HEADER VIRAL PROTEIN 28-MAR-22 7UHZ TITLE POST-FUSION ECTODOMAIN OF HSV-1 GB IN COMPLEX WITH BMPC-23 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: BMPC-23 FAB HEAVY CHAIN; COMPND 3 CHAIN: H, I, J; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: BMPC-23 FAB LIGHT CHAIN; COMPND 7 CHAIN: L, M, N; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN B; COMPND 11 CHAIN: A, B, C; COMPND 12 SYNONYM: GB; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HUMAN ALPHAHERPESVIRUS 1 STRAIN KOS; SOURCE 13 ORGANISM_TAXID: 10306; SOURCE 14 STRAIN: KOS; SOURCE 15 GENE: GB, UL27; SOURCE 16 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7111 KEYWDS GLYCOPROTEIN, FUSOGEN, ANTIBODY, ADCC, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR I.W.WINDSOR,S.L.KONG,S.J.GARFORTH,S.C.ALMO,S.C.HARRISON JRNL AUTH M.KURAOKA,C.BURN ASCHNER,I.W.WINDSOR,A.MAHANT MAHANT, JRNL AUTH 2 S.J.GARFORTH,S.L.KONG,J.M.ACHKAR,S.C.ALMO,G.KELSOE, JRNL AUTH 3 B.C.HEROLD JRNL TITL A NON-NEUTRALIZING GLYCOPROTEIN B MONOCLONAL ANTIBODY JRNL TITL 2 PROTECTS AGAINST HERPES SIMPLEX VIRUS DISEASE IN MICE. JRNL REF J.CLIN.INVEST. 2022 JRNL REFN ISSN 0021-9738 JRNL PMID 36454639 JRNL DOI 10.1172/JCI161968 REMARK 2 REMARK 2 RESOLUTION. 3.30 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) : 3.300 REMARK 3 NUMBER OF PARTICLES : 218056 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 7UHZ 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_1000264225. 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 : TRIMERIC HSV-1 GB IN COMPLEX REMARK 245 WITH THREE BCMP-23 FABS 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 : 7.50 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 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 600.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 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) : 55.80 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: NONAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, I, J, L, M, N, A, B, C 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 ALA H 117 REMARK 465 ALA I 117 REMARK 465 ALA J 117 REMARK 465 ARG L 112 REMARK 465 ARG M 112 REMARK 465 ARG N 112 REMARK 465 ASP A 103 REMARK 465 ILE A 104 REMARK 465 LYS A 105 REMARK 465 ALA A 106 REMARK 465 GLU A 107 REMARK 465 ASN A 108 REMARK 465 THR A 109 REMARK 465 ASP A 110 REMARK 465 THR A 331 REMARK 465 THR A 332 REMARK 465 LYS A 333 REMARK 465 ALA A 334 REMARK 465 ARG A 335 REMARK 465 ALA A 336 REMARK 465 THR A 337 REMARK 465 LEU A 460 REMARK 465 ALA A 461 REMARK 465 GLU A 462 REMARK 465 LEU A 463 REMARK 465 TYR A 464 REMARK 465 VAL A 465 REMARK 465 ARG A 466 REMARK 465 GLU A 467 REMARK 465 HIS A 468 REMARK 465 LEU A 469 REMARK 465 ARG A 470 REMARK 465 GLU A 471 REMARK 465 GLN A 472 REMARK 465 SER A 473 REMARK 465 ARG A 474 REMARK 465 LYS A 475 REMARK 465 PRO A 476 REMARK 465 PRO A 477 REMARK 465 ASN A 478 REMARK 465 PRO A 479 REMARK 465 THR A 480 REMARK 465 PRO A 481 REMARK 465 PRO A 482 REMARK 465 PRO A 483 REMARK 465 PRO A 484 REMARK 465 GLY A 485 REMARK 465 ALA A 486 REMARK 465 SER A 487 REMARK 465 ALA A 488 REMARK 465 ASN A 489 REMARK 465 ALA A 490 REMARK 465 SER A 491 REMARK 465 ASP A 726 REMARK 465 ALA A 727 REMARK 465 ASN A 728 REMARK 465 ALA A 729 REMARK 465 ALA A 730 REMARK 465 ASP B 103 REMARK 465 ILE B 104 REMARK 465 LYS B 105 REMARK 465 ALA B 106 REMARK 465 GLU B 107 REMARK 465 ASN B 108 REMARK 465 THR B 109 REMARK 465 ASP B 110 REMARK 465 THR B 331 REMARK 465 THR B 332 REMARK 465 LYS B 333 REMARK 465 ALA B 334 REMARK 465 ARG B 335 REMARK 465 ALA B 336 REMARK 465 THR B 337 REMARK 465 LEU B 460 REMARK 465 ALA B 461 REMARK 465 GLU B 462 REMARK 465 LEU B 463 REMARK 465 TYR B 464 REMARK 465 VAL B 465 REMARK 465 ARG B 466 REMARK 465 GLU B 467 REMARK 465 HIS B 468 REMARK 465 LEU B 469 REMARK 465 ARG B 470 REMARK 465 GLU B 471 REMARK 465 GLN B 472 REMARK 465 SER B 473 REMARK 465 ARG B 474 REMARK 465 LYS B 475 REMARK 465 PRO B 476 REMARK 465 PRO B 477 REMARK 465 ASN B 478 REMARK 465 PRO B 479 REMARK 465 THR B 480 REMARK 465 PRO B 481 REMARK 465 PRO B 482 REMARK 465 PRO B 483 REMARK 465 PRO B 484 REMARK 465 GLY B 485 REMARK 465 ALA B 486 REMARK 465 SER B 487 REMARK 465 ALA B 488 REMARK 465 ASN B 489 REMARK 465 ALA B 490 REMARK 465 SER B 491 REMARK 465 ASP B 726 REMARK 465 ALA B 727 REMARK 465 ASN B 728 REMARK 465 ALA B 729 REMARK 465 ALA B 730 REMARK 465 ASP C 103 REMARK 465 ILE C 104 REMARK 465 LYS C 105 REMARK 465 ALA C 106 REMARK 465 GLU C 107 REMARK 465 ASN C 108 REMARK 465 THR C 109 REMARK 465 ASP C 110 REMARK 465 THR C 331 REMARK 465 THR C 332 REMARK 465 LYS C 333 REMARK 465 ALA C 334 REMARK 465 ARG C 335 REMARK 465 ALA C 336 REMARK 465 THR C 337 REMARK 465 LEU C 460 REMARK 465 ALA C 461 REMARK 465 GLU C 462 REMARK 465 LEU C 463 REMARK 465 TYR C 464 REMARK 465 VAL C 465 REMARK 465 ARG C 466 REMARK 465 GLU C 467 REMARK 465 HIS C 468 REMARK 465 LEU C 469 REMARK 465 ARG C 470 REMARK 465 GLU C 471 REMARK 465 GLN C 472 REMARK 465 SER C 473 REMARK 465 ARG C 474 REMARK 465 LYS C 475 REMARK 465 PRO C 476 REMARK 465 PRO C 477 REMARK 465 ASN C 478 REMARK 465 PRO C 479 REMARK 465 THR C 480 REMARK 465 PRO C 481 REMARK 465 PRO C 482 REMARK 465 PRO C 483 REMARK 465 PRO C 484 REMARK 465 GLY C 485 REMARK 465 ALA C 486 REMARK 465 SER C 487 REMARK 465 ALA C 488 REMARK 465 ASN C 489 REMARK 465 ALA C 490 REMARK 465 SER C 491 REMARK 465 ASP C 726 REMARK 465 ALA C 727 REMARK 465 ASN C 728 REMARK 465 ALA C 729 REMARK 465 ALA C 730 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 ND2 ASN H 58 O SER A 590 2.03 REMARK 500 O THR A 143 OH TYR A 452 2.10 REMARK 500 O THR C 143 OH TYR C 452 2.10 REMARK 500 O THR B 143 OH TYR B 452 2.10 REMARK 500 NZ LYS A 253 OD1 ASN A 255 2.11 REMARK 500 NZ LYS B 253 OD1 ASN B 255 2.11 REMARK 500 NZ LYS C 253 OD1 ASN C 255 2.11 REMARK 500 OG1 THR A 210 OG1 THR A 221 2.12 REMARK 500 OG1 THR C 210 OG1 THR C 221 2.12 REMARK 500 OG1 THR B 210 OG1 THR B 221 2.12 REMARK 500 O GLU A 152 OH TYR B 689 2.13 REMARK 500 OE1 GLN A 126 OH TYR C 647 2.15 REMARK 500 O ARG C 304 OG SER C 307 2.17 REMARK 500 O ARG B 304 OG SER B 307 2.17 REMARK 500 O ARG A 304 OG SER A 307 2.17 REMARK 500 NZ LYS B 166 O THR B 210 2.19 REMARK 500 NZ LYS A 166 O THR A 210 2.19 REMARK 500 NZ LYS C 166 O THR C 210 2.19 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 L 26 -4.31 65.60 REMARK 500 ALA L 55 -5.20 68.04 REMARK 500 SER M 26 -4.20 65.58 REMARK 500 ALA M 55 -5.29 68.10 REMARK 500 SER N 26 -4.30 65.53 REMARK 500 ALA N 55 -5.22 68.06 REMARK 500 ARG A 225 -3.31 69.26 REMARK 500 ARG A 242 52.19 37.76 REMARK 500 LEU A 252 -168.53 -124.57 REMARK 500 THR A 291 2.82 -69.69 REMARK 500 MET A 297 145.34 -174.85 REMARK 500 PRO A 348 4.01 -64.09 REMARK 500 ARG B 225 -3.33 69.24 REMARK 500 ARG B 242 52.20 37.80 REMARK 500 LEU B 252 -168.48 -124.53 REMARK 500 THR B 291 2.84 -69.66 REMARK 500 MET B 297 145.33 -174.88 REMARK 500 PRO B 348 3.98 -64.01 REMARK 500 ARG C 225 -3.33 69.26 REMARK 500 ARG C 242 52.16 37.82 REMARK 500 LEU C 252 -168.49 -124.53 REMARK 500 THR C 291 2.77 -69.56 REMARK 500 MET C 297 145.29 -174.86 REMARK 500 PRO C 348 4.01 -64.06 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-26520 RELATED DB: EMDB REMARK 900 POST-FUSION ECTODOMAIN OF HSV-1 GB IN COMPLEX WITH BMPC-23 FAB DBREF 7UHZ H 1 117 PDB 7UHZ 7UHZ 1 117 DBREF 7UHZ I 1 117 PDB 7UHZ 7UHZ 1 117 DBREF 7UHZ J 1 117 PDB 7UHZ 7UHZ 1 117 DBREF 7UHZ L 1 112 PDB 7UHZ 7UHZ 1 112 DBREF 7UHZ M 1 112 PDB 7UHZ 7UHZ 1 112 DBREF 7UHZ N 1 112 PDB 7UHZ 7UHZ 1 112 DBREF 7UHZ A 103 730 UNP P06437 GB_HHV1K 103 730 DBREF 7UHZ B 103 730 UNP P06437 GB_HHV1K 103 730 DBREF 7UHZ C 103 730 UNP P06437 GB_HHV1K 103 730 SEQRES 1 H 121 GLN VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 H 121 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY SEQRES 3 H 121 TYR SER PHE THR THR TYR ASP ILE ASN TRP VAL LYS GLU SEQRES 4 H 121 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY TRP ILE TYR SEQRES 5 H 121 PRO ARG GLU GLY SER THR ASN TYR ASN GLU LYS PHE ARG SEQRES 6 H 121 GLY LYS ALA THR LEU THR ALA ASP THR SER SER SER THR SEQRES 7 H 121 ALA TYR MET GLU LEU HIS SER LEU THR SER GLU ASP SER SEQRES 8 H 121 ALA VAL TYR PHE CYS ALA THR TYR GLY SER SER ARG TYR SEQRES 9 H 121 TYR THR MET ASP TYR TRP GLY GLN GLY THR SER VAL THR SEQRES 10 H 121 VAL SER SER ALA SEQRES 1 I 121 GLN VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 I 121 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY SEQRES 3 I 121 TYR SER PHE THR THR TYR ASP ILE ASN TRP VAL LYS GLU SEQRES 4 I 121 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY TRP ILE TYR SEQRES 5 I 121 PRO ARG GLU GLY SER THR ASN TYR ASN GLU LYS PHE ARG SEQRES 6 I 121 GLY LYS ALA THR LEU THR ALA ASP THR SER SER SER THR SEQRES 7 I 121 ALA TYR MET GLU LEU HIS SER LEU THR SER GLU ASP SER SEQRES 8 I 121 ALA VAL TYR PHE CYS ALA THR TYR GLY SER SER ARG TYR SEQRES 9 I 121 TYR THR MET ASP TYR TRP GLY GLN GLY THR SER VAL THR SEQRES 10 I 121 VAL SER SER ALA SEQRES 1 J 121 GLN VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 J 121 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY SEQRES 3 J 121 TYR SER PHE THR THR TYR ASP ILE ASN TRP VAL LYS GLU SEQRES 4 J 121 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY TRP ILE TYR SEQRES 5 J 121 PRO ARG GLU GLY SER THR ASN TYR ASN GLU LYS PHE ARG SEQRES 6 J 121 GLY LYS ALA THR LEU THR ALA ASP THR SER SER SER THR SEQRES 7 J 121 ALA TYR MET GLU LEU HIS SER LEU THR SER GLU ASP SER SEQRES 8 J 121 ALA VAL TYR PHE CYS ALA THR TYR GLY SER SER ARG TYR SEQRES 9 J 121 TYR THR MET ASP TYR TRP GLY GLN GLY THR SER VAL THR SEQRES 10 J 121 VAL SER SER ALA SEQRES 1 L 112 ASP ILE VAL LEU THR GLN SER PRO THR SER LEU ALA VAL SEQRES 2 L 112 SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG ALA SER SEQRES 3 L 112 GLU SER VAL ASP ASN PHE GLY ILE SER PHE MET ASN TRP SEQRES 4 L 112 PHE GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 L 112 TYR ALA ALA SER ASN LEU GLY SER GLY VAL PRO ALA ARG SEQRES 6 L 112 PHE SER GLY SER GLY SER GLY THR ASP PHE SER LEU ASN SEQRES 7 L 112 ILE HIS PRO MET GLU ASP ASP ASP THR ALA MET TYR PHE SEQRES 8 L 112 CYS GLN GLN SER LYS GLU VAL PRO LEU THR PHE GLY ALA SEQRES 9 L 112 GLY THR LYS LEU GLU LEU LYS ARG SEQRES 1 M 112 ASP ILE VAL LEU THR GLN SER PRO THR SER LEU ALA VAL SEQRES 2 M 112 SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG ALA SER SEQRES 3 M 112 GLU SER VAL ASP ASN PHE GLY ILE SER PHE MET ASN TRP SEQRES 4 M 112 PHE GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 M 112 TYR ALA ALA SER ASN LEU GLY SER GLY VAL PRO ALA ARG SEQRES 6 M 112 PHE SER GLY SER GLY SER GLY THR ASP PHE SER LEU ASN SEQRES 7 M 112 ILE HIS PRO MET GLU ASP ASP ASP THR ALA MET TYR PHE SEQRES 8 M 112 CYS GLN GLN SER LYS GLU VAL PRO LEU THR PHE GLY ALA SEQRES 9 M 112 GLY THR LYS LEU GLU LEU LYS ARG SEQRES 1 N 112 ASP ILE VAL LEU THR GLN SER PRO THR SER LEU ALA VAL SEQRES 2 N 112 SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG ALA SER SEQRES 3 N 112 GLU SER VAL ASP ASN PHE GLY ILE SER PHE MET ASN TRP SEQRES 4 N 112 PHE GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 N 112 TYR ALA ALA SER ASN LEU GLY SER GLY VAL PRO ALA ARG SEQRES 6 N 112 PHE SER GLY SER GLY SER GLY THR ASP PHE SER LEU ASN SEQRES 7 N 112 ILE HIS PRO MET GLU ASP ASP ASP THR ALA MET TYR PHE SEQRES 8 N 112 CYS GLN GLN SER LYS GLU VAL PRO LEU THR PHE GLY ALA SEQRES 9 N 112 GLY THR LYS LEU GLU LEU LYS ARG SEQRES 1 A 628 ASP ILE LYS ALA GLU ASN THR ASP ALA ASN PHE TYR VAL SEQRES 2 A 628 CYS PRO PRO PRO THR GLY ALA THR VAL VAL GLN PHE GLU SEQRES 3 A 628 GLN PRO ARG ARG CYS PRO THR ARG PRO GLU GLY GLN ASN SEQRES 4 A 628 TYR THR GLU GLY ILE ALA VAL VAL PHE LYS GLU ASN ILE SEQRES 5 A 628 ALA PRO TYR LYS PHE LYS ALA THR MET TYR TYR LYS ASP SEQRES 6 A 628 VAL THR VAL SER GLN VAL TRP PHE GLY HIS ARG TYR SER SEQRES 7 A 628 GLN PHE MET GLY ILE PHE GLU ASP ARG ALA PRO VAL PRO SEQRES 8 A 628 PHE GLU GLU VAL ILE ASP LYS ILE ASN ALA LYS GLY VAL SEQRES 9 A 628 CYS ARG SER THR ALA LYS TYR VAL ARG ASN ASN LEU GLU SEQRES 10 A 628 THR THR ALA PHE HIS ARG ASP ASP HIS GLU THR ASP MET SEQRES 11 A 628 GLU LEU LYS PRO ALA ASN ALA ALA THR ARG THR SER ARG SEQRES 12 A 628 GLY TRP HIS THR THR ASP LEU LYS TYR ASN PRO SER ARG SEQRES 13 A 628 VAL GLU ALA PHE HIS ARG TYR GLY THR THR VAL ASN CYS SEQRES 14 A 628 ILE VAL GLU GLU VAL ASP ALA ARG SER VAL TYR PRO TYR SEQRES 15 A 628 ASP GLU PHE VAL LEU ALA THR GLY ASP PHE VAL TYR MET SEQRES 16 A 628 SER PRO PHE TYR GLY TYR ARG GLU GLY SER HIS THR GLU SEQRES 17 A 628 HIS THR THR TYR ALA ALA ASP ARG PHE LYS GLN VAL ASP SEQRES 18 A 628 GLY PHE TYR ALA ARG ASP LEU THR THR LYS ALA ARG ALA SEQRES 19 A 628 THR ALA PRO THR THR ARG ASN LEU LEU THR THR PRO LYS SEQRES 20 A 628 PHE THR VAL ALA TRP ASP TRP VAL PRO LYS ARG PRO SER SEQRES 21 A 628 VAL CYS THR MET THR LYS TRP GLN GLU VAL ASP GLU MET SEQRES 22 A 628 LEU ARG SER GLU TYR GLY GLY SER PHE ARG PHE SER SER SEQRES 23 A 628 ASP ALA ILE SER THR THR PHE THR THR ASN LEU THR GLU SEQRES 24 A 628 TYR PRO LEU SER ARG VAL ASP LEU GLY ASP CYS ILE GLY SEQRES 25 A 628 LYS ASP ALA ARG ASP ALA MET ASP ARG ILE PHE ALA ARG SEQRES 26 A 628 ARG TYR ASN ALA THR HIS ILE LYS VAL GLY GLN PRO GLN SEQRES 27 A 628 TYR TYR GLN ALA ASN GLY GLY PHE LEU ILE ALA TYR GLN SEQRES 28 A 628 PRO LEU LEU SER ASN THR LEU ALA GLU LEU TYR VAL ARG SEQRES 29 A 628 GLU HIS LEU ARG GLU GLN SER ARG LYS PRO PRO ASN PRO SEQRES 30 A 628 THR PRO PRO PRO PRO GLY ALA SER ALA ASN ALA SER VAL SEQRES 31 A 628 GLU ARG ILE LYS THR THR SER SER ILE GLU PHE ALA ARG SEQRES 32 A 628 LEU GLN PHE THR TYR ASN HIS ILE GLN ARG HIS VAL ASN SEQRES 33 A 628 ASP MET LEU GLY ARG VAL ALA ILE ALA TRP CYS GLU LEU SEQRES 34 A 628 GLN ASN HIS GLU LEU THR LEU TRP ASN GLU ALA ARG LYS SEQRES 35 A 628 LEU ASN PRO ASN ALA ILE ALA SER VAL THR VAL GLY ARG SEQRES 36 A 628 ARG VAL SER ALA ARG MET LEU GLY ASP VAL MET ALA VAL SEQRES 37 A 628 SER THR CYS VAL PRO VAL ALA ALA ASP ASN VAL ILE VAL SEQRES 38 A 628 GLN ASN SER MET ARG ILE SER SER ARG PRO GLY ALA CYS SEQRES 39 A 628 TYR SER ARG PRO LEU VAL SER PHE ARG TYR GLU ASP GLN SEQRES 40 A 628 GLY PRO LEU VAL GLU GLY GLN LEU GLY GLU ASN ASN GLU SEQRES 41 A 628 LEU ARG LEU THR ARG ASP ALA ILE GLU PRO CYS THR VAL SEQRES 42 A 628 GLY HIS ARG ARG TYR PHE THR PHE GLY GLY GLY TYR VAL SEQRES 43 A 628 TYR PHE GLU GLU TYR ALA TYR SER HIS GLN LEU SER ARG SEQRES 44 A 628 ALA ASP ILE THR THR VAL SER THR PHE ILE ASP LEU ASN SEQRES 45 A 628 ILE THR MET LEU GLU ASP HIS GLU PHE VAL PRO LEU GLU SEQRES 46 A 628 VAL TYR THR ARG HIS GLU ILE LYS ASP SER GLY LEU LEU SEQRES 47 A 628 ASP TYR THR GLU VAL GLN ARG ARG ASN GLN LEU HIS ASP SEQRES 48 A 628 LEU ARG PHE ALA ASP ILE ASP THR VAL ILE HIS ALA ASP SEQRES 49 A 628 ALA ASN ALA ALA SEQRES 1 B 628 ASP ILE LYS ALA GLU ASN THR ASP ALA ASN PHE TYR VAL SEQRES 2 B 628 CYS PRO PRO PRO THR GLY ALA THR VAL VAL GLN PHE GLU SEQRES 3 B 628 GLN PRO ARG ARG CYS PRO THR ARG PRO GLU GLY GLN ASN SEQRES 4 B 628 TYR THR GLU GLY ILE ALA VAL VAL PHE LYS GLU ASN ILE SEQRES 5 B 628 ALA PRO TYR LYS PHE LYS ALA THR MET TYR TYR LYS ASP SEQRES 6 B 628 VAL THR VAL SER GLN VAL TRP PHE GLY HIS ARG TYR SER SEQRES 7 B 628 GLN PHE MET GLY ILE PHE GLU ASP ARG ALA PRO VAL PRO SEQRES 8 B 628 PHE GLU GLU VAL ILE ASP LYS ILE ASN ALA LYS GLY VAL SEQRES 9 B 628 CYS ARG SER THR ALA LYS TYR VAL ARG ASN ASN LEU GLU SEQRES 10 B 628 THR THR ALA PHE HIS ARG ASP ASP HIS GLU THR ASP MET SEQRES 11 B 628 GLU LEU LYS PRO ALA ASN ALA ALA THR ARG THR SER ARG SEQRES 12 B 628 GLY TRP HIS THR THR ASP LEU LYS TYR ASN PRO SER ARG SEQRES 13 B 628 VAL GLU ALA PHE HIS ARG TYR GLY THR THR VAL ASN CYS SEQRES 14 B 628 ILE VAL GLU GLU VAL ASP ALA ARG SER VAL TYR PRO TYR SEQRES 15 B 628 ASP GLU PHE VAL LEU ALA THR GLY ASP PHE VAL TYR MET SEQRES 16 B 628 SER PRO PHE TYR GLY TYR ARG GLU GLY SER HIS THR GLU SEQRES 17 B 628 HIS THR THR TYR ALA ALA ASP ARG PHE LYS GLN VAL ASP SEQRES 18 B 628 GLY PHE TYR ALA ARG ASP LEU THR THR LYS ALA ARG ALA SEQRES 19 B 628 THR ALA PRO THR THR ARG ASN LEU LEU THR THR PRO LYS SEQRES 20 B 628 PHE THR VAL ALA TRP ASP TRP VAL PRO LYS ARG PRO SER SEQRES 21 B 628 VAL CYS THR MET THR LYS TRP GLN GLU VAL ASP GLU MET SEQRES 22 B 628 LEU ARG SER GLU TYR GLY GLY SER PHE ARG PHE SER SER SEQRES 23 B 628 ASP ALA ILE SER THR THR PHE THR THR ASN LEU THR GLU SEQRES 24 B 628 TYR PRO LEU SER ARG VAL ASP LEU GLY ASP CYS ILE GLY SEQRES 25 B 628 LYS ASP ALA ARG ASP ALA MET ASP ARG ILE PHE ALA ARG SEQRES 26 B 628 ARG TYR ASN ALA THR HIS ILE LYS VAL GLY GLN PRO GLN SEQRES 27 B 628 TYR TYR GLN ALA ASN GLY GLY PHE LEU ILE ALA TYR GLN SEQRES 28 B 628 PRO LEU LEU SER ASN THR LEU ALA GLU LEU TYR VAL ARG SEQRES 29 B 628 GLU HIS LEU ARG GLU GLN SER ARG LYS PRO PRO ASN PRO SEQRES 30 B 628 THR PRO PRO PRO PRO GLY ALA SER ALA ASN ALA SER VAL SEQRES 31 B 628 GLU ARG ILE LYS THR THR SER SER ILE GLU PHE ALA ARG SEQRES 32 B 628 LEU GLN PHE THR TYR ASN HIS ILE GLN ARG HIS VAL ASN SEQRES 33 B 628 ASP MET LEU GLY ARG VAL ALA ILE ALA TRP CYS GLU LEU SEQRES 34 B 628 GLN ASN HIS GLU LEU THR LEU TRP ASN GLU ALA ARG LYS SEQRES 35 B 628 LEU ASN PRO ASN ALA ILE ALA SER VAL THR VAL GLY ARG SEQRES 36 B 628 ARG VAL SER ALA ARG MET LEU GLY ASP VAL MET ALA VAL SEQRES 37 B 628 SER THR CYS VAL PRO VAL ALA ALA ASP ASN VAL ILE VAL SEQRES 38 B 628 GLN ASN SER MET ARG ILE SER SER ARG PRO GLY ALA CYS SEQRES 39 B 628 TYR SER ARG PRO LEU VAL SER PHE ARG TYR GLU ASP GLN SEQRES 40 B 628 GLY PRO LEU VAL GLU GLY GLN LEU GLY GLU ASN ASN GLU SEQRES 41 B 628 LEU ARG LEU THR ARG ASP ALA ILE GLU PRO CYS THR VAL SEQRES 42 B 628 GLY HIS ARG ARG TYR PHE THR PHE GLY GLY GLY TYR VAL SEQRES 43 B 628 TYR PHE GLU GLU TYR ALA TYR SER HIS GLN LEU SER ARG SEQRES 44 B 628 ALA ASP ILE THR THR VAL SER THR PHE ILE ASP LEU ASN SEQRES 45 B 628 ILE THR MET LEU GLU ASP HIS GLU PHE VAL PRO LEU GLU SEQRES 46 B 628 VAL TYR THR ARG HIS GLU ILE LYS ASP SER GLY LEU LEU SEQRES 47 B 628 ASP TYR THR GLU VAL GLN ARG ARG ASN GLN LEU HIS ASP SEQRES 48 B 628 LEU ARG PHE ALA ASP ILE ASP THR VAL ILE HIS ALA ASP SEQRES 49 B 628 ALA ASN ALA ALA SEQRES 1 C 628 ASP ILE LYS ALA GLU ASN THR ASP ALA ASN PHE TYR VAL SEQRES 2 C 628 CYS PRO PRO PRO THR GLY ALA THR VAL VAL GLN PHE GLU SEQRES 3 C 628 GLN PRO ARG ARG CYS PRO THR ARG PRO GLU GLY GLN ASN SEQRES 4 C 628 TYR THR GLU GLY ILE ALA VAL VAL PHE LYS GLU ASN ILE SEQRES 5 C 628 ALA PRO TYR LYS PHE LYS ALA THR MET TYR TYR LYS ASP SEQRES 6 C 628 VAL THR VAL SER GLN VAL TRP PHE GLY HIS ARG TYR SER SEQRES 7 C 628 GLN PHE MET GLY ILE PHE GLU ASP ARG ALA PRO VAL PRO SEQRES 8 C 628 PHE GLU GLU VAL ILE ASP LYS ILE ASN ALA LYS GLY VAL SEQRES 9 C 628 CYS ARG SER THR ALA LYS TYR VAL ARG ASN ASN LEU GLU SEQRES 10 C 628 THR THR ALA PHE HIS ARG ASP ASP HIS GLU THR ASP MET SEQRES 11 C 628 GLU LEU LYS PRO ALA ASN ALA ALA THR ARG THR SER ARG SEQRES 12 C 628 GLY TRP HIS THR THR ASP LEU LYS TYR ASN PRO SER ARG SEQRES 13 C 628 VAL GLU ALA PHE HIS ARG TYR GLY THR THR VAL ASN CYS SEQRES 14 C 628 ILE VAL GLU GLU VAL ASP ALA ARG SER VAL TYR PRO TYR SEQRES 15 C 628 ASP GLU PHE VAL LEU ALA THR GLY ASP PHE VAL TYR MET SEQRES 16 C 628 SER PRO PHE TYR GLY TYR ARG GLU GLY SER HIS THR GLU SEQRES 17 C 628 HIS THR THR TYR ALA ALA ASP ARG PHE LYS GLN VAL ASP SEQRES 18 C 628 GLY PHE TYR ALA ARG ASP LEU THR THR LYS ALA ARG ALA SEQRES 19 C 628 THR ALA PRO THR THR ARG ASN LEU LEU THR THR PRO LYS SEQRES 20 C 628 PHE THR VAL ALA TRP ASP TRP VAL PRO LYS ARG PRO SER SEQRES 21 C 628 VAL CYS THR MET THR LYS TRP GLN GLU VAL ASP GLU MET SEQRES 22 C 628 LEU ARG SER GLU TYR GLY GLY SER PHE ARG PHE SER SER SEQRES 23 C 628 ASP ALA ILE SER THR THR PHE THR THR ASN LEU THR GLU SEQRES 24 C 628 TYR PRO LEU SER ARG VAL ASP LEU GLY ASP CYS ILE GLY SEQRES 25 C 628 LYS ASP ALA ARG ASP ALA MET ASP ARG ILE PHE ALA ARG SEQRES 26 C 628 ARG TYR ASN ALA THR HIS ILE LYS VAL GLY GLN PRO GLN SEQRES 27 C 628 TYR TYR GLN ALA ASN GLY GLY PHE LEU ILE ALA TYR GLN SEQRES 28 C 628 PRO LEU LEU SER ASN THR LEU ALA GLU LEU TYR VAL ARG SEQRES 29 C 628 GLU HIS LEU ARG GLU GLN SER ARG LYS PRO PRO ASN PRO SEQRES 30 C 628 THR PRO PRO PRO PRO GLY ALA SER ALA ASN ALA SER VAL SEQRES 31 C 628 GLU ARG ILE LYS THR THR SER SER ILE GLU PHE ALA ARG SEQRES 32 C 628 LEU GLN PHE THR TYR ASN HIS ILE GLN ARG HIS VAL ASN SEQRES 33 C 628 ASP MET LEU GLY ARG VAL ALA ILE ALA TRP CYS GLU LEU SEQRES 34 C 628 GLN ASN HIS GLU LEU THR LEU TRP ASN GLU ALA ARG LYS SEQRES 35 C 628 LEU ASN PRO ASN ALA ILE ALA SER VAL THR VAL GLY ARG SEQRES 36 C 628 ARG VAL SER ALA ARG MET LEU GLY ASP VAL MET ALA VAL SEQRES 37 C 628 SER THR CYS VAL PRO VAL ALA ALA ASP ASN VAL ILE VAL SEQRES 38 C 628 GLN ASN SER MET ARG ILE SER SER ARG PRO GLY ALA CYS SEQRES 39 C 628 TYR SER ARG PRO LEU VAL SER PHE ARG TYR GLU ASP GLN SEQRES 40 C 628 GLY PRO LEU VAL GLU GLY GLN LEU GLY GLU ASN ASN GLU SEQRES 41 C 628 LEU ARG LEU THR ARG ASP ALA ILE GLU PRO CYS THR VAL SEQRES 42 C 628 GLY HIS ARG ARG TYR PHE THR PHE GLY GLY GLY TYR VAL SEQRES 43 C 628 TYR PHE GLU GLU TYR ALA TYR SER HIS GLN LEU SER ARG SEQRES 44 C 628 ALA ASP ILE THR THR VAL SER THR PHE ILE ASP LEU ASN SEQRES 45 C 628 ILE THR MET LEU GLU ASP HIS GLU PHE VAL PRO LEU GLU SEQRES 46 C 628 VAL TYR THR ARG HIS GLU ILE LYS ASP SER GLY LEU LEU SEQRES 47 C 628 ASP TYR THR GLU VAL GLN ARG ARG ASN GLN LEU HIS ASP SEQRES 48 C 628 LEU ARG PHE ALA ASP ILE ASP THR VAL ILE HIS ALA ASP SEQRES 49 C 628 ALA ASN ALA ALA HELIX 1 AA1 SER H 28 TYR H 32 5 5 HELIX 2 AA2 GLU H 61 ARG H 64 5 4 HELIX 3 AA3 SER I 28 TYR I 32 5 5 HELIX 4 AA4 GLU I 61 ARG I 64 5 4 HELIX 5 AA5 SER J 28 TYR J 32 5 5 HELIX 6 AA6 GLU J 61 ARG J 64 5 4 HELIX 7 AA7 GLU L 83 THR L 87 5 5 HELIX 8 AA8 GLU M 83 THR M 87 5 5 HELIX 9 AA9 GLU N 83 THR N 87 5 5 HELIX 10 AB1 PRO A 193 LYS A 200 1 8 HELIX 11 AB2 PHE A 223 ASP A 227 5 5 HELIX 12 AB3 GLY A 306 GLU A 310 5 5 HELIX 13 AB4 ALA A 315 ASP A 317 5 3 HELIX 14 AB5 PRO A 358 VAL A 363 1 6 HELIX 15 AB6 PRO A 403 VAL A 407 5 5 HELIX 16 AB7 GLY A 410 TYR A 429 1 20 HELIX 17 AB8 ILE A 501 ASN A 546 1 46 HELIX 18 AB9 ASN A 546 GLY A 556 1 11 HELIX 19 AC1 ALA A 577 ASP A 579 5 3 HELIX 20 AC2 SER A 660 ILE A 664 5 5 HELIX 21 AC3 THR A 690 SER A 697 1 8 HELIX 22 AC4 ASP A 701 ALA A 717 1 17 HELIX 23 AC5 PRO B 193 LYS B 200 1 8 HELIX 24 AC6 PHE B 223 ASP B 227 5 5 HELIX 25 AC7 GLY B 306 GLU B 310 5 5 HELIX 26 AC8 ALA B 315 ASP B 317 5 3 HELIX 27 AC9 PRO B 358 VAL B 363 1 6 HELIX 28 AD1 PRO B 403 VAL B 407 5 5 HELIX 29 AD2 GLY B 410 TYR B 429 1 20 HELIX 30 AD3 ILE B 501 ASN B 546 1 46 HELIX 31 AD4 ASN B 546 GLY B 556 1 11 HELIX 32 AD5 ALA B 577 ASP B 579 5 3 HELIX 33 AD6 SER B 660 ILE B 664 5 5 HELIX 34 AD7 THR B 690 SER B 697 1 8 HELIX 35 AD8 ASP B 701 ALA B 717 1 17 HELIX 36 AD9 PRO C 193 LYS C 200 1 8 HELIX 37 AE1 PHE C 223 ASP C 227 5 5 HELIX 38 AE2 GLY C 306 GLU C 310 5 5 HELIX 39 AE3 ALA C 315 ASP C 317 5 3 HELIX 40 AE4 PRO C 358 VAL C 363 1 6 HELIX 41 AE5 PRO C 403 VAL C 407 5 5 HELIX 42 AE6 GLY C 410 TYR C 429 1 20 HELIX 43 AE7 ILE C 501 ASN C 546 1 46 HELIX 44 AE8 ASN C 546 GLY C 556 1 11 HELIX 45 AE9 ALA C 577 ASP C 579 5 3 HELIX 46 AF1 SER C 660 ILE C 664 5 5 HELIX 47 AF2 THR C 690 SER C 697 1 8 HELIX 48 AF3 ASP C 701 ALA C 717 1 17 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 SER H 21 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA1 4 THR H 77 MET H 80 -1 O ALA H 78 N CYS H 22 SHEET 4 AA1 4 LEU H 69 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AA2 7 GLU H 10 VAL H 12 0 SHEET 2 AA2 7 ILE H 34 GLU H 39 0 SHEET 3 AA2 7 GLU H 46 ILE H 51 -1 O GLU H 46 N LYS H 38 SHEET 4 AA2 7 THR H 57 TYR H 59 -1 O ASN H 58 N TRP H 50 SHEET 5 AA2 7 ALA H 88 THR H 94 -1 O VAL H 89 N GLU H 39 SHEET 6 AA2 7 TYR H 105 TRP H 106 -1 O TYR H 105 N THR H 94 SHEET 7 AA2 7 THR H 110 VAL H 114 -1 O VAL H 112 N ALA H 88 SHEET 1 AA3 4 GLN I 3 GLN I 6 0 SHEET 2 AA3 4 SER I 21 SER I 25 -1 O LYS I 23 N GLN I 5 SHEET 3 AA3 4 THR I 77 MET I 80 -1 O ALA I 78 N CYS I 22 SHEET 4 AA3 4 LEU I 69 ASP I 72 -1 N ASP I 72 O THR I 77 SHEET 1 AA4 7 GLU I 10 VAL I 12 0 SHEET 2 AA4 7 ILE I 34 GLU I 39 0 SHEET 3 AA4 7 GLU I 46 ILE I 51 -1 O GLU I 46 N LYS I 38 SHEET 4 AA4 7 THR I 57 TYR I 59 -1 O ASN I 58 N TRP I 50 SHEET 5 AA4 7 ALA I 88 THR I 94 -1 O VAL I 89 N GLU I 39 SHEET 6 AA4 7 TYR I 105 TRP I 106 -1 O TYR I 105 N THR I 94 SHEET 7 AA4 7 THR I 110 VAL I 114 -1 O VAL I 112 N ALA I 88 SHEET 1 AA5 4 GLN J 3 GLN J 6 0 SHEET 2 AA5 4 SER J 21 SER J 25 -1 O LYS J 23 N GLN J 5 SHEET 3 AA5 4 THR J 77 MET J 80 -1 O ALA J 78 N CYS J 22 SHEET 4 AA5 4 LEU J 69 ASP J 72 -1 N ASP J 72 O THR J 77 SHEET 1 AA6 7 GLU J 10 VAL J 12 0 SHEET 2 AA6 7 ILE J 34 GLU J 39 0 SHEET 3 AA6 7 GLU J 46 ILE J 51 -1 O GLU J 46 N LYS J 38 SHEET 4 AA6 7 THR J 57 TYR J 59 -1 O ASN J 58 N TRP J 50 SHEET 5 AA6 7 ALA J 88 THR J 94 -1 O VAL J 89 N GLU J 39 SHEET 6 AA6 7 TYR J 105 TRP J 106 -1 O TYR J 105 N THR J 94 SHEET 7 AA6 7 THR J 110 VAL J 114 -1 O VAL J 112 N ALA J 88 SHEET 1 AA7 6 LEU L 11 ALA L 12 0 SHEET 2 AA7 6 THR L 106 GLU L 109 1 O LYS L 107 N LEU L 11 SHEET 3 AA7 6 MET L 89 GLN L 94 -1 N TYR L 90 O THR L 106 SHEET 4 AA7 6 MET L 37 GLN L 42 -1 N PHE L 40 O PHE L 91 SHEET 5 AA7 6 LYS L 49 TYR L 53 -1 O ILE L 52 N TRP L 39 SHEET 6 AA7 6 ASN L 57 LEU L 58 -1 O ASN L 57 N TYR L 53 SHEET 1 AA8 3 ALA L 19 ARG L 24 0 SHEET 2 AA8 3 ASP L 74 ILE L 79 -1 O PHE L 75 N CYS L 23 SHEET 3 AA8 3 PHE L 66 SER L 71 -1 N SER L 67 O ASN L 78 SHEET 1 AA9 2 ASP L 30 ASN L 31 0 SHEET 2 AA9 2 ILE L 34 SER L 35 -1 O ILE L 34 N ASN L 31 SHEET 1 AB1 6 LEU M 11 ALA M 12 0 SHEET 2 AB1 6 THR M 106 GLU M 109 1 O LYS M 107 N LEU M 11 SHEET 3 AB1 6 MET M 89 GLN M 94 -1 N TYR M 90 O THR M 106 SHEET 4 AB1 6 MET M 37 GLN M 42 -1 N PHE M 40 O PHE M 91 SHEET 5 AB1 6 LYS M 49 TYR M 53 -1 O ILE M 52 N TRP M 39 SHEET 6 AB1 6 ASN M 57 LEU M 58 -1 O ASN M 57 N TYR M 53 SHEET 1 AB2 3 ALA M 19 ARG M 24 0 SHEET 2 AB2 3 ASP M 74 ILE M 79 -1 O PHE M 75 N CYS M 23 SHEET 3 AB2 3 PHE M 66 SER M 71 -1 N SER M 67 O ASN M 78 SHEET 1 AB3 2 ASP M 30 ASN M 31 0 SHEET 2 AB3 2 ILE M 34 SER M 35 -1 O ILE M 34 N ASN M 31 SHEET 1 AB4 6 LEU N 11 ALA N 12 0 SHEET 2 AB4 6 THR N 106 GLU N 109 1 O LYS N 107 N LEU N 11 SHEET 3 AB4 6 MET N 89 GLN N 94 -1 N TYR N 90 O THR N 106 SHEET 4 AB4 6 MET N 37 GLN N 42 -1 N PHE N 40 O PHE N 91 SHEET 5 AB4 6 LYS N 49 TYR N 53 -1 O ILE N 52 N TRP N 39 SHEET 6 AB4 6 ASN N 57 LEU N 58 -1 O ASN N 57 N TYR N 53 SHEET 1 AB5 3 ALA N 19 ARG N 24 0 SHEET 2 AB5 3 ASP N 74 ILE N 79 -1 O PHE N 75 N CYS N 23 SHEET 3 AB5 3 PHE N 66 SER N 71 -1 N SER N 67 O ASN N 78 SHEET 1 AB6 2 ASP N 30 ASN N 31 0 SHEET 2 AB6 2 ILE N 34 SER N 35 -1 O ILE N 34 N ASN N 31 SHEET 1 AB7 6 VAL A 574 VAL A 576 0 SHEET 2 AB7 6 PHE A 113 VAL A 115 -1 N VAL A 115 O VAL A 574 SHEET 3 AB7 6 GLU A 622 ARG A 624 1 O LEU A 623 N TYR A 114 SHEET 4 AB7 6 VAL A 613 LEU A 617 -1 N GLN A 616 O ARG A 624 SHEET 5 AB7 6 LEU A 601 PHE A 604 -1 N PHE A 604 O VAL A 613 SHEET 6 AB7 6 VAL A 581 VAL A 583 -1 N ILE A 582 O SER A 603 SHEET 1 AB8 4 VAL A 559 MET A 563 0 SHEET 2 AB8 4 MET A 568 THR A 572 -1 O SER A 571 N SER A 560 SHEET 3 AB8 4 VAL A 124 PHE A 127 -1 N VAL A 125 O MET A 568 SHEET 4 AB8 4 THR C 666 VAL C 667 1 O VAL C 667 N GLN A 126 SHEET 1 AB9 5 GLY A 145 GLU A 152 0 SHEET 2 AB9 5 MET A 366 LYS A 368 -1 O THR A 367 N LYS A 151 SHEET 3 AB9 5 HIS A 433 LYS A 435 0 SHEET 4 AB9 5 GLN A 440 ALA A 444 0 SHEET 5 AB9 5 PHE A 448 SER A 457 -1 O ILE A 450 N TYR A 442 SHEET 1 AC110 TYR A 157 PHE A 175 0 SHEET 2 AC110 SER A 180 ALA A 190 -1 O GLY A 184 N GLN A 172 SHEET 3 AC110 GLY A 246 HIS A 248 0 SHEET 4 AC110 HIS A 263 GLY A 266 -1 O GLY A 266 N SER A 171 SHEET 5 AC110 CYS A 271 SER A 280 -1 O VAL A 273 N TRP A 247 SHEET 6 AC110 PHE A 287 LEU A 289 -1 O VAL A 288 N ARG A 279 SHEET 7 AC110 PHE A 294 VAL A 295 -1 O VAL A 295 N PHE A 287 SHEET 8 AC110 PHE A 319 GLN A 321 0 SHEET 9 AC110 ASN A 343 THR A 346 -1 O LEU A 344 N LYS A 320 SHEET 10 AC110 THR A 351 ALA A 353 -1 O VAL A 352 N LEU A 345 SHEET 1 AC2 2 VAL A 206 ARG A 208 0 SHEET 2 AC2 2 ASP A 231 GLU A 233 -1 O MET A 232 N CYS A 207 SHEET 1 AC3 2 TYR A 213 VAL A 214 0 SHEET 2 AC3 2 GLU A 219 THR A 220 -1 O THR A 220 N TYR A 213 SHEET 1 AC4 2 PHE A 325 TYR A 326 0 SHEET 2 AC4 2 PRO A 339 THR A 340 -1 O THR A 340 N PHE A 325 SHEET 1 AC5 3 LEU A 376 TYR A 380 0 SHEET 2 AC5 3 SER A 383 SER A 388 -1 O SER A 383 N TYR A 380 SHEET 3 AC5 3 THR A 393 ASN A 398 -1 O THR A 393 N SER A 388 SHEET 1 AC6 2 ALA A 595 TYR A 597 0 SHEET 2 AC6 2 ILE A 630 PRO A 632 -1 O GLU A 631 N CYS A 596 SHEET 1 AC7 3 ARG A 638 PHE A 643 0 SHEET 2 AC7 3 GLY A 646 GLU A 651 -1 O GLY A 646 N PHE A 643 SHEET 3 AC7 3 ALA A 654 LEU A 659 -1 O LEU A 659 N TYR A 647 SHEET 1 AC8 4 THR A 665 VAL A 667 0 SHEET 2 AC8 4 VAL B 124 PHE B 127 1 O GLN B 126 N VAL A 667 SHEET 3 AC8 4 MET B 568 THR B 572 -1 O MET B 568 N VAL B 125 SHEET 4 AC8 4 VAL B 559 MET B 563 -1 N SER B 560 O SER B 571 SHEET 1 AC9 6 VAL B 574 VAL B 576 0 SHEET 2 AC9 6 PHE B 113 VAL B 115 -1 N VAL B 115 O VAL B 574 SHEET 3 AC9 6 GLU B 622 ARG B 624 1 O LEU B 623 N TYR B 114 SHEET 4 AC9 6 VAL B 613 LEU B 617 -1 N GLN B 616 O ARG B 624 SHEET 5 AC9 6 LEU B 601 PHE B 604 -1 N PHE B 604 O VAL B 613 SHEET 6 AC9 6 VAL B 581 VAL B 583 -1 N ILE B 582 O SER B 603 SHEET 1 AD1 5 GLY B 145 GLU B 152 0 SHEET 2 AD1 5 MET B 366 LYS B 368 -1 O THR B 367 N LYS B 151 SHEET 3 AD1 5 HIS B 433 LYS B 435 0 SHEET 4 AD1 5 GLN B 440 ALA B 444 0 SHEET 5 AD1 5 PHE B 448 SER B 457 -1 O ILE B 450 N TYR B 442 SHEET 1 AD210 TYR B 157 PHE B 175 0 SHEET 2 AD210 SER B 180 ALA B 190 -1 O GLY B 184 N GLN B 172 SHEET 3 AD210 GLY B 246 HIS B 248 0 SHEET 4 AD210 HIS B 263 GLY B 266 -1 O GLY B 266 N SER B 171 SHEET 5 AD210 CYS B 271 SER B 280 -1 O VAL B 273 N TRP B 247 SHEET 6 AD210 PHE B 287 LEU B 289 -1 O VAL B 288 N ARG B 279 SHEET 7 AD210 PHE B 294 VAL B 295 -1 O VAL B 295 N PHE B 287 SHEET 8 AD210 PHE B 319 GLN B 321 0 SHEET 9 AD210 ASN B 343 THR B 346 -1 O LEU B 344 N LYS B 320 SHEET 10 AD210 THR B 351 ALA B 353 -1 O VAL B 352 N LEU B 345 SHEET 1 AD3 2 VAL B 206 ARG B 208 0 SHEET 2 AD3 2 ASP B 231 GLU B 233 -1 O MET B 232 N CYS B 207 SHEET 1 AD4 2 TYR B 213 VAL B 214 0 SHEET 2 AD4 2 GLU B 219 THR B 220 -1 O THR B 220 N TYR B 213 SHEET 1 AD5 2 PHE B 325 TYR B 326 0 SHEET 2 AD5 2 PRO B 339 THR B 340 -1 O THR B 340 N PHE B 325 SHEET 1 AD6 3 LEU B 376 TYR B 380 0 SHEET 2 AD6 3 SER B 383 SER B 388 -1 O SER B 383 N TYR B 380 SHEET 3 AD6 3 THR B 393 ASN B 398 -1 O THR B 393 N SER B 388 SHEET 1 AD7 2 ALA B 595 TYR B 597 0 SHEET 2 AD7 2 ILE B 630 PRO B 632 -1 O GLU B 631 N CYS B 596 SHEET 1 AD8 3 ARG B 638 PHE B 643 0 SHEET 2 AD8 3 GLY B 646 GLU B 651 -1 O GLY B 646 N PHE B 643 SHEET 3 AD8 3 ALA B 654 LEU B 659 -1 O LEU B 659 N TYR B 647 SHEET 1 AD9 4 THR B 665 VAL B 667 0 SHEET 2 AD9 4 VAL C 124 PHE C 127 1 O GLN C 126 N VAL B 667 SHEET 3 AD9 4 MET C 568 THR C 572 -1 O MET C 568 N VAL C 125 SHEET 4 AD9 4 VAL C 559 MET C 563 -1 N SER C 560 O SER C 571 SHEET 1 AE1 6 VAL C 574 VAL C 576 0 SHEET 2 AE1 6 PHE C 113 VAL C 115 -1 N VAL C 115 O VAL C 574 SHEET 3 AE1 6 GLU C 622 ARG C 624 1 O LEU C 623 N TYR C 114 SHEET 4 AE1 6 VAL C 613 LEU C 617 -1 N GLN C 616 O ARG C 624 SHEET 5 AE1 6 LEU C 601 PHE C 604 -1 N PHE C 604 O VAL C 613 SHEET 6 AE1 6 VAL C 581 VAL C 583 -1 N ILE C 582 O SER C 603 SHEET 1 AE2 5 GLY C 145 GLU C 152 0 SHEET 2 AE2 5 MET C 366 LYS C 368 -1 O THR C 367 N LYS C 151 SHEET 3 AE2 5 HIS C 433 LYS C 435 0 SHEET 4 AE2 5 GLN C 440 ALA C 444 0 SHEET 5 AE2 5 PHE C 448 SER C 457 -1 O ILE C 450 N TYR C 442 SHEET 1 AE310 TYR C 157 PHE C 175 0 SHEET 2 AE310 SER C 180 ALA C 190 -1 O GLY C 184 N GLN C 172 SHEET 3 AE310 GLY C 246 HIS C 248 0 SHEET 4 AE310 HIS C 263 GLY C 266 -1 O GLY C 266 N SER C 171 SHEET 5 AE310 CYS C 271 SER C 280 -1 O VAL C 273 N TRP C 247 SHEET 6 AE310 PHE C 287 LEU C 289 -1 O VAL C 288 N ARG C 279 SHEET 7 AE310 PHE C 294 VAL C 295 -1 O VAL C 295 N PHE C 287 SHEET 8 AE310 PHE C 319 GLN C 321 0 SHEET 9 AE310 ASN C 343 THR C 346 -1 O LEU C 344 N LYS C 320 SHEET 10 AE310 THR C 351 ALA C 353 -1 O VAL C 352 N LEU C 345 SHEET 1 AE4 2 VAL C 206 ARG C 208 0 SHEET 2 AE4 2 ASP C 231 GLU C 233 -1 O MET C 232 N CYS C 207 SHEET 1 AE5 2 TYR C 213 VAL C 214 0 SHEET 2 AE5 2 GLU C 219 THR C 220 -1 O THR C 220 N TYR C 213 SHEET 1 AE6 2 PHE C 325 TYR C 326 0 SHEET 2 AE6 2 PRO C 339 THR C 340 -1 O THR C 340 N PHE C 325 SHEET 1 AE7 3 LEU C 376 TYR C 380 0 SHEET 2 AE7 3 SER C 383 SER C 388 -1 O SER C 383 N TYR C 380 SHEET 3 AE7 3 THR C 393 ASN C 398 -1 O THR C 393 N SER C 388 SHEET 1 AE8 2 ALA C 595 TYR C 597 0 SHEET 2 AE8 2 ILE C 630 PRO C 632 -1 O GLU C 631 N CYS C 596 SHEET 1 AE9 3 ARG C 638 PHE C 643 0 SHEET 2 AE9 3 GLY C 646 GLU C 651 -1 O GLY C 646 N PHE C 643 SHEET 3 AE9 3 ALA C 654 LEU C 659 -1 O LEU C 659 N TYR C 647 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 2 CYS I 22 CYS I 92 1555 1555 2.03 SSBOND 3 CYS J 22 CYS J 92 1555 1555 2.03 SSBOND 4 CYS L 23 CYS L 92 1555 1555 2.03 SSBOND 5 CYS M 23 CYS M 92 1555 1555 2.03 SSBOND 6 CYS N 23 CYS N 92 1555 1555 2.03 SSBOND 7 CYS A 116 CYS A 573 1555 1555 2.03 SSBOND 8 CYS A 133 CYS A 529 1555 1555 2.02 SSBOND 9 CYS A 207 CYS A 271 1555 1555 2.03 SSBOND 10 CYS A 364 CYS A 412 1555 1555 2.03 SSBOND 11 CYS A 596 CYS A 633 1555 1555 2.03 SSBOND 12 CYS B 116 CYS B 573 1555 1555 2.03 SSBOND 13 CYS B 133 CYS B 529 1555 1555 2.02 SSBOND 14 CYS B 207 CYS B 271 1555 1555 2.03 SSBOND 15 CYS B 364 CYS B 412 1555 1555 2.03 SSBOND 16 CYS B 596 CYS B 633 1555 1555 2.03 SSBOND 17 CYS C 116 CYS C 573 1555 1555 2.03 SSBOND 18 CYS C 133 CYS C 529 1555 1555 2.02 SSBOND 19 CYS C 207 CYS C 271 1555 1555 2.03 SSBOND 20 CYS C 364 CYS C 412 1555 1555 2.03 SSBOND 21 CYS C 596 CYS C 633 1555 1555 2.03 CISPEP 1 HIS L 80 PRO L 81 0 -7.75 CISPEP 2 HIS M 80 PRO M 81 0 -7.74 CISPEP 3 HIS N 80 PRO N 81 0 -7.72 CISPEP 4 TYR A 282 PRO A 283 0 6.17 CISPEP 5 TYR B 282 PRO B 283 0 6.13 CISPEP 6 TYR C 282 PRO C 283 0 6.16 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