HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM/INHIBITOR31-MAR-25 9NZ5 TITLE MERSMUT-COV M PROTEIN DIMER IN COMPLEX WITH FAB B COMPND MOL_ID: 1; COMPND 2 MOLECULE: MEMBRANE PROTEIN; COMPND 3 CHAIN: A, D; COMPND 4 SYNONYM: M PROTEIN,E1 GLYCOPROTEIN,MATRIX GLYCOPROTEIN,MEMBRANE COMPND 5 GLYCOPROTEIN; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: FAB B LIGHT CHAIN; COMPND 9 CHAIN: C, E; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: FAB B HEAVY CHAIN; COMPND 13 CHAIN: B, F; COMPND 14 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: M, E, AL079_478421_M; SOURCE 6 EXPRESSION_SYSTEM: MAMMALIAN EXPRESSION VECTOR FLAG-MCS-PCDNA3.1; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 2021188; 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: MAMMALIAN EXPRESSION VECTOR FLAG-MCS-PCDNA3.1; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 2021188; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HUMAN; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: MAMMALIAN EXPRESSION VECTOR FLAG-MCS-PCDNA3.1; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 2021188 KEYWDS M PROTEIN, SARS-COV-2, INHIBITOR BOUND COMPLEX, VIRAL PROTEIN, KEYWDS 2 MEMBRANE PROTEIN-IMMUNE SYSTEM-INHIBITOR COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR M.K.MANN,P.ABEYWICKREMA REVDAT 1 29-OCT-25 9NZ5 0 JRNL AUTH M.K.MANN,P.ABEYWICKREMA JRNL TITL MERSMUT-COV M PROTEIN DIMER IN COMPLEX WITH FAB B JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.15 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX, CRYOSPARC 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) : 3.150 REMARK 3 NUMBER OF PARTICLES : 827876 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 9NZ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-25. REMARK 100 THE DEPOSITION ID IS D_1000294502. 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 : MERSMUT-COV M PROTEIN DIMER IN REMARK 245 COMPLEX WITH FAB B 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 : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1400.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2300.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : DIFFRACTION REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5196.00 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, C, 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 MET A 1 REMARK 465 SER A 2 REMARK 465 ASN A 3 REMARK 465 MET A 4 REMARK 465 THR A 5 REMARK 465 GLN A 6 REMARK 465 LEU A 7 REMARK 465 THR A 8 REMARK 465 GLU A 9 REMARK 465 ARG A 204 REMARK 465 SER A 205 REMARK 465 PRO A 206 REMARK 465 PRO A 207 REMARK 465 ILE A 208 REMARK 465 THR A 209 REMARK 465 ALA A 210 REMARK 465 ASP A 211 REMARK 465 ILE A 212 REMARK 465 GLU A 213 REMARK 465 LEU A 214 REMARK 465 ALA A 215 REMARK 465 LEU A 216 REMARK 465 LEU A 217 REMARK 465 ARG A 218 REMARK 465 ALA A 219 REMARK 465 SER A 220 REMARK 465 ASN A 221 REMARK 465 SER A 222 REMARK 465 LEU A 223 REMARK 465 GLU A 224 REMARK 465 VAL A 225 REMARK 465 LEU A 226 REMARK 465 PHE A 227 REMARK 465 GLN A 228 REMARK 465 GLY A 229 REMARK 465 PRO A 230 REMARK 465 SER A 231 REMARK 465 ARG A 232 REMARK 465 GLY A 233 REMARK 465 GLY A 234 REMARK 465 SER A 235 REMARK 465 GLY A 236 REMARK 465 ALA A 237 REMARK 465 ALA A 238 REMARK 465 ALA A 239 REMARK 465 GLY A 240 REMARK 465 SER A 241 REMARK 465 GLY A 242 REMARK 465 SER A 243 REMARK 465 GLY A 244 REMARK 465 SER A 245 REMARK 465 GLY A 246 REMARK 465 SER A 247 REMARK 465 PRO A 248 REMARK 465 SER A 249 REMARK 465 ARG A 250 REMARK 465 LEU A 251 REMARK 465 GLU A 252 REMARK 465 GLU A 253 REMARK 465 GLU A 254 REMARK 465 LEU A 255 REMARK 465 ARG A 256 REMARK 465 ARG A 257 REMARK 465 ARG A 258 REMARK 465 LEU A 259 REMARK 465 THR A 260 REMARK 465 GLU A 261 REMARK 465 GLY A 262 REMARK 465 SER A 263 REMARK 465 GLU A 264 REMARK 465 PRO A 265 REMARK 465 GLU A 266 REMARK 465 ALA A 267 REMARK 465 MET D 1 REMARK 465 SER D 2 REMARK 465 ASN D 3 REMARK 465 MET D 4 REMARK 465 THR D 5 REMARK 465 GLN D 6 REMARK 465 LEU D 7 REMARK 465 THR D 8 REMARK 465 GLU D 9 REMARK 465 ALA D 10 REMARK 465 GLN D 11 REMARK 465 ARG D 204 REMARK 465 SER D 205 REMARK 465 PRO D 206 REMARK 465 PRO D 207 REMARK 465 ILE D 208 REMARK 465 THR D 209 REMARK 465 ALA D 210 REMARK 465 ASP D 211 REMARK 465 ILE D 212 REMARK 465 GLU D 213 REMARK 465 LEU D 214 REMARK 465 ALA D 215 REMARK 465 LEU D 216 REMARK 465 LEU D 217 REMARK 465 ARG D 218 REMARK 465 ALA D 219 REMARK 465 SER D 220 REMARK 465 ASN D 221 REMARK 465 SER D 222 REMARK 465 LEU D 223 REMARK 465 GLU D 224 REMARK 465 VAL D 225 REMARK 465 LEU D 226 REMARK 465 PHE D 227 REMARK 465 GLN D 228 REMARK 465 GLY D 229 REMARK 465 PRO D 230 REMARK 465 SER D 231 REMARK 465 ARG D 232 REMARK 465 GLY D 233 REMARK 465 GLY D 234 REMARK 465 SER D 235 REMARK 465 GLY D 236 REMARK 465 ALA D 237 REMARK 465 ALA D 238 REMARK 465 ALA D 239 REMARK 465 GLY D 240 REMARK 465 SER D 241 REMARK 465 GLY D 242 REMARK 465 SER D 243 REMARK 465 GLY D 244 REMARK 465 SER D 245 REMARK 465 GLY D 246 REMARK 465 SER D 247 REMARK 465 PRO D 248 REMARK 465 SER D 249 REMARK 465 ARG D 250 REMARK 465 LEU D 251 REMARK 465 GLU D 252 REMARK 465 GLU D 253 REMARK 465 GLU D 254 REMARK 465 LEU D 255 REMARK 465 ARG D 256 REMARK 465 ARG D 257 REMARK 465 ARG D 258 REMARK 465 LEU D 259 REMARK 465 THR D 260 REMARK 465 GLU D 261 REMARK 465 GLY D 262 REMARK 465 SER D 263 REMARK 465 GLU D 264 REMARK 465 PRO D 265 REMARK 465 GLU D 266 REMARK 465 ALA D 267 REMARK 465 ALA C -1 REMARK 465 SER C 0 REMARK 465 ASP B 214 REMARK 465 CYS B 215 REMARK 465 GLY B 216 REMARK 465 SER B 217 REMARK 465 GLY B 218 REMARK 465 SER B 219 REMARK 465 HIS B 220 REMARK 465 HIS B 221 REMARK 465 HIS B 222 REMARK 465 HIS B 223 REMARK 465 HIS B 224 REMARK 465 HIS B 225 REMARK 465 ALA E -1 REMARK 465 SER E 0 REMARK 465 ASP F 214 REMARK 465 CYS F 215 REMARK 465 GLY F 216 REMARK 465 SER F 217 REMARK 465 GLY F 218 REMARK 465 SER F 219 REMARK 465 HIS F 220 REMARK 465 HIS F 221 REMARK 465 HIS F 222 REMARK 465 HIS F 223 REMARK 465 HIS F 224 REMARK 465 HIS F 225 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES 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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) 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 ATM2 ATM3 REMARK 500 ASP E 30 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES REMARK 500 ASP E 171 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES 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 TYR A 36 -4.16 67.06 REMARK 500 ILE A 72 -60.53 -105.57 REMARK 500 HIS A 147 115.74 -160.21 REMARK 500 ILE D 13 -68.43 61.70 REMARK 500 PRO D 39 44.43 -93.05 REMARK 500 SER D 40 -63.48 -104.73 REMARK 500 THR D 44 34.41 -96.24 REMARK 500 ARG D 145 -136.03 57.27 REMARK 500 PHE D 155 50.09 -92.26 REMARK 500 ARG D 162 56.61 -95.62 REMARK 500 ASP C 32 -96.80 55.50 REMARK 500 TYR C 53 -76.68 -83.43 REMARK 500 THR C 54 58.46 -107.93 REMARK 500 THR C 55 -15.76 68.90 REMARK 500 SER C 56 -36.78 -132.74 REMARK 500 THR C 73 -31.29 -131.38 REMARK 500 ASN C 96 -53.92 -121.14 REMARK 500 ILE B 48 -60.87 -96.22 REMARK 500 SER B 134 49.63 -95.01 REMARK 500 TYR E 53 -133.35 -86.06 REMARK 500 THR E 54 71.52 -65.56 REMARK 500 THR E 55 -38.94 72.08 REMARK 500 SER E 67 27.14 -142.31 REMARK 500 SER E 69 -65.35 -94.99 REMARK 500 VAL E 82 90.20 67.24 REMARK 500 ASN E 95 48.92 -94.39 REMARK 500 ASN E 96 -53.21 -120.83 REMARK 500 SER E 175 62.14 60.99 REMARK 500 LYS F 74 49.94 -92.92 REMARK 500 PRO F 189 30.15 -96.31 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-49951 RELATED DB: EMDB REMARK 900 MERSMUT-COV M PROTEIN DIMER IN COMPLEX WITH FAB B DBREF 9NZ5 A 1 219 UNP R9UNX5 R9UNX5_MERS 1 219 DBREF 9NZ5 D 1 219 UNP R9UNX5 R9UNX5_MERS 1 219 DBREF 9NZ5 C -1 218 PDB 9NZ5 9NZ5 -1 218 DBREF 9NZ5 B 1 225 PDB 9NZ5 9NZ5 1 225 DBREF 9NZ5 E -1 218 PDB 9NZ5 9NZ5 -1 218 DBREF 9NZ5 F 1 225 PDB 9NZ5 9NZ5 1 225 SEQADV 9NZ5 ILE A 127 UNP R9UNX5 THR 127 CONFLICT SEQADV 9NZ5 ARG A 145 UNP R9UNX5 ASN 145 CONFLICT SEQADV 9NZ5 LYS A 165 UNP R9UNX5 ASN 165 CONFLICT SEQADV 9NZ5 TYR A 177 UNP R9UNX5 ALA 177 CONFLICT SEQADV 9NZ5 SER A 196 UNP R9UNX5 HIS 196 CONFLICT SEQADV 9NZ5 ARG A 199 UNP R9UNX5 LYS 199 CONFLICT SEQADV 9NZ5 ILE A 200 UNP R9UNX5 ALA 200 CONFLICT SEQADV 9NZ5 SER A 220 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ASN A 221 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 SER A 222 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 LEU A 223 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLU A 224 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 VAL A 225 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 LEU A 226 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 PHE A 227 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLN A 228 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLY A 229 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 PRO A 230 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 SER A 231 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ARG A 232 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLY A 233 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLY A 234 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 SER A 235 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLY A 236 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ALA A 237 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ALA A 238 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ALA A 239 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLY A 240 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 SER A 241 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLY A 242 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 SER A 243 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLY A 244 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 SER A 245 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLY A 246 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 SER A 247 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 PRO A 248 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 SER A 249 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ARG A 250 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 LEU A 251 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLU A 252 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLU A 253 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLU A 254 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 LEU A 255 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ARG A 256 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ARG A 257 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ARG A 258 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 LEU A 259 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 THR A 260 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLU A 261 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLY A 262 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 SER A 263 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLU A 264 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 PRO A 265 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLU A 266 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ALA A 267 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ILE D 127 UNP R9UNX5 THR 127 CONFLICT SEQADV 9NZ5 ARG D 145 UNP R9UNX5 ASN 145 CONFLICT SEQADV 9NZ5 LYS D 165 UNP R9UNX5 ASN 165 CONFLICT SEQADV 9NZ5 TYR D 177 UNP R9UNX5 ALA 177 CONFLICT SEQADV 9NZ5 SER D 196 UNP R9UNX5 HIS 196 CONFLICT SEQADV 9NZ5 ARG D 199 UNP R9UNX5 LYS 199 CONFLICT SEQADV 9NZ5 ILE D 200 UNP R9UNX5 ALA 200 CONFLICT SEQADV 9NZ5 SER D 220 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ASN D 221 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 SER D 222 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 LEU D 223 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLU D 224 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 VAL D 225 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 LEU D 226 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 PHE D 227 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLN D 228 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLY D 229 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 PRO D 230 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 SER D 231 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ARG D 232 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLY D 233 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLY D 234 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 SER D 235 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLY D 236 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ALA D 237 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ALA D 238 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ALA D 239 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLY D 240 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 SER D 241 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLY D 242 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 SER D 243 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLY D 244 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 SER D 245 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLY D 246 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 SER D 247 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 PRO D 248 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 SER D 249 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ARG D 250 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 LEU D 251 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLU D 252 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLU D 253 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLU D 254 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 LEU D 255 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ARG D 256 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ARG D 257 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ARG D 258 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 LEU D 259 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 THR D 260 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLU D 261 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLY D 262 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 SER D 263 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLU D 264 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 PRO D 265 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 GLU D 266 UNP R9UNX5 EXPRESSION TAG SEQADV 9NZ5 ALA D 267 UNP R9UNX5 EXPRESSION TAG SEQRES 1 A 267 MET SER ASN MET THR GLN LEU THR GLU ALA GLN ILE ILE SEQRES 2 A 267 ALA ILE ILE LYS ASP TRP ASN PHE ALA TRP SER LEU ILE SEQRES 3 A 267 PHE LEU LEU ILE THR ILE VAL LEU GLN TYR GLY TYR PRO SEQRES 4 A 267 SER ARG SER MET THR VAL TYR VAL PHE LYS MET PHE VAL SEQRES 5 A 267 LEU TRP LEU LEU TRP PRO SER SER MET ALA LEU SER ILE SEQRES 6 A 267 PHE SER ALA VAL TYR PRO ILE ASP LEU ALA SER GLN ILE SEQRES 7 A 267 ILE SER GLY ILE VAL ALA ALA VAL SER ALA MET MET TRP SEQRES 8 A 267 ILE SER TYR PHE VAL GLN SER ILE ARG LEU PHE MET ARG SEQRES 9 A 267 THR GLY SER TRP TRP SER PHE ASN PRO GLU THR ASN CYS SEQRES 10 A 267 LEU LEU ASN VAL PRO PHE GLY GLY THR ILE VAL VAL ARG SEQRES 11 A 267 PRO LEU VAL GLU ASP SER THR SER VAL THR ALA VAL VAL SEQRES 12 A 267 THR ARG GLY HIS LEU LYS MET ALA GLY MET HIS PHE GLY SEQRES 13 A 267 ALA CYS ASP TYR ASP ARG LEU PRO LYS GLU VAL THR VAL SEQRES 14 A 267 ALA LYS PRO ASN VAL LEU ILE TYR LEU LYS MET VAL LYS SEQRES 15 A 267 ARG GLN SER TYR GLY THR ASN SER GLY VAL ALA ILE TYR SEQRES 16 A 267 SER ARG TYR ARG ILE GLY ASN TYR ARG SER PRO PRO ILE SEQRES 17 A 267 THR ALA ASP ILE GLU LEU ALA LEU LEU ARG ALA SER ASN SEQRES 18 A 267 SER LEU GLU VAL LEU PHE GLN GLY PRO SER ARG GLY GLY SEQRES 19 A 267 SER GLY ALA ALA ALA GLY SER GLY SER GLY SER GLY SER SEQRES 20 A 267 PRO SER ARG LEU GLU GLU GLU LEU ARG ARG ARG LEU THR SEQRES 21 A 267 GLU GLY SER GLU PRO GLU ALA SEQRES 1 D 267 MET SER ASN MET THR GLN LEU THR GLU ALA GLN ILE ILE SEQRES 2 D 267 ALA ILE ILE LYS ASP TRP ASN PHE ALA TRP SER LEU ILE SEQRES 3 D 267 PHE LEU LEU ILE THR ILE VAL LEU GLN TYR GLY TYR PRO SEQRES 4 D 267 SER ARG SER MET THR VAL TYR VAL PHE LYS MET PHE VAL SEQRES 5 D 267 LEU TRP LEU LEU TRP PRO SER SER MET ALA LEU SER ILE SEQRES 6 D 267 PHE SER ALA VAL TYR PRO ILE ASP LEU ALA SER GLN ILE SEQRES 7 D 267 ILE SER GLY ILE VAL ALA ALA VAL SER ALA MET MET TRP SEQRES 8 D 267 ILE SER TYR PHE VAL GLN SER ILE ARG LEU PHE MET ARG SEQRES 9 D 267 THR GLY SER TRP TRP SER PHE ASN PRO GLU THR ASN CYS SEQRES 10 D 267 LEU LEU ASN VAL PRO PHE GLY GLY THR ILE VAL VAL ARG SEQRES 11 D 267 PRO LEU VAL GLU ASP SER THR SER VAL THR ALA VAL VAL SEQRES 12 D 267 THR ARG GLY HIS LEU LYS MET ALA GLY MET HIS PHE GLY SEQRES 13 D 267 ALA CYS ASP TYR ASP ARG LEU PRO LYS GLU VAL THR VAL SEQRES 14 D 267 ALA LYS PRO ASN VAL LEU ILE TYR LEU LYS MET VAL LYS SEQRES 15 D 267 ARG GLN SER TYR GLY THR ASN SER GLY VAL ALA ILE TYR SEQRES 16 D 267 SER ARG TYR ARG ILE GLY ASN TYR ARG SER PRO PRO ILE SEQRES 17 D 267 THR ALA ASP ILE GLU LEU ALA LEU LEU ARG ALA SER ASN SEQRES 18 D 267 SER LEU GLU VAL LEU PHE GLN GLY PRO SER ARG GLY GLY SEQRES 19 D 267 SER GLY ALA ALA ALA GLY SER GLY SER GLY SER GLY SER SEQRES 20 D 267 PRO SER ARG LEU GLU GLU GLU LEU ARG ARG ARG LEU THR SEQRES 21 D 267 GLU GLY SER GLU PRO GLU ALA SEQRES 1 C 220 ALA SER ASP ILE VAL MET THR GLN SER PRO ALA SER LEU SEQRES 2 C 220 ALA VAL SER LEU GLY GLN ARG ALA THR ILE SER CYS LYS SEQRES 3 C 220 ALA SER GLN SER ILE ASP TYR ASP GLY ASP ASN TYR MET SEQRES 4 C 220 ASN TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5 C 220 LEU ILE TYR THR THR SER ASN LEU GLU SER GLY ILE PRO SEQRES 6 C 220 ALA ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 C 220 LEU ASN ILE HIS PRO VAL GLU GLU GLY ASP ALA ALA THR SEQRES 8 C 220 TYR TYR CYS GLN GLN ASN ASN GLU ASP PRO TYR THR PHE SEQRES 9 C 220 GLY GLY GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA SEQRES 10 C 220 ALA PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN SEQRES 11 C 220 LEU THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN SEQRES 12 C 220 ASN PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE SEQRES 13 C 220 ASP GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP SEQRES 14 C 220 THR ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SEQRES 15 C 220 SER THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS SEQRES 16 C 220 ASN SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SEQRES 17 C 220 SER PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 B 225 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 B 225 PRO GLY ALA SER MET LYS ILE SER CYS LYS THR SER GLY SEQRES 3 B 225 TYR SER PHE THR GLY TYR THR MET ASN TRP VAL LYS GLN SEQRES 4 B 225 SER HIS GLY LYS ASN LEU GLU TRP ILE GLY LEU ILE ASN SEQRES 5 B 225 PRO TYR ASN GLY ASP THR SER TYR ASN GLN LYS PHE LYS SEQRES 6 B 225 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR SEQRES 7 B 225 ALA TYR MET GLU LEU LEU SER LEU THR SER GLU ASP SER SEQRES 8 B 225 ALA VAL TYR TYR CYS GLU VAL ILE ASN THR TYR TRP GLY SEQRES 9 B 225 GLN GLY THR LEU VAL THR VAL SER ALA ALA LYS THR THR SEQRES 10 B 225 PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SER ALA ALA SEQRES 11 B 225 GLN THR ASN SER MET VAL THR LEU GLY CYS LEU VAL LYS SEQRES 12 B 225 GLY TYR PHE PRO GLU PRO VAL THR VAL THR TRP ASN SER SEQRES 13 B 225 GLY SER LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 14 B 225 LEU GLN SER ASP LEU TYR THR LEU SER SER SER VAL THR SEQRES 15 B 225 VAL PRO SER SER THR TRP PRO SER GLU THR VAL THR CYS SEQRES 16 B 225 ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS SEQRES 17 B 225 LYS ILE VAL PRO ARG ASP CYS GLY SER GLY SER HIS HIS SEQRES 18 B 225 HIS HIS HIS HIS SEQRES 1 E 220 ALA SER ASP ILE VAL MET THR GLN SER PRO ALA SER LEU SEQRES 2 E 220 ALA VAL SER LEU GLY GLN ARG ALA THR ILE SER CYS LYS SEQRES 3 E 220 ALA SER GLN SER ILE ASP TYR ASP GLY ASP ASN TYR MET SEQRES 4 E 220 ASN TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5 E 220 LEU ILE TYR THR THR SER ASN LEU GLU SER GLY ILE PRO SEQRES 6 E 220 ALA ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 E 220 LEU ASN ILE HIS PRO VAL GLU GLU GLY ASP ALA ALA THR SEQRES 8 E 220 TYR TYR CYS GLN GLN ASN ASN GLU ASP PRO TYR THR PHE SEQRES 9 E 220 GLY GLY GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA SEQRES 10 E 220 ALA PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN SEQRES 11 E 220 LEU THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN SEQRES 12 E 220 ASN PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE SEQRES 13 E 220 ASP GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP SEQRES 14 E 220 THR ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SEQRES 15 E 220 SER THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS SEQRES 16 E 220 ASN SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SEQRES 17 E 220 SER PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 F 225 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 F 225 PRO GLY ALA SER MET LYS ILE SER CYS LYS THR SER GLY SEQRES 3 F 225 TYR SER PHE THR GLY TYR THR MET ASN TRP VAL LYS GLN SEQRES 4 F 225 SER HIS GLY LYS ASN LEU GLU TRP ILE GLY LEU ILE ASN SEQRES 5 F 225 PRO TYR ASN GLY ASP THR SER TYR ASN GLN LYS PHE LYS SEQRES 6 F 225 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR SEQRES 7 F 225 ALA TYR MET GLU LEU LEU SER LEU THR SER GLU ASP SER SEQRES 8 F 225 ALA VAL TYR TYR CYS GLU VAL ILE ASN THR TYR TRP GLY SEQRES 9 F 225 GLN GLY THR LEU VAL THR VAL SER ALA ALA LYS THR THR SEQRES 10 F 225 PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SER ALA ALA SEQRES 11 F 225 GLN THR ASN SER MET VAL THR LEU GLY CYS LEU VAL LYS SEQRES 12 F 225 GLY TYR PHE PRO GLU PRO VAL THR VAL THR TRP ASN SER SEQRES 13 F 225 GLY SER LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 14 F 225 LEU GLN SER ASP LEU TYR THR LEU SER SER SER VAL THR SEQRES 15 F 225 VAL PRO SER SER THR TRP PRO SER GLU THR VAL THR CYS SEQRES 16 F 225 ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS SEQRES 17 F 225 LYS ILE VAL PRO ARG ASP CYS GLY SER GLY SER HIS HIS SEQRES 18 F 225 HIS HIS HIS HIS HELIX 1 AA1 GLN A 11 GLN A 35 1 25 HELIX 2 AA2 TYR A 46 TYR A 70 1 25 HELIX 3 AA3 ASP A 73 THR A 105 1 33 HELIX 4 AA4 SER A 107 ASN A 112 5 6 HELIX 5 AA5 ILE D 13 TYR D 36 1 24 HELIX 6 AA6 TYR D 46 TYR D 70 1 25 HELIX 7 AA7 ASP D 73 ARG D 100 1 28 HELIX 8 AA8 SER D 107 ASN D 112 5 6 HELIX 9 AA9 SER C 125 GLY C 132 1 8 HELIX 10 AB1 THR C 186 HIS C 193 1 8 HELIX 11 AB2 THR B 87 SER B 91 5 5 HELIX 12 AB3 SER B 156 SER B 158 5 3 HELIX 13 AB4 SER E 125 GLY E 132 1 8 HELIX 14 AB5 LYS E 187 HIS E 193 1 7 HELIX 15 AB6 THR F 87 SER F 91 5 5 SHEET 1 AA1 8 THR A 126 PRO A 131 0 SHEET 2 AA1 8 LEU A 118 PHE A 123 -1 N LEU A 119 O ARG A 130 SHEET 3 AA1 8 GLU A 166 ALA A 170 -1 O THR A 168 N ASN A 120 SHEET 4 AA1 8 LEU A 175 TYR A 186 -1 O LEU A 178 N VAL A 167 SHEET 5 AA1 8 SER A 190 GLY A 201 -1 O GLY A 201 N LEU A 175 SHEET 6 AA1 8 SER A 138 VAL A 143 -1 N ALA A 141 O ALA A 193 SHEET 7 AA1 8 LEU A 148 MET A 150 -1 O LYS A 149 N VAL A 142 SHEET 8 AA1 8 MET A 153 HIS A 154 -1 O MET A 153 N MET A 150 SHEET 1 AA2 7 THR D 126 ARG D 130 0 SHEET 2 AA2 7 LEU D 119 PHE D 123 -1 N PHE D 123 O THR D 126 SHEET 3 AA2 7 GLU D 166 ALA D 170 -1 O THR D 168 N ASN D 120 SHEET 4 AA2 7 VAL D 174 SER D 185 -1 O LEU D 178 N VAL D 167 SHEET 5 AA2 7 GLY D 191 ASN D 202 -1 O GLY D 201 N LEU D 175 SHEET 6 AA2 7 SER D 138 VAL D 143 -1 N VAL D 139 O TYR D 195 SHEET 7 AA2 7 LEU D 148 MET D 150 -1 O LYS D 149 N VAL D 142 SHEET 1 AA3 4 THR C 5 GLN C 6 0 SHEET 2 AA3 4 ALA C 19 LYS C 24 -1 O LYS C 24 N THR C 5 SHEET 3 AA3 4 ASP C 74 ILE C 79 -1 O LEU C 77 N ILE C 21 SHEET 4 AA3 4 PHE C 66 SER C 71 -1 N SER C 67 O ASN C 78 SHEET 1 AA4 5 SER C 10 VAL C 13 0 SHEET 2 AA4 5 THR C 106 ILE C 110 1 O LYS C 107 N LEU C 11 SHEET 3 AA4 5 ALA C 88 GLN C 93 -1 N TYR C 90 O THR C 106 SHEET 4 AA4 5 ASN C 38 GLN C 42 -1 N GLN C 42 O THR C 89 SHEET 5 AA4 5 LYS C 49 ILE C 52 -1 O LYS C 49 N GLN C 41 SHEET 1 AA5 4 VAL C 119 PHE C 122 0 SHEET 2 AA5 4 ALA C 134 PHE C 143 -1 O PHE C 139 N SER C 120 SHEET 3 AA5 4 TYR C 177 LEU C 185 -1 O LEU C 185 N ALA C 134 SHEET 4 AA5 4 VAL C 163 TRP C 167 -1 N LEU C 164 O THR C 182 SHEET 1 AA6 4 SER C 157 GLU C 158 0 SHEET 2 AA6 4 ILE C 148 ILE C 154 -1 N ILE C 154 O SER C 157 SHEET 3 AA6 4 SER C 195 HIS C 202 -1 O THR C 197 N LYS C 153 SHEET 4 AA6 4 ILE C 209 VAL C 210 -1 O ILE C 209 N ALA C 200 SHEET 1 AA7 4 SER C 157 GLU C 158 0 SHEET 2 AA7 4 ILE C 148 ILE C 154 -1 N ILE C 154 O SER C 157 SHEET 3 AA7 4 SER C 195 HIS C 202 -1 O THR C 197 N LYS C 153 SHEET 4 AA7 4 PHE C 213 ASN C 214 -1 O PHE C 213 N TYR C 196 SHEET 1 AA8 4 GLN B 3 GLN B 5 0 SHEET 2 AA8 4 SER B 17 SER B 25 -1 O LYS B 23 N GLN B 5 SHEET 3 AA8 4 THR B 78 LEU B 84 -1 O MET B 81 N ILE B 20 SHEET 4 AA8 4 ALA B 68 ASP B 73 -1 N ASP B 73 O THR B 78 SHEET 1 AA9 6 GLU B 10 VAL B 12 0 SHEET 2 AA9 6 THR B 107 VAL B 111 1 O THR B 110 N VAL B 12 SHEET 3 AA9 6 VAL B 93 GLU B 97 -1 N TYR B 94 O THR B 107 SHEET 4 AA9 6 MET B 34 GLN B 39 -1 N GLN B 39 O VAL B 93 SHEET 5 AA9 6 LEU B 45 ILE B 51 -1 O GLU B 46 N LYS B 38 SHEET 6 AA9 6 THR B 58 TYR B 60 -1 O SER B 59 N LEU B 50 SHEET 1 AB1 4 SER B 120 LEU B 124 0 SHEET 2 AB1 4 VAL B 136 TYR B 145 -1 O LEU B 141 N TYR B 122 SHEET 3 AB1 4 LEU B 174 VAL B 183 -1 O VAL B 183 N VAL B 136 SHEET 4 AB1 4 VAL B 169 GLN B 171 -1 N VAL B 169 O THR B 176 SHEET 1 AB2 2 THR B 151 TRP B 154 0 SHEET 2 AB2 2 CYS B 195 ALA B 198 -1 O ALA B 198 N THR B 151 SHEET 1 AB3 2 SER E 10 VAL E 13 0 SHEET 2 AB3 2 LYS E 107 ILE E 110 1 O GLU E 109 N LEU E 11 SHEET 1 AB4 2 ALA E 19 CYS E 23 0 SHEET 2 AB4 2 PHE E 75 ILE E 79 -1 O PHE E 75 N CYS E 23 SHEET 1 AB5 2 ASP E 30 TYR E 31 0 SHEET 2 AB5 2 ASP E 34 ASN E 35 -1 O ASP E 34 N TYR E 31 SHEET 1 AB6 3 LYS E 49 ILE E 52 0 SHEET 2 AB6 3 TRP E 39 GLN E 42 -1 N GLN E 41 O LYS E 49 SHEET 3 AB6 3 THR E 89 CYS E 92 -1 O THR E 89 N GLN E 42 SHEET 1 AB7 2 THR E 118 VAL E 119 0 SHEET 2 AB7 2 LEU E 140 ASN E 141 -1 O ASN E 141 N THR E 118 SHEET 1 AB8 3 GLY E 133 VAL E 136 0 SHEET 2 AB8 3 SER E 180 THR E 186 -1 O LEU E 185 N ALA E 134 SHEET 3 AB8 3 VAL E 163 SER E 166 -1 N LEU E 164 O THR E 182 SHEET 1 AB9 3 ASN E 149 ILE E 154 0 SHEET 2 AB9 3 SER E 195 THR E 201 -1 O THR E 197 N LYS E 153 SHEET 3 AB9 3 ILE E 209 ASN E 214 -1 O PHE E 213 N TYR E 196 SHEET 1 AC1 4 GLN F 3 GLN F 6 0 SHEET 2 AC1 4 LYS F 19 SER F 25 -1 O LYS F 23 N GLN F 5 SHEET 3 AC1 4 THR F 78 LEU F 83 -1 O MET F 81 N ILE F 20 SHEET 4 AC1 4 ALA F 68 THR F 69 -1 N THR F 69 O GLU F 82 SHEET 1 AC2 4 GLN F 3 GLN F 6 0 SHEET 2 AC2 4 LYS F 19 SER F 25 -1 O LYS F 23 N GLN F 5 SHEET 3 AC2 4 THR F 78 LEU F 83 -1 O MET F 81 N ILE F 20 SHEET 4 AC2 4 VAL F 72 ASP F 73 -1 N ASP F 73 O THR F 78 SHEET 1 AC3 6 GLU F 10 VAL F 12 0 SHEET 2 AC3 6 THR F 107 VAL F 111 1 O THR F 110 N VAL F 12 SHEET 3 AC3 6 ALA F 92 GLU F 97 -1 N ALA F 92 O VAL F 109 SHEET 4 AC3 6 MET F 34 GLN F 39 -1 N GLN F 39 O VAL F 93 SHEET 5 AC3 6 LEU F 45 ILE F 51 -1 O GLU F 46 N LYS F 38 SHEET 6 AC3 6 THR F 58 TYR F 60 -1 O SER F 59 N LEU F 50 SHEET 1 AC4 4 SER F 120 TYR F 122 0 SHEET 2 AC4 4 VAL F 136 TYR F 145 -1 O LEU F 141 N TYR F 122 SHEET 3 AC4 4 LEU F 174 VAL F 183 -1 O LEU F 177 N VAL F 142 SHEET 4 AC4 4 VAL F 163 THR F 165 -1 N HIS F 164 O SER F 180 SHEET 1 AC5 4 SER F 120 TYR F 122 0 SHEET 2 AC5 4 VAL F 136 TYR F 145 -1 O LEU F 141 N TYR F 122 SHEET 3 AC5 4 LEU F 174 VAL F 183 -1 O LEU F 177 N VAL F 142 SHEET 4 AC5 4 VAL F 169 GLN F 171 -1 N GLN F 171 O LEU F 174 SHEET 1 AC6 3 THR F 153 TRP F 154 0 SHEET 2 AC6 3 THR F 194 ASN F 196 -1 O ASN F 196 N THR F 153 SHEET 3 AC6 3 ASP F 207 LYS F 209 -1 O LYS F 208 N CYS F 195 SSBOND 1 CYS C 23 CYS C 92 1555 1555 2.03 SSBOND 2 CYS C 138 CYS C 198 1555 1555 2.03 SSBOND 3 CYS B 22 CYS B 96 1555 1555 2.03 SSBOND 4 CYS B 140 CYS B 195 1555 1555 2.03 SSBOND 5 CYS E 23 CYS E 92 1555 1555 2.04 SSBOND 6 CYS E 138 CYS E 198 1555 1555 2.03 SSBOND 7 CYS F 22 CYS F 96 1555 1555 2.03 SSBOND 8 CYS F 140 CYS F 195 1555 1555 2.04 CISPEP 1 TYR C 144 PRO C 145 0 2.04 CISPEP 2 PHE B 146 PRO B 147 0 -6.22 CISPEP 3 GLU B 148 PRO B 149 0 -0.98 CISPEP 4 TRP B 188 PRO B 189 0 -0.89 CISPEP 5 TYR E 144 PRO E 145 0 -5.97 CISPEP 6 PHE F 146 PRO F 147 0 -5.92 CISPEP 7 GLU F 148 PRO F 149 0 -5.16 CISPEP 8 TRP F 188 PRO F 189 0 -2.24 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