HEADER VIRAL PROTEIN 29-JUL-24 9IXV TITLE CRYO-EM STRUCTURE OF MERS-COV S1-NTD BOUND WITH KNIH-88 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE GLYCOPROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HEAVY CHAIN FROM KNIH-88, MONOCLONAL ANTIBODY; COMPND 8 CHAIN: H; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: LIGHT CHAIN FROM KNIH-88, MONOCLONAL ANTIBODY; COMPND 12 CHAIN: L; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MIDDLE EAST RESPIRATORY SYNDROME-RELATED SOURCE 3 CORONAVIRUS; SOURCE 4 ORGANISM_TAXID: 1335626; SOURCE 5 GENE: S, 3; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: HEK293T; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM_CELL_LINE: HEK293T KEYWDS MONOCLONAL ANTIBODY, MERS-COV S1-NTD, KNIH-88, VIRAL PROTEIN-IMMUNE KEYWDS 2 SYSTEM COMPLEX, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR H.JEON,Y.YOO,K.PARK,K.CHOI REVDAT 1 30-APR-25 9IXV 0 JRNL AUTH S.Y.LEE,H.M.WOO,H.JEON,N.Y.KIM,D.S.KIM,C.K.PARK,H.J.KIM, JRNL AUTH 2 K.C.KIM,J.Y.LEE,K.PARK,Y.YOO,K.CHOI,H.LEE JRNL TITL A NOVEL ANTIBODY AGAINST THE NON-RBD REGION OF MIDDLE EAST JRNL TITL 2 RESPIRATORY SYNDROME CORONAVIRUS SPIKE PROTEIN. JRNL REF J.INFECT.DIS. 2025 JRNL REFN ESSN 1537-6613 JRNL PMID 40241666 JRNL DOI 10.1093/INFDIS/JIAF202 REMARK 2 REMARK 2 RESOLUTION. 3.11 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX, PHENIX, COOT REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 5X4R REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE 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) : 3.110 REMARK 3 NUMBER OF PARTICLES : 150340 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 9IXV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1300049912. 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 : CRYO-EM STRUCTURE OF MERS-COV REMARK 245 S1-NTD BOUND WITH KNIH-88 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 600.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2100.00 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) : 6000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 ILE A 2 REMARK 465 HIS A 3 REMARK 465 SER A 4 REMARK 465 VAL A 5 REMARK 465 PHE A 6 REMARK 465 LEU A 7 REMARK 465 LEU A 8 REMARK 465 MET A 9 REMARK 465 PHE A 10 REMARK 465 LEU A 11 REMARK 465 LEU A 12 REMARK 465 THR A 13 REMARK 465 PRO A 14 REMARK 465 THR A 15 REMARK 465 GLU A 16 REMARK 465 SER A 17 REMARK 465 SER A 65 REMARK 465 ASN A 66 REMARK 465 ILE A 67 REMARK 465 THR A 68 REMARK 465 ILE A 69 REMARK 465 THR A 70 REMARK 465 TYR A 71 REMARK 465 GLN A 72 REMARK 465 GLY A 73 REMARK 465 LEU A 74 REMARK 465 TYR A 77 REMARK 465 GLN A 78 REMARK 465 GLY A 79 REMARK 465 SER A 133 REMARK 465 PRO A 134 REMARK 465 SER A 268 REMARK 465 THR A 322 REMARK 465 PHE A 323 REMARK 465 LEU A 324 REMARK 465 VAL A 329 REMARK 465 ASP A 330 REMARK 465 ARG A 335 REMARK 465 PHE A 341 REMARK 465 ASN A 342 REMARK 465 ASP A 343 REMARK 465 LEU A 344 REMARK 465 SER A 345 REMARK 465 GLN A 346 REMARK 465 LEU A 347 REMARK 465 HIS A 348 REMARK 465 CYS A 349 REMARK 465 SER A 350 REMARK 465 GLU H 1 REMARK 465 SER H 130 REMARK 465 SER H 131 REMARK 465 LYS H 132 REMARK 465 SER H 133 REMARK 465 THR H 134 REMARK 465 SER H 135 REMARK 465 GLY H 136 REMARK 465 GLY H 137 REMARK 465 THR H 138 REMARK 465 ALA H 139 REMARK 465 GLN H 174 REMARK 465 SER H 175 REMARK 465 VAL H 187 REMARK 465 PRO H 188 REMARK 465 SER H 189 REMARK 465 SER H 190 REMARK 465 SER H 191 REMARK 465 LEU H 192 REMARK 465 GLY H 193 REMARK 465 THR H 194 REMARK 465 GLN H 195 REMARK 465 THR H 196 REMARK 465 SER L 114 REMARK 465 VAL L 115 REMARK 465 PHE L 116 REMARK 465 ILE L 117 REMARK 465 LYS L 126 REMARK 465 SER L 127 REMARK 465 GLY L 128 REMARK 465 GLU L 143 REMARK 465 GLN L 147 REMARK 465 LYS L 149 REMARK 465 VAL L 150 REMARK 465 ASP L 151 REMARK 465 ASN L 152 REMARK 465 ALA L 153 REMARK 465 LEU L 154 REMARK 465 GLN L 155 REMARK 465 SER L 156 REMARK 465 GLY L 157 REMARK 465 SER L 182 REMARK 465 LYS L 183 REMARK 465 ALA L 184 REMARK 465 ASP L 185 REMARK 465 TYR L 186 REMARK 465 GLU L 187 REMARK 465 LYS L 188 REMARK 465 HIS L 189 REMARK 465 LYS L 190 REMARK 465 VAL L 191 REMARK 465 TYR L 192 REMARK 465 ALA L 193 REMARK 465 CYS L 194 REMARK 465 GLU L 195 REMARK 465 VAL L 196 REMARK 465 THR L 197 REMARK 465 HIS L 198 REMARK 465 GLN L 199 REMARK 465 GLY L 200 REMARK 465 LEU L 201 REMARK 465 SER L 202 REMARK 465 SER L 203 REMARK 465 PRO L 204 REMARK 465 VAL L 205 REMARK 465 THR L 206 REMARK 465 LYS L 207 REMARK 465 SER L 208 REMARK 465 PHE L 209 REMARK 465 ASN L 210 REMARK 465 ARG L 211 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 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 ASN A 104 49.84 -88.92 REMARK 500 ALA A 113 -126.95 57.53 REMARK 500 ILE A 131 -53.63 65.42 REMARK 500 ALA A 138 -168.59 -161.82 REMARK 500 ASN A 166 -156.31 60.58 REMARK 500 THR A 259 -168.39 -127.15 REMARK 500 PHE H 27 -167.85 -161.43 REMARK 500 TYR H 99 -156.21 -149.02 REMARK 500 TRP H 106 176.13 65.90 REMARK 500 ARG L 30 -120.21 56.58 REMARK 500 ALA L 51 -6.71 71.93 REMARK 500 ASN L 138 64.86 62.64 REMARK 500 PRO L 141 -169.76 -75.94 REMARK 500 ASP L 170 -1.96 64.25 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-60978 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF MERS-COV S1-NTD BOUND WITH KNIH-88 FAB DBREF 9IXV A 1 350 UNP K9N5Q8 SPIKE_MERS1 1 350 DBREF 9IXV H 1 216 PDB 9IXV 9IXV 1 216 DBREF 9IXV L 1 214 PDB 9IXV 9IXV 1 214 SEQRES 1 A 350 MET ILE HIS SER VAL PHE LEU LEU MET PHE LEU LEU THR SEQRES 2 A 350 PRO THR GLU SER TYR VAL ASP VAL GLY PRO ASP SER VAL SEQRES 3 A 350 LYS SER ALA CYS ILE GLU VAL ASP ILE GLN GLN THR PHE SEQRES 4 A 350 PHE ASP LYS THR TRP PRO ARG PRO ILE ASP VAL SER LYS SEQRES 5 A 350 ALA ASP GLY ILE ILE TYR PRO GLN GLY ARG THR TYR SER SEQRES 6 A 350 ASN ILE THR ILE THR TYR GLN GLY LEU PHE PRO TYR GLN SEQRES 7 A 350 GLY ASP HIS GLY ASP MET TYR VAL TYR SER ALA GLY HIS SEQRES 8 A 350 ALA THR GLY THR THR PRO GLN LYS LEU PHE VAL ALA ASN SEQRES 9 A 350 TYR SER GLN ASP VAL LYS GLN PHE ALA ASN GLY PHE VAL SEQRES 10 A 350 VAL ARG ILE GLY ALA ALA ALA ASN SER THR GLY THR VAL SEQRES 11 A 350 ILE ILE SER PRO SER THR SER ALA THR ILE ARG LYS ILE SEQRES 12 A 350 TYR PRO ALA PHE MET LEU GLY SER SER VAL GLY ASN PHE SEQRES 13 A 350 SER ASP GLY LYS MET GLY ARG PHE PHE ASN HIS THR LEU SEQRES 14 A 350 VAL LEU LEU PRO ASP GLY CYS GLY THR LEU LEU ARG ALA SEQRES 15 A 350 PHE TYR CYS ILE LEU GLU PRO ARG SER GLY ASN HIS CYS SEQRES 16 A 350 PRO ALA GLY ASN SER TYR THR SER PHE ALA THR TYR HIS SEQRES 17 A 350 THR PRO ALA THR ASP CYS SER ASP GLY ASN TYR ASN ARG SEQRES 18 A 350 ASN ALA SER LEU ASN SER PHE LYS GLU TYR PHE ASN LEU SEQRES 19 A 350 ARG ASN CYS THR PHE MET TYR THR TYR ASN ILE THR GLU SEQRES 20 A 350 ASP GLU ILE LEU GLU TRP PHE GLY ILE THR GLN THR ALA SEQRES 21 A 350 GLN GLY VAL HIS LEU PHE SER SER ARG TYR VAL ASP LEU SEQRES 22 A 350 TYR GLY GLY ASN MET PHE GLN PHE ALA THR LEU PRO VAL SEQRES 23 A 350 TYR ASP THR ILE LYS TYR TYR SER ILE ILE PRO HIS SER SEQRES 24 A 350 ILE ARG SER ILE GLN SER ASP ARG LYS ALA TRP ALA ALA SEQRES 25 A 350 PHE TYR VAL TYR LYS LEU GLN PRO LEU THR PHE LEU LEU SEQRES 26 A 350 ASP PHE SER VAL ASP GLY TYR ILE ARG ARG ALA ILE ASP SEQRES 27 A 350 CYS GLY PHE ASN ASP LEU SER GLN LEU HIS CYS SER SEQRES 1 H 216 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU ILE GLN SEQRES 2 H 216 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 216 PHE THR VAL ILE ASP TYR TYR MET THR TRP VAL ARG GLN SEQRES 4 H 216 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER VAL ILE TYR SEQRES 5 H 216 ALA GLY GLY SER THR TYR TYR ALA ASP SER VAL LYS GLY SEQRES 6 H 216 ARG PHE THR VAL SER ARG ASP TYR SER ARG ASN THR LEU SEQRES 7 H 216 TYR LEU GLN MET ASN SER LEU LYS ALA GLU ASP THR ALA SEQRES 8 H 216 VAL TYR TYR CYS THR ARG ASP TYR LEU ALA ALA GLY GLY SEQRES 9 H 216 LEU TRP GLY GLN GLY ALA LEU VAL THR VAL SER SER ALA SEQRES 10 H 216 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 11 H 216 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 12 H 216 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 13 H 216 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 14 H 216 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 15 H 216 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 16 H 216 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 17 H 216 LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 1 L 214 GLU ILE VAL LEU THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 214 GLN GLY ILE ARG ASN ASN LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY GLN VAL PRO GLU LEU LEU ILE TYR GLY ALA SER SEQRES 5 L 214 ASN LEU LYS PRO GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 ALA SER GLY THR ASP PHE THR LEU THR ILE SER SER MET SEQRES 7 L 214 GLN PRO GLU ASP VAL ALA THR TYR TYR CYS GLN LYS TYR SEQRES 8 L 214 ASP SER ALA PRO LEU THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 L 214 GLU 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 HELIX 1 AA1 ASN A 222 TYR A 231 1 10 HELIX 2 AA2 ILE A 303 ARG A 307 5 5 HELIX 3 AA3 THR H 28 TYR H 32 5 5 HELIX 4 AA4 SER H 159 ALA H 161 5 3 SHEET 1 AA1 2 VAL A 33 ILE A 35 0 SHEET 2 AA1 2 LEU A 100 VAL A 102 1 O VAL A 102 N ASP A 34 SHEET 1 AA2 2 ILE A 56 ILE A 57 0 SHEET 2 AA2 2 ASN A 277 MET A 278 1 O MET A 278 N ILE A 56 SHEET 1 AA3 6 ASP A 83 TYR A 85 0 SHEET 2 AA3 6 PHE A 313 LYS A 317 -1 O VAL A 315 N ASP A 83 SHEET 3 AA3 6 PHE A 116 ILE A 120 -1 N ARG A 119 O TYR A 314 SHEET 4 AA3 6 GLU A 252 GLN A 258 -1 O PHE A 254 N VAL A 118 SHEET 5 AA3 6 VAL A 263 PHE A 266 -1 O PHE A 266 N GLY A 255 SHEET 6 AA3 6 GLN A 280 LEU A 284 -1 O LEU A 284 N VAL A 263 SHEET 1 AA4 6 LYS A 110 GLN A 111 0 SHEET 2 AA4 6 TYR A 292 ILE A 295 -1 O TYR A 293 N LYS A 110 SHEET 3 AA4 6 PHE A 147 GLY A 150 -1 N GLY A 150 O TYR A 292 SHEET 4 AA4 6 THR A 168 ASP A 174 -1 O LEU A 169 N LEU A 149 SHEET 5 AA4 6 LEU A 179 PRO A 189 -1 O ARG A 181 N LEU A 172 SHEET 6 AA4 6 PHE A 232 ASN A 244 -1 O ARG A 235 N ILE A 186 SHEET 1 AA5 2 THR A 127 THR A 129 0 SHEET 2 AA5 2 SER A 137 THR A 139 -1 O ALA A 138 N GLY A 128 SHEET 1 AA6 2 SER A 152 ASN A 155 0 SHEET 2 AA6 2 MET A 161 PHE A 165 -1 O PHE A 165 N SER A 152 SHEET 1 AA7 2 THR A 206 HIS A 208 0 SHEET 2 AA7 2 HIS A 298 ILE A 300 1 O SER A 299 N HIS A 208 SHEET 1 AA8 4 GLN H 3 SER H 7 0 SHEET 2 AA8 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AA8 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AA8 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79 SHEET 1 AA9 6 LEU H 11 ILE H 12 0 SHEET 2 AA9 6 ALA H 110 VAL H 114 1 O THR H 113 N ILE H 12 SHEET 3 AA9 6 ALA H 91 ARG H 97 -1 N TYR H 93 O ALA H 110 SHEET 4 AA9 6 MET H 34 GLN H 39 -1 N GLN H 39 O VAL H 92 SHEET 5 AA9 6 LEU H 45 TYR H 52 -1 O ILE H 51 N MET H 34 SHEET 6 AA9 6 SER H 56 TYR H 59 -1 O TYR H 58 N VAL H 50 SHEET 1 AB1 3 LEU H 141 TYR H 148 0 SHEET 2 AB1 3 TYR H 179 VAL H 185 -1 O VAL H 185 N LEU H 141 SHEET 3 AB1 3 HIS H 167 THR H 168 -1 N HIS H 167 O VAL H 184 SHEET 1 AB2 3 THR H 154 TRP H 157 0 SHEET 2 AB2 3 ILE H 198 HIS H 203 -1 O ASN H 200 N SER H 156 SHEET 3 AB2 3 THR H 208 LYS H 213 -1 O VAL H 210 N VAL H 201 SHEET 1 AB3 2 LEU L 4 SER L 7 0 SHEET 2 AB3 2 THR L 22 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 1 AB4 5 ASN L 53 LEU L 54 0 SHEET 2 AB4 5 GLU L 45 TYR L 49 -1 N TYR L 49 O ASN L 53 SHEET 3 AB4 5 LEU L 33 GLN L 38 -1 N GLN L 37 O GLU L 45 SHEET 4 AB4 5 THR L 85 LYS L 90 -1 O TYR L 87 N TYR L 36 SHEET 5 AB4 5 THR L 102 LYS L 103 -1 O THR L 102 N TYR L 86 SHEET 1 AB5 2 GLY L 64 SER L 67 0 SHEET 2 AB5 2 PHE L 71 LEU L 73 -1 O THR L 72 N SER L 65 SHEET 1 AB6 3 SER L 131 ASN L 137 0 SHEET 2 AB6 3 SER L 174 THR L 180 -1 O LEU L 175 N LEU L 136 SHEET 3 AB6 3 SER L 159 GLN L 160 -1 N GLN L 160 O THR L 178 SSBOND 1 CYS A 30 CYS A 195 1555 1555 2.04 SSBOND 2 CYS A 176 CYS A 214 1555 1555 2.03 SSBOND 3 CYS H 22 CYS H 95 1555 1555 2.03 SSBOND 4 CYS H 143 CYS H 199 1555 1555 2.04 SSBOND 5 CYS L 23 CYS L 88 1555 1555 2.03 CISPEP 1 PHE H 149 PRO H 150 0 -5.41 CISPEP 2 GLU H 151 PRO H 152 0 -1.78 CISPEP 3 SER L 7 PRO L 8 0 -2.85 CISPEP 4 TYR L 140 PRO L 141 0 8.12 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