HEADER IMMUNE SYSTEM 13-MAR-23 8IOW TITLE CRYO-EM STRUCTURE OF THE SARILUMAB FAB/IL-6R COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTERLEUKIN-6 RECEPTOR SUBUNIT ALPHA; COMPND 3 CHAIN: I, D2; COMPND 4 SYNONYM: IL-6 RECEPTOR SUBUNIT ALPHA,IL-6R SUBUNIT ALPHA,IL-6R-ALPHA, COMPND 5 IL-6RA,IL-6R 1,MEMBRANE GLYCOPROTEIN 80,GP80,IL-6R-D2; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: LIGHT CHAIN OF SARILUMAB FAB; COMPND 9 CHAIN: L; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: HEAVY CHAIN OF SARILUMAB FAB; COMPND 13 CHAIN: H; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: IL6R; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; 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 KEYWDS ANTIBODY, IL-6R, STRUCTURAL PROTEIN, IMMUNE SYSTEM EXPDTA ELECTRON MICROSCOPY AUTHOR J.SHE,L.CHEN,M.X.WANG JRNL AUTH J.SHE,M.X.WANG,L.CHEN JRNL TITL CRYO-EM STRUCTURE OF THE SARILUMAB FAB/IL-6R COMPLEX JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.200 REMARK 3 NUMBER OF PARTICLES : 134252 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8IOW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC. REMARK 100 THE DEPOSITION ID IS D_1300035981. 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 : THE SARILUMAB FAB/IL-6R COMPLEX 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 : 8.00 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 REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1400.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2700.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 55.00 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, D2, L, H 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 I 1 REMARK 465 LEU I 2 REMARK 465 ALA I 3 REMARK 465 VAL I 4 REMARK 465 GLY I 5 REMARK 465 CYS I 6 REMARK 465 ALA I 7 REMARK 465 LEU I 8 REMARK 465 LEU I 9 REMARK 465 ALA I 10 REMARK 465 ALA I 11 REMARK 465 LEU I 12 REMARK 465 LEU I 13 REMARK 465 ALA I 14 REMARK 465 ALA I 15 REMARK 465 PRO I 16 REMARK 465 GLY I 17 REMARK 465 ALA I 18 REMARK 465 ALA I 19 REMARK 465 LEU I 20 REMARK 465 ALA I 21 REMARK 465 PRO I 22 REMARK 465 ARG I 23 REMARK 465 ARG I 24 REMARK 465 CYS I 25 REMARK 465 PRO I 26 REMARK 465 ALA I 27 REMARK 465 GLN I 28 REMARK 465 GLU I 29 REMARK 465 VAL I 30 REMARK 465 ALA I 31 REMARK 465 ARG I 32 REMARK 465 GLY I 33 REMARK 465 VAL I 34 REMARK 465 LEU I 35 REMARK 465 THR I 36 REMARK 465 SER I 37 REMARK 465 LEU I 38 REMARK 465 PRO I 39 REMARK 465 GLY I 40 REMARK 465 ASP I 41 REMARK 465 SER I 42 REMARK 465 VAL I 43 REMARK 465 THR I 44 REMARK 465 LEU I 45 REMARK 465 THR I 46 REMARK 465 CYS I 47 REMARK 465 PRO I 48 REMARK 465 GLY I 49 REMARK 465 VAL I 50 REMARK 465 GLU I 51 REMARK 465 PRO I 52 REMARK 465 GLU I 53 REMARK 465 ASP I 54 REMARK 465 ASN I 55 REMARK 465 ALA I 56 REMARK 465 THR I 57 REMARK 465 VAL I 58 REMARK 465 HIS I 59 REMARK 465 TRP I 60 REMARK 465 VAL I 61 REMARK 465 LEU I 62 REMARK 465 ARG I 63 REMARK 465 LYS I 64 REMARK 465 PRO I 65 REMARK 465 ALA I 66 REMARK 465 ALA I 67 REMARK 465 GLY I 68 REMARK 465 SER I 69 REMARK 465 HIS I 70 REMARK 465 PRO I 71 REMARK 465 SER I 72 REMARK 465 ARG I 73 REMARK 465 TRP I 74 REMARK 465 ALA I 75 REMARK 465 GLY I 76 REMARK 465 MET I 77 REMARK 465 GLY I 78 REMARK 465 ARG I 79 REMARK 465 ARG I 80 REMARK 465 LEU I 81 REMARK 465 LEU I 82 REMARK 465 LEU I 83 REMARK 465 ARG I 84 REMARK 465 SER I 85 REMARK 465 VAL I 86 REMARK 465 GLN I 87 REMARK 465 LEU I 88 REMARK 465 HIS I 89 REMARK 465 ASP I 90 REMARK 465 SER I 91 REMARK 465 GLY I 92 REMARK 465 ASN I 93 REMARK 465 TYR I 94 REMARK 465 SER I 95 REMARK 465 CYS I 96 REMARK 465 TYR I 97 REMARK 465 ARG I 98 REMARK 465 ALA I 99 REMARK 465 GLY I 100 REMARK 465 ARG I 101 REMARK 465 PRO I 102 REMARK 465 ALA I 103 REMARK 465 GLY I 104 REMARK 465 THR I 105 REMARK 465 VAL I 106 REMARK 465 HIS I 107 REMARK 465 LEU I 108 REMARK 465 LEU I 109 REMARK 465 VAL I 110 REMARK 465 ASP I 111 REMARK 465 VAL I 112 REMARK 465 PRO I 113 REMARK 465 PRO I 114 REMARK 465 GLU I 115 REMARK 465 GLU I 116 REMARK 465 PRO I 117 REMARK 465 GLN I 118 REMARK 465 LEU I 119 REMARK 465 SER I 120 REMARK 465 CYS I 121 REMARK 465 PHE I 122 REMARK 465 ARG I 123 REMARK 465 LYS I 124 REMARK 465 SER I 125 REMARK 465 PRO I 126 REMARK 465 LEU I 127 REMARK 465 SER I 128 REMARK 465 ASN I 129 REMARK 465 VAL I 130 REMARK 465 VAL I 131 REMARK 465 CYS I 132 REMARK 465 GLU I 133 REMARK 465 TRP I 134 REMARK 465 GLY I 135 REMARK 465 PRO I 136 REMARK 465 ARG I 137 REMARK 465 SER I 138 REMARK 465 THR I 139 REMARK 465 PRO I 140 REMARK 465 SER I 141 REMARK 465 LEU I 142 REMARK 465 THR I 143 REMARK 465 THR I 144 REMARK 465 LYS I 145 REMARK 465 ALA I 146 REMARK 465 VAL I 147 REMARK 465 LEU I 148 REMARK 465 LEU I 149 REMARK 465 VAL I 150 REMARK 465 ARG I 151 REMARK 465 LYS I 152 REMARK 465 PHE I 153 REMARK 465 GLN I 154 REMARK 465 ASN I 155 REMARK 465 SER I 156 REMARK 465 PRO I 157 REMARK 465 ALA I 158 REMARK 465 GLU I 159 REMARK 465 ASP I 160 REMARK 465 PHE I 161 REMARK 465 GLN I 162 REMARK 465 GLU I 163 REMARK 465 PRO I 164 REMARK 465 CYS I 165 REMARK 465 GLN I 166 REMARK 465 TYR I 167 REMARK 465 SER I 168 REMARK 465 GLN I 169 REMARK 465 GLU I 170 REMARK 465 SER I 171 REMARK 465 GLN I 172 REMARK 465 LYS I 173 REMARK 465 PHE I 174 REMARK 465 SER I 175 REMARK 465 CYS I 176 REMARK 465 GLN I 177 REMARK 465 LEU I 178 REMARK 465 ALA I 179 REMARK 465 VAL I 180 REMARK 465 PRO I 181 REMARK 465 GLU I 182 REMARK 465 GLY I 183 REMARK 465 ASP I 184 REMARK 465 SER I 185 REMARK 465 SER I 186 REMARK 465 PHE I 187 REMARK 465 TYR I 188 REMARK 465 ILE I 189 REMARK 465 VAL I 190 REMARK 465 SER I 191 REMARK 465 MET I 192 REMARK 465 CYS I 193 REMARK 465 VAL I 194 REMARK 465 ALA I 195 REMARK 465 SER I 196 REMARK 465 SER I 197 REMARK 465 VAL I 198 REMARK 465 GLY I 199 REMARK 465 SER I 200 REMARK 465 LYS I 201 REMARK 465 PHE I 202 REMARK 465 SER I 203 REMARK 465 LYS I 204 REMARK 465 THR I 205 REMARK 465 GLN I 206 REMARK 465 THR I 207 REMARK 465 PHE I 208 REMARK 465 THR I 313 REMARK 465 PRO I 314 REMARK 465 TRP I 315 REMARK 465 THR I 316 REMARK 465 GLU I 317 REMARK 465 SER I 318 REMARK 465 ARG I 319 REMARK 465 SER I 320 REMARK 465 PRO I 321 REMARK 465 PRO I 322 REMARK 465 ALA I 323 REMARK 465 GLU I 324 REMARK 465 ASN I 325 REMARK 465 GLU I 326 REMARK 465 VAL I 327 REMARK 465 SER I 328 REMARK 465 THR I 329 REMARK 465 PRO I 330 REMARK 465 MET I 331 REMARK 465 GLN I 332 REMARK 465 ALA I 333 REMARK 465 LEU I 334 REMARK 465 THR I 335 REMARK 465 THR I 336 REMARK 465 ASN I 337 REMARK 465 LYS I 338 REMARK 465 ASP I 339 REMARK 465 ASP I 340 REMARK 465 ASP I 341 REMARK 465 ASN I 342 REMARK 465 ILE I 343 REMARK 465 LEU I 344 REMARK 465 PHE I 345 REMARK 465 ARG I 346 REMARK 465 ASP I 347 REMARK 465 SER I 348 REMARK 465 ALA I 349 REMARK 465 ASN I 350 REMARK 465 ALA I 351 REMARK 465 THR I 352 REMARK 465 SER I 353 REMARK 465 LEU I 354 REMARK 465 PRO I 355 REMARK 465 GLY I 356 REMARK 465 SER I 357 REMARK 465 ARG I 358 REMARK 465 ARG I 359 REMARK 465 ARG I 360 REMARK 465 GLY I 361 REMARK 465 SER I 362 REMARK 465 CYS I 363 REMARK 465 GLY I 364 REMARK 465 LEU I 365 REMARK 465 MET D 1 REMARK 465 LEU D 2 REMARK 465 ALA D 3 REMARK 465 VAL D 4 REMARK 465 GLY D 5 REMARK 465 CYS D 6 REMARK 465 ALA D 7 REMARK 465 LEU D 8 REMARK 465 LEU D 9 REMARK 465 ALA D 10 REMARK 465 ALA D 11 REMARK 465 LEU D 12 REMARK 465 LEU D 13 REMARK 465 ALA D 14 REMARK 465 ALA D 15 REMARK 465 PRO D 16 REMARK 465 GLY D 17 REMARK 465 ALA D 18 REMARK 465 ALA D 19 REMARK 465 LEU D 20 REMARK 465 ALA D 21 REMARK 465 PRO D 22 REMARK 465 ARG D 23 REMARK 465 ARG D 24 REMARK 465 CYS D 25 REMARK 465 PRO D 26 REMARK 465 ALA D 27 REMARK 465 GLN D 28 REMARK 465 GLU D 29 REMARK 465 VAL D 30 REMARK 465 ALA D 31 REMARK 465 ARG D 32 REMARK 465 GLY D 33 REMARK 465 VAL D 34 REMARK 465 LEU D 35 REMARK 465 THR D 36 REMARK 465 SER D 37 REMARK 465 LEU D 38 REMARK 465 PRO D 39 REMARK 465 GLY D 40 REMARK 465 ASP D 41 REMARK 465 SER D 42 REMARK 465 VAL D 43 REMARK 465 THR D 44 REMARK 465 LEU D 45 REMARK 465 THR D 46 REMARK 465 CYS D 47 REMARK 465 PRO D 48 REMARK 465 GLY D 49 REMARK 465 VAL D 50 REMARK 465 GLU D 51 REMARK 465 PRO D 52 REMARK 465 GLU D 53 REMARK 465 ASP D 54 REMARK 465 ASN D 55 REMARK 465 ALA D 56 REMARK 465 THR D 57 REMARK 465 VAL D 58 REMARK 465 HIS D 59 REMARK 465 TRP D 60 REMARK 465 VAL D 61 REMARK 465 LEU D 62 REMARK 465 ARG D 63 REMARK 465 LYS D 64 REMARK 465 PRO D 65 REMARK 465 ALA D 66 REMARK 465 ALA D 67 REMARK 465 GLY D 68 REMARK 465 SER D 69 REMARK 465 HIS D 70 REMARK 465 PRO D 71 REMARK 465 SER D 72 REMARK 465 ARG D 73 REMARK 465 TRP D 74 REMARK 465 ALA D 75 REMARK 465 GLY D 76 REMARK 465 MET D 77 REMARK 465 GLY D 78 REMARK 465 ARG D 79 REMARK 465 ARG D 80 REMARK 465 LEU D 81 REMARK 465 LEU D 82 REMARK 465 LEU D 83 REMARK 465 ARG D 84 REMARK 465 SER D 85 REMARK 465 VAL D 86 REMARK 465 GLN D 87 REMARK 465 LEU D 88 REMARK 465 HIS D 89 REMARK 465 ASP D 90 REMARK 465 SER D 91 REMARK 465 GLY D 92 REMARK 465 ASN D 93 REMARK 465 TYR D 94 REMARK 465 SER D 95 REMARK 465 CYS D 96 REMARK 465 TYR D 97 REMARK 465 ARG D 98 REMARK 465 ALA D 99 REMARK 465 GLY D 100 REMARK 465 ARG D 101 REMARK 465 PRO D 102 REMARK 465 ALA D 103 REMARK 465 GLY D 104 REMARK 465 THR D 105 REMARK 465 VAL D 106 REMARK 465 HIS D 107 REMARK 465 LEU D 108 REMARK 465 LEU D 109 REMARK 465 VAL D 110 REMARK 465 ASP D 111 REMARK 465 VAL D 112 REMARK 465 PRO D 113 REMARK 465 PRO D 114 REMARK 465 GLU D 115 REMARK 465 GLU D 116 REMARK 465 PRO D 117 REMARK 465 GLN D 118 REMARK 465 LEU D 119 REMARK 465 TRP D 134 REMARK 465 GLY D 135 REMARK 465 PRO D 136 REMARK 465 ARG D 137 REMARK 465 SER D 138 REMARK 465 THR D 139 REMARK 465 PRO D 140 REMARK 465 SER D 141 REMARK 465 LEU D 142 REMARK 465 THR D 143 REMARK 465 THR D 144 REMARK 465 LYS D 145 REMARK 465 ALA D 146 REMARK 465 VAL D 147 REMARK 465 LEU D 148 REMARK 465 LEU D 149 REMARK 465 VAL D 150 REMARK 465 ARG D 151 REMARK 465 LYS D 152 REMARK 465 PHE D 153 REMARK 465 GLN D 154 REMARK 465 ASN D 155 REMARK 465 SER D 156 REMARK 465 PRO D 157 REMARK 465 ALA D 158 REMARK 465 GLU D 159 REMARK 465 ASP D 160 REMARK 465 PHE D 161 REMARK 465 GLN D 162 REMARK 465 GLU D 163 REMARK 465 PRO D 164 REMARK 465 CYS D 165 REMARK 465 GLN D 166 REMARK 465 TYR D 167 REMARK 465 SER D 168 REMARK 465 GLN D 169 REMARK 465 GLU D 170 REMARK 465 SER D 171 REMARK 465 GLN D 172 REMARK 465 LYS D 173 REMARK 465 PHE D 174 REMARK 465 SER D 175 REMARK 465 CYS D 176 REMARK 465 GLN D 177 REMARK 465 LEU D 178 REMARK 465 ALA D 179 REMARK 465 VAL D 180 REMARK 465 PRO D 181 REMARK 465 GLU D 182 REMARK 465 GLY D 183 REMARK 465 ASP D 184 REMARK 465 SER D 185 REMARK 465 SER D 186 REMARK 465 PHE D 187 REMARK 465 TYR D 188 REMARK 465 ILE D 189 REMARK 465 VAL D 190 REMARK 465 SER D 191 REMARK 465 MET D 192 REMARK 465 CYS D 193 REMARK 465 VAL D 194 REMARK 465 ALA D 195 REMARK 465 SER D 196 REMARK 465 SER D 197 REMARK 465 VAL D 198 REMARK 465 GLY D 199 REMARK 465 SER D 200 REMARK 465 LYS D 201 REMARK 465 PHE D 202 REMARK 465 SER D 203 REMARK 465 LYS D 204 REMARK 465 THR D 205 REMARK 465 GLN D 206 REMARK 465 THR D 207 REMARK 465 PHE D 208 REMARK 465 GLN D 209 REMARK 465 GLY D 210 REMARK 465 CYS D 211 REMARK 465 GLY D 212 REMARK 465 ILE D 213 REMARK 465 LEU D 214 REMARK 465 GLN D 215 REMARK 465 PRO D 216 REMARK 465 ASP D 217 REMARK 465 PRO D 218 REMARK 465 PRO D 219 REMARK 465 ALA D 220 REMARK 465 ASN D 221 REMARK 465 ILE D 222 REMARK 465 THR D 223 REMARK 465 VAL D 224 REMARK 465 THR D 225 REMARK 465 ALA D 226 REMARK 465 VAL D 227 REMARK 465 ALA D 228 REMARK 465 ARG D 229 REMARK 465 ASN D 230 REMARK 465 PRO D 231 REMARK 465 ARG D 232 REMARK 465 TRP D 233 REMARK 465 LEU D 234 REMARK 465 SER D 235 REMARK 465 VAL D 236 REMARK 465 THR D 237 REMARK 465 TRP D 238 REMARK 465 GLN D 239 REMARK 465 ASP D 240 REMARK 465 PRO D 241 REMARK 465 HIS D 242 REMARK 465 SER D 243 REMARK 465 TRP D 244 REMARK 465 ASN D 245 REMARK 465 SER D 246 REMARK 465 SER D 247 REMARK 465 PHE D 248 REMARK 465 TYR D 249 REMARK 465 ARG D 250 REMARK 465 LEU D 251 REMARK 465 ARG D 252 REMARK 465 PHE D 253 REMARK 465 GLU D 254 REMARK 465 LEU D 255 REMARK 465 ARG D 256 REMARK 465 TYR D 257 REMARK 465 ARG D 258 REMARK 465 ALA D 259 REMARK 465 GLU D 260 REMARK 465 ARG D 261 REMARK 465 SER D 262 REMARK 465 LYS D 263 REMARK 465 THR D 264 REMARK 465 PHE D 265 REMARK 465 THR D 266 REMARK 465 THR D 267 REMARK 465 TRP D 268 REMARK 465 MET D 269 REMARK 465 VAL D 270 REMARK 465 LYS D 271 REMARK 465 ASP D 272 REMARK 465 LEU D 273 REMARK 465 GLN D 274 REMARK 465 HIS D 275 REMARK 465 HIS D 276 REMARK 465 CYS D 277 REMARK 465 VAL D 278 REMARK 465 ILE D 279 REMARK 465 HIS D 280 REMARK 465 ASP D 281 REMARK 465 ALA D 282 REMARK 465 TRP D 283 REMARK 465 SER D 284 REMARK 465 GLY D 285 REMARK 465 LEU D 286 REMARK 465 ARG D 287 REMARK 465 HIS D 288 REMARK 465 VAL D 289 REMARK 465 VAL D 290 REMARK 465 GLN D 291 REMARK 465 LEU D 292 REMARK 465 ARG D 293 REMARK 465 ALA D 294 REMARK 465 GLN D 295 REMARK 465 GLU D 296 REMARK 465 GLU D 297 REMARK 465 PHE D 298 REMARK 465 GLY D 299 REMARK 465 GLN D 300 REMARK 465 GLY D 301 REMARK 465 GLU D 302 REMARK 465 TRP D 303 REMARK 465 SER D 304 REMARK 465 GLU D 305 REMARK 465 TRP D 306 REMARK 465 SER D 307 REMARK 465 PRO D 308 REMARK 465 GLU D 309 REMARK 465 ALA D 310 REMARK 465 MET D 311 REMARK 465 GLY D 312 REMARK 465 THR D 313 REMARK 465 PRO D 314 REMARK 465 TRP D 315 REMARK 465 THR D 316 REMARK 465 GLU D 317 REMARK 465 SER D 318 REMARK 465 ARG D 319 REMARK 465 SER D 320 REMARK 465 PRO D 321 REMARK 465 PRO D 322 REMARK 465 ALA D 323 REMARK 465 GLU D 324 REMARK 465 ASN D 325 REMARK 465 GLU D 326 REMARK 465 VAL D 327 REMARK 465 SER D 328 REMARK 465 THR D 329 REMARK 465 PRO D 330 REMARK 465 MET D 331 REMARK 465 GLN D 332 REMARK 465 ALA D 333 REMARK 465 LEU D 334 REMARK 465 THR D 335 REMARK 465 THR D 336 REMARK 465 ASN D 337 REMARK 465 LYS D 338 REMARK 465 ASP D 339 REMARK 465 ASP D 340 REMARK 465 ASP D 341 REMARK 465 ASN D 342 REMARK 465 ILE D 343 REMARK 465 LEU D 344 REMARK 465 PHE D 345 REMARK 465 ARG D 346 REMARK 465 ASP D 347 REMARK 465 SER D 348 REMARK 465 ALA D 349 REMARK 465 ASN D 350 REMARK 465 ALA D 351 REMARK 465 THR D 352 REMARK 465 SER D 353 REMARK 465 LEU D 354 REMARK 465 PRO D 355 REMARK 465 GLY D 356 REMARK 465 SER D 357 REMARK 465 ARG D 358 REMARK 465 ARG D 359 REMARK 465 ARG D 360 REMARK 465 GLY D 361 REMARK 465 SER D 362 REMARK 465 CYS D 363 REMARK 465 GLY D 364 REMARK 465 LEU D 365 REMARK 465 GLU L 213 REMARK 465 CYS L 214 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 LYS H 217 REMARK 465 SER H 218 REMARK 465 CYS H 219 REMARK 465 ASP H 220 REMARK 465 LYS H 221 REMARK 465 THR H 222 REMARK 465 HIS H 223 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 ALA I 228 -175.51 -171.88 REMARK 500 PRO I 231 74.29 -68.78 REMARK 500 ARG I 256 116.50 -162.88 REMARK 500 ASND2 129 79.83 61.54 REMARK 500 ALA L 51 -6.72 68.00 REMARK 500 PRO L 95 82.07 -67.16 REMARK 500 ASN L 138 66.90 60.22 REMARK 500 PRO L 141 -166.64 -79.46 REMARK 500 TYR L 173 -168.91 -105.42 REMARK 500 VAL H 48 -59.51 -122.88 REMARK 500 ASP H 101 -9.58 63.26 REMARK 500 SER H 102 111.23 -164.16 REMARK 500 ASP H 147 65.05 60.92 REMARK 500 SER H 180 117.70 -161.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-35627 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE SARILUMAB FAB/IL-6R COMPLEX DBREF 8IOW I 1 365 UNP P08887 IL6RA_HUMAN 1 365 DBREF 8IOWD2 1 365 UNP P08887 IL6RA_HUMAN 1 365 DBREF 8IOW L 1 214 PDB 8IOW 8IOW 1 214 DBREF 8IOW H 1 223 PDB 8IOW 8IOW 1 223 SEQRES 1 I 365 MET LEU ALA VAL GLY CYS ALA LEU LEU ALA ALA LEU LEU SEQRES 2 I 365 ALA ALA PRO GLY ALA ALA LEU ALA PRO ARG ARG CYS PRO SEQRES 3 I 365 ALA GLN GLU VAL ALA ARG GLY VAL LEU THR SER LEU PRO SEQRES 4 I 365 GLY ASP SER VAL THR LEU THR CYS PRO GLY VAL GLU PRO SEQRES 5 I 365 GLU ASP ASN ALA THR VAL HIS TRP VAL LEU ARG LYS PRO SEQRES 6 I 365 ALA ALA GLY SER HIS PRO SER ARG TRP ALA GLY MET GLY SEQRES 7 I 365 ARG ARG LEU LEU LEU ARG SER VAL GLN LEU HIS ASP SER SEQRES 8 I 365 GLY ASN TYR SER CYS TYR ARG ALA GLY ARG PRO ALA GLY SEQRES 9 I 365 THR VAL HIS LEU LEU VAL ASP VAL PRO PRO GLU GLU PRO SEQRES 10 I 365 GLN LEU SER CYS PHE ARG LYS SER PRO LEU SER ASN VAL SEQRES 11 I 365 VAL CYS GLU TRP GLY PRO ARG SER THR PRO SER LEU THR SEQRES 12 I 365 THR LYS ALA VAL LEU LEU VAL ARG LYS PHE GLN ASN SER SEQRES 13 I 365 PRO ALA GLU ASP PHE GLN GLU PRO CYS GLN TYR SER GLN SEQRES 14 I 365 GLU SER GLN LYS PHE SER CYS GLN LEU ALA VAL PRO GLU SEQRES 15 I 365 GLY ASP SER SER PHE TYR ILE VAL SER MET CYS VAL ALA SEQRES 16 I 365 SER SER VAL GLY SER LYS PHE SER LYS THR GLN THR PHE SEQRES 17 I 365 GLN GLY CYS GLY ILE LEU GLN PRO ASP PRO PRO ALA ASN SEQRES 18 I 365 ILE THR VAL THR ALA VAL ALA ARG ASN PRO ARG TRP LEU SEQRES 19 I 365 SER VAL THR TRP GLN ASP PRO HIS SER TRP ASN SER SER SEQRES 20 I 365 PHE TYR ARG LEU ARG PHE GLU LEU ARG TYR ARG ALA GLU SEQRES 21 I 365 ARG SER LYS THR PHE THR THR TRP MET VAL LYS ASP LEU SEQRES 22 I 365 GLN HIS HIS CYS VAL ILE HIS ASP ALA TRP SER GLY LEU SEQRES 23 I 365 ARG HIS VAL VAL GLN LEU ARG ALA GLN GLU GLU PHE GLY SEQRES 24 I 365 GLN GLY GLU TRP SER GLU TRP SER PRO GLU ALA MET GLY SEQRES 25 I 365 THR PRO TRP THR GLU SER ARG SER PRO PRO ALA GLU ASN SEQRES 26 I 365 GLU VAL SER THR PRO MET GLN ALA LEU THR THR ASN LYS SEQRES 27 I 365 ASP ASP ASP ASN ILE LEU PHE ARG ASP SER ALA ASN ALA SEQRES 28 I 365 THR SER LEU PRO GLY SER ARG ARG ARG GLY SER CYS GLY SEQRES 29 I 365 LEU SEQRES 1D2 365 MET LEU ALA VAL GLY CYS ALA LEU LEU ALA ALA LEU LEU SEQRES 2D2 365 ALA ALA PRO GLY ALA ALA LEU ALA PRO ARG ARG CYS PRO SEQRES 3D2 365 ALA GLN GLU VAL ALA ARG GLY VAL LEU THR SER LEU PRO SEQRES 4D2 365 GLY ASP SER VAL THR LEU THR CYS PRO GLY VAL GLU PRO SEQRES 5D2 365 GLU ASP ASN ALA THR VAL HIS TRP VAL LEU ARG LYS PRO SEQRES 6D2 365 ALA ALA GLY SER HIS PRO SER ARG TRP ALA GLY MET GLY SEQRES 7D2 365 ARG ARG LEU LEU LEU ARG SER VAL GLN LEU HIS ASP SER SEQRES 8D2 365 GLY ASN TYR SER CYS TYR ARG ALA GLY ARG PRO ALA GLY SEQRES 9D2 365 THR VAL HIS LEU LEU VAL ASP VAL PRO PRO GLU GLU PRO SEQRES 10D2 365 GLN LEU SER CYS PHE ARG LYS SER PRO LEU SER ASN VAL SEQRES 11D2 365 VAL CYS GLU TRP GLY PRO ARG SER THR PRO SER LEU THR SEQRES 12D2 365 THR LYS ALA VAL LEU LEU VAL ARG LYS PHE GLN ASN SER SEQRES 13D2 365 PRO ALA GLU ASP PHE GLN GLU PRO CYS GLN TYR SER GLN SEQRES 14D2 365 GLU SER GLN LYS PHE SER CYS GLN LEU ALA VAL PRO GLU SEQRES 15D2 365 GLY ASP SER SER PHE TYR ILE VAL SER MET CYS VAL ALA SEQRES 16D2 365 SER SER VAL GLY SER LYS PHE SER LYS THR GLN THR PHE SEQRES 17D2 365 GLN GLY CYS GLY ILE LEU GLN PRO ASP PRO PRO ALA ASN SEQRES 18D2 365 ILE THR VAL THR ALA VAL ALA ARG ASN PRO ARG TRP LEU SEQRES 19D2 365 SER VAL THR TRP GLN ASP PRO HIS SER TRP ASN SER SER SEQRES 20D2 365 PHE TYR ARG LEU ARG PHE GLU LEU ARG TYR ARG ALA GLU SEQRES 21D2 365 ARG SER LYS THR PHE THR THR TRP MET VAL LYS ASP LEU SEQRES 22D2 365 GLN HIS HIS CYS VAL ILE HIS ASP ALA TRP SER GLY LEU SEQRES 23D2 365 ARG HIS VAL VAL GLN LEU ARG ALA GLN GLU GLU PHE GLY SEQRES 24D2 365 GLN GLY GLU TRP SER GLU TRP SER PRO GLU ALA MET GLY SEQRES 25D2 365 THR PRO TRP THR GLU SER ARG SER PRO PRO ALA GLU ASN SEQRES 26D2 365 GLU VAL SER THR PRO MET GLN ALA LEU THR THR ASN LYS SEQRES 27D2 365 ASP ASP ASP ASN ILE LEU PHE ARG ASP SER ALA ASN ALA SEQRES 28D2 365 THR SER LEU PRO GLY SER ARG ARG ARG GLY SER CYS GLY SEQRES 29D2 365 LEU SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER VAL 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 SER SER TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR GLY ALA SER SEQRES 5 L 214 SER LEU GLU SER GLY VAL PRO SER 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 GLN PRO GLU ASP PHE ALA SER TYR TYR CYS GLN GLN ALA SEQRES 8 L 214 ASN SER PHE PRO TYR THR PHE GLY GLN 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 SEQRES 1 H 223 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 223 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER ARG SEQRES 3 H 223 PHE THR PHE ASP ASP TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 H 223 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY ILE SER SEQRES 5 H 223 TRP ASN SER GLY ARG ILE GLY TYR ALA ASP SER VAL LYS SEQRES 6 H 223 GLY ARG PHE THR ILE SER ARG ASP ASN ALA GLU ASN SER SEQRES 7 H 223 LEU PHE LEU GLN MET ASN GLY LEU ARG ALA GLU ASP THR SEQRES 8 H 223 ALA LEU TYR TYR CYS ALA LYS GLY ARG ASP SER PHE ASP SEQRES 9 H 223 ILE TRP GLY GLN GLY THR MET VAL THR VAL SER SER ALA SEQRES 10 H 223 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 11 H 223 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 12 H 223 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 13 H 223 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 14 H 223 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 15 H 223 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 16 H 223 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 17 H 223 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP LYS SEQRES 18 H 223 THR HIS HET NAG I 401 14 HET NAG I 402 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE FORMUL 5 NAG 2(C8 H15 N O6) HELIX 1 AA1 GLY L 50 SER L 52 5 3 HELIX 2 AA2 GLN L 79 PHE L 83 5 5 HELIX 3 AA3 SER L 121 GLY L 128 1 8 HELIX 4 AA4 LYS L 183 HIS L 189 1 7 HELIX 5 AA5 ARG H 87 THR H 91 5 5 HELIX 6 AA6 PRO H 188 LEU H 192 5 5 HELIX 7 AA7 PRO H 205 ASN H 207 5 3 SHEET 1 AA1 3 THR I 223 THR I 225 0 SHEET 2 AA1 3 SER I 235 THR I 237 -1 O SER I 235 N THR I 225 SHEET 3 AA1 3 HIS I 276 VAL I 278 -1 O CYS I 277 N VAL I 236 SHEET 1 AA2 3 THR I 266 MET I 269 0 SHEET 2 AA2 3 LEU I 251 TYR I 257 -1 N LEU I 255 O TRP I 268 SHEET 3 AA2 3 ALA I 294 GLU I 296 -1 O GLN I 295 N ARG I 252 SHEET 1 AA3 2 VAL I 289 VAL I 290 0 SHEET 2 AA3 2 ALA I 310 MET I 311 -1 O ALA I 310 N VAL I 290 SHEET 1 AA4 4 MET L 4 GLN L 6 0 SHEET 2 AA4 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA4 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA4 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA5 2 SER L 10 ALA L 13 0 SHEET 2 AA5 2 LYS L 103 ILE L 106 1 O GLU L 105 N VAL L 11 SHEET 1 AA6 3 LYS L 45 LEU L 46 0 SHEET 2 AA6 3 LEU L 33 GLN L 38 -1 N GLN L 37 O LYS L 45 SHEET 3 AA6 3 SER L 85 GLN L 90 -1 O SER L 85 N GLN L 38 SHEET 1 AA7 2 ILE L 48 TYR L 49 0 SHEET 2 AA7 2 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AA8 4 SER L 114 PHE L 118 0 SHEET 2 AA8 4 THR L 129 PHE L 139 -1 O ASN L 137 N SER L 114 SHEET 3 AA8 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AA8 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AA9 4 LEU L 154 GLN L 155 0 SHEET 2 AA9 4 LYS L 145 VAL L 150 -1 N TRP L 148 O GLN L 155 SHEET 3 AA9 4 TYR L 192 THR L 197 -1 O ALA L 193 N LYS L 149 SHEET 4 AA9 4 VAL L 205 PHE L 209 -1 O VAL L 205 N VAL L 196 SHEET 1 AB1 2 GLN H 3 SER H 7 0 SHEET 2 AB1 2 SER H 21 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 1 AB2 6 LEU H 11 VAL H 12 0 SHEET 2 AB2 6 MET H 111 VAL H 114 1 O THR H 113 N VAL H 12 SHEET 3 AB2 6 ALA H 92 LYS H 98 -1 N ALA H 92 O VAL H 112 SHEET 4 AB2 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AB2 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AB2 6 ILE H 58 TYR H 60 -1 O GLY H 59 N GLY H 50 SHEET 1 AB3 2 THR H 69 ASP H 73 0 SHEET 2 AB3 2 SER H 78 GLN H 82 -1 O PHE H 80 N SER H 71 SHEET 1 AB4 4 SER H 123 LEU H 127 0 SHEET 2 AB4 4 ALA H 139 TYR H 148 -1 O LEU H 144 N PHE H 125 SHEET 3 AB4 4 TYR H 179 VAL H 187 -1 O TYR H 179 N TYR H 148 SHEET 4 AB4 4 VAL H 166 THR H 168 -1 N HIS H 167 O VAL H 184 SHEET 1 AB5 4 SER H 123 LEU H 127 0 SHEET 2 AB5 4 ALA H 139 TYR H 148 -1 O LEU H 144 N PHE H 125 SHEET 3 AB5 4 TYR H 179 VAL H 187 -1 O TYR H 179 N TYR H 148 SHEET 4 AB5 4 VAL H 172 LEU H 173 -1 N VAL H 172 O SER H 180 SHEET 1 AB6 3 VAL H 153 TRP H 157 0 SHEET 2 AB6 3 TYR H 197 HIS H 203 -1 O ASN H 200 N SER H 156 SHEET 3 AB6 3 THR H 208 VAL H 214 -1 O LYS H 212 N CYS H 199 SSBOND 1 CYSD2 121 CYSD2 132 1555 1555 2.03 SSBOND 2 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 3 CYS L 134 CYS L 194 1555 1555 2.03 SSBOND 4 CYS H 22 CYS H 96 1555 1555 2.02 SSBOND 5 CYS H 143 CYS H 199 1555 1555 2.03 LINK ND2 ASN I 221 C1 NAG I 401 1555 1555 1.45 LINK ND2 ASN I 245 C1 NAG I 402 1555 1555 1.47 CISPEP 1 TYR L 140 PRO L 141 0 4.23 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