HEADER IMMUNE SYSTEM 10-JAN-25 9MSO TITLE CRYSTAL STRUCTURE OF MPXV A35R IN COMPLEX WITH NEUTRALIZING ANTIBODY TITLE 2 EV35-6 COMPND MOL_ID: 1; COMPND 2 MOLECULE: EV35-6 HEAVY CHAIN; COMPND 3 CHAIN: H, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: EV35-6 LIGHT CHAIN; COMPND 7 CHAIN: L, B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: PROTEIN OPG161; COMPND 11 CHAIN: G, I, E, F; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: MONKEYPOX VIRUS; SOURCE 13 ORGANISM_TAXID: 10244; SOURCE 14 GENE: OPG161, MPXVGP145; SOURCE 15 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS ANTIBODY, MPOX, MONKEYPOX, A35, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.YUAN,X.ZHU,I.A.WILSON REVDAT 1 10-SEP-25 9MSO 0 JRNL AUTH R.F.FANTIN,M.YUAN,S.C.PARK,B.BOZARTH,H.COHN,M.IGNACIO, JRNL AUTH 2 P.EARL,A.CIVLJAK,G.LAGHLALI,D.ZHANG,X.ZHU,J.CRANDELL, JRNL AUTH 3 V.MONTEIRO,J.J.CLARK,C.COTTER,M.BURKHARDT,G.SINGH,P.WARANG, JRNL AUTH 4 J.GARCIA-BERNALT DIEGO,K.SRIVASTAVA,L.A.LUGO,L.PISCHEL, JRNL AUTH 5 I.YILDIRIM,S.B.OMER,D.DA SILVA,F.KRAMMER,G.BAJIC,V.SIMON, JRNL AUTH 6 M.SCHOTSAERT,C.LUCAS,I.A.WILSON,B.MOSS,C.H.COELHO JRNL TITL HUMAN MONOCLONAL ANTIBODIES TARGETING A35 PROTECT FROM DEATH JRNL TITL 2 CAUSED BY MPOX. JRNL REF CELL 2025 JRNL REFN ISSN 1097-4172 JRNL PMID 40865529 JRNL DOI 10.1016/J.CELL.2025.08.004 REMARK 2 REMARK 2 RESOLUTION. 3.18 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.21.2_5419: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.18 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.90 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 87.3 REMARK 3 NUMBER OF REFLECTIONS : 21533 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.241 REMARK 3 R VALUE (WORKING SET) : 0.240 REMARK 3 FREE R VALUE : 0.251 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.250 REMARK 3 FREE R VALUE TEST SET COUNT : 1131 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 43.9000 - 6.3500 0.99 3044 172 0.2107 0.2209 REMARK 3 2 6.3500 - 5.0400 0.99 2925 162 0.2227 0.2264 REMARK 3 3 5.0400 - 4.4100 0.95 2784 157 0.2152 0.2154 REMARK 3 4 4.4100 - 4.0000 0.92 2688 149 0.2239 0.2487 REMARK 3 5 4.0000 - 3.7200 0.88 2565 137 0.2638 0.2736 REMARK 3 6 3.7200 - 3.5000 0.86 2476 144 0.2891 0.3026 REMARK 3 7 3.5000 - 3.3200 0.84 2411 121 0.3133 0.3236 REMARK 3 8 3.3200 - 3.1800 0.53 1509 89 0.3485 0.3891 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.620 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.002 NULL REMARK 3 ANGLE : 0.492 NULL REMARK 3 CHIRALITY : 0.040 1410 REMARK 3 PLANARITY : 0.004 1611 REMARK 3 DIHEDRAL : 11.384 3276 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9MSO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1000291737. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-NOV-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.4 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL12-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23030 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.180 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5 REMARK 200 DATA REDUNDANCY : 5.300 REMARK 200 R MERGE (I) : 0.39300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 3.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.25 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31 REMARK 200 COMPLETENESS FOR SHELL (%) : 88.5 REMARK 200 DATA REDUNDANCY IN SHELL : 3.70 REMARK 200 R MERGE FOR SHELL (I) : 1.20800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.13 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% GLYCEROL, 16% PEG-8000 (V/V), AND REMARK 280 0.04 M KH2PO4, PH 7.4, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 36.25200 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.22650 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 82.74850 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.22650 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.25200 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 82.74850 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, G, I 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F 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 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 CYS H 216 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 SER G 90 REMARK 465 THR G 91 REMARK 465 THR G 92 REMARK 465 GLN G 93 REMARK 465 TYR G 94 REMARK 465 ASP G 95 REMARK 465 HIS G 96 REMARK 465 THR G 163 REMARK 465 SER G 164 REMARK 465 ASP G 165 REMARK 465 TYR G 166 REMARK 465 HIS G 184 REMARK 465 HIS G 185 REMARK 465 HIS G 186 REMARK 465 HIS G 187 REMARK 465 HIS G 188 REMARK 465 HIS G 189 REMARK 465 SER I 90 REMARK 465 THR I 91 REMARK 465 THR I 92 REMARK 465 GLN I 93 REMARK 465 TYR I 94 REMARK 465 ASP I 95 REMARK 465 HIS I 96 REMARK 465 LYS I 97 REMARK 465 ASP I 165 REMARK 465 TYR I 166 REMARK 465 GLN I 167 REMARK 465 ASP I 168 REMARK 465 SER I 169 REMARK 465 GLY I 182 REMARK 465 SER I 183 REMARK 465 HIS I 184 REMARK 465 HIS I 185 REMARK 465 HIS I 186 REMARK 465 HIS I 187 REMARK 465 HIS I 188 REMARK 465 HIS I 189 REMARK 465 SER A 127 REMARK 465 SER A 128 REMARK 465 LYS A 129 REMARK 465 SER A 130 REMARK 465 THR A 131 REMARK 465 SER A 132 REMARK 465 GLY A 133 REMARK 465 GLY A 134 REMARK 465 LYS A 214 REMARK 465 SER A 215 REMARK 465 CYS A 216 REMARK 465 GLY B 212 REMARK 465 GLU B 213 REMARK 465 CYS B 214 REMARK 465 SER E 90 REMARK 465 THR E 91 REMARK 465 THR E 92 REMARK 465 GLN E 93 REMARK 465 TYR E 94 REMARK 465 ASP E 95 REMARK 465 HIS E 96 REMARK 465 LYS E 97 REMARK 465 SER E 164 REMARK 465 ASP E 165 REMARK 465 TYR E 166 REMARK 465 GLN E 167 REMARK 465 ASP E 168 REMARK 465 SER E 169 REMARK 465 GLY E 182 REMARK 465 SER E 183 REMARK 465 HIS E 184 REMARK 465 HIS E 185 REMARK 465 HIS E 186 REMARK 465 HIS E 187 REMARK 465 HIS E 188 REMARK 465 HIS E 189 REMARK 465 SER F 90 REMARK 465 THR F 91 REMARK 465 THR F 92 REMARK 465 GLN F 93 REMARK 465 TYR F 94 REMARK 465 ASP F 95 REMARK 465 HIS F 96 REMARK 465 LYS F 97 REMARK 465 GLU F 98 REMARK 465 SER F 164 REMARK 465 ASP F 165 REMARK 465 TYR F 166 REMARK 465 GLN F 167 REMARK 465 ASP F 168 REMARK 465 SER F 169 REMARK 465 SER F 183 REMARK 465 HIS F 184 REMARK 465 HIS F 185 REMARK 465 HIS F 186 REMARK 465 HIS F 187 REMARK 465 HIS F 188 REMARK 465 HIS F 189 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 H 15 -5.63 77.31 REMARK 500 ILE H 48 -60.70 -97.54 REMARK 500 ARG H 66 30.72 -140.64 REMARK 500 ASP H 144 65.45 60.35 REMARK 500 SER L 30 -133.72 57.43 REMARK 500 ASP L 50 14.61 59.69 REMARK 500 ALA L 51 -6.10 70.92 REMARK 500 ASN L 93 -109.60 39.41 REMARK 500 THR I 162 -106.54 55.15 REMARK 500 THR I 163 -151.78 53.66 REMARK 500 SER I 172 -16.16 -141.77 REMARK 500 SER A 15 -4.45 77.60 REMARK 500 ILE A 48 -60.35 -98.14 REMARK 500 ARG A 66 30.35 -140.73 REMARK 500 LYS A 100D 142.69 49.96 REMARK 500 ASP A 144 66.07 60.74 REMARK 500 SER B 30 -132.71 57.93 REMARK 500 ASP B 50 15.11 59.40 REMARK 500 ALA B 51 -6.63 71.58 REMARK 500 SER B 92 -158.46 -149.10 REMARK 500 ASN B 93 94.18 -64.14 REMARK 500 GLN F 106 70.13 57.97 REMARK 500 REMARK 500 REMARK: NULL DBREF 9MSO H 1 216 PDB 9MSO 9MSO 1 216 DBREF 9MSO L 1 214 PDB 9MSO 9MSO 1 214 DBREF1 9MSO G 90 181 UNP PG161_MONPV DBREF2 9MSO G A0A7H0DND2 90 181 DBREF1 9MSO I 90 181 UNP PG161_MONPV DBREF2 9MSO I A0A7H0DND2 90 181 DBREF 9MSO A 1 216 PDB 9MSO 9MSO 1 216 DBREF 9MSO B 1 214 PDB 9MSO 9MSO 1 214 DBREF1 9MSO E 90 181 UNP PG161_MONPV DBREF2 9MSO E A0A7H0DND2 90 181 DBREF1 9MSO F 90 181 UNP PG161_MONPV DBREF2 9MSO F A0A7H0DND2 90 181 SEQADV 9MSO GLY G 182 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO SER G 183 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS G 184 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS G 185 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS G 186 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS G 187 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS G 188 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS G 189 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO GLY I 182 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO SER I 183 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS I 184 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS I 185 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS I 186 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS I 187 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS I 188 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS I 189 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO GLY E 182 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO SER E 183 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS E 184 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS E 185 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS E 186 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS E 187 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS E 188 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS E 189 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO GLY F 182 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO SER F 183 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS F 184 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS F 185 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS F 186 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS F 187 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS F 188 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSO HIS F 189 UNP A0A7H0DND EXPRESSION TAG SEQRES 1 H 228 GLN VAL GLN LEU GLN GLN TRP GLY ALA GLY LEU LEU LYS SEQRES 2 H 228 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 H 228 ALA SER PHE SER GLY TYR TYR TRP THR TRP ILE ARG GLN SEQRES 4 H 228 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY GLU ILE HIS SEQRES 5 H 228 HIS THR GLY ASN THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 H 228 ARG VAL SER ILE SER VAL ASP THR SER LYS ASN GLN PHE SEQRES 7 H 228 SER LEU LYS LEU THR SER VAL THR ALA ALA ASP THR ALA SEQRES 8 H 228 VAL TYR TYR CYS ALA ARG VAL GLY GLY TYR TYR TYR GLY SEQRES 9 H 228 TRP GLY LYS LYS PRO HIS TRP PHE ASP PRO TRP GLY GLN SEQRES 10 H 228 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 H 228 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 H 228 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 H 228 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 H 228 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 H 228 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 H 228 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 H 228 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 H 228 LYS VAL GLU PRO LYS SER CYS SEQRES 1 L 214 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 L 214 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 214 GLN SER VAL SER SER ASP LEU ALA TRP TYR GLN GLN ARG SEQRES 4 L 214 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 L 214 ASN ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN ARG SEQRES 8 L 214 SER ASN TRP GLY PHE THR PHE GLY PRO GLY THR LYS VAL SEQRES 9 L 214 ASP ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS SEQRES 1 G 100 SER THR THR GLN TYR ASP HIS LYS GLU SER CYS ASN GLY SEQRES 2 G 100 LEU TYR TYR GLN GLY SER CYS TYR ILE LEU HIS SER ASP SEQRES 3 G 100 TYR LYS SER PHE GLU ASP ALA LYS ALA ASN CYS ALA ALA SEQRES 4 G 100 GLU SER SER THR LEU PRO ASN LYS SER ASP VAL LEU THR SEQRES 5 G 100 THR TRP LEU ILE ASP TYR VAL GLU ASP THR TRP GLY SER SEQRES 6 G 100 ASP GLY ASN PRO ILE THR LYS THR THR SER ASP TYR GLN SEQRES 7 G 100 ASP SER ASP VAL SER GLN GLU VAL ARG LYS TYR PHE CYS SEQRES 8 G 100 THR GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 I 100 SER THR THR GLN TYR ASP HIS LYS GLU SER CYS ASN GLY SEQRES 2 I 100 LEU TYR TYR GLN GLY SER CYS TYR ILE LEU HIS SER ASP SEQRES 3 I 100 TYR LYS SER PHE GLU ASP ALA LYS ALA ASN CYS ALA ALA SEQRES 4 I 100 GLU SER SER THR LEU PRO ASN LYS SER ASP VAL LEU THR SEQRES 5 I 100 THR TRP LEU ILE ASP TYR VAL GLU ASP THR TRP GLY SER SEQRES 6 I 100 ASP GLY ASN PRO ILE THR LYS THR THR SER ASP TYR GLN SEQRES 7 I 100 ASP SER ASP VAL SER GLN GLU VAL ARG LYS TYR PHE CYS SEQRES 8 I 100 THR GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 A 228 GLN VAL GLN LEU GLN GLN TRP GLY ALA GLY LEU LEU LYS SEQRES 2 A 228 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 A 228 ALA SER PHE SER GLY TYR TYR TRP THR TRP ILE ARG GLN SEQRES 4 A 228 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY GLU ILE HIS SEQRES 5 A 228 HIS THR GLY ASN THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 A 228 ARG VAL SER ILE SER VAL ASP THR SER LYS ASN GLN PHE SEQRES 7 A 228 SER LEU LYS LEU THR SER VAL THR ALA ALA ASP THR ALA SEQRES 8 A 228 VAL TYR TYR CYS ALA ARG VAL GLY GLY TYR TYR TYR GLY SEQRES 9 A 228 TRP GLY LYS LYS PRO HIS TRP PHE ASP PRO TRP GLY GLN SEQRES 10 A 228 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 A 228 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 A 228 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 A 228 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 A 228 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 A 228 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 A 228 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 A 228 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 A 228 LYS VAL GLU PRO LYS SER CYS SEQRES 1 B 214 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 B 214 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 B 214 GLN SER VAL SER SER ASP LEU ALA TRP TYR GLN GLN ARG SEQRES 4 B 214 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 B 214 ASN ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 B 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 214 GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN ARG SEQRES 8 B 214 SER ASN TRP GLY PHE THR PHE GLY PRO GLY THR LYS VAL SEQRES 9 B 214 ASP ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 B 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 B 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 B 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 B 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 B 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 B 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 B 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 B 214 PHE ASN ARG GLY GLU CYS SEQRES 1 E 100 SER THR THR GLN TYR ASP HIS LYS GLU SER CYS ASN GLY SEQRES 2 E 100 LEU TYR TYR GLN GLY SER CYS TYR ILE LEU HIS SER ASP SEQRES 3 E 100 TYR LYS SER PHE GLU ASP ALA LYS ALA ASN CYS ALA ALA SEQRES 4 E 100 GLU SER SER THR LEU PRO ASN LYS SER ASP VAL LEU THR SEQRES 5 E 100 THR TRP LEU ILE ASP TYR VAL GLU ASP THR TRP GLY SER SEQRES 6 E 100 ASP GLY ASN PRO ILE THR LYS THR THR SER ASP TYR GLN SEQRES 7 E 100 ASP SER ASP VAL SER GLN GLU VAL ARG LYS TYR PHE CYS SEQRES 8 E 100 THR GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 F 100 SER THR THR GLN TYR ASP HIS LYS GLU SER CYS ASN GLY SEQRES 2 F 100 LEU TYR TYR GLN GLY SER CYS TYR ILE LEU HIS SER ASP SEQRES 3 F 100 TYR LYS SER PHE GLU ASP ALA LYS ALA ASN CYS ALA ALA SEQRES 4 F 100 GLU SER SER THR LEU PRO ASN LYS SER ASP VAL LEU THR SEQRES 5 F 100 THR TRP LEU ILE ASP TYR VAL GLU ASP THR TRP GLY SER SEQRES 6 F 100 ASP GLY ASN PRO ILE THR LYS THR THR SER ASP TYR GLN SEQRES 7 F 100 ASP SER ASP VAL SER GLN GLU VAL ARG LYS TYR PHE CYS SEQRES 8 F 100 THR GLY SER HIS HIS HIS HIS HIS HIS HELIX 1 AA1 SER H 28 TYR H 32 5 5 HELIX 2 AA2 THR H 83 THR H 87 5 5 HELIX 3 AA3 SER H 187 GLY H 190 5 4 HELIX 4 AA4 GLU L 79 PHE L 83 5 5 HELIX 5 AA5 SER L 121 SER L 127 1 7 HELIX 6 AA6 LYS L 183 GLU L 187 1 5 HELIX 7 AA7 SER G 118 GLU G 129 1 12 HELIX 8 AA8 ASN G 135 LEU G 140 1 6 HELIX 9 AA9 LEU G 144 GLU G 149 1 6 HELIX 10 AB1 SER I 118 GLU I 129 1 12 HELIX 11 AB2 ASN I 135 LEU I 140 1 6 HELIX 12 AB3 LEU I 144 GLU I 149 1 6 HELIX 13 AB4 THR A 73 LYS A 75 5 3 HELIX 14 AB5 THR A 83 THR A 87 5 5 HELIX 15 AB6 SER A 156 ALA A 158 5 3 HELIX 16 AB7 SER A 187 GLN A 192 1 6 HELIX 17 AB8 GLU B 79 PHE B 83 5 5 HELIX 18 AB9 SER B 121 SER B 127 1 7 HELIX 19 AC1 LYS B 183 LYS B 188 1 6 HELIX 20 AC2 SER E 118 GLU E 129 1 12 HELIX 21 AC3 ASN E 135 LEU E 140 1 6 HELIX 22 AC4 LEU E 144 GLU E 149 1 6 HELIX 23 AC5 SER F 118 GLU F 129 1 12 HELIX 24 AC6 ASN F 135 LEU F 140 1 6 HELIX 25 AC7 LEU F 144 GLU F 149 1 6 SHEET 1 AA1 4 GLN H 3 GLY H 8 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O ALA H 23 N GLN H 5 SHEET 3 AA1 4 GLN H 77 LEU H 82 -1 O LEU H 82 N LEU H 18 SHEET 4 AA1 4 VAL H 67 ASP H 72 -1 N ASP H 72 O GLN H 77 SHEET 1 AA2 6 LEU H 11 LEU H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N LEU H 12 SHEET 3 AA2 6 ALA H 88 VAL H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 TRP H 34 GLN H 39 -1 N ILE H 37 O TYR H 91 SHEET 5 AA2 6 GLU H 46 ILE H 51 -1 O ILE H 48 N TRP H 36 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O ASN H 58 N GLU H 50 SHEET 1 AA3 4 LEU H 11 LEU H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N LEU H 12 SHEET 3 AA3 4 ALA H 88 VAL H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 PHE H 100I TRP H 103 -1 O ASP H 101 N ARG H 94 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 SER H 120 LEU H 124 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 TYR H 194 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA6 3 THR H 205 VAL H 211 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 4 LEU L 4 SER L 7 0 SHEET 2 AA7 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA8 6 THR L 10 LEU L 13 0 SHEET 2 AA8 6 THR L 102 ILE L 106 1 O ASP L 105 N LEU L 11 SHEET 3 AA8 6 VAL L 85 SER L 92 -1 N TYR L 86 O THR L 102 SHEET 4 AA8 6 LEU L 33 GLN L 38 -1 N GLN L 38 O VAL L 85 SHEET 5 AA8 6 ARG L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA8 6 ASN L 53 ARG L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AA9 4 THR L 10 LEU L 13 0 SHEET 2 AA9 4 THR L 102 ILE L 106 1 O ASP L 105 N LEU L 11 SHEET 3 AA9 4 VAL L 85 SER L 92 -1 N TYR L 86 O THR L 102 SHEET 4 AA9 4 GLY L 95 PHE L 98 -1 O GLY L 95 N SER L 92 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB1 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136 SHEET 4 AB1 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB2 4 ALA L 153 LEU L 154 0 SHEET 2 AB2 4 ALA L 144 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB2 4 VAL L 191 HIS L 198 -1 O GLU L 195 N GLN L 147 SHEET 4 AB2 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 AB3 4 LEU G 103 TYR G 104 0 SHEET 2 AB3 4 CYS G 109 LYS G 117 -1 O TYR G 110 N LEU G 103 SHEET 3 AB3 4 ARG G 176 GLY G 182 -1 O TYR G 178 N HIS G 113 SHEET 4 AB3 4 SER G 131 THR G 132 -1 N THR G 132 O THR G 181 SHEET 1 AB4 3 LEU I 103 TYR I 105 0 SHEET 2 AB4 3 SER I 108 LYS I 117 -1 O TYR I 110 N LEU I 103 SHEET 3 AB4 3 ARG I 176 CYS I 180 -1 O TYR I 178 N HIS I 113 SHEET 1 AB5 4 GLN A 3 GLY A 8 0 SHEET 2 AB5 4 LEU A 18 SER A 25 -1 O ALA A 23 N GLN A 5 SHEET 3 AB5 4 GLN A 77 LEU A 82 -1 O LEU A 80 N LEU A 20 SHEET 4 AB5 4 VAL A 67 ASP A 72 -1 N ASP A 72 O GLN A 77 SHEET 1 AB6 6 LEU A 11 LEU A 12 0 SHEET 2 AB6 6 THR A 107 VAL A 111 1 O THR A 110 N LEU A 12 SHEET 3 AB6 6 ALA A 88 VAL A 95 -1 N TYR A 90 O THR A 107 SHEET 4 AB6 6 TRP A 34 GLN A 39 -1 N ILE A 37 O TYR A 91 SHEET 5 AB6 6 GLU A 46 ILE A 51 -1 O ILE A 48 N TRP A 36 SHEET 6 AB6 6 THR A 57 TYR A 59 -1 O ASN A 58 N GLU A 50 SHEET 1 AB7 4 LEU A 11 LEU A 12 0 SHEET 2 AB7 4 THR A 107 VAL A 111 1 O THR A 110 N LEU A 12 SHEET 3 AB7 4 ALA A 88 VAL A 95 -1 N TYR A 90 O THR A 107 SHEET 4 AB7 4 PHE A 100I TRP A 103 -1 O ASP A 101 N ARG A 94 SHEET 1 AB8 4 SER A 120 LEU A 124 0 SHEET 2 AB8 4 ALA A 136 TYR A 145 -1 O LYS A 143 N SER A 120 SHEET 3 AB8 4 TYR A 176 VAL A 184 -1 O TYR A 176 N TYR A 145 SHEET 4 AB8 4 VAL A 163 THR A 165 -1 N HIS A 164 O VAL A 181 SHEET 1 AB9 4 SER A 120 LEU A 124 0 SHEET 2 AB9 4 ALA A 136 TYR A 145 -1 O LYS A 143 N SER A 120 SHEET 3 AB9 4 TYR A 176 VAL A 184 -1 O TYR A 176 N TYR A 145 SHEET 4 AB9 4 VAL A 169 LEU A 170 -1 N VAL A 169 O SER A 177 SHEET 1 AC1 3 THR A 151 TRP A 154 0 SHEET 2 AC1 3 TYR A 194 HIS A 200 -1 O ASN A 197 N SER A 153 SHEET 3 AC1 3 THR A 205 VAL A 211 -1 O VAL A 211 N TYR A 194 SHEET 1 AC2 4 LEU B 4 SER B 7 0 SHEET 2 AC2 4 ALA B 19 ALA B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AC2 4 ASP B 70 ILE B 75 -1 O LEU B 73 N LEU B 21 SHEET 4 AC2 4 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AC3 6 THR B 10 LEU B 13 0 SHEET 2 AC3 6 THR B 102 ILE B 106 1 O LYS B 103 N LEU B 11 SHEET 3 AC3 6 VAL B 85 SER B 92 -1 N TYR B 86 O THR B 102 SHEET 4 AC3 6 LEU B 33 GLN B 38 -1 N GLN B 38 O VAL B 85 SHEET 5 AC3 6 ARG B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AC3 6 ASN B 53 ARG B 54 -1 O ASN B 53 N TYR B 49 SHEET 1 AC4 4 THR B 10 LEU B 13 0 SHEET 2 AC4 4 THR B 102 ILE B 106 1 O LYS B 103 N LEU B 11 SHEET 3 AC4 4 VAL B 85 SER B 92 -1 N TYR B 86 O THR B 102 SHEET 4 AC4 4 GLY B 95 PHE B 98 -1 O GLY B 95 N SER B 92 SHEET 1 AC5 4 SER B 114 PHE B 118 0 SHEET 2 AC5 4 THR B 129 PHE B 139 -1 O VAL B 133 N PHE B 118 SHEET 3 AC5 4 TYR B 173 SER B 182 -1 O LEU B 179 N VAL B 132 SHEET 4 AC5 4 SER B 159 VAL B 163 -1 N GLN B 160 O THR B 178 SHEET 1 AC6 4 ALA B 153 LEU B 154 0 SHEET 2 AC6 4 ALA B 144 VAL B 150 -1 N VAL B 150 O ALA B 153 SHEET 3 AC6 4 VAL B 191 HIS B 198 -1 O GLU B 195 N GLN B 147 SHEET 4 AC6 4 VAL B 205 ASN B 210 -1 O VAL B 205 N VAL B 196 SHEET 1 AC7 3 LEU E 103 TYR E 104 0 SHEET 2 AC7 3 CYS E 109 LYS E 117 -1 O TYR E 110 N LEU E 103 SHEET 3 AC7 3 ARG E 176 CYS E 180 -1 O ARG E 176 N LYS E 117 SHEET 1 AC8 3 LEU F 103 TYR F 105 0 SHEET 2 AC8 3 SER F 108 LYS F 117 -1 O TYR F 110 N LEU F 103 SHEET 3 AC8 3 ARG F 176 THR F 181 -1 O TYR F 178 N HIS F 113 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.03 SSBOND 5 CYS G 100 CYS G 109 1555 1555 2.03 SSBOND 6 CYS G 126 CYS G 180 1555 1555 2.04 SSBOND 7 CYS I 100 CYS I 109 1555 1555 2.03 SSBOND 8 CYS I 126 CYS I 180 1555 1555 2.03 SSBOND 9 CYS A 22 CYS A 92 1555 1555 2.03 SSBOND 10 CYS A 140 CYS A 196 1555 1555 2.03 SSBOND 11 CYS B 23 CYS B 88 1555 1555 2.04 SSBOND 12 CYS B 134 CYS B 194 1555 1555 2.03 SSBOND 13 CYS E 100 CYS E 109 1555 1555 2.03 SSBOND 14 CYS E 126 CYS E 180 1555 1555 2.03 SSBOND 15 CYS F 100 CYS F 109 1555 1555 2.03 SSBOND 16 CYS F 126 CYS F 180 1555 1555 2.03 CISPEP 1 ASP H 101 PRO H 102 0 4.94 CISPEP 2 PHE H 146 PRO H 147 0 -6.78 CISPEP 3 GLU H 148 PRO H 149 0 -0.54 CISPEP 4 SER L 7 PRO L 8 0 -2.50 CISPEP 5 TYR L 140 PRO L 141 0 3.19 CISPEP 6 ASP A 101 PRO A 102 0 5.40 CISPEP 7 PHE A 146 PRO A 147 0 -7.74 CISPEP 8 GLU A 148 PRO A 149 0 -1.33 CISPEP 9 SER B 7 PRO B 8 0 -3.02 CISPEP 10 TYR B 140 PRO B 141 0 4.18 CRYST1 72.504 165.497 118.453 90.00 90.00 90.00 P 21 21 21 16 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 0.013792 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006042 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008442 0.00000