LEU PRO PHE GLY TRP LEU ILE VAL GLY VAL ALA LEU
SEQRES 5 B 284 LEU ALA VAL PHE GLN SER ALA SER LYS ILE ILE THR LEU
SEQRES 6 B 284 LYS LYS ARG TRP GLN LEU ALA LEU SER LYS GLY VAL HIS
SEQRES 7 B 284 PHE VAL CYS ASN LEU LEU LEU LEU PHE VAL THR VAL TYR
SEQRES 8 B 284 SER HIS LEU LEU LEU VAL ALA ALA GLY LEU GLU ALA PRO
SEQRES 9 B 284 PHE LEU TYR LEU TYR ALA LEU VAL TYR PHE LEU GLN SER
SEQRES 10 B 284 ILE ASN PHE VAL ARG ILE ILE MET ARG LEU TRP LEU CYS
SEQRES 11 B 284 TRP LYS CYS ARG SER LYS ASN PRO LEU LEU TYR ASP ALA
SEQRES 12 B 284 ASN TYR PHE LEU CYS TRP HIS THR ASN CYS TYR ASP TYR
SEQRES 13 B 284 CYS ILE PRO TYR ASN SER VAL THR SER SER ILE VAL ILE
SEQRES 14 B 284 THR SER GLY ASP GLY THR THR SER PRO ILE SER GLU HIS
SEQRES 15 B 284 ASP TYR GLN ILE GLY GLY TYR THR GLU LYS TRP GLU SER
SEQRES 16 B 284 GLY VAL LYS ASP CYS VAL VAL LEU HIS SER TYR PHE THR
SEQRES 17 B 284 SER ASP TYR TYR GLN LEU TYR SER THR GLN LEU SER THR
SEQRES 18 B 284 ASP THR GLY VAL GLU HIS VAL THR PHE PHE ILE TYR ASN
SEQRES 19 B 284 LYS ILE VAL ASP GLU PRO GLU GLU HIS VAL GLN ILE HIS
SEQRES 20 B 284 THR ILE ASP GLY SER SER GLY VAL VAL ASN PRO VAL MET
SEQRES 21 B 284 GLU PRO ILE TYR ASP GLU PRO THR THR THR THR SER VAL
SEQRES 22 B 284 PRO LEU SER ASN SER LEU GLU VAL LEU PHE GLN
SEQRES 1 C 210 HIS HIS HIS HIS HIS HIS HIS ASP TYR ASP ILE PRO THR
SEQRES 2 C 210 THR GLU ASN LEU TYR PHE GLN GLY SER THR PHE SER LYS
SEQRES 3 C 210 LEU ARG GLU GLN LEU GLY PRO VAL THR GLN GLU PHE TRP
SEQRES 4 C 210 ASP ASN LEU GLU LYS GLU THR GLU GLY LEU ARG GLN GLU
SEQRES 5 C 210 MET SER LYS ASP LEU GLU GLU VAL LYS ALA LYS VAL GLN
SEQRES 6 C 210 PRO TYR LEU ASP ASP PHE GLN LYS LYS TRP GLN GLU GLU
SEQRES 7 C 210 MET GLU LEU TYR ARG GLN LYS VAL GLU PRO LEU ARG ALA
SEQRES 8 C 210 GLU LEU GLN GLU GLY ALA ARG GLN LYS LEU HIS GLU LEU
SEQRES 9 C 210 GLN GLU LYS LEU SER PRO LEU GLY GLU GLU MET ARG ASP
SEQRES 10 C 210 ARG ALA ARG ALA HIS VAL ASP ALA LEU ARG THR HIS LEU
SEQRES 11 C 210 ALA PRO TYR SER ASP GLU LEU ARG GLN ARG LEU ALA ALA
SEQRES 12 C 210 ARG LEU GLU ALA LEU LYS GLU ASN GLY GLY ALA ARG LEU
SEQRES 13 C 210 ALA GLU TYR HIS ALA LYS ALA THR GLU HIS LEU SER THR
SEQRES 14 C 210 LEU SER GLU LYS ALA LYS PRO ALA LEU GLU ASP LEU ARG
SEQRES 15 C 210 GLN GLY LEU LEU PRO VAL LEU GLU SER PHE LYS VAL SER
SEQRES 16 C 210 PHE LEU SER ALA LEU GLU GLU TYR THR LYS LYS LEU ASN
SEQRES 17 C 210 THR GLN
SEQRES 1 D 210 HIS HIS HIS HIS HIS HIS HIS ASP TYR ASP ILE PRO THR
SEQRES 2 D 210 THR GLU ASN LEU TYR PHE GLN GLY SER THR PHE SER LYS
SEQRES 3 D 210 LEU ARG GLU GLN LEU GLY PRO VAL THR GLN GLU PHE TRP
SEQRES 4 D 210 ASP ASN LEU GLU LYS GLU THR GLU GLY LEU ARG GLN GLU
SEQRES 5 D 210 MET SER LYS ASP LEU GLU GLU VAL LYS ALA LYS VAL GLN
SEQRES 6 D 210 PRO TYR LEU ASP ASP PHE GLN LYS LYS TRP GLN GLU GLU
SEQRES 7 D 210 MET GLU LEU TYR ARG GLN LYS VAL GLU PRO LEU ARG ALA
SEQRES 8 D 210 GLU LEU GLN GLU GLY ALA ARG GLN LYS LEU HIS GLU LEU
SEQRES 9 D 210 GLN GLU LYS LEU SER PRO LEU GLY GLU GLU MET ARG ASP
SEQRES 10 D 210 ARG ALA ARG ALA HIS VAL ASP ALA LEU ARG THR HIS LEU
SEQRES 11 D 210 ALA PRO TYR SER ASP GLU LEU ARG GLN ARG LEU ALA ALA
SEQRES 12 D 210 ARG LEU GLU ALA LEU LYS GLU ASN GLY GLY ALA ARG LEU
SEQRES 13 D 210 ALA GLU TYR HIS ALA LYS ALA THR GLU HIS LEU SER THR
SEQRES 14 D 210 LEU SER GLU LYS ALA LYS PRO ALA LEU GLU ASP LEU ARG
SEQRES 15 D 210 GLN GLY LEU LEU PRO VAL LEU GLU SER PHE LYS VAL SER
SEQRES 16 D 210 PHE LEU SER ALA LEU GLU GLU TYR THR LYS LYS LEU ASN
SEQRES 17 D 210 THR GLN
HET PEE A 301 23
HET PEE B 301 23
HETNAM PEE 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE
HETSYN PEE DOPE
FORMUL 5 PEE 2(C41 H78 N O8 P)
FORMUL 7 HOH *122(H2 O)
HELIX 1 AA1 PHE A 43 LYS A 61 1 19
HELIX 2 AA2 LYS A 67 GLY A 100 1 34
HELIX 3 AA3 GLU A 102 PRO A 104 5 3
HELIX 4 AA4 PHE A 105 ARG A 134 1 30
HELIX 5 AA5 LYS A 136 TYR A 141 1 6
HELIX 6 AA6 LEU A 219 GLY A 224 1 6
HELIX 7 AA7 PHE B 43 LYS B 61 1 19
HELIX 8 AA8 LYS B 67 GLY B 100 1 34
HELIX 9 AA9 GLU B 102 PRO B 104 5 3
HELIX 10 AB1 PHE B 105 ARG B 134 1 30
HELIX 11 AB2 LYS B 136 TYR B 141 1 6
HELIX 12 AB3 LEU B 219 GLY B 224 1 6
HELIX 13 AB4 SER C 26 SER C 55 1 30
HELIX 14 AB5 SER D 26 THR D 47 1 22
HELIX 15 AB6 THR D 47 SER D 55 1 9
SHEET 1 AA1 8 ASP A 155 TYR A 160 0
SHEET 2 AA1 8 TYR A 145 HIS A 150 -1 N LEU A 147 O ILE A 158
SHEET 3 AA1 8 CYS A 200 HIS A 204 -1 O VAL A 202 N CYS A 148
SHEET 4 AA1 8 SER A 209 GLN A 218 -1 O ASP A 210 N LEU A 203
SHEET 5 AA1 8 VAL A 228 LYS A 235 -1 O PHE A 230 N GLN A 218
SHEET 6 AA1 8 SER A 166 GLY A 172 -1 N ILE A 169 O PHE A 231
SHEET 7 AA1 8 ASP A 183 ILE A 186 -1 O GLN A 185 N THR A 170
SHEET 8 AA1 8 TYR A 189 LYS A 192 -1 O GLU A 191 N TYR A 184
SHEET 1 AA2 8 ASP B 155 TYR B 160 0
SHEET 2 AA2 8 TYR B 145 HIS B 150 -1 N LEU B 147 O ILE B 158
SHEET 3 AA2 8 CYS B 200 HIS B 204 -1 O VAL B 202 N CYS B 148
SHEET 4 AA2 8 SER B 209 GLN B 218 -1 O ASP B 210 N LEU B 203
SHEET 5 AA2 8 VAL B 228 LYS B 235 -1 O PHE B 230 N GLN B 218
SHEET 6 AA2 8 SER B 166 GLY B 172 -1 N ILE B 169 O PHE B 231
SHEET 7 AA2 8 ASP B 183 ILE B 186 -1 O GLN B 185 N THR B 170
SHEET 8 AA2 8 TYR B 189 LYS B 192 -1 O GLU B 191 N TYR B 184
SITE 1 AC1 9 LYS A 61 ILE A 62 ILE A 63 THR A 64
SITE 2 AC1 9 HOH A 402 ARG B 122 TYR B 206 THR C 36
SITE 3 AC1 9 TRP C 40
SITE 1 AC2 9 ARG A 122 TYR A 206 LYS B 61 ILE B 62
SITE 2 AC2 9 ILE B 63 THR B 64 HOH B 404 THR D 36
SITE 3 AC2 9 TRP D 40
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 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 1 N SER A 40 121.487 105.338 74.455 1.00 57.62 N
ATOM 2 CA SER A 40 120.334 106.060 74.979 1.00 57.62 C
ATOM 3 C SER A 40 119.831 105.432 76.271 1.00 57.62 C
ATOM 4 O SER A 40 120.029 104.242 76.516 1.00 57.62 O
ATOM 5 CB SER A 40 119.208 106.099 73.946 1.00 57.62 C
ATOM 6 OG SER A 40 119.593 106.838 72.801 1.00 57.62 O
ATOM 7 N LEU A 41 119.178 106.245 77.095 1.00 50.64 N
ATOM 8 CA LEU A 41 118.574 105.794 78.342 1.00 50.64 C
ATOM 9 C LEU A 41 117.071 105.679 78.136 1.00 50.64 C
ATOM 10 O LEU A 41 116.405 106.702 77.910 1.00 50.64 O
ATOM 11 CB LEU A 41 118.889 106.760 79.485 1.00 50.64 C
ATOM 12 CG LEU A 41 120.099 106.462 80.371 1.00 50.64 C
ATOM 13 CD1 LEU A 41 121.385 106.457 79.577 1.00 50.64 C
ATOM 14 CD2 LEU A 41 120.175 107.491 81.478 1.00 50.64 C
ATOM 15 N PRO A 42 116.501 104.479 78.175 1.00 47.90 N
ATOM 16 CA PRO A 42 115.062 104.336 77.937 1.00 47.90 C
ATOM 17 C PRO A 42 114.231 104.930 79.064 1.00 47.90 C
ATOM 18 O PRO A 42 114.625 104.954 80.231 1.00 47.90 O
ATOM 19 CB PRO A 42 114.862 102.820 77.840 1.00 47.90 C
ATOM 20 CG PRO A 42 116.035 102.231 78.516 1.00 47.90 C
ATOM 21 CD PRO A 42 117.169 103.187 78.389 1.00 47.90 C
ATOM 22 N PHE A 43 113.048 105.414 78.684 1.00 47.52 N
ATOM 23 CA PHE A 43 112.149 106.063 79.630 1.00 47.52 C
ATOM 24 C PHE A 43 111.498 105.066 80.581 1.00 47.52 C
ATOM 25 O PHE A 43 111.025 105.467 81.646 1.00 47.52 O
ATOM 26 CB PHE A 43 111.050 106.837 78.889 1.00 47.52 C
ATOM 27 CG PHE A 43 111.520 108.101 78.189 1.00 47.52 C
ATOM 28 CD1 PHE A 43 112.862 108.354 77.951 1.00 47.52 C
ATOM 29 CD2 PHE A 43 110.592 109.020 77.731 1.00 47.52 C
ATOM 30 CE1 PHE A 43 113.267 109.503 77.297 1.00 47.52 C
ATOM 31 CE2 PHE A 43 110.994 110.170 77.077 1.00 47.52 C
ATOM 32 CZ PHE A 43 112.332 110.410 76.862 1.00 47.52 C
ATOM 33 N GLY A 44 111.466 103.782 80.219 1.00 44.11 N
ATOM 34 CA GLY A 44 110.729 102.810 81.008 1.00 44.11 C
ATOM 35 C GLY A 44 111.360 102.496 82.350 1.00 44.11 C
ATOM 36 O GLY A 44 110.664 102.084 83.284 1.00 44.11 O
ATOM 37 N TRP A 45 112.678 102.675 82.469 1.00 43.95 N
ATOM 38 CA TRP A 45 113.317 102.480 83.765 1.00 43.95 C
ATOM 39 C TRP A 45 112.875 103.526 84.773 1.00 43.95 C
ATOM 40 O TRP A 45 112.817 103.234 85.969 1.00 43.95 O
ATOM 41 CB TRP A 45 114.839 102.481 83.634 1.00 43.95 C
ATOM 42 CG TRP A 45 115.374 101.279 82.942 1.00 43.95 C
ATOM 43 CD1 TRP A 45 116.033 101.244 81.756 1.00 43.95 C
ATOM 44 CD2 TRP A 45 115.293 99.924 83.397 1.00 43.95 C
ATOM 45 NE1 TRP A 45 116.371 99.954 81.437 1.00 43.95 N
ATOM 46 CE2 TRP A 45 115.927 99.123 82.430 1.00 43.95 C
ATOM 47 CE3 TRP A 45 114.748 99.310 84.530 1.00 43.95 C
ATOM 48 CZ2 TRP A 45 116.031 97.739 82.560 1.00 43.95 C
ATOM 49 CZ3 TRP A 45 114.850 97.941 84.656 1.00 43.95 C
ATOM 50 CH2 TRP A 45 115.488 97.169 83.678 1.00 43.95 C
ATOM 51 N LEU A 46 112.549 104.736 84.316 1.00 38.98 N
ATOM 52 CA LEU A 46 111.982 105.730 85.218 1.00 38.98 C
ATOM 53 C LEU A 46 110.643 105.263 85.776 1.00 38.98 C
ATOM 54 O LEU A 46 110.378 105.415 86.971 1.00 38.98 O
ATOM 55 CB LEU A 46 111.834 107.071 84.504 1.00 38.98 C
ATOM 56 CG LEU A 46 111.318 108.203 85.391 1.00 38.98 C
ATOM 57 CD1 LEU A 46 112.288 108.456 86.532 1.00 38.98 C
ATOM 58 CD2 LEU A 46 111.087 109.469 84.588 1.00 38.98 C
ATOM 59 N ILE A 47 109.803 104.662 84.931 1.00 38.88 N
ATOM 60 CA ILE A 47 108.516 104.142 85.382 1.00 38.88 C
ATOM 61 C ILE A 47 108.707 102.973 86.346 1.00 38.88 C
ATOM 62 O ILE A 47 108.017 102.880 87.368 1.00 38.88 O
ATOM 63 CB ILE A 47 107.651 103.758 84.166 1.00 38.88 C