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HEADER HYDROLASE 12-DEC-23 8RFB
TITLE CRYO-EM STRUCTURE OF THE R243C MUTANT OF HUMAN PROLYL ENDOPEPTIDASE-
TITLE 2 LIKE (PREPL) PROTEIN INVOLVED IN CONGENITAL MYASTHENIC SYNDROME-22
TITLE 3 (CMS22)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL ENDOPEPTIDASE-LIKE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROLYLENDOPEPTIDASE-LIKE;
COMPND 5 EC: 3.4.21.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PREPL, KIAA0436;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS THIO-ESTERASE, HYDROLASE
EXPDTA ELECTRON MICROSCOPY
AUTHOR A.THEODOROPOULOU,E.CAVANI,A.ANTANASIJEVIC,M.J.MARCAIDA,M.DAL PERARO
REVDAT 1 04-SEP-24 8RFB 0
JRNL AUTH Y.MONNENS,A.THEODOROPOULOU,K.ROSIER,K.BHALLA,A.MAHY,
JRNL AUTH 2 R.VANHOUTTE,S.MEULEMANS,E.CAVANI,A.ANTANASIJEVIC,I.LEMMENS,
JRNL AUTH 3 J.A.LEE,C.J.SPELLICY,R.J.SCHROER,R.A.MASELLI,C.G.LAVERTY,
JRNL AUTH 4 P.AGOSTINIS,D.J.PAGLIARINI,S.VERHELST,M.J.MARCAIDA,
JRNL AUTH 5 A.ROCHTUS,M.DAL PERARO,J.W.CREEMERS
JRNL TITL MISSENSE VARIANTS IN CMS22 PATIENTS REVEAL THAT PREPL HAS
JRNL TITL 2 BOTH ENZYMATIC AND NON-ENZYMATIC FUNCTIONS.
JRNL REF JCI INSIGHT 2024
JRNL REFN ISSN 2379-3708
JRNL PMID 39078710
JRNL DOI 10.1172/JCI.INSIGHT.179276
REMARK 2
REMARK 2 RESOLUTION. 4.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : CRYOSPARC
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 4.010
REMARK 3 NUMBER OF PARTICLES : 137436
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 8RFB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-DEC-23.
REMARK 100 THE DEPOSITION ID IS D_1292135220.
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 : CRYOEM STRUCTURE OF THE R243C
REMARK 245 MUTANT OF PROLYL ENDOPEPTIDASE-
REMARK 245 LIKE (PREPL) PROTEIN
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 13.00
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
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) : 1500.00
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) : 6000.00
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 SER A 89
REMARK 465 MET A 90
REMARK 465 ASP A 91
REMARK 465 ALA A 92
REMARK 465 PHE A 93
REMARK 465 GLU A 94
REMARK 465 LYS A 95
REMARK 465 VAL A 96
REMARK 465 ARG A 97
REMARK 465 THR A 98
REMARK 465 LYS A 99
REMARK 465 LEU A 100
REMARK 465 GLU A 101
REMARK 465 THR A 102
REMARK 465 GLN A 103
REMARK 465 PRO A 104
REMARK 465 GLN A 105
REMARK 465 GLU A 106
REMARK 465 GLU A 107
REMARK 465 TYR A 108
REMARK 465 GLU A 109
REMARK 465 ILE A 110
REMARK 465 ASP A 134
REMARK 465 GLU A 135
REMARK 465 GLU A 136
REMARK 465 ALA A 137
REMARK 465 ASP A 138
REMARK 465 ASN A 139
REMARK 465 GLY A 687
REMARK 465 GLY A 688
REMARK 465 ASN A 689
REMARK 465 HIS A 690
REMARK 465 VAL A 691
REMARK 465 ILE A 692
REMARK 465 GLU A 693
REMARK 465 LEU A 721
REMARK 465 LYS A 722
REMARK 465 LYS A 723
REMARK 465 TYR A 724
REMARK 465 LEU A 725
REMARK 465 LYS A 726
REMARK 465 PHE A 727
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 ILE A 111 CG1 CG2 CD1
REMARK 470 ASN A 112 CG OD1 ND2
REMARK 470 VAL A 113 CG1 CG2
REMARK 470 GLU A 114 CG CD OE1 OE2
REMARK 470 VAL A 115 CG1 CG2
REMARK 470 LYS A 116 CG CD CE NZ
REMARK 470 ARG A 131 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 133 CG CD CE NZ
REMARK 470 GLU A 143 CG CD OE1 OE2
REMARK 470 GLU A 149 CG CD OE1 OE2
REMARK 470 LEU A 151 CG CD1 CD2
REMARK 470 LYS A 152 CG CD CE NZ
REMARK 470 ASP A 154 CG OD1 OD2
REMARK 470 GLN A 155 CG CD OE1 NE2
REMARK 470 ASP A 178 CG OD1 OD2
REMARK 470 LYS A 188 CG CD CE NZ
REMARK 470 GLU A 206 CG CD OE1 OE2
REMARK 470 ASP A 213 CG OD1 OD2
REMARK 470 GLU A 214 CG CD OE1 OE2
REMARK 470 ARG A 232 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 239 CG CD CE NZ
REMARK 470 ARG A 240 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 242 CG CD OE1 OE2
REMARK 470 LYS A 248 CG CD CE NZ
REMARK 470 ARG A 306 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 308 CG OD1 OD2
REMARK 470 GLU A 309 CG CD OE1 OE2
REMARK 470 GLU A 321 CG CD OE1 OE2
REMARK 470 LYS A 348 CG CD CE NZ
REMARK 470 ASP A 353 CG OD1 OD2
REMARK 470 LYS A 421 CG CD CE NZ
REMARK 470 LYS A 426 CG CD CE NZ
REMARK 470 GLU A 430 CG CD OE1 OE2
REMARK 470 GLU A 434 CG CD OE1 OE2
REMARK 470 LYS A 463 CG CD CE NZ
REMARK 470 ASP A 468 CG OD1 OD2
REMARK 470 ARG A 524 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 534 CG OD1 OD2
REMARK 470 GLU A 536 CG CD OE1 OE2
REMARK 470 MET A 592 CG SD CE
REMARK 470 MET A 593 CG SD CE
REMARK 470 THR A 595 OG1 CG2
REMARK 470 GLU A 603 CG CD OE1 OE2
REMARK 470 GLU A 606 CG CD OE1 OE2
REMARK 470 GLU A 646 CG CD OE1 OE2
REMARK 470 ARG A 647 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 673 CG CD OE1 OE2
REMARK 470 LYS A 697 CG CD CE NZ
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 PHE A 221 -168.22 -126.34
REMARK 500 ASN A 224 -161.77 69.13
REMARK 500 ARG A 240 -130.14 53.24
REMARK 500 SER A 284 74.23 -153.46
REMARK 500 ASP A 307 67.51 -155.79
REMARK 500 SER A 366 -122.31 58.30
REMARK 500 TYR A 479 -70.36 -122.25
REMARK 500 TYR A 482 18.87 58.99
REMARK 500 ARG A 524 -123.22 -125.95
REMARK 500 SER A 559 -108.12 47.12
REMARK 500 GLN A 632 -178.39 -173.13
REMARK 500 ASP A 713 -161.88 74.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7OBM RELATED DB: PDB
REMARK 900 RELATED ID: EMD-19117 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF THE R243C MUTANT OF HUMAN PROLYL ENDOPEPTIDASE-
REMARK 900 LIKE (PREPL) PROTEIN INVOLVED IN CONGENITAL MYASTHENIC SYNDROME-22
REMARK 900 (CMS22)
DBREF 8RFB A 90 727 UNP Q4J6C6 PPCEL_HUMAN 90 727
SEQADV 8RFB SER A 89 UNP Q4J6C6 EXPRESSION TAG
SEQADV 8RFB CYS A 243 UNP Q4J6C6 ARG 243 ENGINEERED MUTATION
SEQRES 1 A 639 SER MET ASP ALA PHE GLU LYS VAL ARG THR LYS LEU GLU
SEQRES 2 A 639 THR GLN PRO GLN GLU GLU TYR GLU ILE ILE ASN VAL GLU
SEQRES 3 A 639 VAL LYS HIS GLY GLY PHE VAL TYR TYR GLN GLU GLY CYS
SEQRES 4 A 639 CYS LEU VAL ARG SER LYS ASP GLU GLU ALA ASP ASN ASP
SEQRES 5 A 639 ASN TYR GLU VAL LEU PHE ASN LEU GLU GLU LEU LYS LEU
SEQRES 6 A 639 ASP GLN PRO PHE ILE ASP CYS ILE ARG VAL ALA PRO ASP
SEQRES 7 A 639 GLU LYS TYR VAL ALA ALA LYS ILE ARG THR GLU ASP SER
SEQRES 8 A 639 GLU ALA SER THR CYS VAL ILE ILE LYS LEU SER ASP GLN
SEQRES 9 A 639 PRO VAL MET GLU ALA SER PHE PRO ASN VAL SER SER PHE
SEQRES 10 A 639 GLU TRP VAL LYS ASP GLU GLU ASP GLU ASP VAL LEU PHE
SEQRES 11 A 639 TYR THR PHE GLN ARG ASN LEU ARG CYS HIS ASP VAL TYR
SEQRES 12 A 639 ARG ALA THR PHE GLY ASP ASN LYS ARG ASN GLU CYS PHE
SEQRES 13 A 639 TYR THR GLU LYS ASP PRO SER TYR PHE VAL PHE LEU TYR
SEQRES 14 A 639 LEU THR LYS ASP SER ARG PHE LEU THR ILE ASN ILE MET
SEQRES 15 A 639 ASN LYS THR THR SER GLU VAL TRP LEU ILE ASP GLY LEU
SEQRES 16 A 639 SER PRO TRP ASP PRO PRO VAL LEU ILE GLN LYS ARG ILE
SEQRES 17 A 639 HIS GLY VAL LEU TYR TYR VAL GLU HIS ARG ASP ASP GLU
SEQRES 18 A 639 LEU TYR ILE LEU THR ASN VAL GLY GLU PRO THR GLU PHE
SEQRES 19 A 639 LYS LEU MET ARG THR ALA ALA ASP THR PRO ALA ILE MET
SEQRES 20 A 639 ASN TRP ASP LEU PHE PHE THR MET LYS ARG ASN THR LYS
SEQRES 21 A 639 VAL ILE ASP LEU ASP MET PHE LYS ASP HIS CYS VAL LEU
SEQRES 22 A 639 PHE LEU LYS HIS SER ASN LEU LEU TYR VAL ASN VAL ILE
SEQRES 23 A 639 GLY LEU ALA ASP ASP SER VAL ARG SER LEU LYS LEU PRO
SEQRES 24 A 639 PRO TRP ALA CYS GLY PHE ILE MET ASP THR ASN SER ASP
SEQRES 25 A 639 PRO LYS ASN CYS PRO PHE GLN LEU CYS SER PRO ILE ARG
SEQRES 26 A 639 PRO PRO LYS TYR TYR THR TYR LYS PHE ALA GLU GLY LYS
SEQRES 27 A 639 LEU PHE GLU GLU THR GLY HIS GLU ASP PRO ILE THR LYS
SEQRES 28 A 639 THR SER ARG VAL LEU ARG LEU GLU ALA LYS SER LYS ASP
SEQRES 29 A 639 GLY LYS LEU VAL PRO MET THR VAL PHE HIS LYS THR ASP
SEQRES 30 A 639 SER GLU ASP LEU GLN LYS LYS PRO LEU LEU VAL HIS VAL
SEQRES 31 A 639 TYR GLY ALA TYR GLY MET ASP LEU LYS MET ASN PHE ARG
SEQRES 32 A 639 PRO GLU ARG ARG VAL LEU VAL ASP ASP GLY TRP ILE LEU
SEQRES 33 A 639 ALA TYR CYS HIS VAL ARG GLY GLY GLY GLU LEU GLY LEU
SEQRES 34 A 639 GLN TRP HIS ALA ASP GLY ARG LEU THR LYS LYS LEU ASN
SEQRES 35 A 639 GLY LEU ALA ASP LEU GLU ALA CYS ILE LYS THR LEU HIS
SEQRES 36 A 639 GLY GLN GLY PHE SER GLN PRO SER LEU THR THR LEU THR
SEQRES 37 A 639 ALA PHE SER ALA GLY GLY VAL LEU ALA GLY ALA LEU CYS
SEQRES 38 A 639 ASN SER ASN PRO GLU LEU VAL ARG ALA VAL THR LEU GLU
SEQRES 39 A 639 ALA PRO PHE LEU ASP VAL LEU ASN THR MET MET ASP THR
SEQRES 40 A 639 THR LEU PRO LEU THR LEU GLU GLU LEU GLU GLU TRP GLY
SEQRES 41 A 639 ASN PRO SER SER ASP GLU LYS HIS LYS ASN TYR ILE LYS
SEQRES 42 A 639 ARG TYR CYS PRO TYR GLN ASN ILE LYS PRO GLN HIS TYR
SEQRES 43 A 639 PRO SER ILE HIS ILE THR ALA TYR GLU ASN ASP GLU ARG
SEQRES 44 A 639 VAL PRO LEU LYS GLY ILE VAL SER TYR THR GLU LYS LEU
SEQRES 45 A 639 LYS GLU ALA ILE ALA GLU HIS ALA LYS ASP THR GLY GLU
SEQRES 46 A 639 GLY TYR GLN THR PRO ASN ILE ILE LEU ASP ILE GLN PRO
SEQRES 47 A 639 GLY GLY ASN HIS VAL ILE GLU ASP SER HIS LYS LYS ILE
SEQRES 48 A 639 THR ALA GLN ILE LYS PHE LEU TYR GLU GLU LEU GLY LEU
SEQRES 49 A 639 ASP SER THR SER VAL PHE GLU ASP LEU LYS LYS TYR LEU
SEQRES 50 A 639 LYS PHE
HELIX 1 AA1 GLU A 149 LYS A 152 5 4
HELIX 2 AA2 ALA A 333 TRP A 337 5 5
HELIX 3 AA3 PRO A 436 THR A 440 1 5
HELIX 4 AA4 ARG A 491 GLY A 501 1 11
HELIX 5 AA5 GLY A 516 ASP A 522 1 7
HELIX 6 AA6 LYS A 527 GLY A 546 1 20
HELIX 7 AA7 GLN A 549 SER A 551 5 3
HELIX 8 AA8 GLY A 561 ASN A 572 1 12
HELIX 9 AA9 PRO A 573 VAL A 576 5 4
HELIX 10 AB1 ASP A 587 MET A 593 1 7
HELIX 11 AB2 THR A 600 GLU A 605 1 6
HELIX 12 AB3 ASP A 613 CYS A 624 1 12
HELIX 13 AB4 PRO A 649 GLY A 672 1 24
HELIX 14 AB5 SER A 695 GLY A 711 1 17
SHEET 1 AA1 4 GLU A 114 HIS A 117 0
SHEET 2 AA1 4 PHE A 120 GLU A 125 -1 O TYR A 122 N VAL A 115
SHEET 3 AA1 4 CYS A 128 SER A 132 -1 O SER A 132 N VAL A 121
SHEET 4 AA1 4 TYR A 142 ASN A 147 -1 O GLU A 143 N ARG A 131
SHEET 1 AA2 4 PHE A 157 VAL A 163 0
SHEET 2 AA2 4 TYR A 169 ARG A 175 -1 O ARG A 175 N PHE A 157
SHEET 3 AA2 4 THR A 183 LYS A 188 -1 O VAL A 185 N ALA A 172
SHEET 4 AA2 4 MET A 195 PRO A 200 -1 O PHE A 199 N CYS A 184
SHEET 1 AA3 4 VAL A 202 LYS A 209 0
SHEET 2 AA3 4 ASP A 215 ARG A 223 -1 O PHE A 218 N GLU A 206
SHEET 3 AA3 4 CYS A 227 THR A 234 -1 O ALA A 233 N LEU A 217
SHEET 4 AA3 4 ARG A 240 THR A 246 -1 O PHE A 244 N VAL A 230
SHEET 1 AA4 4 PHE A 253 LEU A 258 0
SHEET 2 AA4 4 PHE A 264 MET A 270 -1 O THR A 266 N TYR A 257
SHEET 3 AA4 4 SER A 275 ASP A 281 -1 O TRP A 278 N ILE A 267
SHEET 4 AA4 4 VAL A 290 GLN A 293 -1 O VAL A 290 N LEU A 279
SHEET 1 AA5 4 TYR A 301 HIS A 305 0
SHEET 2 AA5 4 GLU A 309 THR A 314 -1 O TYR A 311 N GLU A 304
SHEET 3 AA5 4 LYS A 323 ALA A 328 -1 O MET A 325 N ILE A 312
SHEET 4 AA5 4 ASP A 338 THR A 342 -1 O PHE A 341 N LEU A 324
SHEET 1 AA6 4 LYS A 348 MET A 354 0
SHEET 2 AA6 4 HIS A 358 HIS A 365 -1 O LYS A 364 N LYS A 348
SHEET 3 AA6 4 LEU A 368 GLY A 375 -1 O ASN A 372 N LEU A 361
SHEET 4 AA6 4 VAL A 381 SER A 383 -1 O ARG A 382 N VAL A 373
SHEET 1 AA7 3 GLY A 392 MET A 395 0
SHEET 2 AA7 3 CYS A 404 SER A 410 -1 O GLN A 407 N ILE A 394
SHEET 3 AA7 3 ARG A 413 TYR A 420 -1 O TYR A 418 N PHE A 406
SHEET 1 AA8 8 SER A 441 ARG A 445 0
SHEET 2 AA8 8 MET A 458 LYS A 463 -1 O HIS A 462 N ARG A 442
SHEET 3 AA8 8 ILE A 503 CYS A 507 -1 O LEU A 504 N PHE A 461
SHEET 4 AA8 8 LEU A 474 VAL A 478 1 N LEU A 475 O ALA A 505
SHEET 5 AA8 8 THR A 553 PHE A 558 1 O THR A 554 N LEU A 474
SHEET 6 AA8 8 ALA A 578 GLU A 582 1 O THR A 580 N LEU A 555
SHEET 7 AA8 8 SER A 636 TYR A 642 1 O SER A 636 N VAL A 579
SHEET 8 AA8 8 ILE A 680 GLN A 685 1 O ILE A 681 N ILE A 639
SHEET 1 AA9 2 ALA A 448 LYS A 449 0
SHEET 2 AA9 2 LEU A 455 VAL A 456 -1 O VAL A 456 N ALA A 448
SSBOND 1 MET A 458 CYS A 538 1555 1555 2.10
SSBOND 2 CYS A 507 CYS A 538 1555 1555 2.67
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
TER 4633 ASP A 720
MASTER 239 0 0 14 37 0 0 6 4632 1 3 50
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