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HEADER HYDROLASE 08-JUN-23 8PBA
TITLE CRYO-EM STRUCTURE OF CAENORHABDITIS ELEGANS DPF-3 (APO)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE FOUR (IV) FAMILY;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;
SOURCE 3 ORGANISM_TAXID: 6239;
SOURCE 4 GENE: DPF-3, CELE_K02F2.1, K02F2.1;
SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7111
KEYWDS DIPEPTIDYLPEPTIDASE, HYDROLASE
EXPDTA ELECTRON MICROSCOPY
AUTHOR R.K.GUDIPATI,S.CAVADINI,G.KEMPF,H.GROSSHANS
REVDAT 1 26-JUN-24 8PBA 0
JRNL AUTH R.K.GUDIPATI,S.CAVADINI,G.KEMPF,H.GROSSHANS
JRNL TITL CRYO-EM STRUCTURE OF CAENORHABDITIS ELEGANS DPF-3 (APO)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : RELION, GCTF, CRYOSPARC, RELION, COOT,
REMARK 3 ISOLDE, ROSETTAEM, CRYOSPARC, 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 : FLEXIBLE FIT
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) : 2.640
REMARK 3 NUMBER OF PARTICLES : 223429
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 8PBA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUN-23.
REMARK 100 THE DEPOSITION ID IS D_1292126219.
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 : HOMODIMERIC COMPLEX OF DPF-3
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.50
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) : 800.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 MET A 2
REMARK 465 PHE A 3
REMARK 465 ASN A 4
REMARK 465 PHE A 5
REMARK 465 TYR A 6
REMARK 465 GLN A 7
REMARK 465 PHE A 8
REMARK 465 LEU A 9
REMARK 465 TYR A 10
REMARK 465 ASN A 11
REMARK 465 LEU A 12
REMARK 465 GLN A 13
REMARK 465 ASN A 14
REMARK 465 VAL A 15
REMARK 465 SER A 16
REMARK 465 PRO A 17
REMARK 465 PHE A 18
REMARK 465 ILE A 19
REMARK 465 ASP A 20
REMARK 465 PHE A 21
REMARK 465 SER A 22
REMARK 465 VAL A 23
REMARK 465 LEU A 24
REMARK 465 LYS A 25
REMARK 465 GLN A 26
REMARK 465 LEU A 27
REMARK 465 THR A 28
REMARK 465 HIS A 29
REMARK 465 THR A 30
REMARK 465 LYS A 31
REMARK 465 MET A 32
REMARK 465 ARG A 33
REMARK 465 TYR A 128
REMARK 465 ASN A 129
REMARK 465 VAL A 130
REMARK 465 ASP A 131
REMARK 465 SER A 132
REMARK 465 TYR A 133
REMARK 465 ILE A 134
REMARK 465 ARG A 135
REMARK 465 LYS A 136
REMARK 465 THR A 137
REMARK 465 PRO A 138
REMARK 465 PRO A 139
REMARK 465 SER A 140
REMARK 465 ALA A 141
REMARK 465 GLU A 142
REMARK 465 PHE A 143
REMARK 465 THR A 144
REMARK 465 LEU A 145
REMARK 465 GLN A 146
REMARK 465 CYS A 147
REMARK 465 GLU A 148
REMARK 465 ARG A 149
REMARK 465 GLN A 150
REMARK 465 ARG A 151
REMARK 465 SER A 152
REMARK 465 GLN A 153
REMARK 465 VAL A 154
REMARK 465 VAL A 155
REMARK 465 THR A 156
REMARK 465 GLY A 157
REMARK 465 ILE A 158
REMARK 465 SER A 159
REMARK 465 ASP A 160
REMARK 465 TYR A 161
REMARK 465 GLU A 162
REMARK 465 ILE A 163
REMARK 465 ARG A 164
REMARK 465 ASN A 165
REMARK 465 GLY A 166
REMARK 465 LYS A 167
REMARK 465 MET A 168
REMARK 465 ILE A 169
REMARK 465 LEU A 170
REMARK 465 MET A 171
REMARK 465 ALA A 172
REMARK 465 GLY A 173
REMARK 465 ASP A 174
REMARK 465 GLN A 175
REMARK 465 LEU A 176
REMARK 465 PHE A 177
REMARK 465 ARG A 178
REMARK 465 TYR A 179
REMARK 465 ASN A 180
REMARK 465 PRO A 181
REMARK 465 LEU A 182
REMARK 465 ASN A 183
REMARK 465 GLU A 184
REMARK 465 ALA A 185
REMARK 465 LEU A 186
REMARK 465 ALA A 187
REMARK 465 ALA A 188
REMARK 465 ILE A 189
REMARK 465 PRO A 190
REMARK 465 ILE A 191
REMARK 465 ALA A 192
REMARK 465 VAL A 193
REMARK 465 PRO A 194
REMARK 465 ASP A 195
REMARK 465 ASP A 196
REMARK 465 GLN A 197
REMARK 465 SER A 198
REMARK 465 SER A 199
REMARK 465 THR A 200
REMARK 465 GLU A 201
REMARK 465 PRO A 202
REMARK 465 MET A 203
REMARK 465 ASP A 204
REMARK 465 ILE A 205
REMARK 465 SER A 206
REMARK 465 GLU A 207
REMARK 465 GLY A 208
REMARK 465 SER A 209
REMARK 465 ILE A 210
REMARK 465 THR A 211
REMARK 465 SER A 212
REMARK 465 GLY A 213
REMARK 465 THR A 214
REMARK 465 LYS A 215
REMARK 465 GLY A 216
REMARK 465 SER A 217
REMARK 465 GLY A 218
REMARK 465 SER A 219
REMARK 465 GLU A 220
REMARK 465 ALA A 221
REMARK 465 PRO A 222
REMARK 465 GLN A 223
REMARK 465 SER A 224
REMARK 465 SER A 225
REMARK 465 THR A 226
REMARK 465 VAL A 227
REMARK 465 PRO A 228
REMARK 465 PRO A 229
REMARK 465 VAL A 230
REMARK 465 THR A 231
REMARK 465 ARG A 232
REMARK 465 ILE A 233
REMARK 465 PRO A 234
REMARK 465 ILE A 235
REMARK 465 LYS A 236
REMARK 465 LYS A 237
REMARK 465 PRO A 238
REMARK 465 THR A 239
REMARK 465 THR A 240
REMARK 465 SER A 241
REMARK 465 THR A 242
REMARK 465 GLU A 243
REMARK 465 LYS A 244
REMARK 465 PRO A 245
REMARK 465 ALA A 246
REMARK 465 THR A 247
REMARK 465 ALA A 248
REMARK 465 PRO A 249
REMARK 465 PRO A 250
REMARK 465 THR A 251
REMARK 465 ASN A 252
REMARK 465 ASN A 253
REMARK 465 PHE A 254
REMARK 465 VAL A 255
REMARK 465 SER A 256
REMARK 465 GLY A 435
REMARK 465 SER A 436
REMARK 465 ILE A 437
REMARK 465 LYS A 438
REMARK 465 GLU A 439
REMARK 465 ASP A 440
REMARK 465 ASN A 441
REMARK 465 LEU A 442
REMARK 465 GLN A 443
REMARK 465 LEU A 444
REMARK 465 SER A 445
REMARK 465 THR A 446
REMARK 465 ASP A 447
REMARK 465 LEU A 448
REMARK 465 ASN A 449
REMARK 465 MET A 450
REMARK 465 GLY A 451
REMARK 465 VAL A 452
REMARK 465 TRP A 453
REMARK 465 ASP A 454
REMARK 465 ASP A 455
REMARK 465 LYS A 456
REMARK 465 SER A 457
REMARK 465 HIS A 458
REMARK 465 GLU A 459
REMARK 465 GLU A 460
REMARK 465 THR A 461
REMARK 465 MET A 462
REMARK 465 GLU A 463
REMARK 465 LYS A 464
REMARK 465 PHE A 919
REMARK 465 GLY A 920
REMARK 465 PRO A 921
REMARK 465 THR A 922
REMARK 465 THR A 923
REMARK 465 ALA A 924
REMARK 465 ALA A 925
REMARK 465 PRO A 926
REMARK 465 ARG A 927
REMARK 465 GLN A 928
REMARK 465 GLY A 929
REMARK 465 PRO A 930
REMARK 465 LEU A 931
REMARK 465 TRP A 932
REMARK 465 SER A 933
REMARK 465 HIS A 934
REMARK 465 PRO A 935
REMARK 465 GLN A 936
REMARK 465 PHE A 937
REMARK 465 GLU A 938
REMARK 465 LYS A 939
REMARK 465 MET B 1
REMARK 465 MET B 2
REMARK 465 PHE B 3
REMARK 465 ASN B 4
REMARK 465 PHE B 5
REMARK 465 TYR B 6
REMARK 465 GLN B 7
REMARK 465 PHE B 8
REMARK 465 LEU B 9
REMARK 465 TYR B 10
REMARK 465 ASN B 11
REMARK 465 LEU B 12
REMARK 465 GLN B 13
REMARK 465 ASN B 14
REMARK 465 VAL B 15
REMARK 465 SER B 16
REMARK 465 PRO B 17
REMARK 465 PHE B 18
REMARK 465 ILE B 19
REMARK 465 ASP B 20
REMARK 465 PHE B 21
REMARK 465 SER B 22
REMARK 465 VAL B 23
REMARK 465 LEU B 24
REMARK 465 LYS B 25
REMARK 465 GLN B 26
REMARK 465 LEU B 27
REMARK 465 THR B 28
REMARK 465 HIS B 29
REMARK 465 THR B 30
REMARK 465 LYS B 31
REMARK 465 MET B 32
REMARK 465 ARG B 33
REMARK 465 TYR B 128
REMARK 465 ASN B 129
REMARK 465 VAL B 130
REMARK 465 ASP B 131
REMARK 465 SER B 132
REMARK 465 TYR B 133
REMARK 465 ILE B 134
REMARK 465 ARG B 135
REMARK 465 LYS B 136
REMARK 465 THR B 137
REMARK 465 PRO B 138
REMARK 465 PRO B 139
REMARK 465 SER B 140
REMARK 465 ALA B 141
REMARK 465 GLU B 142
REMARK 465 PHE B 143
REMARK 465 THR B 144
REMARK 465 LEU B 145
REMARK 465 GLN B 146
REMARK 465 CYS B 147
REMARK 465 GLU B 148
REMARK 465 ARG B 149
REMARK 465 GLN B 150
REMARK 465 ARG B 151
REMARK 465 SER B 152
REMARK 465 GLN B 153
REMARK 465 VAL B 154
REMARK 465 VAL B 155
REMARK 465 THR B 156
REMARK 465 GLY B 157
REMARK 465 ILE B 158
REMARK 465 SER B 159
REMARK 465 ASP B 160
REMARK 465 TYR B 161
REMARK 465 GLU B 162
REMARK 465 ILE B 163
REMARK 465 ARG B 164
REMARK 465 ASN B 165
REMARK 465 GLY B 166
REMARK 465 LYS B 167
REMARK 465 MET B 168
REMARK 465 ILE B 169
REMARK 465 LEU B 170
REMARK 465 MET B 171
REMARK 465 ALA B 172
REMARK 465 GLY B 173
REMARK 465 ASP B 174
REMARK 465 GLN B 175
REMARK 465 LEU B 176
REMARK 465 PHE B 177
REMARK 465 ARG B 178
REMARK 465 TYR B 179
REMARK 465 ASN B 180
REMARK 465 PRO B 181
REMARK 465 LEU B 182
REMARK 465 ASN B 183
REMARK 465 GLU B 184
REMARK 465 ALA B 185
REMARK 465 LEU B 186
REMARK 465 ALA B 187
REMARK 465 ALA B 188
REMARK 465 ILE B 189
REMARK 465 PRO B 190
REMARK 465 ILE B 191
REMARK 465 ALA B 192
REMARK 465 VAL B 193
REMARK 465 PRO B 194
REMARK 465 ASP B 195
REMARK 465 ASP B 196
REMARK 465 GLN B 197
REMARK 465 SER B 198
REMARK 465 SER B 199
REMARK 465 THR B 200
REMARK 465 GLU B 201
REMARK 465 PRO B 202
REMARK 465 MET B 203
REMARK 465 ASP B 204
REMARK 465 ILE B 205
REMARK 465 SER B 206
REMARK 465 GLU B 207
REMARK 465 GLY B 208
REMARK 465 SER B 209
REMARK 465 ILE B 210
REMARK 465 THR B 211
REMARK 465 SER B 212
REMARK 465 GLY B 213
REMARK 465 THR B 214
REMARK 465 LYS B 215
REMARK 465 GLY B 216
REMARK 465 SER B 217
REMARK 465 GLY B 218
REMARK 465 SER B 219
REMARK 465 GLU B 220
REMARK 465 ALA B 221
REMARK 465 PRO B 222
REMARK 465 GLN B 223
REMARK 465 SER B 224
REMARK 465 SER B 225
REMARK 465 THR B 226
REMARK 465 VAL B 227
REMARK 465 PRO B 228
REMARK 465 PRO B 229
REMARK 465 VAL B 230
REMARK 465 THR B 231
REMARK 465 ARG B 232
REMARK 465 ILE B 233
REMARK 465 PRO B 234
REMARK 465 ILE B 235
REMARK 465 LYS B 236
REMARK 465 LYS B 237
REMARK 465 PRO B 238
REMARK 465 THR B 239
REMARK 465 THR B 240
REMARK 465 SER B 241
REMARK 465 THR B 242
REMARK 465 GLU B 243
REMARK 465 LYS B 244
REMARK 465 PRO B 245
REMARK 465 ALA B 246
REMARK 465 THR B 247
REMARK 465 ALA B 248
REMARK 465 PRO B 249
REMARK 465 PRO B 250
REMARK 465 THR B 251
REMARK 465 ASN B 252
REMARK 465 ASN B 253
REMARK 465 PHE B 254
REMARK 465 VAL B 255
REMARK 465 SER B 256
REMARK 465 GLY B 435
REMARK 465 SER B 436
REMARK 465 ILE B 437
REMARK 465 LYS B 438
REMARK 465 GLU B 439
REMARK 465 ASP B 440
REMARK 465 ASN B 441
REMARK 465 LEU B 442
REMARK 465 GLN B 443
REMARK 465 LEU B 444
REMARK 465 SER B 445
REMARK 465 THR B 446
REMARK 465 ASP B 447
REMARK 465 LEU B 448
REMARK 465 ASN B 449
REMARK 465 MET B 450
REMARK 465 GLY B 451
REMARK 465 VAL B 452
REMARK 465 TRP B 453
REMARK 465 ASP B 454
REMARK 465 ASP B 455
REMARK 465 LYS B 456
REMARK 465 SER B 457
REMARK 465 HIS B 458
REMARK 465 GLU B 459
REMARK 465 GLU B 460
REMARK 465 THR B 461
REMARK 465 MET B 462
REMARK 465 GLU B 463
REMARK 465 LYS B 464
REMARK 465 PHE B 919
REMARK 465 GLY B 920
REMARK 465 PRO B 921
REMARK 465 THR B 922
REMARK 465 THR B 923
REMARK 465 ALA B 924
REMARK 465 ALA B 925
REMARK 465 PRO B 926
REMARK 465 ARG B 927
REMARK 465 GLN B 928
REMARK 465 GLY B 929
REMARK 465 PRO B 930
REMARK 465 LEU B 931
REMARK 465 TRP B 932
REMARK 465 SER B 933
REMARK 465 HIS B 934
REMARK 465 PRO B 935
REMARK 465 GLN B 936
REMARK 465 PHE B 937
REMARK 465 GLU B 938
REMARK 465 LYS B 939
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HG1 THR B 91 H ASN B 92 1.28
REMARK 500 HG1 THR A 91 H ASN A 92 1.28
REMARK 500 HG1 THR A 673 H LEU A 675 1.29
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 643 CB - CG - CD1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 TYR B 643 CB - CG - CD1 ANGL. DEV. = -4.3 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 LEU A 429 154.96 63.40
REMARK 500 TYR A 483 -69.32 -125.99
REMARK 500 TYR A 700 -72.93 -121.57
REMARK 500 LYS A 748 19.63 58.32
REMARK 500 SER A 784 -115.97 63.41
REMARK 500 ARG A 892 -137.88 -98.30
REMARK 500 TYR B 483 -68.01 -124.74
REMARK 500 TYR B 700 -72.90 -121.59
REMARK 500 LYS B 748 19.60 58.35
REMARK 500 SER B 784 -116.04 63.44
REMARK 500 ARG B 892 -137.89 -98.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-17582 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF CAENORHABDITIS ELEGANS DPF-3 (APO)
DBREF 8PBA A 1 931 UNP Q965K3 Q965K3_CAEEL 1 927
DBREF 8PBA B 1 931 UNP Q965K3 Q965K3_CAEEL 1 927
SEQADV 8PBA SER A 217 UNP Q965K3 CYS 213 CONFLICT
SEQADV 8PBA GLY A 218 UNP Q965K3 SER 214 CONFLICT
SEQADV 8PBA SER A 219 UNP Q965K3 ASN 215 CONFLICT
SEQADV 8PBA TRP A 932 UNP Q965K3 EXPRESSION TAG
SEQADV 8PBA SER A 933 UNP Q965K3 EXPRESSION TAG
SEQADV 8PBA HIS A 934 UNP Q965K3 EXPRESSION TAG
SEQADV 8PBA PRO A 935 UNP Q965K3 EXPRESSION TAG
SEQADV 8PBA GLN A 936 UNP Q965K3 EXPRESSION TAG
SEQADV 8PBA PHE A 937 UNP Q965K3 EXPRESSION TAG
SEQADV 8PBA GLU A 938 UNP Q965K3 EXPRESSION TAG
SEQADV 8PBA LYS A 939 UNP Q965K3 EXPRESSION TAG
SEQADV 8PBA SER B 217 UNP Q965K3 CYS 213 CONFLICT
SEQADV 8PBA GLY B 218 UNP Q965K3 SER 214 CONFLICT
SEQADV 8PBA SER B 219 UNP Q965K3 ASN 215 CONFLICT
SEQADV 8PBA TRP B 932 UNP Q965K3 EXPRESSION TAG
SEQADV 8PBA SER B 933 UNP Q965K3 EXPRESSION TAG
SEQADV 8PBA HIS B 934 UNP Q965K3 EXPRESSION TAG
SEQADV 8PBA PRO B 935 UNP Q965K3 EXPRESSION TAG
SEQADV 8PBA GLN B 936 UNP Q965K3 EXPRESSION TAG
SEQADV 8PBA PHE B 937 UNP Q965K3 EXPRESSION TAG
SEQADV 8PBA GLU B 938 UNP Q965K3 EXPRESSION TAG
SEQADV 8PBA LYS B 939 UNP Q965K3 EXPRESSION TAG
SEQRES 1 A 935 MET MET PHE ASN PHE TYR GLN PHE LEU TYR ASN LEU GLN
SEQRES 2 A 935 ASN VAL SER PRO PHE ILE ASP PHE SER VAL LEU LYS GLN
SEQRES 3 A 935 LEU THR HIS THR LYS MET ARG GLU ASN GLU PRO ALA ARG
SEQRES 4 A 935 PHE GLU THR ARG SER PHE SER GLN LEU ILE ASP HIS ALA
SEQRES 5 A 935 ARG SER TRP LYS THR GLU VAL ARG GLY MET THR THR GLN
SEQRES 6 A 935 GLY PHE THR LYS ILE SER LEU MET ARG ALA GLU LYS ASP
SEQRES 7 A 935 ARG LEU ASN MET TYR ALA ILE SER SER VAL PRO GLY THR
SEQRES 8 A 935 ASN THR GLN SER ILE PHE SER VAL THR ILE PRO LEU GLU
SEQRES 9 A 935 LEU VAL GLU LYS ALA GLN VAL ALA ASP ARG LYS PHE GLU
SEQRES 10 A 935 LEU LYS LEU LYS SER GLY TYR ASN VAL ASP SER TYR ILE
SEQRES 11 A 935 ARG LYS THR PRO PRO SER ALA GLU PHE THR LEU GLN CYS
SEQRES 12 A 935 GLU ARG GLN ARG SER GLN VAL VAL THR GLY ILE SER ASP
SEQRES 13 A 935 TYR GLU ILE ARG ASN GLY LYS MET ILE LEU MET ALA GLY
SEQRES 14 A 935 ASP GLN LEU PHE ARG TYR ASN PRO LEU ASN GLU ALA LEU
SEQRES 15 A 935 ALA ALA ILE PRO ILE ALA VAL PRO ASP ASP GLN SER SER
SEQRES 16 A 935 THR GLU PRO MET ASP ILE SER GLU GLY SER ILE THR SER
SEQRES 17 A 935 GLY THR LYS GLY SER GLY SER GLU ALA PRO GLN SER SER
SEQRES 18 A 935 THR VAL PRO PRO VAL THR ARG ILE PRO ILE LYS LYS PRO
SEQRES 19 A 935 THR THR SER THR GLU LYS PRO ALA THR ALA PRO PRO THR
SEQRES 20 A 935 ASN ASN PHE VAL SER SER ALA LYS VAL CYS PRO ALA ASP
SEQRES 21 A 935 SER SER LEU LEU ALA TYR VAL LEU ASN LYS GLN VAL TYR
SEQRES 22 A 935 ILE GLU LYS ASN GLY LYS ILE ILE HIS ARG THR SER SER
SEQRES 23 A 935 ASN SER LYS HIS ILE THR ASN GLY VAL PRO SER TYR ILE
SEQRES 24 A 935 VAL GLN GLU GLU LEU GLU ARG PHE GLU GLY ILE TRP TRP
SEQRES 25 A 935 SER GLU SER LYS THR ARG LEU LEU TYR GLU HIS VAL ASN
SEQRES 26 A 935 GLU GLU LYS VAL ALA GLU SER GLN PHE GLY VAL ASN GLY
SEQRES 27 A 935 ASP PRO PRO VAL ALA PRO MET LYS TYR PRO ARG ALA GLY
SEQRES 28 A 935 THR LYS ASN ALA TYR SER THR LEU ARG MET VAL ILE LEU
SEQRES 29 A 935 GLU ASN GLY LYS ALA TYR ASP VAL PRO LEU LYS ASP GLU
SEQRES 30 A 935 VAL ILE TYR LYS HIS CYS PRO PHE TYR GLU TYR ILE THR
SEQRES 31 A 935 ARG ALA GLY PHE PHE SER ASP GLY THR THR VAL TRP VAL
SEQRES 32 A 935 GLN VAL MET SER ARG ASP GLN ALA GLN CYS SER LEU LEU
SEQRES 33 A 935 LEU ILE PRO TYR THR ASP PHE LEU LEU PRO GLU GLU LEU
SEQRES 34 A 935 GLY GLY SER ILE LYS GLU ASP ASN LEU GLN LEU SER THR
SEQRES 35 A 935 ASP LEU ASN MET GLY VAL TRP ASP ASP LYS SER HIS GLU
SEQRES 36 A 935 GLU THR MET GLU LYS PRO PRO ARG GLY LYS LEU ARG GLY
SEQRES 37 A 935 THR VAL GLN ILE HIS LYS ALA ARG ASN ASP TYR TRP ILE
SEQRES 38 A 935 ASN THR HIS ASN ALA ILE TYR PRO LEU LYS ILE THR ASP
SEQRES 39 A 935 GLU GLU HIS PRO MET TYR GLU PHE ILE TYR CYS LEU GLU
SEQRES 40 A 935 LYS PRO ASN GLY SER CYS LEU ALA LEU ILE SER ALA GLU
SEQRES 41 A 935 LEU ASP GLN ASN GLY TYR CYS ARG HIS THR GLU GLU LYS
SEQRES 42 A 935 LEU LEU MET ALA GLU ASN PHE SER ILE ASN LYS SER MET
SEQRES 43 A 935 GLY ILE VAL VAL ASP GLU VAL ARG GLU LEU VAL TYR TYR
SEQRES 44 A 935 VAL ALA ASN GLU SER HIS PRO THR GLU TRP ASN ILE CYS
SEQRES 45 A 935 VAL SER HIS TYR ARG THR GLY GLN HIS ALA GLN LEU THR
SEQRES 46 A 935 GLU SER GLY ILE CYS PHE LYS SER GLU ARG ALA ASN GLY
SEQRES 47 A 935 LYS LEU ALA LEU ASP LEU ASP HIS GLY PHE ALA CYS TYR
SEQRES 48 A 935 MET THR SER VAL GLY SER PRO ALA GLU CYS ARG PHE TYR
SEQRES 49 A 935 SER PHE ARG TRP LYS GLU ASN GLU VAL LEU PRO SER THR
SEQRES 50 A 935 VAL TYR ALA ALA ASN ILE THR VAL SER GLY HIS PRO GLY
SEQRES 51 A 935 GLN PRO ASP LEU HIS PHE ASP SER PRO GLU MET ILE GLU
SEQRES 52 A 935 PHE GLN SER LYS LYS THR GLY LEU MET HIS TYR ALA MET
SEQRES 53 A 935 ILE LEU ARG PRO SER ASN PHE ASP PRO TYR LYS LYS TYR
SEQRES 54 A 935 PRO VAL PHE HIS TYR VAL TYR GLY GLY PRO GLY ILE GLN
SEQRES 55 A 935 ILE VAL HIS ASN ASP PHE SER TRP ILE GLN TYR ILE ARG
SEQRES 56 A 935 PHE CYS ARG LEU GLY TYR VAL VAL VAL PHE ILE ASP ASN
SEQRES 57 A 935 ARG GLY SER ALA HIS ARG GLY ILE GLU PHE GLU ARG HIS
SEQRES 58 A 935 ILE HIS LYS LYS MET GLY THR VAL GLU VAL GLU ASP GLN
SEQRES 59 A 935 VAL GLU GLY LEU GLN MET LEU ALA GLU ARG THR GLY GLY
SEQRES 60 A 935 PHE MET ASP MET SER ARG VAL VAL VAL HIS GLY TRP SER
SEQRES 61 A 935 TYR GLY GLY TYR MET ALA LEU GLN MET ILE ALA LYS HIS
SEQRES 62 A 935 PRO ASN ILE TYR ARG ALA ALA ILE ALA GLY GLY ALA VAL
SEQRES 63 A 935 SER ASP TRP ARG LEU TYR ASP THR ALA TYR THR GLU ARG
SEQRES 64 A 935 TYR MET GLY TYR PRO LEU GLU GLU HIS VAL TYR GLY ALA
SEQRES 65 A 935 SER SER ILE THR GLY LEU VAL GLU LYS LEU PRO ASP GLU
SEQRES 66 A 935 PRO ASN ARG LEU MET LEU VAL HIS GLY LEU MET ASP GLU
SEQRES 67 A 935 ASN VAL HIS PHE ALA HIS LEU THR HIS LEU VAL ASP GLU
SEQRES 68 A 935 CYS ILE LYS LYS GLY LYS TRP HIS GLU LEU VAL ILE PHE
SEQRES 69 A 935 PRO ASN GLU ARG HIS GLY VAL ARG ASN ASN ASP ALA SER
SEQRES 70 A 935 ILE TYR LEU ASP ALA ARG MET MET TYR PHE ALA GLN GLN
SEQRES 71 A 935 ALA ILE GLN GLY PHE GLY PRO THR THR ALA ALA PRO ARG
SEQRES 72 A 935 GLN GLY PRO LEU TRP SER HIS PRO GLN PHE GLU LYS
SEQRES 1 B 935 MET MET PHE ASN PHE TYR GLN PHE LEU TYR ASN LEU GLN
SEQRES 2 B 935 ASN VAL SER PRO PHE ILE ASP PHE SER VAL LEU LYS GLN
SEQRES 3 B 935 LEU THR HIS THR LYS MET ARG GLU ASN GLU PRO ALA ARG
SEQRES 4 B 935 PHE GLU THR ARG SER PHE SER GLN LEU ILE ASP HIS ALA
SEQRES 5 B 935 ARG SER TRP LYS THR GLU VAL ARG GLY MET THR THR GLN
SEQRES 6 B 935 GLY PHE THR LYS ILE SER LEU MET ARG ALA GLU LYS ASP
SEQRES 7 B 935 ARG LEU ASN MET TYR ALA ILE SER SER VAL PRO GLY THR
SEQRES 8 B 935 ASN THR GLN SER ILE PHE SER VAL THR ILE PRO LEU GLU
SEQRES 9 B 935 LEU VAL GLU LYS ALA GLN VAL ALA ASP ARG LYS PHE GLU
SEQRES 10 B 935 LEU LYS LEU LYS SER GLY TYR ASN VAL ASP SER TYR ILE
SEQRES 11 B 935 ARG LYS THR PRO PRO SER ALA GLU PHE THR LEU GLN CYS
SEQRES 12 B 935 GLU ARG GLN ARG SER GLN VAL VAL THR GLY ILE SER ASP
SEQRES 13 B 935 TYR GLU ILE ARG ASN GLY LYS MET ILE LEU MET ALA GLY
SEQRES 14 B 935 ASP GLN LEU PHE ARG TYR ASN PRO LEU ASN GLU ALA LEU
SEQRES 15 B 935 ALA ALA ILE PRO ILE ALA VAL PRO ASP ASP GLN SER SER
SEQRES 16 B 935 THR GLU PRO MET ASP ILE SER GLU GLY SER ILE THR SER
SEQRES 17 B 935 GLY THR LYS GLY SER GLY SER GLU ALA PRO GLN SER SER
SEQRES 18 B 935 THR VAL PRO PRO VAL THR ARG ILE PRO ILE LYS LYS PRO
SEQRES 19 B 935 THR THR SER THR GLU LYS PRO ALA THR ALA PRO PRO THR
SEQRES 20 B 935 ASN ASN PHE VAL SER SER ALA LYS VAL CYS PRO ALA ASP
SEQRES 21 B 935 SER SER LEU LEU ALA TYR VAL LEU ASN LYS GLN VAL TYR
SEQRES 22 B 935 ILE GLU LYS ASN GLY LYS ILE ILE HIS ARG THR SER SER
SEQRES 23 B 935 ASN SER LYS HIS ILE THR ASN GLY VAL PRO SER TYR ILE
SEQRES 24 B 935 VAL GLN GLU GLU LEU GLU ARG PHE GLU GLY ILE TRP TRP
SEQRES 25 B 935 SER GLU SER LYS THR ARG LEU LEU TYR GLU HIS VAL ASN
SEQRES 26 B 935 GLU GLU LYS VAL ALA GLU SER GLN PHE GLY VAL ASN GLY
SEQRES 27 B 935 ASP PRO PRO VAL ALA PRO MET LYS TYR PRO ARG ALA GLY
SEQRES 28 B 935 THR LYS ASN ALA TYR SER THR LEU ARG MET VAL ILE LEU
SEQRES 29 B 935 GLU ASN GLY LYS ALA TYR ASP VAL PRO LEU LYS ASP GLU
SEQRES 30 B 935 VAL ILE TYR LYS HIS CYS PRO PHE TYR GLU TYR ILE THR
SEQRES 31 B 935 ARG ALA GLY PHE PHE SER ASP GLY THR THR VAL TRP VAL
SEQRES 32 B 935 GLN VAL MET SER ARG ASP GLN ALA GLN CYS SER LEU LEU
SEQRES 33 B 935 LEU ILE PRO TYR THR ASP PHE LEU LEU PRO GLU GLU LEU
SEQRES 34 B 935 GLY GLY SER ILE LYS GLU ASP ASN LEU GLN LEU SER THR
SEQRES 35 B 935 ASP LEU ASN MET GLY VAL TRP ASP ASP LYS SER HIS GLU
SEQRES 36 B 935 GLU THR MET GLU LYS PRO PRO ARG GLY LYS LEU ARG GLY
SEQRES 37 B 935 THR VAL GLN ILE HIS LYS ALA ARG ASN ASP TYR TRP ILE
SEQRES 38 B 935 ASN THR HIS ASN ALA ILE TYR PRO LEU LYS ILE THR ASP
SEQRES 39 B 935 GLU GLU HIS PRO MET TYR GLU PHE ILE TYR CYS LEU GLU
SEQRES 40 B 935 LYS PRO ASN GLY SER CYS LEU ALA LEU ILE SER ALA GLU
SEQRES 41 B 935 LEU ASP GLN ASN GLY TYR CYS ARG HIS THR GLU GLU LYS
SEQRES 42 B 935 LEU LEU MET ALA GLU ASN PHE SER ILE ASN LYS SER MET
SEQRES 43 B 935 GLY ILE VAL VAL ASP GLU VAL ARG GLU LEU VAL TYR TYR
SEQRES 44 B 935 VAL ALA ASN GLU SER HIS PRO THR GLU TRP ASN ILE CYS
SEQRES 45 B 935 VAL SER HIS TYR ARG THR GLY GLN HIS ALA GLN LEU THR
SEQRES 46 B 935 GLU SER GLY ILE CYS PHE LYS SER GLU ARG ALA ASN GLY
SEQRES 47 B 935 LYS LEU ALA LEU ASP LEU ASP HIS GLY PHE ALA CYS TYR
SEQRES 48 B 935 MET THR SER VAL GLY SER PRO ALA GLU CYS ARG PHE TYR
SEQRES 49 B 935 SER PHE ARG TRP LYS GLU ASN GLU VAL LEU PRO SER THR
SEQRES 50 B 935 VAL TYR ALA ALA ASN ILE THR VAL SER GLY HIS PRO GLY
SEQRES 51 B 935 GLN PRO ASP LEU HIS PHE ASP SER PRO GLU MET ILE GLU
SEQRES 52 B 935 PHE GLN SER LYS LYS THR GLY LEU MET HIS TYR ALA MET
SEQRES 53 B 935 ILE LEU ARG PRO SER ASN PHE ASP PRO TYR LYS LYS TYR
SEQRES 54 B 935 PRO VAL PHE HIS TYR VAL TYR GLY GLY PRO GLY ILE GLN
SEQRES 55 B 935 ILE VAL HIS ASN ASP PHE SER TRP ILE GLN TYR ILE ARG
SEQRES 56 B 935 PHE CYS ARG LEU GLY TYR VAL VAL VAL PHE ILE ASP ASN
SEQRES 57 B 935 ARG GLY SER ALA HIS ARG GLY ILE GLU PHE GLU ARG HIS
SEQRES 58 B 935 ILE HIS LYS LYS MET GLY THR VAL GLU VAL GLU ASP GLN
SEQRES 59 B 935 VAL GLU GLY LEU GLN MET LEU ALA GLU ARG THR GLY GLY
SEQRES 60 B 935 PHE MET ASP MET SER ARG VAL VAL VAL HIS GLY TRP SER
SEQRES 61 B 935 TYR GLY GLY TYR MET ALA LEU GLN MET ILE ALA LYS HIS
SEQRES 62 B 935 PRO ASN ILE TYR ARG ALA ALA ILE ALA GLY GLY ALA VAL
SEQRES 63 B 935 SER ASP TRP ARG LEU TYR ASP THR ALA TYR THR GLU ARG
SEQRES 64 B 935 TYR MET GLY TYR PRO LEU GLU GLU HIS VAL TYR GLY ALA
SEQRES 65 B 935 SER SER ILE THR GLY LEU VAL GLU LYS LEU PRO ASP GLU
SEQRES 66 B 935 PRO ASN ARG LEU MET LEU VAL HIS GLY LEU MET ASP GLU
SEQRES 67 B 935 ASN VAL HIS PHE ALA HIS LEU THR HIS LEU VAL ASP GLU
SEQRES 68 B 935 CYS ILE LYS LYS GLY LYS TRP HIS GLU LEU VAL ILE PHE
SEQRES 69 B 935 PRO ASN GLU ARG HIS GLY VAL ARG ASN ASN ASP ALA SER
SEQRES 70 B 935 ILE TYR LEU ASP ALA ARG MET MET TYR PHE ALA GLN GLN
SEQRES 71 B 935 ALA ILE GLN GLY PHE GLY PRO THR THR ALA ALA PRO ARG
SEQRES 72 B 935 GLN GLY PRO LEU TRP SER HIS PRO GLN PHE GLU LYS
HELIX 1 AA1 SER A 44 ARG A 60 1 17
HELIX 2 AA2 GLY A 61 THR A 63 5 3
HELIX 3 AA3 PRO A 102 LYS A 108 1 7
HELIX 4 AA4 SER A 301 GLU A 307 1 7
HELIX 5 AA5 ASP A 380 LYS A 385 1 6
HELIX 6 AA6 SER A 400 GLY A 402 5 3
HELIX 7 AA7 THR A 425 PHE A 427 5 3
HELIX 8 AA8 PHE A 712 GLN A 716 5 5
HELIX 9 AA9 TYR A 717 ARG A 722 1 6
HELIX 10 AB1 GLY A 739 ARG A 744 1 6
HELIX 11 AB2 HIS A 745 HIS A 747 5 3
HELIX 12 AB3 VAL A 753 THR A 769 1 17
HELIX 13 AB4 SER A 784 HIS A 797 1 14
HELIX 14 AB5 ASP A 812 TYR A 816 5 5
HELIX 15 AB6 ASP A 817 GLY A 826 1 10
HELIX 16 AB7 GLU A 830 SER A 837 1 8
HELIX 17 AB8 ILE A 839 LEU A 846 5 8
HELIX 18 AB9 HIS A 865 GLY A 880 1 16
HELIX 19 AC1 ASN A 897 GLN A 917 1 21
HELIX 20 AC2 SER B 44 ARG B 60 1 17
HELIX 21 AC3 GLY B 61 THR B 63 5 3
HELIX 22 AC4 PRO B 102 GLU B 107 1 6
HELIX 23 AC5 SER B 301 GLU B 307 1 7
HELIX 24 AC6 ASP B 380 LYS B 385 1 6
HELIX 25 AC7 SER B 400 GLY B 402 5 3
HELIX 26 AC8 THR B 425 PHE B 427 5 3
HELIX 27 AC9 PRO B 430 GLY B 434 5 5
HELIX 28 AD1 PHE B 712 GLN B 716 5 5
HELIX 29 AD2 TYR B 717 ARG B 722 1 6
HELIX 30 AD3 GLY B 739 ARG B 744 1 6
HELIX 31 AD4 HIS B 745 HIS B 747 5 3
HELIX 32 AD5 VAL B 753 THR B 769 1 17
HELIX 33 AD6 SER B 784 HIS B 797 1 14
HELIX 34 AD7 ASP B 812 TYR B 816 5 5
HELIX 35 AD8 ASP B 817 GLY B 826 1 10
HELIX 36 AD9 GLU B 830 SER B 837 1 8
HELIX 37 AE1 ILE B 839 LEU B 846 5 8
HELIX 38 AE2 HIS B 865 GLY B 880 1 16
HELIX 39 AE3 ASN B 897 GLN B 917 1 21
SHEET 1 AA1 5 GLU A 36 PRO A 37 0
SHEET 2 AA1 5 LYS A 691 VAL A 699 1 O LYS A 692 N GLU A 36
SHEET 3 AA1 5 VAL A 726 ILE A 730 1 O VAL A 726 N PHE A 696
SHEET 4 AA1 5 MET A 676 LEU A 682 -1 N LEU A 682 O VAL A 727
SHEET 5 AA1 5 GLU A 664 GLN A 669 -1 N PHE A 668 O HIS A 677
SHEET 1 AA2 6 GLU A 36 PRO A 37 0
SHEET 2 AA2 6 LYS A 691 VAL A 699 1 O LYS A 692 N GLU A 36
SHEET 3 AA2 6 MET A 773 TRP A 783 1 O VAL A 779 N HIS A 697
SHEET 4 AA2 6 ALA A 803 GLY A 807 1 O ILE A 805 N VAL A 780
SHEET 5 AA2 6 LEU A 853 GLY A 858 1 O MET A 854 N ALA A 806
SHEET 6 AA2 6 GLU A 884 PHE A 888 1 O GLU A 884 N LEU A 855
SHEET 1 AA3 8 ILE A 70 GLU A 76 0
SHEET 2 AA3 8 ARG A 79 SER A 87 -1 O TYR A 83 N SER A 71
SHEET 3 AA3 8 GLN A 94 ILE A 101 -1 O PHE A 97 N ALA A 84
SHEET 4 AA3 8 PHE A 116 SER A 122 -1 O LYS A 121 N SER A 98
SHEET 5 AA3 8 SER A 640 VAL A 649 1 O ASN A 646 N PHE A 116
SHEET 6 AA3 8 SER A 621 ARG A 631 -1 N PHE A 627 O ALA A 645
SHEET 7 AA3 8 GLY A 611 SER A 618 -1 N CYS A 614 O ARG A 626
SHEET 8 AA3 8 CYS A 594 LYS A 596 -1 N CYS A 594 O THR A 617
SHEET 1 AA4 8 ILE A 70 GLU A 76 0
SHEET 2 AA4 8 ARG A 79 SER A 87 -1 O TYR A 83 N SER A 71
SHEET 3 AA4 8 GLN A 94 ILE A 101 -1 O PHE A 97 N ALA A 84
SHEET 4 AA4 8 PHE A 116 SER A 122 -1 O LYS A 121 N SER A 98
SHEET 5 AA4 8 SER A 640 VAL A 649 1 O ASN A 646 N PHE A 116
SHEET 6 AA4 8 SER A 621 ARG A 631 -1 N PHE A 627 O ALA A 645
SHEET 7 AA4 8 GLY A 611 SER A 618 -1 N CYS A 614 O ARG A 626
SHEET 8 AA4 8 ALA A 605 ASP A 607 -1 N ASP A 607 O GLY A 611
SHEET 1 AA5 4 ALA A 258 VAL A 260 0
SHEET 2 AA5 4 LEU A 267 LEU A 272 -1 O ALA A 269 N LYS A 259
SHEET 3 AA5 4 GLN A 275 LYS A 280 -1 O TYR A 277 N TYR A 270
SHEET 4 AA5 4 LYS A 283 ARG A 287 -1 O LYS A 283 N LYS A 280
SHEET 1 AA6 3 ILE A 295 ASN A 297 0
SHEET 2 AA6 3 ARG A 322 ASN A 329 -1 O VAL A 328 N THR A 296
SHEET 3 AA6 3 ILE A 314 TRP A 316 -1 N TRP A 315 O LEU A 324
SHEET 1 AA7 4 ILE A 295 ASN A 297 0
SHEET 2 AA7 4 ARG A 322 ASN A 329 -1 O VAL A 328 N THR A 296
SHEET 3 AA7 4 TYR A 360 GLU A 369 -1 O THR A 362 N HIS A 327
SHEET 4 AA7 4 LYS A 372 PRO A 377 -1 O VAL A 376 N MET A 365
SHEET 1 AA8 2 GLU A 335 SER A 336 0
SHEET 2 AA8 2 MET A 349 LYS A 350 -1 O MET A 349 N SER A 336
SHEET 1 AA9 4 TYR A 390 PHE A 398 0
SHEET 2 AA9 4 THR A 404 SER A 411 -1 O GLN A 408 N THR A 394
SHEET 3 AA9 4 GLN A 416 PRO A 423 -1 O ILE A 422 N VAL A 405
SHEET 4 AA9 4 VAL A 474 ARG A 480 -1 O ALA A 479 N CYS A 417
SHEET 1 AB1 4 TYR A 492 PRO A 493 0
SHEET 2 AB1 4 TYR A 504 GLU A 511 -1 O ILE A 507 N TYR A 492
SHEET 3 AB1 4 SER A 516 LEU A 525 -1 O ILE A 521 N PHE A 506
SHEET 4 AB1 4 CYS A 531 THR A 534 -1 O ARG A 532 N GLU A 524
SHEET 1 AB2 4 TYR A 492 PRO A 493 0
SHEET 2 AB2 4 TYR A 504 GLU A 511 -1 O ILE A 507 N TYR A 492
SHEET 3 AB2 4 SER A 516 LEU A 525 -1 O ILE A 521 N PHE A 506
SHEET 4 AB2 4 LYS A 537 LEU A 538 -1 O LYS A 537 N LEU A 520
SHEET 1 AB3 4 VAL A 553 VAL A 554 0
SHEET 2 AB3 4 LEU A 560 HIS A 569 -1 O TYR A 562 N VAL A 553
SHEET 3 AB3 4 GLU A 572 HIS A 579 -1 O CYS A 576 N TYR A 563
SHEET 4 AB3 4 HIS A 585 GLN A 587 -1 O ALA A 586 N VAL A 577
SHEET 1 AB4 5 GLU B 36 PRO B 37 0
SHEET 2 AB4 5 LYS B 691 VAL B 699 1 O LYS B 692 N GLU B 36
SHEET 3 AB4 5 VAL B 726 ILE B 730 1 O VAL B 726 N PHE B 696
SHEET 4 AB4 5 MET B 676 LEU B 682 -1 N LEU B 682 O VAL B 727
SHEET 5 AB4 5 GLU B 664 GLN B 669 -1 N PHE B 668 O HIS B 677
SHEET 1 AB5 6 GLU B 36 PRO B 37 0
SHEET 2 AB5 6 LYS B 691 VAL B 699 1 O LYS B 692 N GLU B 36
SHEET 3 AB5 6 MET B 773 TRP B 783 1 O VAL B 779 N HIS B 697
SHEET 4 AB5 6 ALA B 803 GLY B 807 1 O ILE B 805 N VAL B 780
SHEET 5 AB5 6 LEU B 853 GLY B 858 1 O MET B 854 N ALA B 806
SHEET 6 AB5 6 GLU B 884 PHE B 888 1 O GLU B 884 N LEU B 855
SHEET 1 AB6 8 ILE B 70 GLU B 76 0
SHEET 2 AB6 8 ARG B 79 SER B 87 -1 O TYR B 83 N SER B 71
SHEET 3 AB6 8 GLN B 94 ILE B 101 -1 O PHE B 97 N ALA B 84
SHEET 4 AB6 8 PHE B 116 SER B 122 -1 O LYS B 121 N SER B 98
SHEET 5 AB6 8 SER B 640 VAL B 649 1 O THR B 648 N LEU B 120
SHEET 6 AB6 8 SER B 621 ARG B 631 -1 N PHE B 627 O ALA B 645
SHEET 7 AB6 8 GLY B 611 SER B 618 -1 N CYS B 614 O ARG B 626
SHEET 8 AB6 8 CYS B 594 LYS B 596 -1 N CYS B 594 O THR B 617
SHEET 1 AB7 8 ILE B 70 GLU B 76 0
SHEET 2 AB7 8 ARG B 79 SER B 87 -1 O TYR B 83 N SER B 71
SHEET 3 AB7 8 GLN B 94 ILE B 101 -1 O PHE B 97 N ALA B 84
SHEET 4 AB7 8 PHE B 116 SER B 122 -1 O LYS B 121 N SER B 98
SHEET 5 AB7 8 SER B 640 VAL B 649 1 O THR B 648 N LEU B 120
SHEET 6 AB7 8 SER B 621 ARG B 631 -1 N PHE B 627 O ALA B 645
SHEET 7 AB7 8 GLY B 611 SER B 618 -1 N CYS B 614 O ARG B 626
SHEET 8 AB7 8 ALA B 605 ASP B 607 -1 N ASP B 607 O GLY B 611
SHEET 1 AB8 4 ALA B 258 VAL B 260 0
SHEET 2 AB8 4 LEU B 267 LEU B 272 -1 O ALA B 269 N LYS B 259
SHEET 3 AB8 4 GLN B 275 LYS B 280 -1 O TYR B 277 N TYR B 270
SHEET 4 AB8 4 LYS B 283 ARG B 287 -1 O LYS B 283 N LYS B 280
SHEET 1 AB9 3 ILE B 295 ASN B 297 0
SHEET 2 AB9 3 ARG B 322 ASN B 329 -1 O VAL B 328 N THR B 296
SHEET 3 AB9 3 ILE B 314 TRP B 316 -1 N TRP B 315 O LEU B 324
SHEET 1 AC1 4 ILE B 295 ASN B 297 0
SHEET 2 AC1 4 ARG B 322 ASN B 329 -1 O VAL B 328 N THR B 296
SHEET 3 AC1 4 TYR B 360 GLU B 369 -1 O THR B 362 N HIS B 327
SHEET 4 AC1 4 LYS B 372 PRO B 377 -1 O VAL B 376 N MET B 365
SHEET 1 AC2 2 GLU B 335 SER B 336 0
SHEET 2 AC2 2 MET B 349 LYS B 350 -1 O MET B 349 N SER B 336
SHEET 1 AC3 4 TYR B 390 PHE B 398 0
SHEET 2 AC3 4 THR B 404 SER B 411 -1 O GLN B 408 N THR B 394
SHEET 3 AC3 4 GLN B 416 PRO B 423 -1 O ILE B 422 N VAL B 405
SHEET 4 AC3 4 VAL B 474 ARG B 480 -1 O ALA B 479 N CYS B 417
SHEET 1 AC4 4 TYR B 492 PRO B 493 0
SHEET 2 AC4 4 TYR B 504 GLU B 511 -1 O ILE B 507 N TYR B 492
SHEET 3 AC4 4 SER B 516 LEU B 525 -1 O ILE B 521 N PHE B 506
SHEET 4 AC4 4 CYS B 531 THR B 534 -1 O ARG B 532 N GLU B 524
SHEET 1 AC5 4 TYR B 492 PRO B 493 0
SHEET 2 AC5 4 TYR B 504 GLU B 511 -1 O ILE B 507 N TYR B 492
SHEET 3 AC5 4 SER B 516 LEU B 525 -1 O ILE B 521 N PHE B 506
SHEET 4 AC5 4 LYS B 537 LEU B 538 -1 O LYS B 537 N LEU B 520
SHEET 1 AC6 4 VAL B 553 VAL B 554 0
SHEET 2 AC6 4 LEU B 560 HIS B 569 -1 O TYR B 562 N VAL B 553
SHEET 3 AC6 4 GLU B 572 HIS B 579 -1 O CYS B 576 N TYR B 563
SHEET 4 AC6 4 HIS B 585 GLN B 587 -1 O ALA B 586 N VAL B 577
CISPEP 1 TYR A 827 PRO A 828 0 5.43
CISPEP 2 TYR B 827 PRO B 828 0 5.48
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
TER 11483 GLY A 918
TER 22966 GLY B 918
MASTER 591 0 0 39 112 0 0 611632 2 0 144
END |