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HEADER HYDROLASE 29-NOV-24 9HJJ
TITLE STRUCTURE OF TRYPANOSOMA CRUZI PROLYL OLIGOPEPTIDASE IN THE CLOSE
TITLE 2 STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL ENDOPEPTIDASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.21.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA CRUZI;
SOURCE 3 ORGANISM_TAXID: 5693;
SOURCE 4 GENE: TCPO;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ANTIGEN, CHAGAS DISEASE, PROLYL OLIGOPEPTIDASE, HYDROLASE
EXPDTA ELECTRON MICROSCOPY
AUTHOR S.BATRA,T.J.RAGAN,E.HESKETH,I.CAMPEOTTO
REVDAT 1 01-OCT-25 9HJJ 0
JRNL AUTH S.BATRA,F.OLMO,T.J.RAGAN,M.KAPLAN,V.CALVARESI,A.M.FRANK,
JRNL AUTH 2 C.LANCEY,M.ASSADIPAPARI,C.YING,W.B.STRUWE,E.L.HESKETH,
JRNL AUTH 3 J.M.KELLY,L.BARFOD,I.CAMPEOTTO
JRNL TITL CRYO-EM LED ANALYSIS OF OPEN AND CLOSED CONFORMATIONS OF
JRNL TITL 2 CHAGAS VACCINE CANDIDATE TCPOP.
JRNL REF NAT COMMUN V. 16 7164 2025
JRNL REFN ESSN 2041-1723
JRNL PMID 40764299
JRNL DOI 10.1038/S41467-025-62068-3
REMARK 2
REMARK 2 RESOLUTION. 3.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : PHENIX
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : 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) : 3.820
REMARK 3 NUMBER OF PARTICLES : 126459
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: DYNAMIGHT
REMARK 4
REMARK 4 9HJJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-NOV-24.
REMARK 100 THE DEPOSITION ID IS D_1292143379.
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 : TRYPANOSOMA CRUZI PROLYL
REMARK 245 OLIGOPEPTIDASE
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 : 7.40
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 : TFS KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 800.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2400.00
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) : 3694.00
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 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 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 LEU A -7
REMARK 465 VAL A -6
REMARK 465 PRO A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
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 29 30.91 -98.32
REMARK 500 HIS A 180 -128.50 34.90
REMARK 500 ARG A 188 -175.40 -172.02
REMARK 500 ALA A 191 -2.80 70.43
REMARK 500 GLN A 193 38.77 39.29
REMARK 500 ASP A 195 -163.34 -79.84
REMARK 500 VAL A 196 -72.97 72.05
REMARK 500 ALA A 200 -2.32 67.88
REMARK 500 ALA A 204 -9.09 72.89
REMARK 500 HIS A 231 70.76 -114.91
REMARK 500 ASP A 308 23.28 48.29
REMARK 500 ALA A 309 94.15 -161.51
REMARK 500 LYS A 312 65.74 61.48
REMARK 500 ILE A 327 -63.57 -90.89
REMARK 500 SER A 333 -168.44 -126.21
REMARK 500 LYS A 342 -106.41 48.34
REMARK 500 ASP A 352 51.44 38.74
REMARK 500 ARG A 361 -166.67 -78.19
REMARK 500 PRO A 371 49.01 -86.75
REMARK 500 PHE A 396 -70.65 -62.59
REMARK 500 LEU A 397 55.52 -97.11
REMARK 500 LEU A 398 77.79 -153.97
REMARK 500 VAL A 427 -71.97 70.40
REMARK 500 ASN A 471 19.53 58.32
REMARK 500 ARG A 514 -123.05 51.47
REMARK 500 THR A 541 117.19 -161.22
REMARK 500 SER A 548 -119.42 55.05
REMARK 500 THR A 584 -154.92 47.47
REMARK 500 TRP A 589 33.45 -96.07
REMARK 500 PRO A 656 -152.79 -83.28
REMARK 500 ALA A 664 -164.26 -163.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-52216 RELATED DB: EMDB
REMARK 900 STRUCTURE OF TRYPANOSOMA CRUZI PROLYL OLIGOPEPTIDASE IN THE CLOSE
REMARK 900 STATE
DBREF 9HJJ A 1 697 UNP Q71MD6 Q71MD6_TRYCR 1 697
SEQADV 9HJJ HIS A -16 UNP Q71MD6 EXPRESSION TAG
SEQADV 9HJJ HIS A -15 UNP Q71MD6 EXPRESSION TAG
SEQADV 9HJJ HIS A -14 UNP Q71MD6 EXPRESSION TAG
SEQADV 9HJJ HIS A -13 UNP Q71MD6 EXPRESSION TAG
SEQADV 9HJJ HIS A -12 UNP Q71MD6 EXPRESSION TAG
SEQADV 9HJJ HIS A -11 UNP Q71MD6 EXPRESSION TAG
SEQADV 9HJJ SER A -10 UNP Q71MD6 EXPRESSION TAG
SEQADV 9HJJ SER A -9 UNP Q71MD6 EXPRESSION TAG
SEQADV 9HJJ GLY A -8 UNP Q71MD6 EXPRESSION TAG
SEQADV 9HJJ LEU A -7 UNP Q71MD6 EXPRESSION TAG
SEQADV 9HJJ VAL A -6 UNP Q71MD6 EXPRESSION TAG
SEQADV 9HJJ PRO A -5 UNP Q71MD6 EXPRESSION TAG
SEQADV 9HJJ ARG A -4 UNP Q71MD6 EXPRESSION TAG
SEQADV 9HJJ GLY A -3 UNP Q71MD6 EXPRESSION TAG
SEQADV 9HJJ SER A -2 UNP Q71MD6 EXPRESSION TAG
SEQADV 9HJJ HIS A -1 UNP Q71MD6 EXPRESSION TAG
SEQADV 9HJJ MET A 0 UNP Q71MD6 EXPRESSION TAG
SEQRES 1 A 714 HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO ARG
SEQRES 2 A 714 GLY SER HIS MET MET ARG SER VAL TYR PRO LEU ALA ARG
SEQRES 3 A 714 ARG SER MET ALA ALA TYR THR MET HIS ASN MET THR VAL
SEQRES 4 A 714 PRO GLU PRO TYR ASP TYR LEU GLU ASP PRO GLU ASN PRO
SEQRES 5 A 714 GLU THR LYS THR PHE VAL ASN GLU GLN ASN ALA PHE PHE
SEQRES 6 A 714 GLU GLU TYR PHE ALA SER GLU ALA GLU LEU ARG LYS LYS
SEQRES 7 A 714 ILE PHE GLU SER ILE SER ASN SER GLN ASP TYR PRO ARG
SEQRES 8 A 714 THR SER ASN PRO SER TYR ILE ASN GLY HIS TYR TYR TYR
SEQRES 9 A 714 TYR HIS ASN SER GLY LEU GLN ASN GLN SER VAL LEU MET
SEQRES 10 A 714 ARG ALA MET SER LEU THR ASP THR ALA PRO SER ILE PHE
SEQRES 11 A 714 LEU ASP PRO ASN SER MET SER SER ASP GLY THR THR ALA
SEQRES 12 A 714 LEU LYS ALA THR ALA TRP SER GLU ASP GLU SER MET LEU
SEQRES 13 A 714 ALA TYR SER LEU SER ASP LYS GLY SER ASP TRP GLN ARG
SEQRES 14 A 714 ILE HIS VAL ARG ARG ALA ASP THR VAL GLU ASP THR SER
SEQRES 15 A 714 ASP VAL ILE GLU TRP ALA LYS PHE THR ALA ILE ALA TRP
SEQRES 16 A 714 TRP HIS ASN LEU GLY PHE PHE TYR THR ARG TYR PRO ALA
SEQRES 17 A 714 LEU GLN GLY ASP VAL ASP LYS GLY ALA GLU THR ASP ALA
SEQRES 18 A 714 ALA GLN ASP ALA PHE ILE CYS PHE HIS ARG ILE GLY ARG
SEQRES 19 A 714 PRO GLN ASP GLU ASP VAL VAL ILE LEU SER VAL PRO GLU
SEQRES 20 A 714 HIS PRO GLN TRP ASN MET GLY ALA SER VAL SER ASP CYS
SEQRES 21 A 714 HIS SER TYR VAL ILE VAL VAL LEU PHE ASP GLY CYS GLU
SEQRES 22 A 714 PRO HIS ASN LEU VAL TRP VAL ALA GLU LEU PRO SER VAL
SEQRES 23 A 714 GLU LYS GLY LEU GLY SER GLU PRO LEU VAL PHE LYS LYS
SEQRES 24 A 714 LEU VAL ASN GLU PHE ALA GLY ARG TYR THR TYR LEU GLY
SEQRES 25 A 714 ASN GLU GLY SER THR PHE TYR PHE VAL THR THR ARG ASP
SEQRES 26 A 714 ALA PRO ARG LYS LYS ILE VAL SER ILE ASP ILE HIS THR
SEQRES 27 A 714 GLY GLN GLU THR VAL ILE VAL GLU GLN GLN ARG SER VAL
SEQRES 28 A 714 LEU SER GLN ALA ALA LEU VAL LYS LYS THR LEU LEU LEU
SEQRES 29 A 714 ALA TYR LEU GLU ASP VAL LYS ASP VAL PHE TYR TYR CYS
SEQRES 30 A 714 ARG LEU GLU ASP PRO THR LEU ASN ALA ILE PRO LEU PRO
SEQRES 31 A 714 ILE GLY THR ILE THR SER PHE PHE SER ASP ARG LYS LYS
SEQRES 32 A 714 ASP PHE VAL SER PHE LYS ILE THR SER PHE LEU LEU PRO
SEQRES 33 A 714 GLY ARG SER PHE PHE LEU ASP ILE ASN ASP PRO GLN SER
SEQRES 34 A 714 SER LEU ARG VAL PHE LYS ASP ASP THR VAL GLU GLY LEU
SEQRES 35 A 714 LEU VAL ASP ASP PHE VAL THR GLU GLN THR PHE TYR ASN
SEQRES 36 A 714 SER SER ASP GLY VAL ARG ILE PRO MET PHE ILE VAL TYR
SEQRES 37 A 714 ARG LYS GLY SER VAL SER SER GLU SER PRO LEU LEU LEU
SEQRES 38 A 714 TYR GLY TYR GLY GLY PHE ASN ILE PRO LEU THR PRO ALA
SEQRES 39 A 714 PHE SER SER SER ARG MET VAL PHE LEU ARG ASP LEU GLY
SEQRES 40 A 714 GLY VAL LEU ALA VAL LEU ASN ILE ARG GLY GLY GLY GLU
SEQRES 41 A 714 TYR GLY GLU GLU TRP HIS ASP ALA GLY ARG ARG ALA CYS
SEQRES 42 A 714 LYS GLN ASN CYS PHE THR ASP PHE ILE GLU GLY ALA LYS
SEQRES 43 A 714 PHE LEU HIS ARG GLN GLY TYR GLY SER PRO GLN THR THR
SEQRES 44 A 714 ALA ILE MET GLY GLY SER ASN GLY GLY LEU LEU VAL ALA
SEQRES 45 A 714 ALA VAL ALA ASN GLN ALA PRO GLU LEU PHE ARG CYS VAL
SEQRES 46 A 714 VAL CYS ARG VAL GLY VAL LEU ASP MET TYR LYS PHE HIS
SEQRES 47 A 714 LYS PHE THR ILE GLY HIS ALA TRP LYS SER ASP TYR GLY
SEQRES 48 A 714 ASP PRO GLU LYS GLU GLU ASP PHE ARG VAL LEU GLN GLN
SEQRES 49 A 714 TYR SER PRO LEU HIS ASN ILE LYS SER GLY ILE LYS TYR
SEQRES 50 A 714 PRO ALA ILE LEU VAL VAL THR GLY ASP HIS ASP ASP ARG
SEQRES 51 A 714 VAL VAL PRO LEU HIS SER LEU LYS TYR VAL ALA THR LEU
SEQRES 52 A 714 GLN HIS MET ASN PRO ASN GLU GLY GLY PRO PHE LEU ALA
SEQRES 53 A 714 ARG ILE GLU VAL ALA ALA GLY HIS GLY ALA GLY LYS PRO
SEQRES 54 A 714 THR SER LYS ILE LEU ARG GLU ALA GLY ASP ILE TYR THR
SEQRES 55 A 714 PHE ILE ALA LYS ASN ILE ASN ALA SER TRP LYS GLU
HELIX 1 AA1 TYR A 26 ASP A 31 5 6
HELIX 2 AA2 ASN A 34 ALA A 53 1 20
HELIX 3 AA3 GLU A 55 ASN A 68 1 14
HELIX 4 AA4 TYR A 189 GLY A 194 5 6
HELIX 5 AA5 GLY A 199 ASP A 203 5 5
HELIX 6 AA6 SER A 268 GLY A 272 5 5
HELIX 7 AA7 ASP A 409 LEU A 414 1 6
HELIX 8 AA8 SER A 479 LEU A 489 1 11
HELIX 9 AA9 GLY A 505 GLY A 512 1 8
HELIX 10 AB1 ARG A 513 CYS A 516 5 4
HELIX 11 AB2 LYS A 517 GLY A 535 1 19
HELIX 12 AB3 SER A 548 ALA A 561 1 14
HELIX 13 AB4 PHE A 583 LYS A 590 5 8
HELIX 14 AB5 LYS A 598 GLN A 606 1 9
HELIX 15 AB6 GLN A 607 TYR A 608 5 2
HELIX 16 AB7 SER A 609 ASN A 613 5 5
HELIX 17 AB8 PRO A 636 HIS A 648 1 13
HELIX 18 AB9 PRO A 672 ILE A 691 1 20
SHEET 1 AA1 2 THR A 16 MET A 17 0
SHEET 2 AA1 2 MET A 20 THR A 21 -1 N MET A 20 O MET A 17
SHEET 1 AA2 4 SER A 79 ILE A 81 0
SHEET 2 AA2 4 HIS A 84 HIS A 89 -1 O TYR A 86 N SER A 79
SHEET 3 AA2 4 VAL A 98 ALA A 102 -1 O VAL A 98 N HIS A 89
SHEET 4 AA2 4 SER A 111 LEU A 114 -1 O LEU A 114 N LEU A 99
SHEET 1 AA3 2 ALA A 126 LEU A 127 0
SHEET 2 AA3 2 LEU A 143 SER A 144 -1 O SER A 144 N ALA A 126
SHEET 1 AA4 4 ALA A 177 TRP A 179 0
SHEET 2 AA4 4 GLY A 183 ARG A 188 -1 O GLY A 183 N TRP A 179
SHEET 3 AA4 4 PHE A 209 ARG A 214 -1 O CYS A 211 N TYR A 186
SHEET 4 AA4 4 VAL A 224 SER A 227 -1 O LEU A 226 N ILE A 210
SHEET 1 AA5 3 ASN A 235 VAL A 240 0
SHEET 2 AA5 3 VAL A 247 PHE A 252 -1 O ILE A 248 N SER A 239
SHEET 3 AA5 3 ASN A 259 ALA A 264 -1 O TRP A 262 N VAL A 249
SHEET 1 AA6 4 TYR A 291 GLU A 297 0
SHEET 2 AA6 4 THR A 300 THR A 305 -1 O VAL A 304 N THR A 292
SHEET 3 AA6 4 LYS A 313 ASP A 318 -1 O LYS A 313 N THR A 305
SHEET 4 AA6 4 VAL A 326 VAL A 328 -1 O VAL A 328 N ILE A 314
SHEET 1 AA7 4 LEU A 335 VAL A 341 0
SHEET 2 AA7 4 THR A 344 LEU A 350 -1 O THR A 344 N VAL A 341
SHEET 3 AA7 4 ASP A 355 CYS A 360 -1 O CYS A 360 N LEU A 345
SHEET 4 AA7 4 ASN A 368 ALA A 369 -1 O ASN A 368 N TYR A 359
SHEET 1 AA8 4 THR A 376 SER A 382 0
SHEET 2 AA8 4 VAL A 389 SER A 395 -1 O THR A 394 N THR A 376
SHEET 3 AA8 4 LEU A 398 LEU A 405 -1 O ARG A 401 N ILE A 393
SHEET 4 AA8 4 ARG A 415 ASP A 419 -1 O LYS A 418 N SER A 402
SHEET 1 AA9 8 PHE A 430 TYR A 437 0
SHEET 2 AA9 8 ILE A 445 ARG A 452 -1 O TYR A 451 N VAL A 431
SHEET 3 AA9 8 VAL A 492 LEU A 496 -1 O VAL A 495 N PHE A 448
SHEET 4 AA9 8 LEU A 462 TYR A 465 1 N LEU A 463 O ALA A 494
SHEET 5 AA9 8 ALA A 543 GLY A 547 1 O ALA A 543 N LEU A 462
SHEET 6 AA9 8 CYS A 567 ARG A 571 1 O VAL A 569 N ILE A 544
SHEET 7 AA9 8 ALA A 622 GLY A 628 1 O ALA A 622 N VAL A 568
SHEET 8 AA9 8 PHE A 657 LEU A 658 1 O LEU A 658 N VAL A 625
SHEET 1 AB1 8 PHE A 430 TYR A 437 0
SHEET 2 AB1 8 ILE A 445 ARG A 452 -1 O TYR A 451 N VAL A 431
SHEET 3 AB1 8 VAL A 492 LEU A 496 -1 O VAL A 495 N PHE A 448
SHEET 4 AB1 8 LEU A 462 TYR A 465 1 N LEU A 463 O ALA A 494
SHEET 5 AB1 8 ALA A 543 GLY A 547 1 O ALA A 543 N LEU A 462
SHEET 6 AB1 8 CYS A 567 ARG A 571 1 O VAL A 569 N ILE A 544
SHEET 7 AB1 8 ALA A 622 GLY A 628 1 O ALA A 622 N VAL A 568
SHEET 8 AB1 8 ILE A 661 GLU A 662 1 O GLU A 662 N THR A 627
CISPEP 1 GLY A 655 PRO A 656 0 -3.05
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 5533 GLU A 697
MASTER 173 0 0 18 43 0 0 6 5532 1 0 55
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