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HEADER HYDROLASE 08-OCT-21 7PX8
TITLE CRYOEM STRUCTURE OF MAMMALIAN ACYLAMINOACYL-PEPTIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYLAMINO-ACID-RELEASING ENZYME;
COMPND 3 CHAIN: A, B, C, D
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA DOMESTICUS;
SOURCE 3 ORGANISM_COMMON: DOMESTIC PIG;
SOURCE 4 ORGANISM_TAXID: 9825
KEYWDS ACYLAMINOACYL-PEPTIDASE, TETRAMER, ACLYPEPTIDE-HYDROLASE, OXIDIZED
KEYWDS 2 PROTEIN HYDROLASE, SERINE-PROTEASE, HYDROLASE
EXPDTA ELECTRON MICROSCOPY
AUTHOR A.J.KISS-SZEMAN,V.HARMAT,D.K.MENYHARD,P.STRANER,I.JAKLI,N.HOSOGI,
AUTHOR 2 A.PERCZEL
REVDAT 1 25-MAY-22 7PX8 0
JRNL AUTH A.J.KISS-SZEMAN,P.STRANER,I.JAKLI,N.HOSOGI,V.HARMAT,
JRNL AUTH 2 D.K.MENYHARD,A.PERCZEL
JRNL TITL CRYO-EM STRUCTURE OF ACYLPEPTIDE HYDROLASE REVEALS SUBSTRATE
JRNL TITL 2 SELECTION BY MULTIMERIZATION AND A MULTI-STATE
JRNL TITL 3 SERINE-PROTEASE TRIAD
JRNL REF CHEM SCI 2022
JRNL REFN ESSN 2041-6539
JRNL DOI 10.1039/D2SC02276A
REMARK 2
REMARK 2 RESOLUTION. 3.27 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : JADAS, CTFFIND
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) : 3.270
REMARK 3 NUMBER OF PARTICLES : 50604
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING ONLY
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 7PX8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-OCT-21.
REMARK 100 THE DEPOSITION ID IS D_1292118571.
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 : HOMOTETRAMER OF ACYLAMINOACYL
REMARK 245 -PEPTIDASE
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 6.00
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 : 1157
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : JEOL CRYO ARM 300
REMARK 245 DETECTOR TYPE : GATAN K3 (6K 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 : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4000.00
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 GLU A 2
REMARK 465 ARG A 3
REMARK 465 GLN A 4
REMARK 465 VAL A 5
REMARK 465 LEU A 6
REMARK 465 LEU A 7
REMARK 465 SER A 8
REMARK 465 GLY A 110
REMARK 465 GLY A 111
REMARK 465 THR A 112
REMARK 465 GLY A 113
REMARK 465 THR A 114
REMARK 465 ALA A 115
REMARK 465 ASP A 183
REMARK 465 VAL A 184
REMARK 465 THR A 185
REMARK 465 GLY A 186
REMARK 465 SER A 187
REMARK 465 ASP A 188
REMARK 465 ASP A 189
REMARK 465 GLU A 190
REMARK 465 MET A 191
REMARK 465 ALA A 192
REMARK 465 ARG A 193
REMARK 465 THR A 194
REMARK 465 LYS A 195
REMARK 465 LYS A 196
REMARK 465 PRO A 197
REMARK 465 ASP A 198
REMARK 465 GLU A 496
REMARK 465 LYS A 497
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 ARG B 3
REMARK 465 GLN B 4
REMARK 465 VAL B 5
REMARK 465 LEU B 6
REMARK 465 LEU B 7
REMARK 465 SER B 8
REMARK 465 GLY B 110
REMARK 465 GLY B 111
REMARK 465 THR B 112
REMARK 465 GLY B 113
REMARK 465 THR B 114
REMARK 465 ALA B 115
REMARK 465 ASP B 183
REMARK 465 VAL B 184
REMARK 465 THR B 185
REMARK 465 GLY B 186
REMARK 465 SER B 187
REMARK 465 ASP B 188
REMARK 465 ASP B 189
REMARK 465 GLU B 190
REMARK 465 MET B 191
REMARK 465 ALA B 192
REMARK 465 ARG B 193
REMARK 465 THR B 194
REMARK 465 LYS B 195
REMARK 465 LYS B 196
REMARK 465 PRO B 197
REMARK 465 ASP B 198
REMARK 465 GLU B 496
REMARK 465 LYS B 497
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 ARG C 3
REMARK 465 GLN C 4
REMARK 465 VAL C 5
REMARK 465 LEU C 6
REMARK 465 LEU C 7
REMARK 465 SER C 8
REMARK 465 TYR C 39
REMARK 465 GLY C 110
REMARK 465 GLY C 111
REMARK 465 THR C 112
REMARK 465 GLY C 113
REMARK 465 THR C 114
REMARK 465 ALA C 115
REMARK 465 ASP C 183
REMARK 465 VAL C 184
REMARK 465 THR C 185
REMARK 465 GLY C 186
REMARK 465 SER C 187
REMARK 465 ASP C 188
REMARK 465 ASP C 189
REMARK 465 GLU C 190
REMARK 465 MET C 191
REMARK 465 ALA C 192
REMARK 465 ARG C 193
REMARK 465 THR C 194
REMARK 465 LYS C 195
REMARK 465 LYS C 196
REMARK 465 PRO C 197
REMARK 465 ASP C 198
REMARK 465 GLU C 496
REMARK 465 LYS C 497
REMARK 465 MET D 1
REMARK 465 GLU D 2
REMARK 465 ARG D 3
REMARK 465 GLN D 4
REMARK 465 VAL D 5
REMARK 465 LEU D 6
REMARK 465 LEU D 7
REMARK 465 SER D 8
REMARK 465 TYR D 39
REMARK 465 GLY D 110
REMARK 465 GLY D 111
REMARK 465 THR D 112
REMARK 465 GLY D 113
REMARK 465 THR D 114
REMARK 465 ALA D 115
REMARK 465 ASP D 183
REMARK 465 VAL D 184
REMARK 465 THR D 185
REMARK 465 GLY D 186
REMARK 465 SER D 187
REMARK 465 ASP D 188
REMARK 465 ASP D 189
REMARK 465 GLU D 190
REMARK 465 MET D 191
REMARK 465 ALA D 192
REMARK 465 ARG D 193
REMARK 465 THR D 194
REMARK 465 LYS D 195
REMARK 465 LYS D 196
REMARK 465 PRO D 197
REMARK 465 ASP D 198
REMARK 465 GLU D 496
REMARK 465 LYS D 497
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 GLU A 9 CG CD OE1 OE2
REMARK 470 GLU A 11 CG CD OE1 OE2
REMARK 470 GLU A 12 CG CD OE1 OE2
REMARK 470 GLN A 38 CG CD OE1 NE2
REMARK 470 TYR A 39 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 49 CG CD OE1 OE2
REMARK 470 GLU A 59 CG CD OE1 OE2
REMARK 470 ASP A 72 CG OD1 OD2
REMARK 470 ASP A 74 CG OD1 OD2
REMARK 470 ARG A 89 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 116 CG CD OE1 OE2
REMARK 470 GLU A 117 CG CD OE1 OE2
REMARK 470 LYS A 131 NZ
REMARK 470 GLU A 139 CG CD OE1 OE2
REMARK 470 ASP A 148 CG OD1 OD2
REMARK 470 SER A 158 OG
REMARK 470 THR A 160 OG1 CG2
REMARK 470 LYS A 172 CG CD CE NZ
REMARK 470 GLU A 174 CG CD OE1 OE2
REMARK 470 GLN A 178 CD OE1 NE2
REMARK 470 LYS A 180 NZ
REMARK 470 LEU A 182 CG CD1 CD2
REMARK 470 GLN A 199 CG CD OE1 NE2
REMARK 470 ASN A 215 CG OD1 ND2
REMARK 470 GLU A 230 CG CD OE1 OE2
REMARK 470 GLU A 238 CG CD OE1 OE2
REMARK 470 GLU A 242 CG CD OE1 OE2
REMARK 470 LYS A 291 CD CE NZ
REMARK 470 ASP A 297 CG OD1 OD2
REMARK 470 GLU A 298 CG CD OE1 OE2
REMARK 470 SER A 299 OG
REMARK 470 GLN A 351 CD OE1 NE2
REMARK 470 GLU A 354 CG CD OE1 OE2
REMARK 470 ASP A 372 CG OD1 OD2
REMARK 470 GLN A 394 CG CD OE1 NE2
REMARK 470 MET A 395 CG SD CE
REMARK 470 LYS A 411 NZ
REMARK 470 ASP A 416 CG OD1 OD2
REMARK 470 LYS A 443 CG CD CE NZ
REMARK 470 GLU A 456 CG CD OE1 OE2
REMARK 470 GLN A 473 CG CD OE1 NE2
REMARK 470 VAL A 477 CG1 CG2
REMARK 470 THR A 498 OG1 CG2
REMARK 470 GLN A 499 CG CD OE1 NE2
REMARK 470 GLU A 573 CG CD OE1 OE2
REMARK 470 GLU A 574 CG CD OE1 OE2
REMARK 470 HIS A 575 CG ND1 CD2 CE1 NE2
REMARK 470 ASP A 577 CG OD1 OD2
REMARK 470 SER A 622 OG
REMARK 470 SER A 636 OG
REMARK 470 ASP A 640 CG OD1 OD2
REMARK 470 LEU A 642 CG CD1 CD2
REMARK 470 ASP A 653 CG OD1 OD2
REMARK 470 LYS A 664 NZ
REMARK 470 GLU A 674 CG CD OE1 OE2
REMARK 470 GLU A 685 CG CD OE1 OE2
REMARK 470 ASN A 694 CG OD1 ND2
REMARK 470 LYS A 704 CE NZ
REMARK 470 SER A 710 OG
REMARK 470 GLU A 711 CD OE1 OE2
REMARK 470 GLU A 713 CG CD OE1 OE2
REMARK 470 GLU B 9 CG CD OE1 OE2
REMARK 470 GLU B 11 CG CD OE1 OE2
REMARK 470 GLU B 12 CG CD OE1 OE2
REMARK 470 GLN B 38 CG CD OE1 NE2
REMARK 470 TYR B 39 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 59 CG CD OE1 OE2
REMARK 470 ASP B 72 CG OD1 OD2
REMARK 470 ASP B 74 CG OD1 OD2
REMARK 470 ARG B 89 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 116 CG CD OE1 OE2
REMARK 470 LYS B 131 NZ
REMARK 470 GLU B 139 CG CD OE1 OE2
REMARK 470 ASP B 148 CG OD1 OD2
REMARK 470 SER B 158 OG
REMARK 470 THR B 160 OG1 CG2
REMARK 470 LYS B 172 CG CD CE NZ
REMARK 470 GLU B 174 CD OE1 OE2
REMARK 470 GLN B 178 CD OE1 NE2
REMARK 470 LYS B 180 CG CD CE NZ
REMARK 470 LEU B 182 CG CD1 CD2
REMARK 470 GLN B 199 CG CD OE1 NE2
REMARK 470 ASN B 215 CG OD1 ND2
REMARK 470 GLU B 230 CG CD OE1 OE2
REMARK 470 GLU B 238 CG CD OE1 OE2
REMARK 470 GLU B 242 CG CD OE1 OE2
REMARK 470 LYS B 291 CE NZ
REMARK 470 ASP B 297 CG OD1 OD2
REMARK 470 GLU B 298 CG CD OE1 OE2
REMARK 470 SER B 299 OG
REMARK 470 GLN B 351 CG CD OE1 NE2
REMARK 470 GLU B 354 CG CD OE1 OE2
REMARK 470 ASP B 372 CG OD1 OD2
REMARK 470 GLN B 394 CG CD OE1 NE2
REMARK 470 MET B 395 CG SD CE
REMARK 470 SER B 397 OG
REMARK 470 LYS B 411 NZ
REMARK 470 ASP B 416 CG OD1 OD2
REMARK 470 LYS B 443 CG CD CE NZ
REMARK 470 GLU B 456 CG CD OE1 OE2
REMARK 470 GLN B 473 CG CD OE1 NE2
REMARK 470 VAL B 477 CG1 CG2
REMARK 470 THR B 498 OG1 CG2
REMARK 470 GLN B 499 CG CD OE1 NE2
REMARK 470 GLU B 573 CG CD OE1 OE2
REMARK 470 GLU B 574 CG CD OE1 OE2
REMARK 470 ASP B 577 CG OD1 OD2
REMARK 470 SER B 622 OG
REMARK 470 SER B 636 OG
REMARK 470 ASP B 640 CG OD1 OD2
REMARK 470 ASP B 653 CG OD1 OD2
REMARK 470 LYS B 664 NZ
REMARK 470 GLU B 674 CG CD OE1 OE2
REMARK 470 GLU B 685 CG CD OE1 OE2
REMARK 470 LYS B 704 CE NZ
REMARK 470 SER B 710 OG
REMARK 470 GLU B 711 CD OE1 OE2
REMARK 470 GLU B 713 CG CD OE1 OE2
REMARK 470 SER B 732 OG
REMARK 470 GLU C 9 CG CD OE1 OE2
REMARK 470 GLU C 11 CG CD OE1 OE2
REMARK 470 GLU C 12 CG CD OE1 OE2
REMARK 470 GLN C 38 CG CD OE1 NE2
REMARK 470 GLU C 59 CG CD OE1 OE2
REMARK 470 ASP C 72 CG OD1 OD2
REMARK 470 ASP C 74 CG OD1 OD2
REMARK 470 ARG C 89 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 116 CG CD OE1 OE2
REMARK 470 LYS C 131 NZ
REMARK 470 GLU C 139 CG CD OE1 OE2
REMARK 470 ASP C 148 CG OD1 OD2
REMARK 470 SER C 158 OG
REMARK 470 THR C 160 OG1 CG2
REMARK 470 LYS C 172 CG CD CE NZ
REMARK 470 GLN C 178 CD OE1 NE2
REMARK 470 LYS C 180 NZ
REMARK 470 LEU C 182 CG CD1 CD2
REMARK 470 GLN C 199 CG CD OE1 NE2
REMARK 470 ASN C 215 CG OD1 ND2
REMARK 470 SER C 218 OG
REMARK 470 GLU C 230 CG CD OE1 OE2
REMARK 470 GLU C 238 CG CD OE1 OE2
REMARK 470 GLU C 242 CG CD OE1 OE2
REMARK 470 THR C 288 OG1 CG2
REMARK 470 LYS C 291 CE NZ
REMARK 470 ASP C 297 CG OD1 OD2
REMARK 470 GLU C 298 CG CD OE1 OE2
REMARK 470 SER C 299 OG
REMARK 470 GLN C 351 CG CD OE1 NE2
REMARK 470 GLU C 354 CG CD OE1 OE2
REMARK 470 ASP C 372 CG OD1 OD2
REMARK 470 GLN C 394 CG CD OE1 NE2
REMARK 470 MET C 395 CG SD CE
REMARK 470 LYS C 411 NZ
REMARK 470 ASP C 416 CG OD1 OD2
REMARK 470 LYS C 443 CG CD CE NZ
REMARK 470 GLU C 456 CG CD OE1 OE2
REMARK 470 GLN C 473 CG CD OE1 NE2
REMARK 470 VAL C 477 CG1 CG2
REMARK 470 THR C 498 OG1 CG2
REMARK 470 GLN C 499 CG CD OE1 NE2
REMARK 470 GLU C 573 CG CD OE1 OE2
REMARK 470 GLU C 574 CG CD OE1 OE2
REMARK 470 ASP C 577 CG OD1 OD2
REMARK 470 SER C 622 OG
REMARK 470 SER C 636 OG
REMARK 470 ASP C 640 CG OD1 OD2
REMARK 470 ASP C 653 CG OD1 OD2
REMARK 470 LYS C 664 NZ
REMARK 470 GLU C 674 CG CD OE1 OE2
REMARK 470 GLU C 685 CG CD OE1 OE2
REMARK 470 LYS C 704 CE NZ
REMARK 470 SER C 710 OG
REMARK 470 GLU C 711 CD OE1 OE2
REMARK 470 GLU C 713 CG CD OE1 OE2
REMARK 470 GLU D 9 CG CD OE1 OE2
REMARK 470 GLU D 11 CG CD OE1 OE2
REMARK 470 GLU D 12 CG CD OE1 OE2
REMARK 470 GLN D 38 CG CD OE1 NE2
REMARK 470 GLU D 59 CG CD OE1 OE2
REMARK 470 ASP D 72 CG OD1 OD2
REMARK 470 ASP D 74 CG OD1 OD2
REMARK 470 ARG D 89 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 116 CG CD OE1 OE2
REMARK 470 GLU D 117 CG CD OE1 OE2
REMARK 470 LYS D 131 NZ
REMARK 470 GLU D 139 CG CD OE1 OE2
REMARK 470 ASP D 148 CG OD1 OD2
REMARK 470 SER D 158 OG
REMARK 470 THR D 160 OG1 CG2
REMARK 470 LYS D 172 CG CD CE NZ
REMARK 470 GLN D 178 CD OE1 NE2
REMARK 470 LYS D 180 NZ
REMARK 470 LEU D 182 CG CD1 CD2
REMARK 470 GLN D 199 CG CD OE1 NE2
REMARK 470 ASN D 215 CG OD1 ND2
REMARK 470 GLU D 230 CG CD OE1 OE2
REMARK 470 GLU D 238 CG CD OE1 OE2
REMARK 470 GLU D 242 CG CD OE1 OE2
REMARK 470 LYS D 291 CE NZ
REMARK 470 ASP D 297 CG OD1 OD2
REMARK 470 GLU D 298 CG CD OE1 OE2
REMARK 470 SER D 299 OG
REMARK 470 GLN D 351 CD OE1 NE2
REMARK 470 GLU D 354 CG CD OE1 OE2
REMARK 470 ASP D 372 CG OD1 OD2
REMARK 470 GLN D 394 CG CD OE1 NE2
REMARK 470 MET D 395 CG SD CE
REMARK 470 LYS D 411 NZ
REMARK 470 LYS D 443 CG CD CE NZ
REMARK 470 GLU D 456 CG CD OE1 OE2
REMARK 470 GLN D 473 CG CD OE1 NE2
REMARK 470 VAL D 477 CG1 CG2
REMARK 470 ASN D 493 CG OD1 ND2
REMARK 470 THR D 498 OG1 CG2
REMARK 470 GLN D 499 CG CD OE1 NE2
REMARK 470 GLU D 574 CG CD OE1 OE2
REMARK 470 ASP D 577 CG OD1 OD2
REMARK 470 SER D 622 OG
REMARK 470 SER D 636 OG
REMARK 470 SER D 638 OG
REMARK 470 ASP D 640 CG OD1 OD2
REMARK 470 ASP D 653 CG OD1 OD2
REMARK 470 LYS D 664 NZ
REMARK 470 GLU D 674 CG CD OE1 OE2
REMARK 470 GLU D 685 CG CD OE1 OE2
REMARK 470 LYS D 704 CE NZ
REMARK 470 SER D 710 OG
REMARK 470 GLU D 711 CD OE1 OE2
REMARK 470 GLU D 713 CG CD OE1 OE2
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 LYS A 126 -125.22 60.06
REMARK 500 SER A 304 70.43 52.29
REMARK 500 ARG A 383 -119.35 62.81
REMARK 500 SER A 587 -103.19 57.45
REMARK 500 LYS B 126 -125.26 60.39
REMARK 500 SER B 304 71.08 58.89
REMARK 500 VAL B 344 -60.46 -96.74
REMARK 500 GLN B 351 116.86 -161.99
REMARK 500 GLN B 474 50.49 -93.86
REMARK 500 SER B 587 -100.98 62.71
REMARK 500 SER B 622 78.93 -101.68
REMARK 500 LYS C 126 -124.76 60.16
REMARK 500 ASN C 277 57.03 -94.00
REMARK 500 SER C 304 70.86 56.15
REMARK 500 ARG C 383 -121.18 63.05
REMARK 500 ASP C 418 -1.23 70.02
REMARK 500 SER C 587 -15.76 70.78
REMARK 500 HIS C 588 -25.28 -141.56
REMARK 500 LYS D 126 -120.36 55.67
REMARK 500 ASN D 277 57.23 -94.26
REMARK 500 SER D 304 71.02 58.33
REMARK 500 VAL D 344 -60.23 -97.16
REMARK 500 ARG D 383 -119.25 63.36
REMARK 500 GLU D 574 59.48 -92.02
REMARK 500 SER D 587 -100.66 58.90
REMARK 500 SER D 587 -61.83 -103.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-13691 RELATED DB: EMDB
REMARK 900 CRYOEM STRUCTURE OF MAMMALIAN ACYLAMINOACYL-PEPTIDASE
DBREF 7PX8 A 1 732 UNP P19205 ACPH_PIG 1 732
DBREF 7PX8 B 1 732 UNP P19205 ACPH_PIG 1 732
DBREF 7PX8 C 1 732 UNP P19205 ACPH_PIG 1 732
DBREF 7PX8 D 1 732 UNP P19205 ACPH_PIG 1 732
SEQRES 1 A 732 MET GLU ARG GLN VAL LEU LEU SER GLU PRO GLU GLU ALA
SEQRES 2 A 732 ALA ALA LEU TYR ARG GLY LEU SER ARG GLN PRO ALA LEU
SEQRES 3 A 732 SER ALA ALA CYS LEU GLY PRO GLU VAL THR THR GLN TYR
SEQRES 4 A 732 GLY GLY ARG TYR ARG THR VAL HIS THR GLU TRP THR GLN
SEQRES 5 A 732 ARG ASP LEU GLU ARG MET GLU ASN ILE ARG PHE CYS ARG
SEQRES 6 A 732 GLN TYR LEU VAL PHE HIS ASP GLY ASP SER VAL VAL PHE
SEQRES 7 A 732 ALA GLY PRO ALA GLY ASN SER VAL GLU THR ARG GLY GLU
SEQRES 8 A 732 LEU LEU SER ARG GLU SER PRO SER GLY THR MET LYS ALA
SEQRES 9 A 732 VAL LEU ARG LYS ALA GLY GLY THR GLY THR ALA GLU GLU
SEQRES 10 A 732 LYS GLN PHE LEU GLU VAL TRP GLU LYS ASN ARG LYS LEU
SEQRES 11 A 732 LYS SER PHE ASN LEU SER ALA LEU GLU LYS HIS GLY PRO
SEQRES 12 A 732 VAL TYR GLU ASP ASP CYS PHE GLY CYS LEU SER TRP SER
SEQRES 13 A 732 HIS SER GLU THR HIS LEU LEU TYR VAL ALA ASP LYS LYS
SEQRES 14 A 732 ARG PRO LYS ALA GLU SER PHE PHE GLN THR LYS ALA LEU
SEQRES 15 A 732 ASP VAL THR GLY SER ASP ASP GLU MET ALA ARG THR LYS
SEQRES 16 A 732 LYS PRO ASP GLN ALA ILE LYS GLY ASP GLN PHE LEU PHE
SEQRES 17 A 732 TYR GLU ASP TRP GLY GLU ASN MET VAL SER LYS SER THR
SEQRES 18 A 732 PRO VAL LEU CYS VAL LEU ASP ILE GLU SER GLY ASN ILE
SEQRES 19 A 732 SER VAL LEU GLU GLY VAL PRO GLU SER VAL SER PRO GLY
SEQRES 20 A 732 GLN ALA PHE TRP ALA PRO GLY ASP THR GLY VAL VAL PHE
SEQRES 21 A 732 VAL GLY TRP TRP HIS GLU PRO PHE ARG LEU GLY ILE ARG
SEQRES 22 A 732 PHE CYS THR ASN ARG ARG SER ALA LEU TYR TYR VAL ASP
SEQRES 23 A 732 LEU THR GLY GLY LYS CYS GLU LEU LEU SER ASP GLU SER
SEQRES 24 A 732 VAL ALA VAL THR SER PRO ARG LEU SER PRO ASP GLN CYS
SEQRES 25 A 732 ARG ILE VAL TYR LEU ARG PHE PRO SER LEU VAL PRO HIS
SEQRES 26 A 732 GLN GLN CYS GLY GLN LEU CYS LEU TYR ASP TRP TYR THR
SEQRES 27 A 732 ARG VAL THR SER VAL VAL VAL ASP ILE VAL PRO ARG GLN
SEQRES 28 A 732 LEU GLY GLU ASP PHE SER GLY ILE TYR CYS SER LEU LEU
SEQRES 29 A 732 PRO LEU GLY CYS TRP SER ALA ASP SER GLN ARG VAL VAL
SEQRES 30 A 732 PHE ASP SER PRO GLN ARG SER ARG GLN ASP LEU PHE ALA
SEQRES 31 A 732 VAL ASP THR GLN MET GLY SER VAL THR SER LEU THR ALA
SEQRES 32 A 732 GLY GLY SER GLY GLY SER TRP LYS LEU LEU THR ILE ASP
SEQRES 33 A 732 ARG ASP LEU MET VAL VAL GLN PHE SER THR PRO SER VAL
SEQRES 34 A 732 PRO PRO SER LEU LYS VAL GLY PHE LEU PRO PRO ALA GLY
SEQRES 35 A 732 LYS GLU GLN ALA VAL SER TRP VAL SER LEU GLU GLU ALA
SEQRES 36 A 732 GLU PRO PHE PRO ASP ILE SER TRP SER ILE ARG VAL LEU
SEQRES 37 A 732 GLN PRO PRO PRO GLN GLN GLU HIS VAL GLN TYR ALA GLY
SEQRES 38 A 732 LEU ASP PHE GLU ALA ILE LEU LEU GLN PRO SER ASN SER
SEQRES 39 A 732 PRO GLU LYS THR GLN VAL PRO MET VAL VAL MET PRO HIS
SEQRES 40 A 732 GLY GLY PRO HIS SER SER PHE VAL THR ALA TRP MET LEU
SEQRES 41 A 732 PHE PRO ALA MET LEU CYS LYS MET GLY PHE ALA VAL LEU
SEQRES 42 A 732 LEU VAL ASN TYR ARG GLY SER THR GLY PHE GLY GLN ASP
SEQRES 43 A 732 SER ILE LEU SER LEU PRO GLY ASN VAL GLY HIS GLN ASP
SEQRES 44 A 732 VAL LYS ASP VAL GLN PHE ALA VAL GLU GLN VAL LEU GLN
SEQRES 45 A 732 GLU GLU HIS PHE ASP ALA GLY ARG VAL ALA LEU MET GLY
SEQRES 46 A 732 GLY SER HIS GLY GLY PHE LEU SER CYS HIS LEU ILE GLY
SEQRES 47 A 732 GLN TYR PRO GLU THR TYR SER ALA CYS VAL VAL ARG ASN
SEQRES 48 A 732 PRO VAL ILE ASN ILE ALA SER MET MET GLY SER THR ASP
SEQRES 49 A 732 ILE PRO ASP TRP CYS MET VAL GLU ALA GLY PHE SER TYR
SEQRES 50 A 732 SER SER ASP CYS LEU PRO ASP LEU SER VAL TRP ALA ALA
SEQRES 51 A 732 MET LEU ASP LYS SER PRO ILE LYS TYR ALA PRO GLN VAL
SEQRES 52 A 732 LYS THR PRO LEU LEU LEU MET LEU GLY GLN GLU ASP ARG
SEQRES 53 A 732 ARG VAL PRO PHE LYS GLN GLY MET GLU TYR TYR ARG VAL
SEQRES 54 A 732 LEU LYS ALA ARG ASN VAL PRO VAL ARG LEU LEU LEU TYR
SEQRES 55 A 732 PRO LYS SER THR HIS ALA LEU SER GLU VAL GLU VAL GLU
SEQRES 56 A 732 SER ASP SER PHE MET ASN ALA VAL LEU TRP LEU CYS THR
SEQRES 57 A 732 HIS LEU GLY SER
SEQRES 1 B 732 MET GLU ARG GLN VAL LEU LEU SER GLU PRO GLU GLU ALA
SEQRES 2 B 732 ALA ALA LEU TYR ARG GLY LEU SER ARG GLN PRO ALA LEU
SEQRES 3 B 732 SER ALA ALA CYS LEU GLY PRO GLU VAL THR THR GLN TYR
SEQRES 4 B 732 GLY GLY ARG TYR ARG THR VAL HIS THR GLU TRP THR GLN
SEQRES 5 B 732 ARG ASP LEU GLU ARG MET GLU ASN ILE ARG PHE CYS ARG
SEQRES 6 B 732 GLN TYR LEU VAL PHE HIS ASP GLY ASP SER VAL VAL PHE
SEQRES 7 B 732 ALA GLY PRO ALA GLY ASN SER VAL GLU THR ARG GLY GLU
SEQRES 8 B 732 LEU LEU SER ARG GLU SER PRO SER GLY THR MET LYS ALA
SEQRES 9 B 732 VAL LEU ARG LYS ALA GLY GLY THR GLY THR ALA GLU GLU
SEQRES 10 B 732 LYS GLN PHE LEU GLU VAL TRP GLU LYS ASN ARG LYS LEU
SEQRES 11 B 732 LYS SER PHE ASN LEU SER ALA LEU GLU LYS HIS GLY PRO
SEQRES 12 B 732 VAL TYR GLU ASP ASP CYS PHE GLY CYS LEU SER TRP SER
SEQRES 13 B 732 HIS SER GLU THR HIS LEU LEU TYR VAL ALA ASP LYS LYS
SEQRES 14 B 732 ARG PRO LYS ALA GLU SER PHE PHE GLN THR LYS ALA LEU
SEQRES 15 B 732 ASP VAL THR GLY SER ASP ASP GLU MET ALA ARG THR LYS
SEQRES 16 B 732 LYS PRO ASP GLN ALA ILE LYS GLY ASP GLN PHE LEU PHE
SEQRES 17 B 732 TYR GLU ASP TRP GLY GLU ASN MET VAL SER LYS SER THR
SEQRES 18 B 732 PRO VAL LEU CYS VAL LEU ASP ILE GLU SER GLY ASN ILE
SEQRES 19 B 732 SER VAL LEU GLU GLY VAL PRO GLU SER VAL SER PRO GLY
SEQRES 20 B 732 GLN ALA PHE TRP ALA PRO GLY ASP THR GLY VAL VAL PHE
SEQRES 21 B 732 VAL GLY TRP TRP HIS GLU PRO PHE ARG LEU GLY ILE ARG
SEQRES 22 B 732 PHE CYS THR ASN ARG ARG SER ALA LEU TYR TYR VAL ASP
SEQRES 23 B 732 LEU THR GLY GLY LYS CYS GLU LEU LEU SER ASP GLU SER
SEQRES 24 B 732 VAL ALA VAL THR SER PRO ARG LEU SER PRO ASP GLN CYS
SEQRES 25 B 732 ARG ILE VAL TYR LEU ARG PHE PRO SER LEU VAL PRO HIS
SEQRES 26 B 732 GLN GLN CYS GLY GLN LEU CYS LEU TYR ASP TRP TYR THR
SEQRES 27 B 732 ARG VAL THR SER VAL VAL VAL ASP ILE VAL PRO ARG GLN
SEQRES 28 B 732 LEU GLY GLU ASP PHE SER GLY ILE TYR CYS SER LEU LEU
SEQRES 29 B 732 PRO LEU GLY CYS TRP SER ALA ASP SER GLN ARG VAL VAL
SEQRES 30 B 732 PHE ASP SER PRO GLN ARG SER ARG GLN ASP LEU PHE ALA
SEQRES 31 B 732 VAL ASP THR GLN MET GLY SER VAL THR SER LEU THR ALA
SEQRES 32 B 732 GLY GLY SER GLY GLY SER TRP LYS LEU LEU THR ILE ASP
SEQRES 33 B 732 ARG ASP LEU MET VAL VAL GLN PHE SER THR PRO SER VAL
SEQRES 34 B 732 PRO PRO SER LEU LYS VAL GLY PHE LEU PRO PRO ALA GLY
SEQRES 35 B 732 LYS GLU GLN ALA VAL SER TRP VAL SER LEU GLU GLU ALA
SEQRES 36 B 732 GLU PRO PHE PRO ASP ILE SER TRP SER ILE ARG VAL LEU
SEQRES 37 B 732 GLN PRO PRO PRO GLN GLN GLU HIS VAL GLN TYR ALA GLY
SEQRES 38 B 732 LEU ASP PHE GLU ALA ILE LEU LEU GLN PRO SER ASN SER
SEQRES 39 B 732 PRO GLU LYS THR GLN VAL PRO MET VAL VAL MET PRO HIS
SEQRES 40 B 732 GLY GLY PRO HIS SER SER PHE VAL THR ALA TRP MET LEU
SEQRES 41 B 732 PHE PRO ALA MET LEU CYS LYS MET GLY PHE ALA VAL LEU
SEQRES 42 B 732 LEU VAL ASN TYR ARG GLY SER THR GLY PHE GLY GLN ASP
SEQRES 43 B 732 SER ILE LEU SER LEU PRO GLY ASN VAL GLY HIS GLN ASP
SEQRES 44 B 732 VAL LYS ASP VAL GLN PHE ALA VAL GLU GLN VAL LEU GLN
SEQRES 45 B 732 GLU GLU HIS PHE ASP ALA GLY ARG VAL ALA LEU MET GLY
SEQRES 46 B 732 GLY SER HIS GLY GLY PHE LEU SER CYS HIS LEU ILE GLY
SEQRES 47 B 732 GLN TYR PRO GLU THR TYR SER ALA CYS VAL VAL ARG ASN
SEQRES 48 B 732 PRO VAL ILE ASN ILE ALA SER MET MET GLY SER THR ASP
SEQRES 49 B 732 ILE PRO ASP TRP CYS MET VAL GLU ALA GLY PHE SER TYR
SEQRES 50 B 732 SER SER ASP CYS LEU PRO ASP LEU SER VAL TRP ALA ALA
SEQRES 51 B 732 MET LEU ASP LYS SER PRO ILE LYS TYR ALA PRO GLN VAL
SEQRES 52 B 732 LYS THR PRO LEU LEU LEU MET LEU GLY GLN GLU ASP ARG
SEQRES 53 B 732 ARG VAL PRO PHE LYS GLN GLY MET GLU TYR TYR ARG VAL
SEQRES 54 B 732 LEU LYS ALA ARG ASN VAL PRO VAL ARG LEU LEU LEU TYR
SEQRES 55 B 732 PRO LYS SER THR HIS ALA LEU SER GLU VAL GLU VAL GLU
SEQRES 56 B 732 SER ASP SER PHE MET ASN ALA VAL LEU TRP LEU CYS THR
SEQRES 57 B 732 HIS LEU GLY SER
SEQRES 1 C 732 MET GLU ARG GLN VAL LEU LEU SER GLU PRO GLU GLU ALA
SEQRES 2 C 732 ALA ALA LEU TYR ARG GLY LEU SER ARG GLN PRO ALA LEU
SEQRES 3 C 732 SER ALA ALA CYS LEU GLY PRO GLU VAL THR THR GLN TYR
SEQRES 4 C 732 GLY GLY ARG TYR ARG THR VAL HIS THR GLU TRP THR GLN
SEQRES 5 C 732 ARG ASP LEU GLU ARG MET GLU ASN ILE ARG PHE CYS ARG
SEQRES 6 C 732 GLN TYR LEU VAL PHE HIS ASP GLY ASP SER VAL VAL PHE
SEQRES 7 C 732 ALA GLY PRO ALA GLY ASN SER VAL GLU THR ARG GLY GLU
SEQRES 8 C 732 LEU LEU SER ARG GLU SER PRO SER GLY THR MET LYS ALA
SEQRES 9 C 732 VAL LEU ARG LYS ALA GLY GLY THR GLY THR ALA GLU GLU
SEQRES 10 C 732 LYS GLN PHE LEU GLU VAL TRP GLU LYS ASN ARG LYS LEU
SEQRES 11 C 732 LYS SER PHE ASN LEU SER ALA LEU GLU LYS HIS GLY PRO
SEQRES 12 C 732 VAL TYR GLU ASP ASP CYS PHE GLY CYS LEU SER TRP SER
SEQRES 13 C 732 HIS SER GLU THR HIS LEU LEU TYR VAL ALA ASP LYS LYS
SEQRES 14 C 732 ARG PRO LYS ALA GLU SER PHE PHE GLN THR LYS ALA LEU
SEQRES 15 C 732 ASP VAL THR GLY SER ASP ASP GLU MET ALA ARG THR LYS
SEQRES 16 C 732 LYS PRO ASP GLN ALA ILE LYS GLY ASP GLN PHE LEU PHE
SEQRES 17 C 732 TYR GLU ASP TRP GLY GLU ASN MET VAL SER LYS SER THR
SEQRES 18 C 732 PRO VAL LEU CYS VAL LEU ASP ILE GLU SER GLY ASN ILE
SEQRES 19 C 732 SER VAL LEU GLU GLY VAL PRO GLU SER VAL SER PRO GLY
SEQRES 20 C 732 GLN ALA PHE TRP ALA PRO GLY ASP THR GLY VAL VAL PHE
SEQRES 21 C 732 VAL GLY TRP TRP HIS GLU PRO PHE ARG LEU GLY ILE ARG
SEQRES 22 C 732 PHE CYS THR ASN ARG ARG SER ALA LEU TYR TYR VAL ASP
SEQRES 23 C 732 LEU THR GLY GLY LYS CYS GLU LEU LEU SER ASP GLU SER
SEQRES 24 C 732 VAL ALA VAL THR SER PRO ARG LEU SER PRO ASP GLN CYS
SEQRES 25 C 732 ARG ILE VAL TYR LEU ARG PHE PRO SER LEU VAL PRO HIS
SEQRES 26 C 732 GLN GLN CYS GLY GLN LEU CYS LEU TYR ASP TRP TYR THR
SEQRES 27 C 732 ARG VAL THR SER VAL VAL VAL ASP ILE VAL PRO ARG GLN
SEQRES 28 C 732 LEU GLY GLU ASP PHE SER GLY ILE TYR CYS SER LEU LEU
SEQRES 29 C 732 PRO LEU GLY CYS TRP SER ALA ASP SER GLN ARG VAL VAL
SEQRES 30 C 732 PHE ASP SER PRO GLN ARG SER ARG GLN ASP LEU PHE ALA
SEQRES 31 C 732 VAL ASP THR GLN MET GLY SER VAL THR SER LEU THR ALA
SEQRES 32 C 732 GLY GLY SER GLY GLY SER TRP LYS LEU LEU THR ILE ASP
SEQRES 33 C 732 ARG ASP LEU MET VAL VAL GLN PHE SER THR PRO SER VAL
SEQRES 34 C 732 PRO PRO SER LEU LYS VAL GLY PHE LEU PRO PRO ALA GLY
SEQRES 35 C 732 LYS GLU GLN ALA VAL SER TRP VAL SER LEU GLU GLU ALA
SEQRES 36 C 732 GLU PRO PHE PRO ASP ILE SER TRP SER ILE ARG VAL LEU
SEQRES 37 C 732 GLN PRO PRO PRO GLN GLN GLU HIS VAL GLN TYR ALA GLY
SEQRES 38 C 732 LEU ASP PHE GLU ALA ILE LEU LEU GLN PRO SER ASN SER
SEQRES 39 C 732 PRO GLU LYS THR GLN VAL PRO MET VAL VAL MET PRO HIS
SEQRES 40 C 732 GLY GLY PRO HIS SER SER PHE VAL THR ALA TRP MET LEU
SEQRES 41 C 732 PHE PRO ALA MET LEU CYS LYS MET GLY PHE ALA VAL LEU
SEQRES 42 C 732 LEU VAL ASN TYR ARG GLY SER THR GLY PHE GLY GLN ASP
SEQRES 43 C 732 SER ILE LEU SER LEU PRO GLY ASN VAL GLY HIS GLN ASP
SEQRES 44 C 732 VAL LYS ASP VAL GLN PHE ALA VAL GLU GLN VAL LEU GLN
SEQRES 45 C 732 GLU GLU HIS PHE ASP ALA GLY ARG VAL ALA LEU MET GLY
SEQRES 46 C 732 GLY SER HIS GLY GLY PHE LEU SER CYS HIS LEU ILE GLY
SEQRES 47 C 732 GLN TYR PRO GLU THR TYR SER ALA CYS VAL VAL ARG ASN
SEQRES 48 C 732 PRO VAL ILE ASN ILE ALA SER MET MET GLY SER THR ASP
SEQRES 49 C 732 ILE PRO ASP TRP CYS MET VAL GLU ALA GLY PHE SER TYR
SEQRES 50 C 732 SER SER ASP CYS LEU PRO ASP LEU SER VAL TRP ALA ALA
SEQRES 51 C 732 MET LEU ASP LYS SER PRO ILE LYS TYR ALA PRO GLN VAL
SEQRES 52 C 732 LYS THR PRO LEU LEU LEU MET LEU GLY GLN GLU ASP ARG
SEQRES 53 C 732 ARG VAL PRO PHE LYS GLN GLY MET GLU TYR TYR ARG VAL
SEQRES 54 C 732 LEU LYS ALA ARG ASN VAL PRO VAL ARG LEU LEU LEU TYR
SEQRES 55 C 732 PRO LYS SER THR HIS ALA LEU SER GLU VAL GLU VAL GLU
SEQRES 56 C 732 SER ASP SER PHE MET ASN ALA VAL LEU TRP LEU CYS THR
SEQRES 57 C 732 HIS LEU GLY SER
SEQRES 1 D 732 MET GLU ARG GLN VAL LEU LEU SER GLU PRO GLU GLU ALA
SEQRES 2 D 732 ALA ALA LEU TYR ARG GLY LEU SER ARG GLN PRO ALA LEU
SEQRES 3 D 732 SER ALA ALA CYS LEU GLY PRO GLU VAL THR THR GLN TYR
SEQRES 4 D 732 GLY GLY ARG TYR ARG THR VAL HIS THR GLU TRP THR GLN
SEQRES 5 D 732 ARG ASP LEU GLU ARG MET GLU ASN ILE ARG PHE CYS ARG
SEQRES 6 D 732 GLN TYR LEU VAL PHE HIS ASP GLY ASP SER VAL VAL PHE
SEQRES 7 D 732 ALA GLY PRO ALA GLY ASN SER VAL GLU THR ARG GLY GLU
SEQRES 8 D 732 LEU LEU SER ARG GLU SER PRO SER GLY THR MET LYS ALA
SEQRES 9 D 732 VAL LEU ARG LYS ALA GLY GLY THR GLY THR ALA GLU GLU
SEQRES 10 D 732 LYS GLN PHE LEU GLU VAL TRP GLU LYS ASN ARG LYS LEU
SEQRES 11 D 732 LYS SER PHE ASN LEU SER ALA LEU GLU LYS HIS GLY PRO
SEQRES 12 D 732 VAL TYR GLU ASP ASP CYS PHE GLY CYS LEU SER TRP SER
SEQRES 13 D 732 HIS SER GLU THR HIS LEU LEU TYR VAL ALA ASP LYS LYS
SEQRES 14 D 732 ARG PRO LYS ALA GLU SER PHE PHE GLN THR LYS ALA LEU
SEQRES 15 D 732 ASP VAL THR GLY SER ASP ASP GLU MET ALA ARG THR LYS
SEQRES 16 D 732 LYS PRO ASP GLN ALA ILE LYS GLY ASP GLN PHE LEU PHE
SEQRES 17 D 732 TYR GLU ASP TRP GLY GLU ASN MET VAL SER LYS SER THR
SEQRES 18 D 732 PRO VAL LEU CYS VAL LEU ASP ILE GLU SER GLY ASN ILE
SEQRES 19 D 732 SER VAL LEU GLU GLY VAL PRO GLU SER VAL SER PRO GLY
SEQRES 20 D 732 GLN ALA PHE TRP ALA PRO GLY ASP THR GLY VAL VAL PHE
SEQRES 21 D 732 VAL GLY TRP TRP HIS GLU PRO PHE ARG LEU GLY ILE ARG
SEQRES 22 D 732 PHE CYS THR ASN ARG ARG SER ALA LEU TYR TYR VAL ASP
SEQRES 23 D 732 LEU THR GLY GLY LYS CYS GLU LEU LEU SER ASP GLU SER
SEQRES 24 D 732 VAL ALA VAL THR SER PRO ARG LEU SER PRO ASP GLN CYS
SEQRES 25 D 732 ARG ILE VAL TYR LEU ARG PHE PRO SER LEU VAL PRO HIS
SEQRES 26 D 732 GLN GLN CYS GLY GLN LEU CYS LEU TYR ASP TRP TYR THR
SEQRES 27 D 732 ARG VAL THR SER VAL VAL VAL ASP ILE VAL PRO ARG GLN
SEQRES 28 D 732 LEU GLY GLU ASP PHE SER GLY ILE TYR CYS SER LEU LEU
SEQRES 29 D 732 PRO LEU GLY CYS TRP SER ALA ASP SER GLN ARG VAL VAL
SEQRES 30 D 732 PHE ASP SER PRO GLN ARG SER ARG GLN ASP LEU PHE ALA
SEQRES 31 D 732 VAL ASP THR GLN MET GLY SER VAL THR SER LEU THR ALA
SEQRES 32 D 732 GLY GLY SER GLY GLY SER TRP LYS LEU LEU THR ILE ASP
SEQRES 33 D 732 ARG ASP LEU MET VAL VAL GLN PHE SER THR PRO SER VAL
SEQRES 34 D 732 PRO PRO SER LEU LYS VAL GLY PHE LEU PRO PRO ALA GLY
SEQRES 35 D 732 LYS GLU GLN ALA VAL SER TRP VAL SER LEU GLU GLU ALA
SEQRES 36 D 732 GLU PRO PHE PRO ASP ILE SER TRP SER ILE ARG VAL LEU
SEQRES 37 D 732 GLN PRO PRO PRO GLN GLN GLU HIS VAL GLN TYR ALA GLY
SEQRES 38 D 732 LEU ASP PHE GLU ALA ILE LEU LEU GLN PRO SER ASN SER
SEQRES 39 D 732 PRO GLU LYS THR GLN VAL PRO MET VAL VAL MET PRO HIS
SEQRES 40 D 732 GLY GLY PRO HIS SER SER PHE VAL THR ALA TRP MET LEU
SEQRES 41 D 732 PHE PRO ALA MET LEU CYS LYS MET GLY PHE ALA VAL LEU
SEQRES 42 D 732 LEU VAL ASN TYR ARG GLY SER THR GLY PHE GLY GLN ASP
SEQRES 43 D 732 SER ILE LEU SER LEU PRO GLY ASN VAL GLY HIS GLN ASP
SEQRES 44 D 732 VAL LYS ASP VAL GLN PHE ALA VAL GLU GLN VAL LEU GLN
SEQRES 45 D 732 GLU GLU HIS PHE ASP ALA GLY ARG VAL ALA LEU MET GLY
SEQRES 46 D 732 GLY SER HIS GLY GLY PHE LEU SER CYS HIS LEU ILE GLY
SEQRES 47 D 732 GLN TYR PRO GLU THR TYR SER ALA CYS VAL VAL ARG ASN
SEQRES 48 D 732 PRO VAL ILE ASN ILE ALA SER MET MET GLY SER THR ASP
SEQRES 49 D 732 ILE PRO ASP TRP CYS MET VAL GLU ALA GLY PHE SER TYR
SEQRES 50 D 732 SER SER ASP CYS LEU PRO ASP LEU SER VAL TRP ALA ALA
SEQRES 51 D 732 MET LEU ASP LYS SER PRO ILE LYS TYR ALA PRO GLN VAL
SEQRES 52 D 732 LYS THR PRO LEU LEU LEU MET LEU GLY GLN GLU ASP ARG
SEQRES 53 D 732 ARG VAL PRO PHE LYS GLN GLY MET GLU TYR TYR ARG VAL
SEQRES 54 D 732 LEU LYS ALA ARG ASN VAL PRO VAL ARG LEU LEU LEU TYR
SEQRES 55 D 732 PRO LYS SER THR HIS ALA LEU SER GLU VAL GLU VAL GLU
SEQRES 56 D 732 SER ASP SER PHE MET ASN ALA VAL LEU TRP LEU CYS THR
SEQRES 57 D 732 HIS LEU GLY SER
HELIX 1 AA1 GLU A 9 SER A 21 1 13
HELIX 2 AA2 LEU A 135 GLU A 139 1 5
HELIX 3 AA3 PRO A 253 ASP A 255 5 3
HELIX 4 AA4 MET A 519 LYS A 527 1 9
HELIX 5 AA5 GLY A 544 LEU A 549 1 6
HELIX 6 AA6 GLN A 558 LEU A 571 1 14
HELIX 7 AA7 SER A 587 TYR A 600 1 14
HELIX 8 AA8 ASN A 615 MET A 620 1 6
HELIX 9 AA9 PRO A 626 GLY A 634 1 9
HELIX 10 AB1 ASP A 644 SER A 655 1 12
HELIX 11 AB2 PHE A 680 ARG A 693 1 14
HELIX 12 AB3 GLU A 711 GLY A 731 1 21
HELIX 13 AB4 PRO B 10 SER B 21 1 12
HELIX 14 AB5 LEU B 135 GLU B 139 1 5
HELIX 15 AB6 PRO B 253 ASP B 255 5 3
HELIX 16 AB7 MET B 519 LYS B 527 1 9
HELIX 17 AB8 GLY B 544 LEU B 551 1 8
HELIX 18 AB9 GLN B 558 LEU B 571 1 14
HELIX 19 AC1 SER B 587 TYR B 600 1 14
HELIX 20 AC2 ASN B 615 SER B 622 1 8
HELIX 21 AC3 PRO B 626 GLY B 634 1 9
HELIX 22 AC4 ASP B 644 SER B 655 1 12
HELIX 23 AC5 TYR B 659 VAL B 663 5 5
HELIX 24 AC6 PHE B 680 ARG B 693 1 14
HELIX 25 AC7 GLU B 711 LEU B 730 1 20
HELIX 26 AC8 PRO C 10 SER C 21 1 12
HELIX 27 AC9 LEU C 135 GLU C 139 1 5
HELIX 28 AD1 PRO C 253 ASP C 255 5 3
HELIX 29 AD2 PRO C 471 GLU C 475 5 5
HELIX 30 AD3 MET C 519 LYS C 527 1 9
HELIX 31 AD4 GLY C 544 LEU C 551 1 8
HELIX 32 AD5 HIS C 557 GLN C 572 1 16
HELIX 33 AD6 HIS C 588 TYR C 600 1 13
HELIX 34 AD7 ASN C 615 MET C 620 1 6
HELIX 35 AD8 PRO C 626 GLY C 634 1 9
HELIX 36 AD9 ASP C 644 LYS C 654 1 11
HELIX 37 AE1 SER C 655 VAL C 663 5 9
HELIX 38 AE2 PHE C 680 ARG C 693 1 14
HELIX 39 AE3 GLU C 711 GLY C 731 1 21
HELIX 40 AE4 PRO D 10 SER D 21 1 12
HELIX 41 AE5 LEU D 135 GLU D 139 1 5
HELIX 42 AE6 PRO D 253 ASP D 255 5 3
HELIX 43 AE7 PRO D 471 GLU D 475 5 5
HELIX 44 AE8 MET D 519 LYS D 527 1 9
HELIX 45 AE9 GLY D 544 LEU D 551 1 8
HELIX 46 AF1 HIS D 557 GLU D 573 1 17
HELIX 47 AF2 HIS D 588 TYR D 600 1 13
HELIX 48 AF3 ASN D 615 SER D 622 1 8
HELIX 49 AF4 PRO D 626 GLY D 634 1 9
HELIX 50 AF5 ASP D 644 SER D 655 1 12
HELIX 51 AF6 PRO D 656 VAL D 663 5 8
HELIX 52 AF7 PHE D 680 ARG D 693 1 14
HELIX 53 AF8 GLU D 711 LEU D 730 1 20
SHEET 1 AA1 4 ALA A 25 LEU A 31 0
SHEET 2 AA1 4 ARG A 42 ASP A 54 -1 O GLU A 49 N ALA A 28
SHEET 3 AA1 4 GLU A 59 HIS A 71 -1 O GLU A 59 N ASP A 54
SHEET 4 AA1 4 VAL A 76 PRO A 81 -1 O GLY A 80 N LEU A 68
SHEET 1 AA2 4 VAL A 35 THR A 36 0
SHEET 2 AA2 4 ARG A 42 ASP A 54 -1 O TYR A 43 N VAL A 35
SHEET 3 AA2 4 GLU A 59 HIS A 71 -1 O GLU A 59 N ASP A 54
SHEET 4 AA2 4 VAL A 86 THR A 88 -1 O THR A 88 N ARG A 62
SHEET 1 AA3 4 GLU A 91 GLU A 96 0
SHEET 2 AA3 4 MET A 102 LYS A 108 -1 O ALA A 104 N ARG A 95
SHEET 3 AA3 4 GLN A 119 GLU A 125 -1 O GLU A 122 N VAL A 105
SHEET 4 AA3 4 ARG A 128 ASN A 134 -1 O LYS A 131 N VAL A 123
SHEET 1 AA4 4 LEU A 153 TRP A 155 0
SHEET 2 AA4 4 HIS A 161 ASP A 167 -1 O LEU A 163 N SER A 154
SHEET 3 AA4 4 PRO A 222 ASP A 228 -1 O CYS A 225 N TYR A 164
SHEET 4 AA4 4 ILE A 234 VAL A 236 -1 O SER A 235 N VAL A 226
SHEET 1 AA5 2 ALA A 173 GLU A 174 0
SHEET 2 AA5 2 ILE A 201 LYS A 202 1 O ILE A 201 N GLU A 174
SHEET 1 AA6 4 VAL A 244 TRP A 251 0
SHEET 2 AA6 4 GLY A 257 TRP A 264 -1 O VAL A 259 N PHE A 250
SHEET 3 AA6 4 SER A 280 ASP A 286 -1 O VAL A 285 N VAL A 258
SHEET 4 AA6 4 GLU A 293 LEU A 294 -1 O GLU A 293 N TYR A 284
SHEET 1 AA7 4 ALA A 301 LEU A 307 0
SHEET 2 AA7 4 ARG A 313 PHE A 319 -1 O PHE A 319 N ALA A 301
SHEET 3 AA7 4 GLN A 330 ASP A 335 -1 O TYR A 334 N ILE A 314
SHEET 4 AA7 4 VAL A 340 VAL A 345 -1 O VAL A 344 N LEU A 331
SHEET 1 AA8 3 ARG A 375 GLN A 382 0
SHEET 2 AA8 3 ARG A 385 ASP A 392 -1 O VAL A 391 N VAL A 376
SHEET 3 AA8 3 VAL A 398 SER A 400 -1 O THR A 399 N ALA A 390
SHEET 1 AA9 4 SER A 409 ASP A 416 0
SHEET 2 AA9 4 LEU A 419 SER A 425 -1 O VAL A 421 N THR A 414
SHEET 3 AA9 4 LEU A 433 PHE A 437 -1 O LYS A 434 N VAL A 422
SHEET 4 AA9 4 TRP A 449 GLU A 453 -1 O VAL A 450 N VAL A 435
SHEET 1 AB1 8 ILE A 461 LEU A 468 0
SHEET 2 AB1 8 PHE A 484 PRO A 491 -1 O PHE A 484 N LEU A 468
SHEET 3 AB1 8 ALA A 531 ASN A 536 -1 O VAL A 532 N LEU A 489
SHEET 4 AB1 8 MET A 502 PRO A 506 1 N VAL A 503 O LEU A 533
SHEET 5 AB1 8 VAL A 581 MET A 584 1 O ALA A 582 N VAL A 504
SHEET 6 AB1 8 ALA A 606 ARG A 610 1 O ALA A 606 N LEU A 583
SHEET 7 AB1 8 LEU A 667 GLY A 672 1 O LEU A 668 N VAL A 609
SHEET 8 AB1 8 VAL A 697 TYR A 702 1 O ARG A 698 N LEU A 669
SHEET 1 AB2 4 ALA B 25 LEU B 31 0
SHEET 2 AB2 4 ARG B 42 ASP B 54 -1 O GLU B 49 N ALA B 28
SHEET 3 AB2 4 GLU B 59 HIS B 71 -1 O PHE B 63 N TRP B 50
SHEET 4 AB2 4 VAL B 76 PRO B 81 -1 O GLY B 80 N LEU B 68
SHEET 1 AB3 4 VAL B 35 THR B 36 0
SHEET 2 AB3 4 ARG B 42 ASP B 54 -1 O TYR B 43 N VAL B 35
SHEET 3 AB3 4 GLU B 59 HIS B 71 -1 O PHE B 63 N TRP B 50
SHEET 4 AB3 4 VAL B 86 THR B 88 -1 O THR B 88 N ARG B 62
SHEET 1 AB4 4 GLU B 91 GLU B 96 0
SHEET 2 AB4 4 MET B 102 LYS B 108 -1 O ALA B 104 N ARG B 95
SHEET 3 AB4 4 GLN B 119 GLU B 125 -1 O PHE B 120 N ARG B 107
SHEET 4 AB4 4 ARG B 128 ASN B 134 -1 O ARG B 128 N GLU B 125
SHEET 1 AB5 4 LEU B 153 TRP B 155 0
SHEET 2 AB5 4 HIS B 161 ASP B 167 -1 O LEU B 163 N SER B 154
SHEET 3 AB5 4 PRO B 222 ASP B 228 -1 O CYS B 225 N TYR B 164
SHEET 4 AB5 4 ILE B 234 VAL B 236 -1 O SER B 235 N VAL B 226
SHEET 1 AB6 2 ALA B 173 GLU B 174 0
SHEET 2 AB6 2 ILE B 201 LYS B 202 1 O ILE B 201 N GLU B 174
SHEET 1 AB7 4 VAL B 244 TRP B 251 0
SHEET 2 AB7 4 GLY B 257 TRP B 264 -1 O VAL B 259 N PHE B 250
SHEET 3 AB7 4 SER B 280 ASP B 286 -1 O VAL B 285 N VAL B 258
SHEET 4 AB7 4 GLU B 293 LEU B 294 -1 O GLU B 293 N TYR B 284
SHEET 1 AB8 4 ALA B 301 LEU B 307 0
SHEET 2 AB8 4 ARG B 313 PHE B 319 -1 O LEU B 317 N THR B 303
SHEET 3 AB8 4 GLN B 330 ASP B 335 -1 O CYS B 332 N TYR B 316
SHEET 4 AB8 4 VAL B 340 VAL B 343 -1 O SER B 342 N LEU B 333
SHEET 1 AB9 3 ARG B 375 PRO B 381 0
SHEET 2 AB9 3 GLN B 386 ASP B 392 -1 O PHE B 389 N PHE B 378
SHEET 3 AB9 3 VAL B 398 SER B 400 -1 O THR B 399 N ALA B 390
SHEET 1 AC1 4 SER B 409 ASP B 416 0
SHEET 2 AC1 4 LEU B 419 SER B 425 -1 O VAL B 421 N THR B 414
SHEET 3 AC1 4 LEU B 433 PHE B 437 -1 O LYS B 434 N VAL B 422
SHEET 4 AC1 4 TRP B 449 GLU B 453 -1 O VAL B 450 N VAL B 435
SHEET 1 AC2 5 ILE B 461 LEU B 468 0
SHEET 2 AC2 5 PHE B 484 PRO B 491 -1 O PHE B 484 N LEU B 468
SHEET 3 AC2 5 ALA B 531 ASN B 536 -1 O LEU B 534 N ILE B 487
SHEET 4 AC2 5 VAL B 500 PRO B 506 1 N MET B 505 O LEU B 533
SHEET 5 AC2 5 PHE B 576 LEU B 583 1 O ALA B 582 N VAL B 504
SHEET 1 AC3 4 GLY B 585 GLY B 586 0
SHEET 2 AC3 4 CYS B 607 ARG B 610 1 O VAL B 608 N GLY B 585
SHEET 3 AC3 4 LEU B 667 GLY B 672 1 O LEU B 668 N VAL B 609
SHEET 4 AC3 4 VAL B 697 TYR B 702 1 O ARG B 698 N LEU B 669
SHEET 1 AC4 4 ALA C 25 LEU C 31 0
SHEET 2 AC4 4 ARG C 42 ASP C 54 -1 O THR C 51 N ALA C 25
SHEET 3 AC4 4 GLU C 59 HIS C 71 -1 O VAL C 69 N ARG C 44
SHEET 4 AC4 4 VAL C 76 PRO C 81 -1 O GLY C 80 N LEU C 68
SHEET 1 AC5 4 VAL C 35 THR C 36 0
SHEET 2 AC5 4 ARG C 42 ASP C 54 -1 O TYR C 43 N VAL C 35
SHEET 3 AC5 4 GLU C 59 HIS C 71 -1 O VAL C 69 N ARG C 44
SHEET 4 AC5 4 VAL C 86 THR C 88 -1 O THR C 88 N ARG C 62
SHEET 1 AC6 4 GLU C 91 GLU C 96 0
SHEET 2 AC6 4 MET C 102 LYS C 108 -1 O ALA C 104 N ARG C 95
SHEET 3 AC6 4 GLN C 119 GLU C 125 -1 O PHE C 120 N ARG C 107
SHEET 4 AC6 4 ARG C 128 ASN C 134 -1 O LYS C 131 N VAL C 123
SHEET 1 AC7 4 LEU C 153 TRP C 155 0
SHEET 2 AC7 4 HIS C 161 ASP C 167 -1 O LEU C 163 N SER C 154
SHEET 3 AC7 4 PRO C 222 ASP C 228 -1 O CYS C 225 N TYR C 164
SHEET 4 AC7 4 ILE C 234 VAL C 236 -1 O SER C 235 N VAL C 226
SHEET 1 AC8 2 ALA C 173 GLU C 174 0
SHEET 2 AC8 2 ILE C 201 LYS C 202 1 O ILE C 201 N GLU C 174
SHEET 1 AC9 3 VAL C 244 PRO C 246 0
SHEET 2 AC9 3 GLY C 257 TRP C 264 -1 O TRP C 263 N SER C 245
SHEET 3 AC9 3 PHE C 250 TRP C 251 -1 N PHE C 250 O VAL C 259
SHEET 1 AD1 4 VAL C 244 PRO C 246 0
SHEET 2 AD1 4 GLY C 257 TRP C 264 -1 O TRP C 263 N SER C 245
SHEET 3 AD1 4 SER C 280 ASP C 286 -1 O VAL C 285 N VAL C 258
SHEET 4 AD1 4 GLU C 293 LEU C 294 -1 O GLU C 293 N TYR C 284
SHEET 1 AD2 4 ALA C 301 LEU C 307 0
SHEET 2 AD2 4 ARG C 313 PHE C 319 -1 O PHE C 319 N ALA C 301
SHEET 3 AD2 4 GLN C 330 ASP C 335 -1 O CYS C 332 N TYR C 316
SHEET 4 AD2 4 THR C 341 VAL C 343 -1 O SER C 342 N LEU C 333
SHEET 1 AD3 3 ARG C 375 GLN C 382 0
SHEET 2 AD3 3 ARG C 385 ASP C 392 -1 O PHE C 389 N PHE C 378
SHEET 3 AD3 3 VAL C 398 SER C 400 -1 O THR C 399 N ALA C 390
SHEET 1 AD4 4 SER C 409 ASP C 416 0
SHEET 2 AD4 4 LEU C 419 SER C 425 -1 O VAL C 421 N THR C 414
SHEET 3 AD4 4 LEU C 433 PHE C 437 -1 O GLY C 436 N MET C 420
SHEET 4 AD4 4 VAL C 450 GLU C 453 -1 O VAL C 450 N VAL C 435
SHEET 1 AD5 8 ILE C 461 LEU C 468 0
SHEET 2 AD5 8 PHE C 484 PRO C 491 -1 O ALA C 486 N ARG C 466
SHEET 3 AD5 8 ALA C 531 ASN C 536 -1 O LEU C 534 N ILE C 487
SHEET 4 AD5 8 VAL C 500 PRO C 506 1 N MET C 505 O LEU C 533
SHEET 5 AD5 8 PHE C 576 GLY C 585 1 O ALA C 582 N VAL C 504
SHEET 6 AD5 8 ALA C 606 VAL C 609 1 O VAL C 608 N GLY C 585
SHEET 7 AD5 8 LEU C 667 GLY C 672 1 O LEU C 668 N VAL C 609
SHEET 8 AD5 8 VAL C 697 TYR C 702 1 O ARG C 698 N LEU C 669
SHEET 1 AD6 4 ALA D 25 LEU D 31 0
SHEET 2 AD6 4 ARG D 42 ASP D 54 -1 O GLU D 49 N SER D 27
SHEET 3 AD6 4 GLU D 59 HIS D 71 -1 O ARG D 65 N THR D 48
SHEET 4 AD6 4 VAL D 76 PRO D 81 -1 O PHE D 78 N PHE D 70
SHEET 1 AD7 4 VAL D 35 THR D 36 0
SHEET 2 AD7 4 ARG D 42 ASP D 54 -1 O TYR D 43 N VAL D 35
SHEET 3 AD7 4 GLU D 59 HIS D 71 -1 O ARG D 65 N THR D 48
SHEET 4 AD7 4 VAL D 86 THR D 88 -1 O THR D 88 N ARG D 62
SHEET 1 AD8 4 GLU D 91 GLU D 96 0
SHEET 2 AD8 4 MET D 102 LYS D 108 -1 O LEU D 106 N LEU D 92
SHEET 3 AD8 4 GLN D 119 GLU D 125 -1 O PHE D 120 N ARG D 107
SHEET 4 AD8 4 ARG D 128 ASN D 134 -1 O LYS D 131 N VAL D 123
SHEET 1 AD9 4 LEU D 153 TRP D 155 0
SHEET 2 AD9 4 HIS D 161 ASP D 167 -1 O LEU D 163 N SER D 154
SHEET 3 AD9 4 PRO D 222 ASP D 228 -1 O CYS D 225 N TYR D 164
SHEET 4 AD9 4 ILE D 234 VAL D 236 -1 O SER D 235 N VAL D 226
SHEET 1 AE1 2 ALA D 173 GLU D 174 0
SHEET 2 AE1 2 ILE D 201 LYS D 202 1 O ILE D 201 N GLU D 174
SHEET 1 AE2 4 VAL D 244 TRP D 251 0
SHEET 2 AE2 4 GLY D 257 TRP D 264 -1 O VAL D 259 N PHE D 250
SHEET 3 AE2 4 SER D 280 ASP D 286 -1 O TYR D 283 N PHE D 260
SHEET 4 AE2 4 GLU D 293 LEU D 294 -1 O GLU D 293 N TYR D 284
SHEET 1 AE3 4 ALA D 301 LEU D 307 0
SHEET 2 AE3 4 ARG D 313 PHE D 319 -1 O LEU D 317 N THR D 303
SHEET 3 AE3 4 GLN D 330 ASP D 335 -1 O CYS D 332 N TYR D 316
SHEET 4 AE3 4 THR D 341 VAL D 345 -1 O VAL D 344 N LEU D 331
SHEET 1 AE4 3 ARG D 375 GLN D 382 0
SHEET 2 AE4 3 ARG D 385 ASP D 392 -1 O ARG D 385 N GLN D 382
SHEET 3 AE4 3 VAL D 398 SER D 400 -1 O THR D 399 N ALA D 390
SHEET 1 AE5 4 SER D 409 ASP D 416 0
SHEET 2 AE5 4 LEU D 419 SER D 425 -1 O VAL D 421 N THR D 414
SHEET 3 AE5 4 LEU D 433 PHE D 437 -1 O GLY D 436 N MET D 420
SHEET 4 AE5 4 TRP D 449 GLU D 453 -1 O VAL D 450 N VAL D 435
SHEET 1 AE6 8 ILE D 461 LEU D 468 0
SHEET 2 AE6 8 PHE D 484 PRO D 491 -1 O PHE D 484 N LEU D 468
SHEET 3 AE6 8 ALA D 531 ASN D 536 -1 O LEU D 534 N ILE D 487
SHEET 4 AE6 8 MET D 502 PRO D 506 1 N VAL D 503 O ALA D 531
SHEET 5 AE6 8 VAL D 581 SER D 587 1 O ALA D 582 N MET D 502
SHEET 6 AE6 8 VAL D 608 PRO D 612 1 O ARG D 610 N SER D 587
SHEET 7 AE6 8 LEU D 667 GLY D 672 1 O LEU D 668 N VAL D 609
SHEET 8 AE6 8 VAL D 697 TYR D 702 1 O ARG D 698 N LEU D 669
CISPEP 1 GLU A 266 PRO A 267 0 1.73
CISPEP 2 GLY A 509 PRO A 510 0 9.84
CISPEP 3 GLU B 266 PRO B 267 0 0.82
CISPEP 4 GLY B 509 PRO B 510 0 0.73
CISPEP 5 GLU C 266 PRO C 267 0 0.37
CISPEP 6 GLY C 509 PRO C 510 0 9.47
CISPEP 7 GLU D 266 PRO D 267 0 0.18
CISPEP 8 GLY D 509 PRO D 510 0 7.77
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 5339 SER A 732
TER 10699 SER B 732
TER 16060 SER C 732
TER 21413 SER D 732
MASTER 513 0 0 53 168 0 0 621163 4 0 228
END |