HEADER IMMUNE SYSTEM 02-MAY-22 7UVL TITLE IGA1 PROTEASE WITH IGA1 SUBSTRATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: LPXTG-MOTIF CELL WALL ANCHOR DOMAIN PROTEIN; COMPND 3 CHAIN: P; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: IMMUNOGLOBULIN ALPHA-1 HEAVY CONSTANT; COMPND 8 CHAIN: B, A; COMPND 9 SYNONYM: IG ALPHA-1 CHAIN C REGION,IG ALPHA-1 CHAIN C REGION BUR,IG COMPND 10 ALPHA-1 CHAIN C REGION TRO; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: IMMUNOGLOBULIN ALPHA-1 LIGHT CHAIN; COMPND 14 CHAIN: L; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: IMMUNOGLOBULIN ALPHA-1 HEAVY CHAIN; COMPND 18 CHAIN: H; COMPND 19 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GEMELLA HAEMOLYSANS; SOURCE 3 ORGANISM_TAXID: 1379; SOURCE 4 GENE: GEMHA0001_0491; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 GENE: IGHA1; SOURCE 12 EXPRESSION_SYSTEM: MUS SP.; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 10095; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM: MUS SP.; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 10095; SOURCE 19 MOL_ID: 4; SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 21 ORGANISM_TAXID: 9606; SOURCE 22 EXPRESSION_SYSTEM: MUS SP.; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 10095 KEYWDS COMPLEX, IMMUNE SYSTEM EXPDTA ELECTRON MICROSCOPY AUTHOR Z.E.EISENMESSER,H.ZHENG JRNL AUTH J.S.REDZIC,J.RAHKOLA,N.TRAN,T.HOLYOAK,E.LEE, JRNL AUTH 2 A.J.MARTIN-GALIANO,N.MEYER,H.ZHENG,E.EISENMESSER JRNL TITL A SUBSTRATE-INDUCED GATING MECHANISM IS CONSERVED AMONG JRNL TITL 2 GRAM-POSITIVE IGA1 METALLOPROTEASES. JRNL REF COMMUN BIOL V. 5 1190 2022 JRNL REFN ESSN 2399-3642 JRNL PMID 36336763 JRNL DOI 10.1038/S42003-022-04173-3 REMARK 2 REMARK 2 RESOLUTION. 3.56 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL 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) : 3.560 REMARK 3 NUMBER OF PARTICLES : 205808 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 7UVL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000264977. 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 : IGA1 PROTEASE WITH IGA1 REMARK 245 SUBSTRATE 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 K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 5000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : OTHER REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 49.00 REMARK 245 ILLUMINATION MODE : OTHER REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : OTHER 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, B, A, L, H 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 LYS P 1298 REMARK 465 VAL P 1299 REMARK 465 VAL P 1300 REMARK 465 GLN P 1301 REMARK 465 VAL P 1302 REMARK 465 ASP P 1303 REMARK 465 ASP P 1304 REMARK 465 GLU P 1305 REMARK 465 VAL P 1306 REMARK 465 LEU P 1307 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 ARG P 980 CG CD NE CZ NH1 NH2 REMARK 470 LYS P 981 CG CD CE NZ REMARK 470 ASP P 985 CG OD1 OD2 REMARK 470 ARG B 245 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 254 CG CD OE1 OE2 REMARK 470 SER B 260 OG REMARK 470 GLU B 261 CG CD OE1 OE2 REMARK 470 LEU B 271 CG CD1 CD2 REMARK 470 ARG B 272 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 273 CG OD1 OD2 REMARK 470 SER B 275 OG REMARK 470 LYS B 287 CG CD CE NZ REMARK 470 GLU B 295 CG CD OE1 OE2 REMARK 470 ARG B 296 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 297 CG OD1 OD2 REMARK 470 LEU B 298 CG CD1 CD2 REMARK 470 CYS B 301 SG REMARK 470 TYR B 302 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 CYS B 311 SG REMARK 470 GLU B 313 CG CD OE1 OE2 REMARK 470 HIS B 317 CG ND1 CD2 CE1 NE2 REMARK 470 LYS B 319 CG CD CE NZ REMARK 470 GLU B 329 CG CD OE1 OE2 REMARK 470 SER B 330 OG REMARK 470 LYS B 331 CG CD CE NZ REMARK 470 LEU B 338 CG CD1 CD2 REMARK 470 SER B 339 OG REMARK 470 SER B 341 OG REMARK 470 ARG B 346 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 357 CG CD OE1 OE2 REMARK 470 GLU B 358 CG CD OE1 OE2 REMARK 470 LEU B 359 CG CD1 CD2 REMARK 470 LEU B 361 CG CD1 CD2 REMARK 470 ASN B 362 CG OD1 ND2 REMARK 470 GLU B 363 CG CD OE1 OE2 REMARK 470 LYS B 377 CG CD CE NZ REMARK 470 GLN B 388 CG CD OE1 NE2 REMARK 470 ARG B 392 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 393 CG CD OE1 OE2 REMARK 470 LYS B 394 CG CD CE NZ REMARK 470 SER B 405 OG REMARK 470 GLN B 406 CG CD OE1 NE2 REMARK 470 GLU B 422 CG CD OE1 OE2 REMARK 470 LYS B 425 CG CD CE NZ REMARK 470 LYS B 426 CG CD CE NZ REMARK 470 ASP B 428 CG OD1 OD2 REMARK 470 LYS B 446 CG CD CE NZ REMARK 470 ARG B 450 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 245 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 254 CG CD OE1 OE2 REMARK 470 SER A 260 OG REMARK 470 GLU A 261 CG CD OE1 OE2 REMARK 470 LEU A 271 CG CD1 CD2 REMARK 470 ARG A 272 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 273 CG OD1 OD2 REMARK 470 SER A 275 OG REMARK 470 LYS A 287 CG CD CE NZ REMARK 470 GLU A 295 CG CD OE1 OE2 REMARK 470 ARG A 296 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 297 CG OD1 OD2 REMARK 470 LEU A 298 CG CD1 CD2 REMARK 470 CYS A 301 SG REMARK 470 TYR A 302 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 CYS A 311 SG REMARK 470 GLU A 313 CG CD OE1 OE2 REMARK 470 HIS A 317 CG ND1 CD2 CE1 NE2 REMARK 470 LYS A 319 CG CD CE NZ REMARK 470 GLU A 329 CG CD OE1 OE2 REMARK 470 SER A 330 OG REMARK 470 LYS A 331 CG CD CE NZ REMARK 470 LEU A 338 CG CD1 CD2 REMARK 470 SER A 339 OG REMARK 470 SER A 341 OG REMARK 470 ARG A 346 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 357 CG CD OE1 OE2 REMARK 470 GLU A 358 CG CD OE1 OE2 REMARK 470 LEU A 359 CG CD1 CD2 REMARK 470 LEU A 361 CG CD1 CD2 REMARK 470 ASN A 362 CG OD1 ND2 REMARK 470 GLU A 363 CG CD OE1 OE2 REMARK 470 LYS A 377 CG CD CE NZ REMARK 470 GLN A 388 CG CD OE1 NE2 REMARK 470 ARG A 392 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 393 CG CD OE1 OE2 REMARK 470 LYS A 394 CG CD CE NZ REMARK 470 SER A 405 OG REMARK 470 GLN A 406 CG CD OE1 NE2 REMARK 470 GLU A 422 CG CD OE1 OE2 REMARK 470 LYS A 425 CG CD CE NZ REMARK 470 LYS A 426 CG CD CE NZ REMARK 470 ASP A 428 CG OD1 OD2 REMARK 470 LYS A 446 CG CD CE NZ REMARK 470 ARG A 450 CG CD NE CZ NH1 NH2 REMARK 470 ARG L 32 CD NE CZ NH1 NH2 REMARK 470 LYS L 174 CG CD CE NZ REMARK 470 GLU H 1 CG CD OE1 OE2 REMARK 470 ASN H 54 CG OD1 ND2 REMARK 470 GLU H 56 CD OE1 OE2 REMARK 470 SER H 57 OG 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 OH TYR P 1172 O ASN P 1200 2.16 REMARK 500 O VAL P 2059 OG SER P 2063 2.18 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 SER P 946 -168.70 -160.11 REMARK 500 ALA P 956 33.64 -98.38 REMARK 500 ASP P 995 13.91 -140.10 REMARK 500 THR P1024 -62.09 -95.64 REMARK 500 ASN P1083 62.51 60.92 REMARK 500 SER P1157 145.73 -170.50 REMARK 500 ASN P1202 -117.06 60.58 REMARK 500 GLU P1250 -165.48 -79.71 REMARK 500 ILE P1275 -62.47 -107.52 REMARK 500 LYS P1338 115.93 -161.98 REMARK 500 PHE P1344 -7.29 73.29 REMARK 500 LYS P1406 50.73 38.16 REMARK 500 ASN P1462 54.27 -92.20 REMARK 500 ASP P1570 -133.58 56.53 REMARK 500 LYS P1622 -3.92 68.48 REMARK 500 LEU P1641 70.22 58.66 REMARK 500 GLU P1678 -4.12 72.31 REMARK 500 PRO P1690 -173.73 -68.60 REMARK 500 GLU P1767 15.29 59.26 REMARK 500 PHE P1797 14.05 55.74 REMARK 500 ILE P1857 -63.98 -98.48 REMARK 500 ALA P1874 -61.99 -91.20 REMARK 500 LEU P1906 15.72 55.28 REMARK 500 PRO P1966 44.51 -77.48 REMARK 500 ASP P2038 -64.04 -94.64 REMARK 500 MET P2058 -70.26 63.44 REMARK 500 LYS P2099 10.30 -140.01 REMARK 500 THR P2141 59.76 37.23 REMARK 500 ASP P2192 -165.85 -78.06 REMARK 500 ARG P2194 -125.43 54.70 REMARK 500 LEU B 257 -61.07 -94.69 REMARK 500 LEU A 257 -60.54 -94.85 REMARK 500 ALA A 274 -169.94 -77.78 REMARK 500 PRO A 283 52.97 -90.00 REMARK 500 LEU L 55 -2.97 70.20 REMARK 500 ASN L 143 60.08 37.07 REMARK 500 VAL H 48 -62.57 -123.09 REMARK 500 PRO H 155 127.88 -37.70 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLU H 154 PRO H 155 -147.42 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-26813 RELATED DB: EMDB REMARK 900 IGA1 PROTEASE WITH IGA1 SUBSTRATE DBREF 7UVL P 907 2201 UNP C5NYF3 C5NYF3_9BACL 884 2178 DBREF 7UVL B 242 450 UNP P01876 IGHA1_HUMAN 123 331 DBREF 7UVL A 242 450 UNP P01876 IGHA1_HUMAN 123 331 DBREF 7UVL L 1 219 PDB 7UVL 7UVL 1 219 DBREF 7UVL H 1 232 PDB 7UVL 7UVL 1 232 SEQADV 7UVL ALA P 1848 UNP C5NYF3 GLU 1825 ENGINEERED MUTATION SEQRES 1 P 1295 ASP GLU LYS LYS ASP ASP ILE LYS GLU GLU LYS GLN VAL SEQRES 2 P 1295 ASP LYS LYS LEU GLU LEU ARG ASN ILE SER ASN VAL GLU SEQRES 3 P 1295 LEU TYR THR LEU GLU ASN ASN LYS TYR ARG HIS VAL SER SEQRES 4 P 1295 SER LEU SER SER VAL PRO THR ASN PRO GLU ALA TYR PHE SEQRES 5 P 1295 MET LYS VAL LYS SER GLU ASN PHE LYS ASP VAL MET LEU SEQRES 6 P 1295 PRO VAL LYS SER ILE GLU SER ALA ARG LYS ASP ASN GLN SEQRES 7 P 1295 ASP VAL TYR LYS ILE VAL GLY GLN ALA ASN ASP LEU ILE SEQRES 8 P 1295 GLN HIS GLU ASN ASN ILE THR LEU GLU ASN TYR THR TYR SEQRES 9 P 1295 TYR LEU PRO LYS THR VAL ASN SER GLU ASN GLY VAL TYR SEQRES 10 P 1295 THR SER PHE LYS ASN LEU VAL ASP ALA MET ASN ILE ASN SEQRES 11 P 1295 PRO TYR GLY THR PHE ARG LEU GLY ALA THR MET ASP ALA SEQRES 12 P 1295 ARG GLU VAL GLU LEU SER ASP GLY GLN GLU SER TYR ILE SEQRES 13 P 1295 ASN LYS GLU PHE SER GLY LYS LEU ILE GLY GLU ASN LYS SEQRES 14 P 1295 GLY LYS TYR TYR ALA ILE TYR ASN LEU LYS LYS PRO LEU SEQRES 15 P 1295 PHE LYS ALA LEU SER HIS ALA THR ILE GLN ASP LEU SER SEQRES 16 P 1295 ILE LYS GLU ALA ASN VAL SER SER LYS GLU ASP ALA ALA SEQRES 17 P 1295 THR ILE ALA LYS GLU ALA LYS ASN ASP THR THR ILE ALA SEQRES 18 P 1295 ASN VAL HIS SER SER GLY VAL ILE ALA GLY GLU ARG SER SEQRES 19 P 1295 ILE GLY GLY LEU ILE SER GLN VAL THR ASP SER THR ILE SEQRES 20 P 1295 SER ASN SER SER PHE THR GLY ARG ILE THR ASN THR TYR SEQRES 21 P 1295 ASP THR THR ALA THR TYR GLN ILE GLY GLY LEU VAL GLY SEQRES 22 P 1295 LYS LEU SER GLY VAL GLY ALA LEU ILE GLU LYS SER ILE SEQRES 23 P 1295 SER SER ILE ASP MET ALA THR ASN ALA ASN THR GLY ASP SEQRES 24 P 1295 GLN VAL VAL GLY GLY VAL ALA GLY VAL VAL ASP LYS LYS SEQRES 25 P 1295 ALA THR ILE ARG ASN SER TYR VAL GLU GLY ASN LEU ASN SEQRES 26 P 1295 ASN VAL LYS PRO PHE GLY LYS VAL GLY GLY VAL VAL GLY SEQRES 27 P 1295 ASN LEU TRP ASP ARG GLU THR SER GLU VAL SER ASN SER SEQRES 28 P 1295 GLY ASN LEU THR ASN VAL LEU SER ASP VAL ASN VAL THR SEQRES 29 P 1295 ASN GLY ASN ALA ILE ALA GLY TYR ASP PHE ASN GLY ILE SEQRES 30 P 1295 LYS ALA THR ASN THR TYR SER ASN LYS ASN ASN LYS VAL SEQRES 31 P 1295 VAL LYS VAL VAL GLN VAL ASP ASP GLU VAL LEU SER LYS SEQRES 32 P 1295 ASP SER GLU GLU GLN ARG GLY THR VAL LEU GLU ASN ASN SEQRES 33 P 1295 ILE VAL LEU GLU LYS LYS ILE GLU LEU VAL PRO LYS LYS SEQRES 34 P 1295 ASN THR LYS ILE GLU ASP PHE ASN PHE SER SER ARG TYR SEQRES 35 P 1295 GLU THR ASP TYR LYS ASN LEU LYS ASP ALA ASP VAL SER SEQRES 36 P 1295 ARG LEU ARG VAL TYR LYS ASN ILE GLU LYS LEU LEU PRO SEQRES 37 P 1295 PHE TYR ASN ARG GLU THR ILE VAL LYS TYR GLY ASN LEU SEQRES 38 P 1295 VAL ASP ALA ASN ASN THR LEU TYR THR LYS ASP LEU VAL SEQRES 39 P 1295 SER VAL VAL PRO MET LYS ASP LYS GLU VAL ILE SER ASP SEQRES 40 P 1295 ILE ASN LYS ASN LYS THR SER ILE ASN LYS LEU LEU LEU SEQRES 41 P 1295 HIS TYR SER ASP ASN THR SER GLN THR LEU ASP ILE LYS SEQRES 42 P 1295 TYR LEU GLN ASP PHE SER LYS VAL ALA GLU TYR GLU ILE SEQRES 43 P 1295 ALA ASN THR LYS LEU ILE TYR THR PRO ASN THR LEU LEU SEQRES 44 P 1295 HIS SER TYR ASN ASN ILE VAL LYS ALA VAL LEU ASN ASP SEQRES 45 P 1295 LEU LYS SER VAL GLN TYR ASP SER ASP ALA VAL ARG LYS SEQRES 46 P 1295 VAL LEU ASP ILE SER SER ASN ILE LYS LEU THR GLU LEU SEQRES 47 P 1295 TYR LEU ASP GLU GLN PHE THR LYS THR LYS ALA ASN ILE SEQRES 48 P 1295 GLU ASP SER LEU SER LYS LEU LEU SER ALA ASP ALA VAL SEQRES 49 P 1295 ILE ALA GLU ASN SER ASN SER ILE ILE ASP ASN TYR VAL SEQRES 50 P 1295 ILE GLU LYS ILE LYS ASN ASN LYS GLU ALA LEU LEU LEU SEQRES 51 P 1295 GLY LEU THR TYR LEU GLU ARG TRP TYR ASN PHE LYS TYR SEQRES 52 P 1295 ASP ASN THR SER ALA LYS ASP LEU VAL LEU TYR HIS LEU SEQRES 53 P 1295 ASP PHE PHE GLY LYS SER ASN SER SER ALA LEU ASP ASN SEQRES 54 P 1295 VAL ILE GLU LEU GLY LYS SER GLY PHE ASN ASN LEU LEU SEQRES 55 P 1295 ALA LYS ASN ASN VAL ILE THR TYR ASN VAL LEU LEU SER SEQRES 56 P 1295 LYS ASN TYR GLY THR GLU GLY LEU PHE LYS ALA LEU GLU SEQRES 57 P 1295 GLY TYR ARG LYS VAL PHE LEU PRO ASN VAL SER ASN ASN SEQRES 58 P 1295 ASP TRP PHE LYS THR GLN SER LYS ALA TYR ILE VAL GLU SEQRES 59 P 1295 GLU LYS SER THR ILE PRO GLU VAL SER SER LYS GLN SER SEQRES 60 P 1295 LYS GLN GLY THR GLU HIS SER ILE GLY VAL TYR ASP ARG SEQRES 61 P 1295 LEU THR SER PRO SER TRP LYS TYR GLN SER MET VAL LEU SEQRES 62 P 1295 PRO LEU LEU THR LEU PRO GLU GLU LYS MET ILE PHE MET SEQRES 63 P 1295 ILE ALA ASN ILE SER THR ILE GLY PHE GLY ALA TYR ASP SEQRES 64 P 1295 ARG TYR ARG SER SER GLU TYR PRO LYS GLY ASP LYS LEU SEQRES 65 P 1295 ASN ARG PHE VAL GLU GLU ASN ALA GLN ALA ALA ALA LYS SEQRES 66 P 1295 ARG PHE ARG ASP HIS TYR ASP TYR TRP TYR LYS ILE LEU SEQRES 67 P 1295 ASP LYS GLU ASN LYS GLU LYS LEU PHE ARG SER VAL LEU SEQRES 68 P 1295 VAL TYR ASP ALA PHE ARG PHE GLY ASN ASP THR ASN LYS SEQRES 69 P 1295 GLU THR GLN GLU ALA ASN PHE GLU THR ASN ASN PRO VAL SEQRES 70 P 1295 ILE LYS ASN PHE PHE GLY PRO ALA GLY ASN ASN VAL VAL SEQRES 71 P 1295 HIS ASN LYS HIS GLY ALA TYR ALA THR GLY ASP ALA PHE SEQRES 72 P 1295 TYR TYR MET ALA TYR ARG MET LEU ASP LYS SER GLY ALA SEQRES 73 P 1295 VAL THR TYR THR HIS ALA MET THR HIS ASN SER ASP ARG SEQRES 74 P 1295 GLU ILE TYR LEU GLY GLY TYR GLY ARG ARG SER GLY LEU SEQRES 75 P 1295 GLY PRO GLU PHE TYR ALA LYS GLY LEU LEU GLN ALA PRO SEQRES 76 P 1295 ASP HIS SER TYR ASP PRO THR ILE THR ILE ASN SER VAL SEQRES 77 P 1295 LEU LYS TYR ASP ASP SER GLU ASN SER THR ARG LEU GLN SEQRES 78 P 1295 ILE ALA ASP PRO THR GLN ARG PHE THR ASN VAL GLU ASP SEQRES 79 P 1295 LEU HIS ASN TYR MET HIS ASN MET PHE ASP LEU ILE TYR SEQRES 80 P 1295 THR LEU GLU ILE LEU GLU GLY ARG ALA VAL ALA LYS LEU SEQRES 81 P 1295 ASP TYR ASN GLU LYS ASN ASP LEU LEU ARG LYS ILE GLU SEQRES 82 P 1295 ASN ILE TYR LYS LYS ASP PRO ASP GLY ASN SER VAL TYR SEQRES 83 P 1295 ALA THR ASN ALA VAL ARG ARG LEU THR SER ASP GLU ILE SEQRES 84 P 1295 LYS ASN LEU THR SER PHE ASP LYS LEU ILE GLU ASN ASP SEQRES 85 P 1295 VAL ILE THR ARG ARG GLY TYR ILE ASP GLN GLY GLU TYR SEQRES 86 P 1295 GLU ARG ASN GLY TYR HIS THR ILE ASN LEU PHE SER PRO SEQRES 87 P 1295 ILE TYR SER ALA LEU SER SER LYS ILE GLY THR PRO GLY SEQRES 88 P 1295 ASP LEU MET GLY ARG ARG MET ALA PHE GLU LEU LEU ALA SEQRES 89 P 1295 ALA LYS GLY TYR LYS GLU GLY MET VAL PRO TYR ILE SER SEQRES 90 P 1295 ASN GLN TYR GLU LYS GLU ALA LYS ASP ARG GLY SER LYS SEQRES 91 P 1295 ILE ARG SER TYR GLY LYS GLU ILE GLY LEU VAL THR ASP SEQRES 92 P 1295 ASP LEU VAL LEU GLU LYS VAL PHE ASN LYS LYS TYR GLY SEQRES 93 P 1295 SER TRP VAL GLU PHE LYS LYS ASP MET TYR LYS GLU ARG SEQRES 94 P 1295 VAL GLU GLN PHE SER LYS LEU ASN ARG VAL SER PHE PHE SEQRES 95 P 1295 ASP PRO ASN GLY PRO TRP GLY ARG GLN LYS ASN VAL THR SEQRES 96 P 1295 VAL ASN ASN ILE SER VAL LEU GLU LYS MET ILE GLU THR SEQRES 97 P 1295 ALA VAL ARG GLU ASP ALA GLU ASP PHE THR ALA GLN VAL SEQRES 98 P 1295 TYR PRO ASP THR ASN SER ARG VAL LEU LYS LEU LYS LYS SEQRES 99 P 1295 ALA ILE PHE LYS ALA TYR LEU ASP GLN THR LYS ASP PHE SEQRES 100 P 1295 ARG THR SER ILE PHE GLY GLY LYS SEQRES 1 B 209 CYS HIS PRO ARG LEU SER LEU HIS ARG PRO ALA LEU GLU SEQRES 2 B 209 ASP LEU LEU LEU GLY SER GLU ALA ASN LEU THR CYS THR SEQRES 3 B 209 LEU THR GLY LEU ARG ASP ALA SER GLY VAL THR PHE THR SEQRES 4 B 209 TRP THR PRO SER SER GLY LYS SER ALA VAL GLN GLY PRO SEQRES 5 B 209 PRO GLU ARG ASP LEU CYS GLY CYS TYR SER VAL SER SER SEQRES 6 B 209 VAL LEU PRO GLY CYS ALA GLU PRO TRP ASN HIS GLY LYS SEQRES 7 B 209 THR PHE THR CYS THR ALA ALA TYR PRO GLU SER LYS THR SEQRES 8 B 209 PRO LEU THR ALA THR LEU SER LYS SER GLY ASN THR PHE SEQRES 9 B 209 ARG PRO GLU VAL HIS LEU LEU PRO PRO PRO SER GLU GLU SEQRES 10 B 209 LEU ALA LEU ASN GLU LEU VAL THR LEU THR CYS LEU ALA SEQRES 11 B 209 ARG GLY PHE SER PRO LYS ASP VAL LEU VAL ARG TRP LEU SEQRES 12 B 209 GLN GLY SER GLN GLU LEU PRO ARG GLU LYS TYR LEU THR SEQRES 13 B 209 TRP ALA SER ARG GLN GLU PRO SER GLN GLY THR THR THR SEQRES 14 B 209 PHE ALA VAL THR SER ILE LEU ARG VAL ALA ALA GLU ASP SEQRES 15 B 209 TRP LYS LYS GLY ASP THR PHE SER CYS MET VAL GLY HIS SEQRES 16 B 209 GLU ALA LEU PRO LEU ALA PHE THR GLN LYS THR ILE ASP SEQRES 17 B 209 ARG SEQRES 1 A 209 CYS HIS PRO ARG LEU SER LEU HIS ARG PRO ALA LEU GLU SEQRES 2 A 209 ASP LEU LEU LEU GLY SER GLU ALA ASN LEU THR CYS THR SEQRES 3 A 209 LEU THR GLY LEU ARG ASP ALA SER GLY VAL THR PHE THR SEQRES 4 A 209 TRP THR PRO SER SER GLY LYS SER ALA VAL GLN GLY PRO SEQRES 5 A 209 PRO GLU ARG ASP LEU CYS GLY CYS TYR SER VAL SER SER SEQRES 6 A 209 VAL LEU PRO GLY CYS ALA GLU PRO TRP ASN HIS GLY LYS SEQRES 7 A 209 THR PHE THR CYS THR ALA ALA TYR PRO GLU SER LYS THR SEQRES 8 A 209 PRO LEU THR ALA THR LEU SER LYS SER GLY ASN THR PHE SEQRES 9 A 209 ARG PRO GLU VAL HIS LEU LEU PRO PRO PRO SER GLU GLU SEQRES 10 A 209 LEU ALA LEU ASN GLU LEU VAL THR LEU THR CYS LEU ALA SEQRES 11 A 209 ARG GLY PHE SER PRO LYS ASP VAL LEU VAL ARG TRP LEU SEQRES 12 A 209 GLN GLY SER GLN GLU LEU PRO ARG GLU LYS TYR LEU THR SEQRES 13 A 209 TRP ALA SER ARG GLN GLU PRO SER GLN GLY THR THR THR SEQRES 14 A 209 PHE ALA VAL THR SER ILE LEU ARG VAL ALA ALA GLU ASP SEQRES 15 A 209 TRP LYS LYS GLY ASP THR PHE SER CYS MET VAL GLY HIS SEQRES 16 A 209 GLU ALA LEU PRO LEU ALA PHE THR GLN LYS THR ILE ASP SEQRES 17 A 209 ARG SEQRES 1 L 219 ASP ILE VAL MET THR GLN SER PRO LEU SER LEU SER VAL SEQRES 2 L 219 THR PRO GLY GLU PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 L 219 GLN SER LEU LEU ARG ARG ASP GLY HIS ASN ASP LEU GLU SEQRES 4 L 219 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN PRO LEU SEQRES 5 L 219 ILE TYR LEU GLY SER THR ARG ALA SER GLY VAL PRO ASP SEQRES 6 L 219 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 219 LYS ILE ILE ARG VAL GLU ALA GLU ASP ALA GLY THR TYR SEQRES 8 L 219 TYR CYS MET GLN ASN LYS GLN THR PRO LEU THR PHE GLY SEQRES 9 L 219 GLN GLY THR ARG LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 L 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 L 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 L 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 L 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 L 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 L 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 L 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 L 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 H 232 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 232 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 H 232 PHE THR LEU SER GLY SER ASN VAL HIS TRP VAL ARG GLN SEQRES 4 H 232 ALA SER GLY LYS GLY LEU GLU TRP VAL GLY ARG ILE LYS SEQRES 5 H 232 ARG ASN ALA GLU SER ASP ALA THR ALA TYR ALA ALA SER SEQRES 6 H 232 MET ARG GLY ARG LEU THR ILE SER ARG ASP ASP SER LYS SEQRES 7 H 232 ASN THR ALA PHE LEU GLN MET ASN SER LEU LYS SER ASP SEQRES 8 H 232 ASP THR ALA MET TYR TYR CYS VAL ILE ARG GLY ASP VAL SEQRES 9 H 232 TYR ASN ARG GLN TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10 H 232 SER SER ALA SER PRO THR SER PRO LYS VAL PHE PRO LEU SEQRES 11 H 232 SER LEU CYS SER THR GLN PRO ASP GLY ASN VAL VAL ILE SEQRES 12 H 232 ALA CYS LEU VAL GLN GLY PHE PHE PRO GLN GLU PRO LEU SEQRES 13 H 232 SER VAL THR TRP SER GLU SER GLY GLN GLY VAL THR ALA SEQRES 14 H 232 ARG ASN PHE PRO PRO SER GLN ASP ALA SER GLY ASP LEU SEQRES 15 H 232 TYR THR THR SER SER GLN LEU THR LEU PRO ALA THR GLN SEQRES 16 H 232 CYS LEU ALA GLY LYS SER VAL THR CYS HIS VAL LYS HIS SEQRES 17 H 232 TYR THR ASN PRO SER GLN ASP VAL THR VAL PRO CYS PRO SEQRES 18 H 232 VAL PRO SER THR PRO PRO THR PRO SER PRO SER HELIX 1 AA1 SER P 1025 ASN P 1036 1 12 HELIX 2 AA2 VAL P 1332 ASN P 1336 5 5 HELIX 3 AA3 ARG P 1362 LEU P 1373 1 12 HELIX 4 AA4 ASN P 1377 LEU P 1387 1 11 HELIX 5 AA5 ASN P 1392 THR P 1396 5 5 HELIX 6 AA6 SER P 1412 ASN P 1417 1 6 HELIX 7 AA7 TYR P 1468 SER P 1481 1 14 HELIX 8 AA8 SER P 1486 LEU P 1493 1 8 HELIX 9 AA9 LEU P 1506 ASN P 1516 1 11 HELIX 10 AB1 ASN P 1516 ALA P 1529 1 14 HELIX 11 AB2 SER P 1537 ASN P 1550 1 14 HELIX 12 AB3 ASN P 1550 TYR P 1565 1 16 HELIX 13 AB4 ALA P 1574 TYR P 1580 1 7 HELIX 14 AB5 HIS P 1581 PHE P 1585 5 5 HELIX 15 AB6 SER P 1591 LYS P 1601 1 11 HELIX 16 AB7 GLY P 1603 LEU P 1608 1 6 HELIX 17 AB8 ASN P 1611 LEU P 1619 1 9 HELIX 18 AB9 GLY P 1628 PHE P 1640 1 13 HELIX 19 AC1 SER P 1645 SER P 1654 1 10 HELIX 20 AC2 ILE P 1665 LYS P 1674 1 10 HELIX 21 AC3 GLY P 1682 SER P 1689 1 8 HELIX 22 AC4 TYR P 1694 LEU P 1699 5 6 HELIX 23 AC5 TYR P 1724 ARG P 1728 1 5 HELIX 24 AC6 GLY P 1735 LEU P 1764 1 30 HELIX 25 AC7 ASN P 1768 ARG P 1774 5 7 HELIX 26 AC8 ASN P 1801 PHE P 1807 1 7 HELIX 27 AC9 ASP P 1838 SER P 1853 1 16 HELIX 28 AD1 ASP P 1910 PHE P 1915 1 6 HELIX 29 AD2 ASN P 1917 LYS P 1945 1 29 HELIX 30 AD3 ASP P 1947 LEU P 1954 1 8 HELIX 31 AD4 THR P 1981 LEU P 1988 1 8 HELIX 32 AD5 SER P 1990 ASP P 1998 1 9 HELIX 33 AD6 ASP P 2038 LYS P 2052 1 15 HELIX 34 AD7 TYR P 2066 GLY P 2074 1 9 HELIX 35 AD8 THR P 2088 PHE P 2097 1 10 HELIX 36 AD9 SER P 2103 LEU P 2122 1 20 HELIX 37 AE1 ASN P 2144 ALA P 2160 1 17 HELIX 38 AE2 SER P 2173 THR P 2190 1 18 HELIX 39 AE3 ALA B 252 LEU B 258 1 7 HELIX 40 AE4 LEU B 298 GLY B 300 5 3 HELIX 41 AE5 CYS B 311 HIS B 317 1 7 HELIX 42 AE6 PRO B 355 ASN B 362 1 8 HELIX 43 AE7 PRO B 391 GLU B 393 5 3 HELIX 44 AE8 ALA B 420 GLY B 427 1 8 HELIX 45 AE9 ALA A 252 LEU A 258 1 7 HELIX 46 AF1 LEU A 298 GLY A 300 5 3 HELIX 47 AF2 CYS A 311 GLY A 318 1 8 HELIX 48 AF3 PRO A 355 ASN A 362 1 8 HELIX 49 AF4 PRO A 391 TYR A 395 5 5 HELIX 50 AF5 ALA A 420 GLY A 427 1 8 HELIX 51 AF6 SER L 126 SER L 132 1 7 HELIX 52 AF7 LYS L 188 HIS L 194 1 7 HELIX 53 AF8 LYS H 89 THR H 93 5 5 HELIX 54 AF9 ALA H 193 ALA H 198 1 6 SHEET 1 AA1 8 ILE P 928 VAL P 931 0 SHEET 2 AA1 8 TYR P 934 THR P 935 0 SHEET 3 AA1 8 ARG P 942 HIS P 943 -1 O ARG P 942 N THR P 935 SHEET 4 AA1 8 TYR P 957 SER P 963 -1 O PHE P 958 N TYR P 934 SHEET 5 AA1 8 VAL P 969 ALA P 979 -1 O LEU P 971 N MET P 959 SHEET 6 AA1 8 VAL P 986 GLY P 991 -1 O LYS P 988 N GLU P 977 SHEET 7 AA1 8 THR P1009 LEU P1012 -1 O LEU P1012 N TYR P 987 SHEET 8 AA1 8 VAL P1530 ILE P1531 1 O VAL P1530 N MET P 970 SHEET 1 AA2 2 GLN P 998 GLU P1000 0 SHEET 2 AA2 2 ILE P1003 LEU P1005 -1 O LEU P1005 N GLN P 998 SHEET 1 AA315 THR P1040 ARG P1042 0 SHEET 2 AA315 LEU P1070 GLY P1072 1 O LEU P1070 N PHE P1041 SHEET 3 AA315 THR P1096 GLN P1098 1 O GLN P1098 N ILE P1071 SHEET 4 AA315 SER P1101 ILE P1102 0 SHEET 5 AA315 SER P1108 SER P1109 0 SHEET 6 AA315 THR P1125 ALA P1127 1 O ALA P1127 N ILE P1097 SHEET 7 AA315 HIS P1130 GLY P1137 1 O ALA P1136 N SER P1109 SHEET 8 AA315 THR P1152 ASN P1164 1 O ARG P1161 N ILE P1135 SHEET 9 AA315 LEU P1187 THR P1199 1 O ASP P1196 N GLY P1160 SHEET 10 AA315 THR P1220 ARG P1222 1 O ARG P1222 N LYS P1190 SHEET 11 AA315 TYR P1225 VAL P1226 1 O TYR P1225 N SER P1193 SHEET 12 AA315 LEU P1230 ASN P1232 1 O ASN P1231 N THR P1199 SHEET 13 AA315 ASN P1259 THR P1261 1 O THR P1261 N ILE P1221 SHEET 14 AA315 VAL P1263 SER P1265 1 O LEU P1264 N VAL P1226 SHEET 15 AA315 THR P1288 SER P1290 1 O TYR P1289 N VAL P1263 SHEET 1 AA4 2 MET P1047 ASP P1048 0 SHEET 2 AA4 2 ILE P1081 TYR P1082 1 O TYR P1082 N MET P1047 SHEET 1 AA5 6 LEU P1092 SER P1093 0 SHEET 2 AA5 6 ALA P1117 ASN P1122 1 O LYS P1121 N LEU P1092 SHEET 3 AA5 6 ILE P1145 VAL P1148 1 O GLN P1147 N LYS P1118 SHEET 4 AA5 6 VAL P1178 SER P1182 1 O LYS P1180 N VAL P1148 SHEET 5 AA5 6 ALA P1212 ASP P1216 1 O ASP P1216 N LEU P1181 SHEET 6 AA5 6 VAL P1243 ASN P1245 1 O ASN P1245 N VAL P1215 SHEET 1 AA6 2 ASP P1112 ALA P1114 0 SHEET 2 AA6 2 SER P1140 GLY P1142 1 O SER P1140 N ALA P1113 SHEET 1 AA7 3 GLN P1173 GLY P1175 0 SHEET 2 AA7 3 VAL P1207 GLY P1209 1 O VAL P1207 N ILE P1174 SHEET 3 AA7 3 LYS P1238 GLY P1240 1 O GLY P1240 N VAL P1208 SHEET 1 AA8 3 ASP P1398 VAL P1402 0 SHEET 2 AA8 3 LEU P1425 TYR P1428 -1 O HIS P1427 N LEU P1399 SHEET 3 AA8 3 SER P1433 GLN P1434 -1 O GLN P1434 N LEU P1426 SHEET 1 AA9 3 LYS P1439 TYR P1440 0 SHEET 2 AA9 3 TYR P1450 ILE P1452 -1 O GLU P1451 N LYS P1439 SHEET 3 AA9 3 LEU P1457 TYR P1459 -1 O TYR P1459 N TYR P1450 SHEET 1 AB1 2 LYS P1568 TYR P1569 0 SHEET 2 AB1 2 THR P1572 SER P1573 -1 O THR P1572 N TYR P1569 SHEET 1 AB2 6 TYR P1657 VAL P1659 0 SHEET 2 AB2 6 ILE P1710 ALA P1714 1 O MET P1712 N TYR P1657 SHEET 3 AB2 6 THR P1718 ALA P1723 -1 O GLY P1720 N ILE P1713 SHEET 4 AB2 6 VAL P1776 TYR P1779 1 O VAL P1776 N ILE P1719 SHEET 5 AB2 6 PHE P1829 TYR P1830 1 O PHE P1829 N LEU P1777 SHEET 6 AB2 6 TYR P1823 ALA P1824 -1 N TYR P1823 O TYR P1830 SHEET 1 AB3 4 VAL P1999 THR P2001 0 SHEET 2 AB3 4 LEU P1955 ILE P1961 -1 N ARG P1956 O ILE P2000 SHEET 3 AB3 4 THR P1974 ARG P1978 -1 O ALA P1976 N GLU P1959 SHEET 4 AB3 4 GLU P2010 TYR P2011 -1 O TYR P2011 N ASN P1975 SHEET 1 AB4 2 ILE P2077 SER P2079 0 SHEET 2 AB4 2 LYS P2082 ILE P2084 -1 O ILE P2084 N ILE P2077 SHEET 1 AB5 5 ARG B 245 HIS B 249 0 SHEET 2 AB5 5 LEU B 264 LEU B 271 -1 O THR B 267 N SER B 247 SHEET 3 AB5 5 VAL B 290 GLN B 291 0 SHEET 4 AB5 5 GLU B 295 ARG B 296 0 SHEET 5 AB5 5 TYR B 302 LEU B 308 -1 O SER B 303 N GLU B 295 SHEET 1 AB6 3 THR B 278 TRP B 281 0 SHEET 2 AB6 3 PHE B 321 TYR B 327 -1 O THR B 324 N THR B 280 SHEET 3 AB6 3 SER B 330 LEU B 338 -1 O LEU B 338 N PHE B 321 SHEET 1 AB7 5 GLU B 348 LEU B 352 0 SHEET 2 AB7 5 VAL B 365 PHE B 374 -1 O ARG B 372 N GLU B 348 SHEET 3 AB7 5 TYR B 395 THR B 397 0 SHEET 4 AB7 5 ARG B 401 GLN B 402 0 SHEET 5 AB7 5 PHE B 411 VAL B 419 -1 O ALA B 412 N ARG B 401 SHEET 1 AB8 4 GLN B 388 GLU B 389 0 SHEET 2 AB8 4 VAL B 379 GLN B 385 -1 N GLN B 385 O GLN B 388 SHEET 3 AB8 4 PHE B 430 HIS B 436 -1 O GLY B 435 N LEU B 380 SHEET 4 AB8 4 PHE B 443 ILE B 448 -1 O THR B 444 N VAL B 434 SHEET 1 AB9 5 ARG A 245 HIS A 249 0 SHEET 2 AB9 5 LEU A 264 LEU A 271 -1 O THR A 269 N ARG A 245 SHEET 3 AB9 5 VAL A 290 GLN A 291 0 SHEET 4 AB9 5 GLU A 295 ARG A 296 0 SHEET 5 AB9 5 TYR A 302 LEU A 308 -1 O SER A 303 N GLU A 295 SHEET 1 AC1 3 THR A 278 TRP A 281 0 SHEET 2 AC1 3 PHE A 321 TYR A 327 -1 O THR A 324 N THR A 280 SHEET 3 AC1 3 SER A 330 LEU A 338 -1 O ALA A 336 N CYS A 323 SHEET 1 AC2 4 GLU A 348 LEU A 352 0 SHEET 2 AC2 4 VAL A 365 PHE A 374 -1 O THR A 368 N LEU A 352 SHEET 3 AC2 4 PHE A 411 VAL A 419 -1 O VAL A 413 N ALA A 371 SHEET 4 AC2 4 LEU A 396 THR A 397 -1 N LEU A 396 O ILE A 416 SHEET 1 AC3 4 GLN A 388 GLU A 389 0 SHEET 2 AC3 4 VAL A 379 GLN A 385 -1 N GLN A 385 O GLN A 388 SHEET 3 AC3 4 PHE A 430 HIS A 436 -1 O GLY A 435 N LEU A 380 SHEET 4 AC3 4 PHE A 443 ILE A 448 -1 O THR A 444 N VAL A 434 SHEET 1 AC4 2 MET L 4 GLN L 6 0 SHEET 2 AC4 2 CYS L 23 SER L 25 -1 O ARG L 24 N THR L 5 SHEET 1 AC5 2 SER L 10 VAL L 13 0 SHEET 2 AC5 2 ARG L 108 ILE L 111 1 O GLU L 110 N LEU L 11 SHEET 1 AC6 2 ALA L 19 ILE L 21 0 SHEET 2 AC6 2 LEU L 78 ILE L 80 -1 O LEU L 78 N ILE L 21 SHEET 1 AC7 3 GLN L 50 PRO L 51 0 SHEET 2 AC7 3 LEU L 38 LEU L 42 -1 N LEU L 42 O GLN L 50 SHEET 3 AC7 3 CYS L 93 GLN L 95 -1 O MET L 94 N GLU L 39 SHEET 1 AC8 4 VAL L 120 PHE L 123 0 SHEET 2 AC8 4 THR L 134 PHE L 144 -1 O VAL L 138 N PHE L 123 SHEET 3 AC8 4 TYR L 178 SER L 187 -1 O TYR L 178 N PHE L 144 SHEET 4 AC8 4 GLN L 165 VAL L 168 -1 N SER L 167 O SER L 181 SHEET 1 AC9 3 LEU L 159 GLN L 160 0 SHEET 2 AC9 3 ALA L 149 LYS L 154 -1 N TRP L 153 O GLN L 160 SHEET 3 AC9 3 GLU L 200 HIS L 203 -1 O GLU L 200 N GLN L 152 SHEET 1 AD1 2 VAL L 196 ALA L 198 0 SHEET 2 AD1 2 SER L 213 ASN L 215 -1 O PHE L 214 N TYR L 197 SHEET 1 AD2 4 VAL H 5 SER H 7 0 SHEET 2 AD2 4 LEU H 18 ALA H 23 -1 O ALA H 23 N VAL H 5 SHEET 3 AD2 4 THR H 80 MET H 85 -1 O LEU H 83 N LEU H 20 SHEET 4 AD2 4 SER H 73 ASP H 75 -1 N ASP H 75 O THR H 80 SHEET 1 AD3 5 THR H 60 TYR H 62 0 SHEET 2 AD3 5 LEU H 45 ILE H 51 -1 N ARG H 50 O ALA H 61 SHEET 3 AD3 5 ASN H 33 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 4 AD3 5 ALA H 94 ARG H 101 -1 O MET H 95 N GLN H 39 SHEET 5 AD3 5 THR H 113 VAL H 115 -1 O THR H 113 N TYR H 96 SHEET 1 AD4 5 LYS H 126 PHE H 128 0 SHEET 2 AD4 5 ASN H 140 PHE H 150 -1 O GLN H 148 N LYS H 126 SHEET 3 AD4 5 ARG H 170 ASN H 171 0 SHEET 4 AD4 5 SER H 175 GLN H 176 0 SHEET 5 AD4 5 TYR H 183 PRO H 192 -1 O THR H 184 N SER H 175 SHEET 1 AD5 3 VAL H 158 THR H 159 0 SHEET 2 AD5 3 VAL H 202 VAL H 206 -1 O HIS H 205 N THR H 159 SHEET 3 AD5 3 VAL H 216 VAL H 218 -1 O VAL H 218 N VAL H 202 SSBOND 1 CYS B 266 CYS B 323 1555 1555 2.03 SSBOND 2 CYS B 369 CYS B 432 1555 1555 2.03 SSBOND 3 CYS A 266 CYS A 323 1555 1555 2.03 SSBOND 4 CYS A 369 CYS A 432 1555 1555 2.03 SSBOND 5 CYS L 23 CYS L 93 1555 1555 2.03 SSBOND 6 CYS L 139 CYS L 199 1555 1555 2.03 SSBOND 7 CYS H 22 CYS H 98 1555 1555 2.03 SSBOND 8 CYS H 145 CYS H 204 1555 1555 2.03 SSBOND 9 CYS H 196 CYS H 220 1555 1555 2.03 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