HEADER MEMBRANE PROTEIN 10-SEP-24 9DLF TITLE ARABINOSYLTRANSFERASE AFTB IN COMPLEX WITH FAB_B3 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ARABINOSYLTRANSFERASE AFTB; COMPND 3 CHAIN: C; COMPND 4 SYNONYM: TERMINAL BETA-(1->2)-ARABINOFURANOSYLTRANSFERASE; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: FAB_B3 LIGHT CHAIN; COMPND 8 CHAIN: A; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: FAB_B3 HEAVY CHAIN; COMPND 12 CHAIN: B; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MYCOLICIBACTERIUM CHUBUENSE; SOURCE 3 ORGANISM_TAXID: 1800; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_COMMON: HUMAN; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_COMMON: HUMAN; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ARABINOSYLTRANSFERASE, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR Y.LIU,F.MANCIA REVDAT 1 25-JUN-25 9DLF 0 JRNL AUTH Y.LIU,C.M.BROWN,N.BORGES,R.N.NOBRE,S.ERRAMILLI, JRNL AUTH 2 M.BELCHER DUFRISNE,B.KLOSS,S.GIACOMETTI,A.M.ESTEVES, JRNL AUTH 3 C.G.TIMOTEO,P.TOKARZ,R.J.CATER,T.L.LOWARY,Y.S.MORITA, JRNL AUTH 4 A.A.KOSSIAKOFF,H.SANTOS,P.J.STANSFELD,R.NYGAARD,F.MANCIA JRNL TITL MECHANISTIC STUDIES OF MYCOBACTERIAL GLYCOLIPID BIOSYNTHESIS JRNL TITL 2 BY THE MANNOSYLTRANSFERASE PIME. JRNL REF NAT COMMUN V. 16 3974 2025 JRNL REFN ESSN 2041-1723 JRNL PMID 40301322 JRNL DOI 10.1038/S41467-025-57843-1 REMARK 2 REMARK 2 RESOLUTION. 2.85 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 : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.850 REMARK 3 NUMBER OF PARTICLES : 192312 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9DLF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1000288322. 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 : ARABINOSYLTRANSFERASE AFTB IN REMARK 245 COMPLEX WITH FAB_B3 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00 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) : 5800.00 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 C 1 REMARK 465 PRO C 2 REMARK 465 GLN C 3 REMARK 465 SER C 4 REMARK 465 SER C 5 REMARK 465 SER C 6 REMARK 465 ALA C 7 REMARK 465 ASP C 8 REMARK 465 ARG C 9 REMARK 465 LEU C 10 REMARK 465 SER C 11 REMARK 465 ARG C 12 REMARK 465 PRO C 13 REMARK 465 PHE C 14 REMARK 465 THR C 15 REMARK 465 GLU C 16 REMARK 465 ALA C 17 REMARK 465 ALA C 18 REMARK 465 ALA C 19 REMARK 465 THR C 20 REMARK 465 ARG C 21 REMARK 465 LEU C 22 REMARK 465 ASN C 23 REMARK 465 ARG C 24 REMARK 465 TRP C 25 REMARK 465 PRO C 26 REMARK 465 ALA C 27 REMARK 465 PHE C 28 REMARK 465 SER C 323 REMARK 465 TRP C 324 REMARK 465 GLY C 325 REMARK 465 ASP C 326 REMARK 465 ARG C 327 REMARK 465 GLY C 328 REMARK 465 ALA C 329 REMARK 465 ARG C 330 REMARK 465 LYS C 331 REMARK 465 GLU C 332 REMARK 465 SER C 333 REMARK 465 GLY C 334 REMARK 465 PRO C 658 REMARK 465 PRO C 659 REMARK 465 TYR C 660 REMARK 465 THR C 661 REMARK 465 GLY C 662 REMARK 465 LEU C 663 REMARK 465 PRO C 664 REMARK 465 PRO C 665 REMARK 465 THR C 666 REMARK 465 GLY C 667 REMARK 465 PRO C 668 REMARK 465 ALA C 669 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 VAL C 359 CG1 CG2 REMARK 470 VAL C 498 CG1 CG2 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 CD2 LEU C 137 O17 6OU C 701 1.95 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 THR C 93 -11.15 69.38 REMARK 500 ARG C 400 -111.09 57.22 REMARK 500 ASN C 426 56.24 -95.64 REMARK 500 ALA C 432 49.85 -86.63 REMARK 500 ARG C 494 -167.65 -105.68 REMARK 500 ASP C 506 -3.06 73.13 REMARK 500 ARG C 634 56.49 -96.58 REMARK 500 ALA A 51 -9.51 68.77 REMARK 500 GLU B 89 30.15 -91.72 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-46976 RELATED DB: EMDB REMARK 900 ARABINOSYLTRANSFERASE AFTB IN COMPLEX WITH FAB_B3 DBREF1 9DLF C 1 668 UNP A0A0J6VB96_MYCCU DBREF2 9DLF C A0A0J6VB96 1 668 DBREF 9DLF A 0 108 PDB 9DLF 9DLF 0 108 DBREF 9DLF B 1 126 PDB 9DLF 9DLF 1 126 SEQADV 9DLF ALA C 669 UNP A0A0J6VB9 EXPRESSION TAG SEQRES 1 C 669 MET PRO GLN SER SER SER ALA ASP ARG LEU SER ARG PRO SEQRES 2 C 669 PHE THR GLU ALA ALA ALA THR ARG LEU ASN ARG TRP PRO SEQRES 3 C 669 ALA PHE PRO TYR HIS VAL TRP VAL ARG VAL SER LEU TRP SEQRES 4 C 669 VAL SER VAL VAL THR VAL ALA ALA LEU PHE GLY TRP GLY SEQRES 5 C 669 ALA TRP GLN ARG ARG TRP ILE ALA ASP ASP GLY LEU ILE SEQRES 6 C 669 VAL LEU ARG THR VAL ARG ASN LEU LEU ALA GLY ASN GLY SEQRES 7 C 669 PRO VAL PHE ASN ALA GLY GLU ARG VAL GLU ALA ASN THR SEQRES 8 C 669 SER THR VAL TRP SER TYR LEU VAL THR LEU GLY GLY PHE SEQRES 9 C 669 VAL ALA GLY SER ALA ARG LEU GLU TYR VAL ALA LEU VAL SEQRES 10 C 669 LEU ALA LEU THR LEU SER VAL LEU GLY VAL VAL LEU VAL SEQRES 11 C 669 MET PHE GLY THR ALA ARG LEU TYR ALA PRO GLY LEU THR SEQRES 12 C 669 GLY ARG ARG ALA VAL PHE LEU PRO ALA GLY ALA LEU VAL SEQRES 13 C 669 TYR ILE ALA ILE PRO PRO ALA ARG ASP PHE ALA THR SER SEQRES 14 C 669 GLY LEU GLU ASN GLY LEU VAL LEU ALA TYR LEU GLY LEU SEQRES 15 C 669 LEU TRP TRP MET MET VAL CYS TRP SER GLN GLY LEU ARG SEQRES 16 C 669 ARG PRO ASP GLY GLU ARG THR SER ARG GLY PHE ASP ALA SEQRES 17 C 669 THR LEU ALA VAL VAL ALA GLY MET SER VAL LEU VAL ARG SEQRES 18 C 669 PRO GLU LEU ALA LEU ILE GLY GLY LEU ALA LEU VAL MET SEQRES 19 C 669 MET LEU VAL ALA ALA PRO THR TRP ARG ARG ARG LEU ALA SEQRES 20 C 669 LEU VAL VAL VAL GLY GLY LEU ILE PRO VAL ALA TYR GLN SEQRES 21 C 669 ILE PHE ARG MET GLY TYR TYR GLY LEU LEU VAL PRO GLY SEQRES 22 C 669 THR ALA LEU ALA LYS ASP ALA SER GLY ALA LYS TRP ASP SEQRES 23 C 669 GLN GLY LEU VAL TYR LEU ALA ASN PHE ASN GLN PRO TYR SEQRES 24 C 669 LEU LEU TRP ALA PRO ALA VAL LEU LEU ILE GLY LEU GLY SEQRES 25 C 669 LEU MET VAL LEU LEU LEU ARG GLY ARG PRO SER TRP GLY SEQRES 26 C 669 ASP ARG GLY ALA ARG LYS GLU SER GLY TRP ILE ALA ARG SEQRES 27 C 669 THR VAL GLN SER PRO PRO ALA VAL VAL ALA PHE MET LEU SEQRES 28 C 669 ILE SER GLY LEU LEU GLN ALA VAL TYR TRP ILE ARG GLN SEQRES 29 C 669 GLY GLY ASP PHE MET HIS GLY ARG VAL LEU LEU THR PRO SEQRES 30 C 669 LEU PHE CYS LEU LEU ALA PRO VAL ALA VAL ILE PRO LEU SEQRES 31 C 669 LEU LEU PRO ASP ARG SER ARG MET ALA ARG GLY ALA GLY SEQRES 32 C 669 TYR LEU TYR ALA GLY ALA THR ALA VAL LEU TRP LEU ALA SEQRES 33 C 669 VAL ALA GLY TRP ALA LEU TRP ALA ALA ASN SER PRO GLY SEQRES 34 C 669 MET GLY ALA ASP ALA THR ARG VAL THR TYR SER GLY ILE SEQRES 35 C 669 VAL ASP GLU ARG ARG PHE TYR SER GLN ALA THR GLY HIS SEQRES 36 C 669 ALA HIS PRO LEU THR ALA ALA ASP TYR LEU ASP TYR PRO SEQRES 37 C 669 ARG MET ARG ALA VAL LEU THR ALA ILE GLU ASN THR PRO SEQRES 38 C 669 ASP GLY ALA LEU LEU LEU PRO SER GLY ASP TYR ASP ARG SEQRES 39 C 669 TRP ASP VAL VAL PRO ALA LEU PRO PRO PRO PRO ASP VAL SEQRES 40 C 669 ARG ALA ALA ALA VAL GLY GLY TYR VAL GLY PRO HIS THR SEQRES 41 C 669 VAL PHE PHE THR ASN LEU GLY MET LEU GLY MET ASN VAL SEQRES 42 C 669 GLY LEU ASP VAL ARG VAL ILE ASP GLN ILE GLY LEU ALA SEQRES 43 C 669 ASN PRO LEU ALA ALA HIS THR ALA ARG LEU THR ASP GLY SEQRES 44 C 669 ARG ILE GLY HIS ASP LYS ASN LEU PHE PRO ASP TRP ALA SEQRES 45 C 669 VAL ALA GLU GLY PRO PHE LEU LYS GLU PRO PRO TRP ILE SEQRES 46 C 669 PRO GLN TYR LEU ASP GLU ASP TRP ILE ARG GLN ALA GLU SEQRES 47 C 669 ALA ALA LEU LYS CYS PRO GLU THR ASP LYS VAL LEU ASP SEQRES 48 C 669 ALA ILE ARG ALA PRO MET GLY PHE ARG ARG PHE LEU SER SEQRES 49 C 669 ASN VAL MET HIS ALA ALA GLU TYR THR ARG TYR ARG ILE SEQRES 50 C 669 ASP ARG VAL PRO LEU TYR GLU LEU ALA ARG CYS GLY LEU SEQRES 51 C 669 PRO VAL PRO GLU PRO VAL ASP PRO PRO TYR THR GLY LEU SEQRES 52 C 669 PRO PRO THR GLY PRO ALA SEQRES 1 A 109 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 A 109 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 A 109 GLN SER VAL SER SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 A 109 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 A 109 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 A 109 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 A 109 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 A 109 SER PRO PRO TYR GLY PRO ILE THR PHE GLY GLN GLY THR SEQRES 9 A 109 LYS VAL GLU LEU LYS SEQRES 1 B 126 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 126 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 126 PHE ASN VAL SER SER SER TYR ILE HIS TRP VAL ARG GLN SEQRES 4 B 126 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SER ILE SER SEQRES 5 B 126 SER TYR TYR GLY TYR THR SER TYR ALA ASP SER VAL LYS SEQRES 6 B 126 GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR SEQRES 7 B 126 ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 B 126 ALA VAL TYR TYR CYS ALA ARG GLY TYR MET TYR SER HIS SEQRES 9 B 126 TRP VAL TYR SER TYR GLY ALA ILE ASP TYR TRP GLY GLN SEQRES 10 B 126 GLY THR LEU VAL THR VAL SER SER ALA HET 6OU C 701 49 HETNAM 6OU [(2~{R})-1-[2-AZANYLETHOXY(OXIDANYL)PHOSPHORYL]OXY-3- HETNAM 2 6OU HEXADECANOYLOXY-PROPAN-2-YL] (~{Z})-OCTADEC-9-ENOATE FORMUL 4 6OU C39 H76 N O8 P HELIX 1 AA1 HIS C 31 GLN C 55 1 25 HELIX 2 AA2 ASP C 62 ALA C 75 1 14 HELIX 3 AA3 VAL C 94 ALA C 106 1 13 HELIX 4 AA4 LEU C 111 ALA C 139 1 29 HELIX 5 AA5 PRO C 140 THR C 143 5 4 HELIX 6 AA6 ALA C 152 ILE C 160 1 9 HELIX 7 AA7 ILE C 160 PHE C 166 1 7 HELIX 8 AA8 GLU C 172 GLY C 193 1 22 HELIX 9 AA9 SER C 203 MET C 216 1 14 HELIX 10 AB1 MET C 216 ARG C 221 1 6 HELIX 11 AB2 LEU C 224 ALA C 239 1 16 HELIX 12 AB3 THR C 241 GLY C 253 1 13 HELIX 13 AB4 GLY C 253 GLY C 268 1 16 HELIX 14 AB5 GLY C 273 LYS C 278 1 6 HELIX 15 AB6 LYS C 284 GLN C 297 1 14 HELIX 16 AB7 LEU C 301 GLY C 320 1 20 HELIX 17 AB8 ILE C 336 GLN C 341 1 6 HELIX 18 AB9 SER C 342 GLY C 365 1 24 HELIX 19 AC1 GLY C 371 VAL C 373 5 3 HELIX 20 AC2 LEU C 374 LEU C 382 1 9 HELIX 21 AC3 ALA C 383 VAL C 385 5 3 HELIX 22 AC4 ARG C 400 ASN C 426 1 27 HELIX 23 AC5 ASP C 444 THR C 453 1 10 HELIX 24 AC6 ALA C 462 TYR C 467 5 6 HELIX 25 AC7 MET C 470 ASN C 479 1 10 HELIX 26 AC8 LEU C 526 GLY C 534 1 9 HELIX 27 AC9 LEU C 549 THR C 553 5 5 HELIX 28 AD1 PHE C 568 GLU C 575 1 8 HELIX 29 AD2 GLU C 581 ILE C 585 5 5 HELIX 30 AD3 ASP C 590 LEU C 601 1 12 HELIX 31 AD4 CYS C 603 ILE C 613 1 11 HELIX 32 AD5 GLY C 618 HIS C 628 1 11 HELIX 33 AD6 HIS C 628 ARG C 634 1 7 HELIX 34 AD7 VAL C 640 GLY C 649 1 10 HELIX 35 AD8 GLN A 79 PHE A 83 5 5 SHEET 1 AA1 2 ALA C 147 PRO C 151 0 SHEET 2 AA1 2 VAL C 387 LEU C 391 -1 O ILE C 388 N LEU C 150 SHEET 1 AA2 4 TRP C 495 PRO C 499 0 SHEET 2 AA2 4 ALA C 484 PRO C 488 -1 N LEU C 487 O ASP C 496 SHEET 3 AA2 4 HIS C 519 PHE C 522 1 O PHE C 522 N LEU C 486 SHEET 4 AA2 4 ARG C 538 ILE C 540 1 O ARG C 538 N VAL C 521 SHEET 1 AA3 4 THR A 4 SER A 6 0 SHEET 2 AA3 4 ARG A 17 ARG A 23 -1 O ARG A 23 N THR A 4 SHEET 3 AA3 4 ASP A 70 SER A 76 -1 O LEU A 73 N ILE A 20 SHEET 4 AA3 4 PHE A 62 SER A 67 -1 N SER A 67 O ASP A 70 SHEET 1 AA4 6 SER A 9 ALA A 12 0 SHEET 2 AA4 6 THR A 103 LEU A 107 1 O LYS A 104 N LEU A 10 SHEET 3 AA4 6 THR A 85 GLN A 90 -1 N TYR A 86 O THR A 103 SHEET 4 AA4 6 ALA A 34 GLN A 38 -1 N GLN A 38 O THR A 85 SHEET 5 AA4 6 LYS A 45 TYR A 49 -1 O LYS A 45 N GLN A 37 SHEET 6 AA4 6 SER A 53 LEU A 54 -1 O SER A 53 N TYR A 49 SHEET 1 AA5 4 SER A 9 ALA A 12 0 SHEET 2 AA5 4 THR A 103 LEU A 107 1 O LYS A 104 N LEU A 10 SHEET 3 AA5 4 THR A 85 GLN A 90 -1 N TYR A 86 O THR A 103 SHEET 4 AA5 4 THR A 98 PHE A 99 -1 O THR A 98 N GLN A 90 SHEET 1 AA6 4 GLN B 3 SER B 7 0 SHEET 2 AA6 4 GLY B 16 SER B 25 -1 O ALA B 23 N VAL B 5 SHEET 3 AA6 4 THR B 78 LEU B 86 -1 O LEU B 86 N GLY B 16 SHEET 4 AA6 4 PHE B 68 ASP B 73 -1 N THR B 69 O GLN B 82 SHEET 1 AA7 5 TYR B 57 TYR B 60 0 SHEET 2 AA7 5 LEU B 45 SER B 52 -1 N SER B 52 O TYR B 57 SHEET 3 AA7 5 ILE B 34 GLN B 39 -1 N TRP B 36 O VAL B 48 SHEET 4 AA7 5 ALA B 92 MET B 101 -1 O TYR B 95 N VAL B 37 SHEET 5 AA7 5 SER B 108 TRP B 115 -1 O ASP B 113 N ARG B 98 SHEET 1 AA8 5 TYR B 57 TYR B 60 0 SHEET 2 AA8 5 LEU B 45 SER B 52 -1 N SER B 52 O TYR B 57 SHEET 3 AA8 5 ILE B 34 GLN B 39 -1 N TRP B 36 O VAL B 48 SHEET 4 AA8 5 ALA B 92 MET B 101 -1 O TYR B 95 N VAL B 37 SHEET 5 AA8 5 THR B 119 VAL B 121 -1 O VAL B 121 N ALA B 92 SSBOND 1 CYS A 22 CYS A 88 1555 1555 2.04 CISPEP 1 SER A 6 PRO A 7 0 -3.22 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