HEADER STRUCTURAL PROTEIN 08-AUG-22 8DZW TITLE RSV F TRIMER BOUND TO RSV-199 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: RSV FUSION PROTEIN; COMPND 3 CHAIN: A, B, C; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: RSV-199 LIGHT CHAIN PROTEIN; COMPND 8 CHAIN: L, M, N; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: RSV-199 HEAVY CHAIN PROTEIN; COMPND 12 CHAIN: H, I, J; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN RESPIRATORY SYNCYTIAL VIRUS A2; SOURCE 3 ORGANISM_TAXID: 11259; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HEK293-6E; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: HEK293-6E; SOURCE 16 MOL_ID: 3; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_COMMON: HUMAN; SOURCE 19 ORGANISM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 23 EXPRESSION_SYSTEM_CELL_LINE: HEK293-6E KEYWDS HUMAN ANTIBODIES, RSV AND MPV FUSION PROTEIN, COMPLEX CRYO-EM KEYWDS 2 STRUCTURE, VIRAL PROTEIN AND ANTIVIRAL PROTEIN, STRUCTURAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR X.WEN,T.S.JARDETZKY JRNL AUTH X.WEN,N.SURYADEVARA,N.KOSE,J.LIU,X.ZHAN,L.S.HANDAL, JRNL AUTH 2 L.E.WILLIAMSON,A.TRIVETTE,R.H.CARNAHAN,T.S.JARDETZKY, JRNL AUTH 3 J.E.CROWE JR. JRNL TITL POTENT CROSS-NEUTRALIZATION OF RESPIRATORY SYNCYTIAL VIRUS JRNL TITL 2 AND HUMAN METAPNEUMOVIRUS THROUGH A STRUCTURALLY CONSERVED JRNL TITL 3 ANTIBODY RECOGNITION MODE. JRNL REF CELL HOST MICROBE 2023 JRNL REFN ESSN 1934-6069 JRNL PMID 37516111 JRNL DOI 10.1016/J.CHOM.2023.07.002 REMARK 2 REMARK 2 RESOLUTION. 2.46 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, CRYOSPARC, UCSF CHIMERA, REMARK 3 PHENIX, CRYOSPARC, CRYOSPARC, CRYOSPARC, REMARK 3 COOT REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 5U68 REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : RIGID BODY 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) : 2.460 REMARK 3 NUMBER OF PARTICLES : 476914 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING ONLY REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8DZW 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_1000265262. 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 : RSV FUSION PROTEIN COMPLEX WITH REMARK 245 RSV-199 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.50 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 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 4508.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 40000.00 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) : 50.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 81000 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: A, B, C, L, H, M, I, N, J 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 THR A 100 REMARK 465 PRO A 101 REMARK 465 ALA A 102 REMARK 465 ALA A 103 REMARK 465 ASN A 104 REMARK 465 ASN A 105 REMARK 465 ARG A 106 REMARK 465 ALA A 107 REMARK 465 ARG A 108 REMARK 465 ARG A 109 REMARK 465 GLU A 110 REMARK 465 LEU A 111 REMARK 465 PRO A 112 REMARK 465 ARG A 113 REMARK 465 PHE A 114 REMARK 465 MET A 115 REMARK 465 ASN A 116 REMARK 465 TYR A 117 REMARK 465 THR A 118 REMARK 465 LEU A 119 REMARK 465 ASN A 120 REMARK 465 ASN A 121 REMARK 465 ALA A 122 REMARK 465 LYS A 123 REMARK 465 LYS A 124 REMARK 465 THR A 125 REMARK 465 ASN A 126 REMARK 465 VAL A 127 REMARK 465 THR A 128 REMARK 465 LEU A 129 REMARK 465 SER A 130 REMARK 465 LYS A 131 REMARK 465 LYS A 132 REMARK 465 ARG A 133 REMARK 465 LYS A 134 REMARK 465 ARG A 135 REMARK 465 ARG A 136 REMARK 465 VAL A 207 REMARK 465 ASN A 208 REMARK 465 LYS A 209 REMARK 465 THR B 100 REMARK 465 PRO B 101 REMARK 465 ALA B 102 REMARK 465 ALA B 103 REMARK 465 ASN B 104 REMARK 465 ASN B 105 REMARK 465 ARG B 106 REMARK 465 ALA B 107 REMARK 465 ARG B 108 REMARK 465 ARG B 109 REMARK 465 GLU B 110 REMARK 465 LEU B 111 REMARK 465 PRO B 112 REMARK 465 ARG B 113 REMARK 465 PHE B 114 REMARK 465 MET B 115 REMARK 465 ASN B 116 REMARK 465 TYR B 117 REMARK 465 THR B 118 REMARK 465 LEU B 119 REMARK 465 ASN B 120 REMARK 465 ASN B 121 REMARK 465 ALA B 122 REMARK 465 LYS B 123 REMARK 465 LYS B 124 REMARK 465 THR B 125 REMARK 465 ASN B 126 REMARK 465 VAL B 127 REMARK 465 THR B 128 REMARK 465 LEU B 129 REMARK 465 SER B 130 REMARK 465 LYS B 131 REMARK 465 LYS B 132 REMARK 465 ARG B 133 REMARK 465 LYS B 134 REMARK 465 ARG B 135 REMARK 465 ARG B 136 REMARK 465 VAL B 207 REMARK 465 ASN B 208 REMARK 465 LYS B 209 REMARK 465 THR C 100 REMARK 465 PRO C 101 REMARK 465 ALA C 102 REMARK 465 ALA C 103 REMARK 465 ASN C 104 REMARK 465 ASN C 105 REMARK 465 ARG C 106 REMARK 465 ALA C 107 REMARK 465 ARG C 108 REMARK 465 ARG C 109 REMARK 465 GLU C 110 REMARK 465 LEU C 111 REMARK 465 PRO C 112 REMARK 465 ARG C 113 REMARK 465 PHE C 114 REMARK 465 MET C 115 REMARK 465 ASN C 116 REMARK 465 TYR C 117 REMARK 465 THR C 118 REMARK 465 LEU C 119 REMARK 465 ASN C 120 REMARK 465 ASN C 121 REMARK 465 ALA C 122 REMARK 465 LYS C 123 REMARK 465 LYS C 124 REMARK 465 THR C 125 REMARK 465 ASN C 126 REMARK 465 VAL C 127 REMARK 465 THR C 128 REMARK 465 LEU C 129 REMARK 465 SER C 130 REMARK 465 LYS C 131 REMARK 465 LYS C 132 REMARK 465 ARG C 133 REMARK 465 LYS C 134 REMARK 465 ARG C 135 REMARK 465 ARG C 136 REMARK 465 VAL C 207 REMARK 465 ASN C 208 REMARK 465 LYS C 209 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 HG1 THR M 146 HG1 THR M 197 1.26 REMARK 500 HG1 THR M 146 OG1 THR M 197 1.37 REMARK 500 O PRO N 7 HG1 THR N 102 1.42 REMARK 500 O GLY C 329 HG SER C 330 1.45 REMARK 500 HD22 ASN B 426 O GLY B 446 1.48 REMARK 500 OD2 ASP B 392 HG SER B 491 1.50 REMARK 500 O GLY B 329 HG SER B 330 1.51 REMARK 500 OD2 ASP C 392 HG SER C 491 1.54 REMARK 500 H VAL N 33 OD1 ASP N 51 1.54 REMARK 500 OE1 GLN A 284 HH TYR A 306 1.55 REMARK 500 OE2 GLU B 92 HG SER B 238 1.57 REMARK 500 OE1 GLN C 284 HH TYR C 306 1.57 REMARK 500 OD2 ASP A 392 HG SER A 491 1.59 REMARK 500 OE2 GLU A 92 HG SER A 238 1.59 REMARK 500 OG1 THR M 146 OG1 THR M 197 2.11 REMARK 500 OD1 ASN N 29 OD1 ASP N 92 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 TYR L 49 C TYR L 49 O -0.152 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 CYS A 69 56.62 33.27 REMARK 500 GLN A 202 -6.16 76.77 REMARK 500 LEU A 204 67.16 -116.60 REMARK 500 THR A 245 -72.80 -67.38 REMARK 500 CYS A 290 -56.13 -120.04 REMARK 500 GLU A 294 -130.16 55.03 REMARK 500 ASP A 338 35.25 -99.45 REMARK 500 SER A 362 -123.20 54.04 REMARK 500 ASN A 363 40.78 -101.74 REMARK 500 ARG A 507 25.11 -143.20 REMARK 500 ASN B 27 -90.39 -155.46 REMARK 500 THR B 245 -72.69 -67.44 REMARK 500 GLU B 294 -127.04 50.84 REMARK 500 ASP B 310 35.74 71.83 REMARK 500 ASN B 345 -65.79 -96.18 REMARK 500 ALA B 346 44.26 -143.16 REMARK 500 SER B 362 -123.18 54.04 REMARK 500 ASN B 363 40.77 -101.77 REMARK 500 ASN C 27 -62.38 -93.63 REMARK 500 ASN C 70 170.15 159.27 REMARK 500 THR C 245 -72.76 -67.52 REMARK 500 GLU C 294 -123.35 58.28 REMARK 500 ASP C 310 36.69 72.28 REMARK 500 ASP C 338 54.05 -94.85 REMARK 500 SER C 362 -123.18 54.04 REMARK 500 ASN C 363 40.82 -101.80 REMARK 500 ASN L 29 -63.43 -107.54 REMARK 500 PRO L 40 -38.18 -38.95 REMARK 500 ASP L 51 -50.96 77.23 REMARK 500 ASP L 60 -8.42 76.34 REMARK 500 ALA L 84 -169.29 -161.59 REMARK 500 SER L 90 -165.09 -125.94 REMARK 500 ASN L 95A -133.58 52.89 REMARK 500 ASN L 129 27.70 48.18 REMARK 500 ASP L 152 -127.53 52.08 REMARK 500 GLU L 211 17.33 52.53 REMARK 500 VAL H 48 -61.04 -108.85 REMARK 500 ILE H 100 -79.38 -119.64 REMARK 500 THR H 131 -162.17 -126.40 REMARK 500 SER H 132 -130.39 59.95 REMARK 500 ASN H 155 42.60 -108.06 REMARK 500 SER H 215 -128.69 46.92 REMARK 500 ASP M 51 -48.89 72.81 REMARK 500 ASN M 95A -135.74 54.10 REMARK 500 ASN M 129 27.18 48.61 REMARK 500 ASP M 152 -117.54 54.27 REMARK 500 GLU M 211 17.89 53.01 REMARK 500 ILE I 100 -75.33 -116.79 REMARK 500 THR I 131 -165.73 -126.01 REMARK 500 SER I 132 -127.87 65.24 REMARK 500 REMARK 500 THIS ENTRY HAS 69 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-27808 RELATED DB: EMDB REMARK 900 REPERTOIRE STUDIES OF HUMAN ANTIBODIES TO RSV AND MPV F DBREF1 8DZW A 26 509 UNP A0A2H4WLA4_HRSV DBREF2 8DZW A A0A2H4WLA4 26 509 DBREF1 8DZW B 26 509 UNP A0A2H4WLA4_HRSV DBREF2 8DZW B A0A2H4WLA4 26 509 DBREF1 8DZW C 26 509 UNP A0A2H4WLA4_HRSV DBREF2 8DZW C A0A2H4WLA4 26 509 DBREF 8DZW L 1 213 PDB 8DZW 8DZW 1 213 DBREF 8DZW H 1 216 PDB 8DZW 8DZW 1 216 DBREF 8DZW M 1 213 PDB 8DZW 8DZW 1 213 DBREF 8DZW I 1 216 PDB 8DZW 8DZW 1 216 DBREF 8DZW N 1 213 PDB 8DZW 8DZW 1 213 DBREF 8DZW J 1 216 PDB 8DZW 8DZW 1 216 SEQADV 8DZW VAL A 152 UNP A0A2H4WLA ILE 152 ENGINEERED MUTATION SEQADV 8DZW CYS A 155 UNP A0A2H4WLA SER 155 ENGINEERED MUTATION SEQADV 8DZW PHE A 190 UNP A0A2H4WLA SER 190 ENGINEERED MUTATION SEQADV 8DZW CYS A 290 UNP A0A2H4WLA SER 290 ENGINEERED MUTATION SEQADV 8DZW VAL B 152 UNP A0A2H4WLA ILE 152 ENGINEERED MUTATION SEQADV 8DZW CYS B 155 UNP A0A2H4WLA SER 155 ENGINEERED MUTATION SEQADV 8DZW PHE B 190 UNP A0A2H4WLA SER 190 ENGINEERED MUTATION SEQADV 8DZW CYS B 290 UNP A0A2H4WLA SER 290 ENGINEERED MUTATION SEQADV 8DZW VAL C 152 UNP A0A2H4WLA ILE 152 ENGINEERED MUTATION SEQADV 8DZW CYS C 155 UNP A0A2H4WLA SER 155 ENGINEERED MUTATION SEQADV 8DZW PHE C 190 UNP A0A2H4WLA SER 190 ENGINEERED MUTATION SEQADV 8DZW CYS C 290 UNP A0A2H4WLA SER 290 ENGINEERED MUTATION SEQRES 1 A 484 GLN ASN ILE THR GLU GLU PHE TYR GLN SER THR CYS SER SEQRES 2 A 484 ALA VAL SER LYS GLY TYR LEU SER ALA LEU ARG THR GLY SEQRES 3 A 484 TRP TYR THR SER VAL ILE THR ILE GLU LEU SER ASN ILE SEQRES 4 A 484 LYS GLU ASN LYS CYS ASN GLY THR ASP ALA LYS VAL LYS SEQRES 5 A 484 LEU ILE LYS GLN GLU LEU ASP LYS TYR LYS ASN ALA VAL SEQRES 6 A 484 THR GLU LEU GLN LEU LEU MET GLN SER THR PRO ALA ALA SEQRES 7 A 484 ASN ASN ARG ALA ARG ARG GLU LEU PRO ARG PHE MET ASN SEQRES 8 A 484 TYR THR LEU ASN ASN ALA LYS LYS THR ASN VAL THR LEU SEQRES 9 A 484 SER LYS LYS ARG LYS ARG ARG PHE LEU GLY PHE LEU LEU SEQRES 10 A 484 GLY VAL GLY SER ALA ILE ALA SER GLY VAL ALA VAL CYS SEQRES 11 A 484 LYS VAL LEU HIS LEU GLU GLY GLU VAL ASN LYS ILE LYS SEQRES 12 A 484 SER ALA LEU LEU SER THR ASN LYS ALA VAL VAL SER LEU SEQRES 13 A 484 SER ASN GLY VAL SER VAL LEU THR PHE LYS VAL LEU ASP SEQRES 14 A 484 LEU LYS ASN TYR ILE ASP LYS GLN LEU LEU PRO ILE VAL SEQRES 15 A 484 ASN LYS GLN SER CYS SER ILE SER ASN ILE GLU THR VAL SEQRES 16 A 484 ILE GLU PHE GLN GLN LYS ASN ASN ARG LEU LEU GLU ILE SEQRES 17 A 484 THR ARG GLU PHE SER VAL ASN ALA GLY VAL THR THR PRO SEQRES 18 A 484 VAL SER THR TYR MET LEU THR ASN SER GLU LEU LEU SER SEQRES 19 A 484 LEU ILE ASN ASP MET PRO ILE THR ASN ASP GLN LYS LYS SEQRES 20 A 484 LEU MET SER ASN ASN VAL GLN ILE VAL ARG GLN GLN SER SEQRES 21 A 484 TYR SER ILE MET CYS ILE ILE LYS GLU GLU VAL LEU ALA SEQRES 22 A 484 TYR VAL VAL GLN LEU PRO LEU TYR GLY VAL ILE ASP THR SEQRES 23 A 484 PRO CYS TRP LYS LEU HIS THR SER PRO LEU CYS THR THR SEQRES 24 A 484 ASN THR LYS GLU GLY SER ASN ILE CYS LEU THR ARG THR SEQRES 25 A 484 ASP ARG GLY TRP TYR CYS ASP ASN ALA GLY SER VAL SER SEQRES 26 A 484 PHE PHE PRO GLN ALA GLU THR CYS LYS VAL GLN SER ASN SEQRES 27 A 484 ARG VAL PHE CYS ASP THR MET ASN SER LEU THR LEU PRO SEQRES 28 A 484 SER GLU VAL ASN LEU CYS ASN VAL ASP ILE PHE ASN PRO SEQRES 29 A 484 LYS TYR ASP CYS LYS ILE MET THR SER LYS THR ASP VAL SEQRES 30 A 484 SER SER SER VAL ILE THR SER LEU GLY ALA ILE VAL SER SEQRES 31 A 484 CYS TYR GLY LYS THR LYS CYS THR ALA SER ASN LYS ASN SEQRES 32 A 484 ARG GLY ILE ILE LYS THR PHE SER ASN GLY CYS ASP TYR SEQRES 33 A 484 VAL SER ASN LYS GLY VAL ASP THR VAL SER VAL GLY ASN SEQRES 34 A 484 THR LEU TYR TYR VAL ASN LYS GLN GLU GLY LYS SER LEU SEQRES 35 A 484 TYR VAL LYS GLY GLU PRO ILE ILE ASN PHE TYR ASP PRO SEQRES 36 A 484 LEU VAL PHE PRO SER ASP GLU PHE ASP ALA SER ILE SER SEQRES 37 A 484 GLN VAL ASN GLU LYS ILE ASN GLN SER LEU ALA PHE ILE SEQRES 38 A 484 ARG LYS SER SEQRES 1 B 484 GLN ASN ILE THR GLU GLU PHE TYR GLN SER THR CYS SER SEQRES 2 B 484 ALA VAL SER LYS GLY TYR LEU SER ALA LEU ARG THR GLY SEQRES 3 B 484 TRP TYR THR SER VAL ILE THR ILE GLU LEU SER ASN ILE SEQRES 4 B 484 LYS GLU ASN LYS CYS ASN GLY THR ASP ALA LYS VAL LYS SEQRES 5 B 484 LEU ILE LYS GLN GLU LEU ASP LYS TYR LYS ASN ALA VAL SEQRES 6 B 484 THR GLU LEU GLN LEU LEU MET GLN SER THR PRO ALA ALA SEQRES 7 B 484 ASN ASN ARG ALA ARG ARG GLU LEU PRO ARG PHE MET ASN SEQRES 8 B 484 TYR THR LEU ASN ASN ALA LYS LYS THR ASN VAL THR LEU SEQRES 9 B 484 SER LYS LYS ARG LYS ARG ARG PHE LEU GLY PHE LEU LEU SEQRES 10 B 484 GLY VAL GLY SER ALA ILE ALA SER GLY VAL ALA VAL CYS SEQRES 11 B 484 LYS VAL LEU HIS LEU GLU GLY GLU VAL ASN LYS ILE LYS SEQRES 12 B 484 SER ALA LEU LEU SER THR ASN LYS ALA VAL VAL SER LEU SEQRES 13 B 484 SER ASN GLY VAL SER VAL LEU THR PHE LYS VAL LEU ASP SEQRES 14 B 484 LEU LYS ASN TYR ILE ASP LYS GLN LEU LEU PRO ILE VAL SEQRES 15 B 484 ASN LYS GLN SER CYS SER ILE SER ASN ILE GLU THR VAL SEQRES 16 B 484 ILE GLU PHE GLN GLN LYS ASN ASN ARG LEU LEU GLU ILE SEQRES 17 B 484 THR ARG GLU PHE SER VAL ASN ALA GLY VAL THR THR PRO SEQRES 18 B 484 VAL SER THR TYR MET LEU THR ASN SER GLU LEU LEU SER SEQRES 19 B 484 LEU ILE ASN ASP MET PRO ILE THR ASN ASP GLN LYS LYS SEQRES 20 B 484 LEU MET SER ASN ASN VAL GLN ILE VAL ARG GLN GLN SER SEQRES 21 B 484 TYR SER ILE MET CYS ILE ILE LYS GLU GLU VAL LEU ALA SEQRES 22 B 484 TYR VAL VAL GLN LEU PRO LEU TYR GLY VAL ILE ASP THR SEQRES 23 B 484 PRO CYS TRP LYS LEU HIS THR SER PRO LEU CYS THR THR SEQRES 24 B 484 ASN THR LYS GLU GLY SER ASN ILE CYS LEU THR ARG THR SEQRES 25 B 484 ASP ARG GLY TRP TYR CYS ASP ASN ALA GLY SER VAL SER SEQRES 26 B 484 PHE PHE PRO GLN ALA GLU THR CYS LYS VAL GLN SER ASN SEQRES 27 B 484 ARG VAL PHE CYS ASP THR MET ASN SER LEU THR LEU PRO SEQRES 28 B 484 SER GLU VAL ASN LEU CYS ASN VAL ASP ILE PHE ASN PRO SEQRES 29 B 484 LYS TYR ASP CYS LYS ILE MET THR SER LYS THR ASP VAL SEQRES 30 B 484 SER SER SER VAL ILE THR SER LEU GLY ALA ILE VAL SER SEQRES 31 B 484 CYS TYR GLY LYS THR LYS CYS THR ALA SER ASN LYS ASN SEQRES 32 B 484 ARG GLY ILE ILE LYS THR PHE SER ASN GLY CYS ASP TYR SEQRES 33 B 484 VAL SER ASN LYS GLY VAL ASP THR VAL SER VAL GLY ASN SEQRES 34 B 484 THR LEU TYR TYR VAL ASN LYS GLN GLU GLY LYS SER LEU SEQRES 35 B 484 TYR VAL LYS GLY GLU PRO ILE ILE ASN PHE TYR ASP PRO SEQRES 36 B 484 LEU VAL PHE PRO SER ASP GLU PHE ASP ALA SER ILE SER SEQRES 37 B 484 GLN VAL ASN GLU LYS ILE ASN GLN SER LEU ALA PHE ILE SEQRES 38 B 484 ARG LYS SER SEQRES 1 C 484 GLN ASN ILE THR GLU GLU PHE TYR GLN SER THR CYS SER SEQRES 2 C 484 ALA VAL SER LYS GLY TYR LEU SER ALA LEU ARG THR GLY SEQRES 3 C 484 TRP TYR THR SER VAL ILE THR ILE GLU LEU SER ASN ILE SEQRES 4 C 484 LYS GLU ASN LYS CYS ASN GLY THR ASP ALA LYS VAL LYS SEQRES 5 C 484 LEU ILE LYS GLN GLU LEU ASP LYS TYR LYS ASN ALA VAL SEQRES 6 C 484 THR GLU LEU GLN LEU LEU MET GLN SER THR PRO ALA ALA SEQRES 7 C 484 ASN ASN ARG ALA ARG ARG GLU LEU PRO ARG PHE MET ASN SEQRES 8 C 484 TYR THR LEU ASN ASN ALA LYS LYS THR ASN VAL THR LEU SEQRES 9 C 484 SER LYS LYS ARG LYS ARG ARG PHE LEU GLY PHE LEU LEU SEQRES 10 C 484 GLY VAL GLY SER ALA ILE ALA SER GLY VAL ALA VAL CYS SEQRES 11 C 484 LYS VAL LEU HIS LEU GLU GLY GLU VAL ASN LYS ILE LYS SEQRES 12 C 484 SER ALA LEU LEU SER THR ASN LYS ALA VAL VAL SER LEU SEQRES 13 C 484 SER ASN GLY VAL SER VAL LEU THR PHE LYS VAL LEU ASP SEQRES 14 C 484 LEU LYS ASN TYR ILE ASP LYS GLN LEU LEU PRO ILE VAL SEQRES 15 C 484 ASN LYS GLN SER CYS SER ILE SER ASN ILE GLU THR VAL SEQRES 16 C 484 ILE GLU PHE GLN GLN LYS ASN ASN ARG LEU LEU GLU ILE SEQRES 17 C 484 THR ARG GLU PHE SER VAL ASN ALA GLY VAL THR THR PRO SEQRES 18 C 484 VAL SER THR TYR MET LEU THR ASN SER GLU LEU LEU SER SEQRES 19 C 484 LEU ILE ASN ASP MET PRO ILE THR ASN ASP GLN LYS LYS SEQRES 20 C 484 LEU MET SER ASN ASN VAL GLN ILE VAL ARG GLN GLN SER SEQRES 21 C 484 TYR SER ILE MET CYS ILE ILE LYS GLU GLU VAL LEU ALA SEQRES 22 C 484 TYR VAL VAL GLN LEU PRO LEU TYR GLY VAL ILE ASP THR SEQRES 23 C 484 PRO CYS TRP LYS LEU HIS THR SER PRO LEU CYS THR THR SEQRES 24 C 484 ASN THR LYS GLU GLY SER ASN ILE CYS LEU THR ARG THR SEQRES 25 C 484 ASP ARG GLY TRP TYR CYS ASP ASN ALA GLY SER VAL SER SEQRES 26 C 484 PHE PHE PRO GLN ALA GLU THR CYS LYS VAL GLN SER ASN SEQRES 27 C 484 ARG VAL PHE CYS ASP THR MET ASN SER LEU THR LEU PRO SEQRES 28 C 484 SER GLU VAL ASN LEU CYS ASN VAL ASP ILE PHE ASN PRO SEQRES 29 C 484 LYS TYR ASP CYS LYS ILE MET THR SER LYS THR ASP VAL SEQRES 30 C 484 SER SER SER VAL ILE THR SER LEU GLY ALA ILE VAL SER SEQRES 31 C 484 CYS TYR GLY LYS THR LYS CYS THR ALA SER ASN LYS ASN SEQRES 32 C 484 ARG GLY ILE ILE LYS THR PHE SER ASN GLY CYS ASP TYR SEQRES 33 C 484 VAL SER ASN LYS GLY VAL ASP THR VAL SER VAL GLY ASN SEQRES 34 C 484 THR LEU TYR TYR VAL ASN LYS GLN GLU GLY LYS SER LEU SEQRES 35 C 484 TYR VAL LYS GLY GLU PRO ILE ILE ASN PHE TYR ASP PRO SEQRES 36 C 484 LEU VAL PHE PRO SER ASP GLU PHE ASP ALA SER ILE SER SEQRES 37 C 484 GLN VAL ASN GLU LYS ILE ASN GLN SER LEU ALA PHE ILE SEQRES 38 C 484 ARG LYS SER SEQRES 1 L 216 GLN ALA VAL VAL THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 L 216 PRO GLY GLN ARG VAL ILE ILE SER CYS THR GLY SER GLY SEQRES 3 L 216 SER ASN LEU GLY ALA ASP TYR GLY VAL HIS TRP TYR GLN SEQRES 4 L 216 GLN LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR GLY SEQRES 5 L 216 ASP ARG ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 L 216 GLY SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7 L 216 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 L 216 SER TYR ASP ARG SER LEU ASN TRP VAL PHE GLY GLY GLY SEQRES 9 L 216 THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 L 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 L 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 L 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 L 216 SER PRO VAL ASN ALA GLY VAL GLU THR THR LYS PRO SER SEQRES 14 L 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 L 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS LYS SER TYR SEQRES 16 L 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 L 216 THR VAL ALA PRO ALA GLU CYS SER SEQRES 1 H 225 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL LYS SEQRES 2 H 225 PRO GLY GLY SER LEU ARG VAL SER CYS VAL VAL SER GLY SEQRES 3 H 225 PHE THR PHE SER SER TYR ARG MET HIS TRP VAL ARG GLN SEQRES 4 H 225 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE THR SEQRES 5 H 225 ALA SER SER SER TYR ILE ASN TYR ALA GLU SER VAL LYS SEQRES 6 H 225 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 H 225 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 225 ALA VAL TYR TYR CYS ALA ARG ASP GLU ASN THR GLY ILE SEQRES 9 H 225 SER HIS TYR TRP PHE ASP PRO TRP GLY GLN GLY THR LEU SEQRES 10 H 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 H 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 H 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 H 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 H 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 H 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 H 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 H 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 H 225 PRO LYS SER CYS SEQRES 1 M 216 GLN ALA VAL VAL THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 M 216 PRO GLY GLN ARG VAL ILE ILE SER CYS THR GLY SER GLY SEQRES 3 M 216 SER ASN LEU GLY ALA ASP TYR GLY VAL HIS TRP TYR GLN SEQRES 4 M 216 GLN LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR GLY SEQRES 5 M 216 ASP ARG ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 M 216 GLY SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7 M 216 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 M 216 SER TYR ASP ARG SER LEU ASN TRP VAL PHE GLY GLY GLY SEQRES 9 M 216 THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 M 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 M 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 M 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 M 216 SER PRO VAL ASN ALA GLY VAL GLU THR THR LYS PRO SER SEQRES 14 M 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 M 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS LYS SER TYR SEQRES 16 M 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 M 216 THR VAL ALA PRO ALA GLU CYS SER SEQRES 1 I 225 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL LYS SEQRES 2 I 225 PRO GLY GLY SER LEU ARG VAL SER CYS VAL VAL SER GLY SEQRES 3 I 225 PHE THR PHE SER SER TYR ARG MET HIS TRP VAL ARG GLN SEQRES 4 I 225 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE THR SEQRES 5 I 225 ALA SER SER SER TYR ILE ASN TYR ALA GLU SER VAL LYS SEQRES 6 I 225 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 I 225 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 I 225 ALA VAL TYR TYR CYS ALA ARG ASP GLU ASN THR GLY ILE SEQRES 9 I 225 SER HIS TYR TRP PHE ASP PRO TRP GLY GLN GLY THR LEU SEQRES 10 I 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 I 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 I 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 I 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 I 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 I 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 I 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 I 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 I 225 PRO LYS SER CYS SEQRES 1 N 216 GLN ALA VAL VAL THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 N 216 PRO GLY GLN ARG VAL ILE ILE SER CYS THR GLY SER GLY SEQRES 3 N 216 SER ASN LEU GLY ALA ASP TYR GLY VAL HIS TRP TYR GLN SEQRES 4 N 216 GLN LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR GLY SEQRES 5 N 216 ASP ARG ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 N 216 GLY SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7 N 216 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 N 216 SER TYR ASP ARG SER LEU ASN TRP VAL PHE GLY GLY GLY SEQRES 9 N 216 THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 N 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 N 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 N 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 N 216 SER PRO VAL ASN ALA GLY VAL GLU THR THR LYS PRO SER SEQRES 14 N 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 N 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS LYS SER TYR SEQRES 16 N 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 N 216 THR VAL ALA PRO ALA GLU CYS SER SEQRES 1 J 225 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL LYS SEQRES 2 J 225 PRO GLY GLY SER LEU ARG VAL SER CYS VAL VAL SER GLY SEQRES 3 J 225 PHE THR PHE SER SER TYR ARG MET HIS TRP VAL ARG GLN SEQRES 4 J 225 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE THR SEQRES 5 J 225 ALA SER SER SER TYR ILE ASN TYR ALA GLU SER VAL LYS SEQRES 6 J 225 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 J 225 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 J 225 ALA VAL TYR TYR CYS ALA ARG ASP GLU ASN THR GLY ILE SEQRES 9 J 225 SER HIS TYR TRP PHE ASP PRO TRP GLY GLN GLY THR LEU SEQRES 10 J 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 J 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 J 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 J 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 J 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 J 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 J 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 J 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 J 225 PRO LYS SER CYS HELIX 1 AA1 ASP A 73 MET A 97 1 25 HELIX 2 AA2 LEU A 138 LEU A 142 5 5 HELIX 3 AA3 ILE A 148 HIS A 159 1 12 HELIX 4 AA4 GLY A 162 ALA A 170 1 9 HELIX 5 AA5 LEU A 195 LYS A 201 1 7 HELIX 6 AA6 ILE A 217 VAL A 239 1 23 HELIX 7 AA7 THR A 253 ASP A 263 1 11 HELIX 8 AA8 THR A 267 ASN A 276 1 10 HELIX 9 AA9 ASN A 277 GLN A 284 1 8 HELIX 10 AB1 GLN A 354 CYS A 358 5 5 HELIX 11 AB2 MET A 370 SER A 372 5 3 HELIX 12 AB3 PRO A 376 VAL A 379 5 4 HELIX 13 AB4 ASN A 380 ASP A 385 1 6 HELIX 14 AB5 PRO A 473 TYR A 478 5 6 HELIX 15 AB6 ASP A 479 PHE A 483 5 5 HELIX 16 AB7 ILE A 492 ILE A 506 1 15 HELIX 17 AB8 ASP B 73 MET B 97 1 25 HELIX 18 AB9 LEU B 138 LEU B 142 5 5 HELIX 19 AC1 ILE B 148 HIS B 159 1 12 HELIX 20 AC2 GLY B 162 LEU B 172 1 11 HELIX 21 AC3 LEU B 195 GLN B 202 1 8 HELIX 22 AC4 ILE B 217 ASN B 227 1 11 HELIX 23 AC5 ASN B 227 VAL B 239 1 13 HELIX 24 AC6 THR B 253 ASP B 263 1 11 HELIX 25 AC7 THR B 267 ASN B 276 1 10 HELIX 26 AC8 ASN B 277 GLN B 284 1 8 HELIX 27 AC9 MET B 370 SER B 372 5 3 HELIX 28 AD1 PRO B 376 VAL B 379 5 4 HELIX 29 AD2 ASN B 380 ASP B 385 1 6 HELIX 30 AD3 PRO B 473 TYR B 478 5 6 HELIX 31 AD4 ASP B 479 PHE B 483 5 5 HELIX 32 AD5 ILE B 492 PHE B 505 1 14 HELIX 33 AD6 ALA C 74 MET C 97 1 24 HELIX 34 AD7 LEU C 138 LEU C 142 5 5 HELIX 35 AD8 ILE C 148 HIS C 159 1 12 HELIX 36 AD9 GLY C 162 LEU C 172 1 11 HELIX 37 AE1 LEU C 195 LEU C 203 1 9 HELIX 38 AE2 ILE C 217 VAL C 239 1 23 HELIX 39 AE3 THR C 253 MET C 264 1 12 HELIX 40 AE4 THR C 267 ASN C 276 1 10 HELIX 41 AE5 ASN C 277 GLN C 284 1 8 HELIX 42 AE6 GLN C 354 CYS C 358 5 5 HELIX 43 AE7 MET C 370 SER C 372 5 3 HELIX 44 AE8 PRO C 376 VAL C 379 5 4 HELIX 45 AE9 ASN C 380 ASP C 385 1 6 HELIX 46 AF1 PRO C 473 TYR C 478 5 6 HELIX 47 AF2 ASP C 479 PHE C 483 5 5 HELIX 48 AF3 ILE C 492 PHE C 505 1 14 HELIX 49 AF4 GLN L 79 GLU L 83 5 5 HELIX 50 AF5 SER L 122 GLN L 127 1 6 HELIX 51 AF6 THR L 182 HIS L 189 1 8 HELIX 52 AF7 THR H 28 TYR H 32 5 5 HELIX 53 AF8 ARG H 83 THR H 87 5 5 HELIX 54 AF9 GLN M 79 GLU M 83 5 5 HELIX 55 AG1 SER M 122 ALA M 128 1 7 HELIX 56 AG2 THR M 182 HIS M 189 1 8 HELIX 57 AG3 THR I 28 TYR I 32 5 5 HELIX 58 AG4 ARG I 83 THR I 87 5 5 HELIX 59 AG5 PRO I 202 ASN I 204 5 3 HELIX 60 AG6 GLN N 79 GLU N 83 5 5 HELIX 61 AG7 SER N 122 GLN N 127 1 6 HELIX 62 AG8 THR N 182 HIS N 189 1 8 HELIX 63 AG9 THR J 28 TYR J 32 5 5 HELIX 64 AH1 ARG J 83 THR J 87 5 5 HELIX 65 AH2 SER J 187 LEU J 189 5 3 SHEET 1 AA1 9 THR A 29 TYR A 33 0 SHEET 2 AA1 9 SER A 38 ARG A 49 -1 O SER A 38 N TYR A 33 SHEET 3 AA1 9 VAL A 308 THR A 318 -1 O HIS A 317 N ALA A 39 SHEET 4 AA1 9 GLY A 340 CYS A 343 -1 O TYR A 342 N TRP A 314 SHEET 5 AA1 9 VAL A 349 PHE A 352 -1 O SER A 350 N CYS A 343 SHEET 6 AA1 9 LYS A 359 GLN A 361 0 SHEET 7 AA1 9 ARG A 364 ASP A 368 -1 O PHE A 366 N LYS A 359 SHEET 8 AA1 9 LEU A 373 LEU A 375 -1 O LEU A 375 N VAL A 349 SHEET 9 AA1 9 LYS A 465 VAL A 469 1 O LEU A 467 N PHE A 32 SHEET 1 AA2 6 LYS A 176 SER A 180 0 SHEET 2 AA2 6 SER A 186 ASP A 194 -1 O THR A 189 N ALA A 177 SHEET 3 AA2 6 GLY A 51 GLU A 60 1 N VAL A 56 O LEU A 188 SHEET 4 AA2 6 VAL A 296 LEU A 305 -1 O LEU A 303 N TYR A 53 SHEET 5 AA2 6 TYR A 286 LYS A 293 -1 N ILE A 291 O ALA A 298 SHEET 6 AA2 6 VAL A 243 THR A 244 -1 N THR A 244 O SER A 287 SHEET 1 AA3 4 LEU A 321 CYS A 322 0 SHEET 2 AA3 4 CYS A 333 ARG A 336 -1 O LEU A 334 N LEU A 321 SHEET 3 AA3 4 LYS A 394 SER A 398 -1 O MET A 396 N THR A 335 SHEET 4 AA3 4 GLU A 487 SER A 491 -1 O GLU A 487 N THR A 397 SHEET 1 AA4 3 SER A 404 ILE A 407 0 SHEET 2 AA4 3 GLY A 411 CYS A 416 -1 O ILE A 413 N VAL A 406 SHEET 3 AA4 3 GLY A 438 SER A 443 -1 O ASP A 440 N VAL A 414 SHEET 1 AA5 4 GLY A 430 THR A 434 0 SHEET 2 AA5 4 CYS A 422 ASN A 426 -1 N ALA A 424 O ILE A 432 SHEET 3 AA5 4 THR A 449 VAL A 452 -1 O THR A 449 N SER A 425 SHEET 4 AA5 4 THR A 455 TYR A 458 -1 O TYR A 457 N VAL A 450 SHEET 1 AA613 THR B 29 TYR B 33 0 SHEET 2 AA613 SER B 38 GLU B 60 -1 O SER B 38 N TYR B 33 SHEET 3 AA613 LYS B 176 SER B 180 0 SHEET 4 AA613 SER B 186 ASP B 194 -1 O THR B 189 N ALA B 177 SHEET 5 AA613 VAL B 243 THR B 244 0 SHEET 6 AA613 TYR B 286 LYS B 293 -1 O SER B 287 N THR B 244 SHEET 7 AA613 VAL B 296 THR B 318 -1 O VAL B 300 N ILE B 288 SHEET 8 AA613 GLY B 340 ASP B 344 -1 O TYR B 342 N TRP B 314 SHEET 9 AA613 VAL B 349 PHE B 352 -1 O SER B 350 N CYS B 343 SHEET 10 AA613 CYS B 358 GLN B 361 0 SHEET 11 AA613 ARG B 364 ASP B 368 -1 O PHE B 366 N LYS B 359 SHEET 12 AA613 LEU B 373 LEU B 375 -1 O LEU B 375 N VAL B 349 SHEET 13 AA613 LYS B 465 VAL B 469 1 O VAL B 469 N PHE B 32 SHEET 1 AA7 4 LEU B 321 CYS B 322 0 SHEET 2 AA7 4 CYS B 333 ARG B 336 -1 O LEU B 334 N LEU B 321 SHEET 3 AA7 4 LYS B 394 SER B 398 -1 O MET B 396 N THR B 335 SHEET 4 AA7 4 GLU B 487 SER B 491 -1 O GLU B 487 N THR B 397 SHEET 1 AA8 3 SER B 404 ILE B 407 0 SHEET 2 AA8 3 GLY B 411 CYS B 416 -1 O ILE B 413 N VAL B 406 SHEET 3 AA8 3 GLY B 438 SER B 443 -1 O ASP B 440 N VAL B 414 SHEET 1 AA9 4 GLY B 430 THR B 434 0 SHEET 2 AA9 4 CYS B 422 ASN B 426 -1 N ALA B 424 O ILE B 432 SHEET 3 AA9 4 THR B 449 VAL B 452 -1 O SER B 451 N THR B 423 SHEET 4 AA9 4 THR B 455 TYR B 458 -1 O TYR B 457 N VAL B 450 SHEET 1 AB113 THR C 29 TYR C 33 0 SHEET 2 AB113 SER C 38 GLU C 60 -1 O SER C 38 N TYR C 33 SHEET 3 AB113 LYS C 176 SER C 180 0 SHEET 4 AB113 SER C 186 ASP C 194 -1 O THR C 189 N ALA C 177 SHEET 5 AB113 VAL C 243 THR C 244 0 SHEET 6 AB113 TYR C 286 LYS C 293 -1 O SER C 287 N THR C 244 SHEET 7 AB113 VAL C 296 THR C 318 -1 O ALA C 298 N ILE C 291 SHEET 8 AB113 GLY C 340 ASN C 345 -1 O TYR C 342 N TRP C 314 SHEET 9 AB113 SER C 348 PHE C 352 -1 O SER C 348 N ASN C 345 SHEET 10 AB113 LYS C 359 GLN C 361 0 SHEET 11 AB113 ARG C 364 ASP C 368 -1 O PHE C 366 N LYS C 359 SHEET 12 AB113 LEU C 373 LEU C 375 -1 O LEU C 375 N VAL C 349 SHEET 13 AB113 LYS C 465 VAL C 469 1 O LYS C 465 N GLU C 30 SHEET 1 AB2 4 LEU C 321 CYS C 322 0 SHEET 2 AB2 4 CYS C 333 ARG C 336 -1 O LEU C 334 N LEU C 321 SHEET 3 AB2 4 LYS C 394 SER C 398 -1 O SER C 398 N CYS C 333 SHEET 4 AB2 4 GLU C 487 SER C 491 -1 O GLU C 487 N THR C 397 SHEET 1 AB3 3 SER C 404 ILE C 407 0 SHEET 2 AB3 3 GLY C 411 CYS C 416 -1 O ILE C 413 N VAL C 406 SHEET 3 AB3 3 GLY C 438 SER C 443 -1 O ASP C 440 N VAL C 414 SHEET 1 AB4 4 GLY C 430 THR C 434 0 SHEET 2 AB4 4 CYS C 422 ASN C 426 -1 N ALA C 424 O ILE C 432 SHEET 3 AB4 4 THR C 449 VAL C 452 -1 O THR C 449 N SER C 425 SHEET 4 AB4 4 THR C 455 TYR C 458 -1 O TYR C 457 N VAL C 450 SHEET 1 AB5 6 SER L 9 GLY L 13 0 SHEET 2 AB5 6 HIS L 34 GLN L 38 0 SHEET 3 AB5 6 LYS L 45 ILE L 48 -1 O LEU L 47 N TRP L 35 SHEET 4 AB5 6 ASP L 85 ASP L 92 -1 O GLN L 89 N HIS L 34 SHEET 5 AB5 6 ASN L 95A VAL L 97 -1 O ASN L 95A N ASP L 92 SHEET 6 AB5 6 THR L 102 VAL L 106 -1 O THR L 102 N TYR L 86 SHEET 1 AB6 3 ARG L 18 THR L 24 0 SHEET 2 AB6 3 SER L 70 THR L 76 -1 O ALA L 71 N CYS L 23 SHEET 3 AB6 3 PHE L 62 SER L 67 -1 N SER L 63 O ALA L 74 SHEET 1 AB7 5 SER L 115 PHE L 119 0 SHEET 2 AB7 5 ALA L 131 PHE L 140 -1 O SER L 138 N SER L 115 SHEET 3 AB7 5 VAL L 160 THR L 162 0 SHEET 4 AB7 5 SER L 166 LYS L 167 0 SHEET 5 AB7 5 TYR L 173 LEU L 181 -1 O ALA L 174 N SER L 166 SHEET 1 AB8 5 VAL L 145 ALA L 151 0 SHEET 2 AB8 5 SER L 154 VAL L 156 -1 O VAL L 156 N TRP L 149 SHEET 3 AB8 5 TYR L 192 HIS L 198 -1 O SER L 193 N LYS L 150 SHEET 4 AB8 5 SER L 201 VAL L 203 -1 O SER L 201 N HIS L 198 SHEET 5 AB8 5 THR L 206 VAL L 207 -1 O VAL L 207 N TYR L 192 SHEET 1 AB9 4 GLN H 3 SER H 7 0 SHEET 2 AB9 4 SER H 17 SER H 25 -1 O VAL H 23 N VAL H 5 SHEET 3 AB9 4 SER H 77 ASN H 82A-1 O MET H 82 N LEU H 18 SHEET 4 AB9 4 PHE H 67 ASP H 72 -1 N ASP H 72 O SER H 77 SHEET 1 AC1 6 MET H 34 GLN H 39 0 SHEET 2 AC1 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 3 AC1 6 ILE H 57 TYR H 59 -1 O ASN H 58 N SER H 50 SHEET 4 AC1 6 ALA H 88 ASN H 97 -1 O TYR H 91 N VAL H 37 SHEET 5 AC1 6 TYR H 100C TRP H 103 -1 O TRP H 100D N GLU H 96 SHEET 6 AC1 6 THR H 107 VAL H 109 -1 O THR H 107 N TYR H 90 SHEET 1 AC2 4 SER H 120 LEU H 124 0 SHEET 2 AC2 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AC2 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AC2 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AC3 3 THR H 151 SER H 153 0 SHEET 2 AC3 3 ILE H 195 ASN H 199 -1 O ASN H 197 N SER H 153 SHEET 3 AC3 3 VAL H 207 LYS H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AC4 6 SER M 9 GLY M 13 0 SHEET 2 AC4 6 HIS M 34 GLN M 38 0 SHEET 3 AC4 6 LYS M 45 ILE M 48 -1 O LEU M 47 N TRP M 35 SHEET 4 AC4 6 ASP M 85 ASP M 92 -1 O ASP M 85 N GLN M 38 SHEET 5 AC4 6 ASN M 95A PHE M 98 -1 O VAL M 97 N SER M 90 SHEET 6 AC4 6 THR M 102 VAL M 106 -1 O THR M 102 N TYR M 86 SHEET 1 AC5 3 ARG M 18 THR M 24 0 SHEET 2 AC5 3 SER M 70 THR M 76 -1 O ALA M 71 N CYS M 23 SHEET 3 AC5 3 PHE M 62 SER M 67 -1 N SER M 63 O ALA M 74 SHEET 1 AC6 5 SER M 115 PHE M 119 0 SHEET 2 AC6 5 ALA M 131 PHE M 140 -1 O LEU M 136 N THR M 117 SHEET 3 AC6 5 VAL M 160 THR M 162 0 SHEET 4 AC6 5 SER M 166 LYS M 167 0 SHEET 5 AC6 5 TYR M 173 LEU M 181 -1 O ALA M 174 N SER M 166 SHEET 1 AC7 5 THR M 146 ALA M 151 0 SHEET 2 AC7 5 SER M 154 VAL M 156 -1 O VAL M 156 N TRP M 149 SHEET 3 AC7 5 TYR M 192 HIS M 198 -1 O SER M 193 N LYS M 150 SHEET 4 AC7 5 SER M 201 VAL M 203 -1 O SER M 201 N HIS M 198 SHEET 5 AC7 5 THR M 206 VAL M 207 -1 O VAL M 207 N TYR M 192 SHEET 1 AC8 4 GLN I 3 SER I 7 0 SHEET 2 AC8 4 SER I 17 SER I 25 -1 O SER I 21 N SER I 7 SHEET 3 AC8 4 SER I 77 ASN I 82A-1 O MET I 82 N LEU I 18 SHEET 4 AC8 4 PHE I 67 ASP I 72 -1 N SER I 70 O TYR I 79 SHEET 1 AC9 7 VAL I 11 VAL I 12 0 SHEET 2 AC9 7 MET I 34 GLN I 39 0 SHEET 3 AC9 7 LEU I 45 ILE I 51 -1 O VAL I 48 N TRP I 36 SHEET 4 AC9 7 ILE I 57 TYR I 59 -1 O ASN I 58 N SER I 50 SHEET 5 AC9 7 ALA I 88 ASN I 97 -1 O TYR I 91 N VAL I 37 SHEET 6 AC9 7 TYR I 100C TRP I 103 -1 O TRP I 100D N GLU I 96 SHEET 7 AC9 7 THR I 107 VAL I 111 -1 O VAL I 109 N ALA I 88 SHEET 1 AD1 4 SER I 120 LEU I 124 0 SHEET 2 AD1 4 THR I 135 TYR I 145 -1 O LEU I 141 N PHE I 122 SHEET 3 AD1 4 TYR I 176 PRO I 185 -1 O VAL I 184 N ALA I 136 SHEET 4 AD1 4 VAL I 163 THR I 165 -1 N HIS I 164 O VAL I 181 SHEET 1 AD2 3 VAL I 150 SER I 153 0 SHEET 2 AD2 3 ILE I 195 HIS I 200 -1 O ASN I 199 N THR I 151 SHEET 3 AD2 3 VAL I 207 LYS I 210 -1 O VAL I 207 N VAL I 198 SHEET 1 AD3 6 SER N 9 GLY N 13 0 SHEET 2 AD3 6 HIS N 34 GLN N 38 0 SHEET 3 AD3 6 LYS N 45 ILE N 48 -1 O LEU N 47 N TRP N 35 SHEET 4 AD3 6 ASP N 85 ASP N 92 -1 O GLN N 89 N HIS N 34 SHEET 5 AD3 6 ASN N 95A PHE N 98 -1 O ASN N 95A N ASP N 92 SHEET 6 AD3 6 THR N 102 VAL N 106 -1 O THR N 102 N TYR N 86 SHEET 1 AD4 3 VAL N 19 THR N 24 0 SHEET 2 AD4 3 SER N 70 ILE N 75 -1 O ALA N 71 N CYS N 23 SHEET 3 AD4 3 PHE N 62 SER N 67 -1 N SER N 63 O ALA N 74 SHEET 1 AD5 5 SER N 115 PHE N 119 0 SHEET 2 AD5 5 ALA N 131 PHE N 140 -1 O LEU N 136 N THR N 117 SHEET 3 AD5 5 VAL N 160 THR N 162 0 SHEET 4 AD5 5 SER N 166 LYS N 167 0 SHEET 5 AD5 5 TYR N 173 LEU N 181 -1 O ALA N 174 N SER N 166 SHEET 1 AD6 5 THR N 146 ALA N 151 0 SHEET 2 AD6 5 SER N 154 PRO N 155 -1 O SER N 154 N ALA N 151 SHEET 3 AD6 5 TYR N 192 HIS N 198 -1 O THR N 197 N THR N 146 SHEET 4 AD6 5 SER N 201 VAL N 203 -1 O SER N 201 N HIS N 198 SHEET 5 AD6 5 THR N 206 VAL N 207 -1 O VAL N 207 N TYR N 192 SHEET 1 AD7 4 GLN J 3 SER J 7 0 SHEET 2 AD7 4 SER J 17 SER J 25 -1 O SER J 21 N SER J 7 SHEET 3 AD7 4 SER J 77 ASN J 82A-1 O MET J 82 N LEU J 18 SHEET 4 AD7 4 PHE J 67 ASP J 72 -1 N SER J 70 O TYR J 79 SHEET 1 AD8 6 MET J 34 GLN J 39 0 SHEET 2 AD8 6 LEU J 45 ILE J 51 -1 O VAL J 48 N TRP J 36 SHEET 3 AD8 6 ILE J 57 TYR J 59 -1 O ASN J 58 N SER J 50 SHEET 4 AD8 6 ALA J 88 ASN J 97 -1 O TYR J 91 N VAL J 37 SHEET 5 AD8 6 TYR J 100C TRP J 103 -1 O TRP J 100D N GLU J 96 SHEET 6 AD8 6 THR J 107 VAL J 109 -1 O THR J 107 N TYR J 90 SHEET 1 AD9 4 PHE J 122 LEU J 124 0 SHEET 2 AD9 4 THR J 135 TYR J 145 -1 O LEU J 141 N PHE J 122 SHEET 3 AD9 4 TYR J 176 PRO J 185 -1 O VAL J 184 N ALA J 136 SHEET 4 AD9 4 VAL J 163 THR J 165 -1 N HIS J 164 O VAL J 181 SHEET 1 AE1 3 VAL J 150 VAL J 152 0 SHEET 2 AE1 3 ILE J 195 HIS J 200 -1 O ASN J 199 N THR J 151 SHEET 3 AE1 3 VAL J 207 LYS J 210 -1 O VAL J 207 N VAL J 198 SSBOND 1 CYS A 37 CYS A 439 1555 1555 2.03 SSBOND 2 CYS A 69 CYS A 212 1555 1555 2.01 SSBOND 3 CYS A 155 CYS A 290 1555 1555 2.04 SSBOND 4 CYS A 313 CYS A 343 1555 1555 2.03 SSBOND 5 CYS A 322 CYS A 333 1555 1555 2.03 SSBOND 6 CYS A 358 CYS A 367 1555 1555 2.03 SSBOND 7 CYS A 382 CYS A 393 1555 1555 2.03 SSBOND 8 CYS A 416 CYS A 422 1555 1555 2.04 SSBOND 9 CYS B 37 CYS B 439 1555 1555 2.03 SSBOND 10 CYS B 69 CYS B 212 1555 1555 2.03 SSBOND 11 CYS B 155 CYS B 290 1555 1555 2.04 SSBOND 12 CYS B 313 CYS B 343 1555 1555 2.03 SSBOND 13 CYS B 322 CYS B 333 1555 1555 2.03 SSBOND 14 CYS B 358 CYS B 367 1555 1555 2.03 SSBOND 15 CYS B 382 CYS B 393 1555 1555 2.03 SSBOND 16 CYS B 416 CYS B 422 1555 1555 2.04 SSBOND 17 CYS C 37 CYS C 439 1555 1555 2.03 SSBOND 18 CYS C 69 CYS C 212 1555 1555 1.97 SSBOND 19 CYS C 155 CYS C 290 1555 1555 2.04 SSBOND 20 CYS C 313 CYS C 343 1555 1555 2.03 SSBOND 21 CYS C 322 CYS C 333 1555 1555 2.03 SSBOND 22 CYS C 358 CYS C 367 1555 1555 2.03 SSBOND 23 CYS C 382 CYS C 393 1555 1555 2.03 SSBOND 24 CYS C 416 CYS C 422 1555 1555 2.04 SSBOND 25 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 26 CYS L 135 CYS L 194 1555 1555 2.04 SSBOND 27 CYS L 212 CYS H 216 1555 1555 2.03 SSBOND 28 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 29 CYS H 140 CYS H 196 1555 1555 1.99 SSBOND 30 CYS M 23 CYS M 88 1555 1555 2.04 SSBOND 31 CYS M 135 CYS M 194 1555 1555 2.03 SSBOND 32 CYS M 212 CYS I 216 1555 1555 2.03 SSBOND 33 CYS I 22 CYS I 92 1555 1555 2.04 SSBOND 34 CYS I 140 CYS I 196 1555 1555 2.01 SSBOND 35 CYS N 23 CYS N 88 1555 1555 2.04 SSBOND 36 CYS N 135 CYS N 194 1555 1555 2.03 SSBOND 37 CYS N 212 CYS J 216 1555 1555 2.03 SSBOND 38 CYS J 22 CYS J 92 1555 1555 2.04 SSBOND 39 CYS J 140 CYS J 196 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