HEADER IMMUNE SYSTEM 28-JAN-24 8Y31 TITLE THE CRYSTAL STRUCTURE OF THE QX006N-FAB/IFNAR1-SD123 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: QX006N-FAB-LC; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: QX006N-FAB-HC; COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: INTERFERON ALPHA/BETA RECEPTOR 1; COMPND 11 CHAIN: E, F; COMPND 12 SYNONYM: IFN-R-1,IFN-ALPHA/BETA RECEPTOR 1,CYTOKINE RECEPTOR CLASS-II COMPND 13 MEMBER 1,CYTOKINE RECEPTOR FAMILY 2 MEMBER 1,CRF2-1,TYPE I INTERFERON COMPND 14 RECEPTOR 1; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_COMMON: HUMAN; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 GENE: IFNAR1, IFNAR; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS IFNAR1, QX006N, THE QX006N-FAB-IFNAR1-SD123 COMPLEX, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR W.LI,W.FENG REVDAT 1 04-DEC-24 8Y31 0 JRNL AUTH X.CHEN,H.KE,W.LI,L.YIN,W.CHEN,T.CHEN,Y.WU,J.QIU,W.FENG JRNL TITL STRUCTURAL BASIS FOR THE RECOGNITION OF IFNAR1 BY THE JRNL TITL 2 HUMANIZED THERAPEUTIC MONOCLONAL ANTIBODY QX006N FOR THE JRNL TITL 3 TREATMENT OF SYSTEMIC LUPUS ERYTHEMATOSUS. JRNL REF INT.J.BIOL.MACROMOL. V. 268 31721 2024 JRNL REFN ISSN 0141-8130 JRNL PMID 38649079 JRNL DOI 10.1016/J.IJBIOMAC.2024.131721 REMARK 2 REMARK 2 RESOLUTION. 2.68 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.18.2_3874: ???) 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) : 2.68 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.89 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 3 NUMBER OF REFLECTIONS : 35675 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.197 REMARK 3 R VALUE (WORKING SET) : 0.194 REMARK 3 FREE R VALUE : 0.239 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 1747 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 46.8900 - 6.1400 0.99 2909 122 0.1732 0.1738 REMARK 3 2 6.1400 - 4.8800 0.99 2843 168 0.1755 0.2002 REMARK 3 3 4.8800 - 4.2600 0.99 2860 130 0.1560 0.2239 REMARK 3 4 4.2600 - 3.8700 0.98 2824 150 0.1824 0.2192 REMARK 3 5 3.8700 - 3.5900 0.99 2827 131 0.2013 0.2599 REMARK 3 6 3.5900 - 3.3800 0.98 2779 151 0.2167 0.2647 REMARK 3 7 3.3800 - 3.2100 0.99 2856 113 0.2125 0.2614 REMARK 3 8 3.2100 - 3.0700 0.99 2813 151 0.2142 0.2956 REMARK 3 9 3.0700 - 2.9500 0.99 2812 169 0.2290 0.2613 REMARK 3 10 2.9500 - 2.8500 0.99 2822 153 0.2384 0.3102 REMARK 3 11 2.8500 - 2.7600 0.99 2799 160 0.2446 0.2806 REMARK 3 12 2.7600 - 2.6800 0.98 2784 149 0.2816 0.3764 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 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) : 0.350 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.090 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 : 0.004 8452 REMARK 3 ANGLE : 0.775 11496 REMARK 3 CHIRALITY : 0.049 1288 REMARK 3 PLANARITY : 0.005 1470 REMARK 3 DIHEDRAL : 20.209 3022 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 8Y31 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JAN-24. REMARK 100 THE DEPOSITION ID IS D_1300044727. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-DEC-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL02U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC REMARK 200 DATA SCALING SOFTWARE : AUTOPROC REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35675 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.680 REMARK 200 RESOLUTION RANGE LOW (A) : 68.060 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6 REMARK 200 DATA REDUNDANCY : 5.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.68 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.83 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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 (%): 36.41 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 8%(W/V) PEG3350 50 MM NA-CITRATE PH REMARK 280 5.5, 100 MM (NH4)2CITRATE, 250 MM NACL, 5 MM REMARK 280 HEXADECYLTRIMETHYLAMMONIUM BROMIDE, EVAPORATION, REMARK 280 RECRYSTALLIZATION, TEMPERATURE 289K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 60.51550 REMARK 290 SMTRY3 2 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 CYS A 216 REMARK 465 CYS B 222 REMARK 465 GLY B 223 REMARK 465 GLY B 224 REMARK 465 HIS B 225 REMARK 465 HIS B 226 REMARK 465 HIS B 227 REMARK 465 HIS B 228 REMARK 465 HIS B 229 REMARK 465 HIS B 230 REMARK 465 CYS C 216 REMARK 465 CYS D 222 REMARK 465 GLY D 223 REMARK 465 GLY D 224 REMARK 465 HIS D 225 REMARK 465 HIS D 226 REMARK 465 HIS D 227 REMARK 465 HIS D 228 REMARK 465 HIS D 229 REMARK 465 HIS D 230 REMARK 465 MET E 1 REMARK 465 MET E 2 REMARK 465 VAL E 3 REMARK 465 VAL E 4 REMARK 465 LEU E 5 REMARK 465 LEU E 6 REMARK 465 GLY E 7 REMARK 465 ALA E 8 REMARK 465 THR E 9 REMARK 465 THR E 10 REMARK 465 LEU E 11 REMARK 465 VAL E 12 REMARK 465 LEU E 13 REMARK 465 VAL E 14 REMARK 465 ALA E 15 REMARK 465 VAL E 16 REMARK 465 ALA E 17 REMARK 465 PRO E 18 REMARK 465 TRP E 19 REMARK 465 VAL E 20 REMARK 465 LEU E 21 REMARK 465 SER E 22 REMARK 465 ALA E 23 REMARK 465 ALA E 24 REMARK 465 ALA E 25 REMARK 465 GLY E 26 REMARK 465 GLY E 27 REMARK 465 LYS E 28 REMARK 465 ASN E 29 REMARK 465 LEU E 30 REMARK 465 LYS E 31 REMARK 465 SER E 32 REMARK 465 PRO E 33 REMARK 465 GLN E 34 REMARK 465 LYS E 35 REMARK 465 VAL E 36 REMARK 465 GLU E 37 REMARK 465 VAL E 38 REMARK 465 ASP E 39 REMARK 465 ILE E 40 REMARK 465 ILE E 41 REMARK 465 ASP E 42 REMARK 465 ASP E 43 REMARK 465 ASN E 44 REMARK 465 PHE E 45 REMARK 465 ILE E 46 REMARK 465 LEU E 47 REMARK 465 ARG E 48 REMARK 465 TRP E 49 REMARK 465 ASN E 50 REMARK 465 ARG E 51 REMARK 465 SER E 52 REMARK 465 ASP E 53 REMARK 465 GLU E 54 REMARK 465 SER E 55 REMARK 465 VAL E 56 REMARK 465 GLY E 57 REMARK 465 ASN E 58 REMARK 465 VAL E 59 REMARK 465 THR E 60 REMARK 465 PHE E 61 REMARK 465 SER E 62 REMARK 465 PHE E 63 REMARK 465 ASP E 64 REMARK 465 TYR E 65 REMARK 465 GLN E 66 REMARK 465 LYS E 67 REMARK 465 THR E 68 REMARK 465 GLY E 69 REMARK 465 MET E 70 REMARK 465 ASP E 71 REMARK 465 ASN E 72 REMARK 465 TRP E 73 REMARK 465 ILE E 74 REMARK 465 LYS E 75 REMARK 465 LEU E 76 REMARK 465 SER E 77 REMARK 465 GLY E 78 REMARK 465 CYS E 79 REMARK 465 GLN E 80 REMARK 465 ASN E 81 REMARK 465 ILE E 82 REMARK 465 THR E 83 REMARK 465 SER E 84 REMARK 465 THR E 85 REMARK 465 LYS E 86 REMARK 465 CYS E 87 REMARK 465 ASN E 88 REMARK 465 PHE E 89 REMARK 465 SER E 90 REMARK 465 SER E 91 REMARK 465 LEU E 92 REMARK 465 LYS E 93 REMARK 465 LEU E 94 REMARK 465 ASN E 95 REMARK 465 VAL E 96 REMARK 465 TYR E 97 REMARK 465 GLU E 98 REMARK 465 GLU E 99 REMARK 465 ILE E 100 REMARK 465 LYS E 101 REMARK 465 LEU E 102 REMARK 465 ARG E 103 REMARK 465 ILE E 104 REMARK 465 ARG E 105 REMARK 465 ALA E 106 REMARK 465 GLU E 107 REMARK 465 LYS E 108 REMARK 465 GLU E 109 REMARK 465 ASN E 110 REMARK 465 THR E 111 REMARK 465 SER E 112 REMARK 465 SER E 113 REMARK 465 TRP E 114 REMARK 465 TYR E 115 REMARK 465 GLU E 116 REMARK 465 VAL E 117 REMARK 465 ASP E 118 REMARK 465 SER E 119 REMARK 465 PHE E 120 REMARK 465 THR E 121 REMARK 465 PRO E 122 REMARK 465 PHE E 123 REMARK 465 ARG E 124 REMARK 465 LYS E 125 REMARK 465 ALA E 126 REMARK 465 GLN E 127 REMARK 465 ILE E 128 REMARK 465 GLY E 129 REMARK 465 PRO E 130 REMARK 465 PRO E 131 REMARK 465 GLU E 132 REMARK 465 VAL E 133 REMARK 465 HIS E 134 REMARK 465 LEU E 135 REMARK 465 GLU E 136 REMARK 465 ALA E 137 REMARK 465 GLU E 138 REMARK 465 ASP E 139 REMARK 465 LYS E 140 REMARK 465 ALA E 141 REMARK 465 ILE E 142 REMARK 465 VAL E 143 REMARK 465 ILE E 144 REMARK 465 HIS E 145 REMARK 465 ILE E 146 REMARK 465 SER E 147 REMARK 465 PRO E 148 REMARK 465 GLY E 149 REMARK 465 THR E 150 REMARK 465 LYS E 151 REMARK 465 ASP E 152 REMARK 465 SER E 153 REMARK 465 VAL E 154 REMARK 465 MET E 155 REMARK 465 TRP E 156 REMARK 465 ALA E 157 REMARK 465 LEU E 158 REMARK 465 ASP E 159 REMARK 465 GLY E 160 REMARK 465 LEU E 161 REMARK 465 SER E 162 REMARK 465 PHE E 163 REMARK 465 THR E 164 REMARK 465 TYR E 165 REMARK 465 SER E 166 REMARK 465 LEU E 167 REMARK 465 VAL E 168 REMARK 465 ILE E 169 REMARK 465 TRP E 170 REMARK 465 LYS E 171 REMARK 465 ASN E 172 REMARK 465 SER E 173 REMARK 465 SER E 174 REMARK 465 GLY E 175 REMARK 465 VAL E 176 REMARK 465 GLU E 177 REMARK 465 GLU E 178 REMARK 465 ARG E 179 REMARK 465 ILE E 180 REMARK 465 GLU E 181 REMARK 465 ASN E 182 REMARK 465 ILE E 183 REMARK 465 TYR E 184 REMARK 465 SER E 185 REMARK 465 ARG E 186 REMARK 465 HIS E 187 REMARK 465 LYS E 188 REMARK 465 ILE E 189 REMARK 465 TYR E 190 REMARK 465 LYS E 191 REMARK 465 LEU E 192 REMARK 465 SER E 193 REMARK 465 PRO E 194 REMARK 465 GLU E 195 REMARK 465 THR E 196 REMARK 465 THR E 197 REMARK 465 TYR E 198 REMARK 465 CYS E 199 REMARK 465 LEU E 200 REMARK 465 LYS E 201 REMARK 465 VAL E 202 REMARK 465 LYS E 203 REMARK 465 ALA E 204 REMARK 465 ALA E 205 REMARK 465 LEU E 206 REMARK 465 LEU E 207 REMARK 465 THR E 208 REMARK 465 SER E 209 REMARK 465 TRP E 210 REMARK 465 LYS E 211 REMARK 465 ILE E 212 REMARK 465 GLY E 213 REMARK 465 VAL E 214 REMARK 465 TYR E 215 REMARK 465 SER E 216 REMARK 465 PRO E 217 REMARK 465 VAL E 218 REMARK 465 HIS E 219 REMARK 465 CYS E 220 REMARK 465 ILE E 221 REMARK 465 LYS E 222 REMARK 465 THR E 223 REMARK 465 THR E 224 REMARK 465 VAL E 225 REMARK 465 GLU E 226 REMARK 465 ASN E 227 REMARK 465 ALA E 330 REMARK 465 PHE E 331 REMARK 465 LEU E 332 REMARK 465 LEU E 333 REMARK 465 GLU E 334 REMARK 465 VAL E 335 REMARK 465 LEU E 336 REMARK 465 PHE E 337 REMARK 465 GLN E 338 REMARK 465 GLY E 339 REMARK 465 PRO E 340 REMARK 465 HIS E 341 REMARK 465 HIS E 342 REMARK 465 HIS E 343 REMARK 465 HIS E 344 REMARK 465 HIS E 345 REMARK 465 HIS E 346 REMARK 465 MET F 1 REMARK 465 MET F 2 REMARK 465 VAL F 3 REMARK 465 VAL F 4 REMARK 465 LEU F 5 REMARK 465 LEU F 6 REMARK 465 GLY F 7 REMARK 465 ALA F 8 REMARK 465 THR F 9 REMARK 465 THR F 10 REMARK 465 LEU F 11 REMARK 465 VAL F 12 REMARK 465 LEU F 13 REMARK 465 VAL F 14 REMARK 465 ALA F 15 REMARK 465 VAL F 16 REMARK 465 ALA F 17 REMARK 465 PRO F 18 REMARK 465 TRP F 19 REMARK 465 VAL F 20 REMARK 465 LEU F 21 REMARK 465 SER F 22 REMARK 465 ALA F 23 REMARK 465 ALA F 24 REMARK 465 ALA F 25 REMARK 465 GLY F 26 REMARK 465 GLY F 27 REMARK 465 LYS F 28 REMARK 465 ASN F 29 REMARK 465 LEU F 30 REMARK 465 LYS F 31 REMARK 465 SER F 32 REMARK 465 PRO F 33 REMARK 465 GLN F 34 REMARK 465 LYS F 35 REMARK 465 VAL F 36 REMARK 465 GLU F 37 REMARK 465 VAL F 38 REMARK 465 ASP F 39 REMARK 465 ILE F 40 REMARK 465 ILE F 41 REMARK 465 ASP F 42 REMARK 465 ASP F 43 REMARK 465 ASN F 44 REMARK 465 PHE F 45 REMARK 465 ILE F 46 REMARK 465 LEU F 47 REMARK 465 ARG F 48 REMARK 465 TRP F 49 REMARK 465 ASN F 50 REMARK 465 ARG F 51 REMARK 465 SER F 52 REMARK 465 ASP F 53 REMARK 465 GLU F 54 REMARK 465 SER F 55 REMARK 465 VAL F 56 REMARK 465 GLY F 57 REMARK 465 ASN F 58 REMARK 465 VAL F 59 REMARK 465 THR F 60 REMARK 465 PHE F 61 REMARK 465 SER F 62 REMARK 465 PHE F 63 REMARK 465 ASP F 64 REMARK 465 TYR F 65 REMARK 465 GLN F 66 REMARK 465 LYS F 67 REMARK 465 THR F 68 REMARK 465 GLY F 69 REMARK 465 MET F 70 REMARK 465 ASP F 71 REMARK 465 ASN F 72 REMARK 465 TRP F 73 REMARK 465 ILE F 74 REMARK 465 LYS F 75 REMARK 465 LEU F 76 REMARK 465 SER F 77 REMARK 465 GLY F 78 REMARK 465 CYS F 79 REMARK 465 GLN F 80 REMARK 465 ASN F 81 REMARK 465 ILE F 82 REMARK 465 THR F 83 REMARK 465 SER F 84 REMARK 465 THR F 85 REMARK 465 LYS F 86 REMARK 465 CYS F 87 REMARK 465 ASN F 88 REMARK 465 PHE F 89 REMARK 465 SER F 90 REMARK 465 SER F 91 REMARK 465 LEU F 92 REMARK 465 LYS F 93 REMARK 465 LEU F 94 REMARK 465 ASN F 95 REMARK 465 VAL F 96 REMARK 465 TYR F 97 REMARK 465 GLU F 98 REMARK 465 GLU F 99 REMARK 465 ILE F 100 REMARK 465 LYS F 101 REMARK 465 LEU F 102 REMARK 465 ARG F 103 REMARK 465 ILE F 104 REMARK 465 ARG F 105 REMARK 465 ALA F 106 REMARK 465 GLU F 107 REMARK 465 LYS F 108 REMARK 465 GLU F 109 REMARK 465 ASN F 110 REMARK 465 THR F 111 REMARK 465 SER F 112 REMARK 465 SER F 113 REMARK 465 TRP F 114 REMARK 465 TYR F 115 REMARK 465 GLU F 116 REMARK 465 VAL F 117 REMARK 465 ASP F 118 REMARK 465 SER F 119 REMARK 465 PHE F 120 REMARK 465 THR F 121 REMARK 465 PRO F 122 REMARK 465 PHE F 123 REMARK 465 ARG F 124 REMARK 465 LYS F 125 REMARK 465 ALA F 126 REMARK 465 GLN F 127 REMARK 465 ILE F 128 REMARK 465 GLY F 129 REMARK 465 PRO F 130 REMARK 465 PRO F 131 REMARK 465 GLU F 132 REMARK 465 VAL F 133 REMARK 465 HIS F 134 REMARK 465 LEU F 135 REMARK 465 GLU F 136 REMARK 465 ALA F 137 REMARK 465 GLU F 138 REMARK 465 ASP F 139 REMARK 465 LYS F 140 REMARK 465 ALA F 141 REMARK 465 ILE F 142 REMARK 465 VAL F 143 REMARK 465 ILE F 144 REMARK 465 HIS F 145 REMARK 465 ILE F 146 REMARK 465 SER F 147 REMARK 465 PRO F 148 REMARK 465 GLY F 149 REMARK 465 THR F 150 REMARK 465 LYS F 151 REMARK 465 ASP F 152 REMARK 465 SER F 153 REMARK 465 VAL F 154 REMARK 465 MET F 155 REMARK 465 TRP F 156 REMARK 465 ALA F 157 REMARK 465 LEU F 158 REMARK 465 ASP F 159 REMARK 465 GLY F 160 REMARK 465 LEU F 161 REMARK 465 SER F 162 REMARK 465 PHE F 163 REMARK 465 THR F 164 REMARK 465 TYR F 165 REMARK 465 SER F 166 REMARK 465 LEU F 167 REMARK 465 VAL F 168 REMARK 465 ILE F 169 REMARK 465 TRP F 170 REMARK 465 LYS F 171 REMARK 465 ASN F 172 REMARK 465 SER F 173 REMARK 465 SER F 174 REMARK 465 GLY F 175 REMARK 465 VAL F 176 REMARK 465 GLU F 177 REMARK 465 GLU F 178 REMARK 465 ARG F 179 REMARK 465 ILE F 180 REMARK 465 GLU F 181 REMARK 465 ASN F 182 REMARK 465 ILE F 183 REMARK 465 TYR F 184 REMARK 465 SER F 185 REMARK 465 ARG F 186 REMARK 465 HIS F 187 REMARK 465 LYS F 188 REMARK 465 ILE F 189 REMARK 465 TYR F 190 REMARK 465 LYS F 191 REMARK 465 LEU F 192 REMARK 465 SER F 193 REMARK 465 PRO F 194 REMARK 465 GLU F 195 REMARK 465 THR F 196 REMARK 465 THR F 197 REMARK 465 TYR F 198 REMARK 465 CYS F 199 REMARK 465 LEU F 200 REMARK 465 LYS F 201 REMARK 465 VAL F 202 REMARK 465 LYS F 203 REMARK 465 ALA F 204 REMARK 465 ALA F 205 REMARK 465 LEU F 206 REMARK 465 LEU F 207 REMARK 465 THR F 208 REMARK 465 SER F 209 REMARK 465 TRP F 210 REMARK 465 LYS F 211 REMARK 465 ILE F 212 REMARK 465 GLY F 213 REMARK 465 VAL F 214 REMARK 465 TYR F 215 REMARK 465 SER F 216 REMARK 465 PRO F 217 REMARK 465 VAL F 218 REMARK 465 HIS F 219 REMARK 465 CYS F 220 REMARK 465 ILE F 221 REMARK 465 LYS F 222 REMARK 465 THR F 223 REMARK 465 THR F 224 REMARK 465 VAL F 225 REMARK 465 GLU F 226 REMARK 465 ASN F 227 REMARK 465 ALA F 330 REMARK 465 PHE F 331 REMARK 465 LEU F 332 REMARK 465 LEU F 333 REMARK 465 GLU F 334 REMARK 465 VAL F 335 REMARK 465 LEU F 336 REMARK 465 PHE F 337 REMARK 465 GLN F 338 REMARK 465 GLY F 339 REMARK 465 PRO F 340 REMARK 465 HIS F 341 REMARK 465 HIS F 342 REMARK 465 HIS F 343 REMARK 465 HIS F 344 REMARK 465 HIS F 345 REMARK 465 HIS F 346 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 A 30 -136.32 57.43 REMARK 500 ALA A 51 -39.74 75.45 REMARK 500 VAL B 102 -56.22 -126.64 REMARK 500 SER B 134 -93.36 -130.80 REMARK 500 SER C 30 -135.54 57.47 REMARK 500 ALA C 51 -52.44 77.45 REMARK 500 VAL D 102 -55.45 -128.05 REMARK 500 SER D 134 -83.97 -132.79 REMARK 500 ASN E 241 -127.34 55.42 REMARK 500 LEU E 274 49.31 -86.88 REMARK 500 ASN E 313 -58.25 -123.53 REMARK 500 ILE E 328 13.34 80.17 REMARK 500 ASN F 241 -128.07 55.39 REMARK 500 ASN F 272 32.74 38.61 REMARK 500 LEU F 274 48.46 -85.33 REMARK 500 REMARK 500 REMARK: NULL DBREF 8Y31 A 1 216 PDB 8Y31 8Y31 1 216 DBREF 8Y31 B 1 230 PDB 8Y31 8Y31 1 230 DBREF 8Y31 C 1 216 PDB 8Y31 8Y31 1 216 DBREF 8Y31 D 1 230 PDB 8Y31 8Y31 1 230 DBREF 8Y31 E 1 333 UNP P17181 INAR1_HUMAN 1 333 DBREF 8Y31 F 1 333 UNP P17181 INAR1_HUMAN 1 333 SEQADV 8Y31 GLU E 334 UNP P17181 EXPRESSION TAG SEQADV 8Y31 VAL E 335 UNP P17181 EXPRESSION TAG SEQADV 8Y31 LEU E 336 UNP P17181 EXPRESSION TAG SEQADV 8Y31 PHE E 337 UNP P17181 EXPRESSION TAG SEQADV 8Y31 GLN E 338 UNP P17181 EXPRESSION TAG SEQADV 8Y31 GLY E 339 UNP P17181 EXPRESSION TAG SEQADV 8Y31 PRO E 340 UNP P17181 EXPRESSION TAG SEQADV 8Y31 HIS E 341 UNP P17181 EXPRESSION TAG SEQADV 8Y31 HIS E 342 UNP P17181 EXPRESSION TAG SEQADV 8Y31 HIS E 343 UNP P17181 EXPRESSION TAG SEQADV 8Y31 HIS E 344 UNP P17181 EXPRESSION TAG SEQADV 8Y31 HIS E 345 UNP P17181 EXPRESSION TAG SEQADV 8Y31 HIS E 346 UNP P17181 EXPRESSION TAG SEQADV 8Y31 GLU F 334 UNP P17181 EXPRESSION TAG SEQADV 8Y31 VAL F 335 UNP P17181 EXPRESSION TAG SEQADV 8Y31 LEU F 336 UNP P17181 EXPRESSION TAG SEQADV 8Y31 PHE F 337 UNP P17181 EXPRESSION TAG SEQADV 8Y31 GLN F 338 UNP P17181 EXPRESSION TAG SEQADV 8Y31 GLY F 339 UNP P17181 EXPRESSION TAG SEQADV 8Y31 PRO F 340 UNP P17181 EXPRESSION TAG SEQADV 8Y31 HIS F 341 UNP P17181 EXPRESSION TAG SEQADV 8Y31 HIS F 342 UNP P17181 EXPRESSION TAG SEQADV 8Y31 HIS F 343 UNP P17181 EXPRESSION TAG SEQADV 8Y31 HIS F 344 UNP P17181 EXPRESSION TAG SEQADV 8Y31 HIS F 345 UNP P17181 EXPRESSION TAG SEQADV 8Y31 HIS F 346 UNP P17181 EXPRESSION TAG SEQRES 1 A 216 ALA ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 A 216 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 A 216 GLN SER ILE SER ASN GLN LEU SER TRP TYR GLN GLN LYS SEQRES 4 A 216 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP ALA SER SEQRES 5 A 216 SER LEU ALA SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 A 216 ARG SER GLY THR LYS PHE THR LEU THR ILE SER SER LEU SEQRES 7 A 216 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS LEU GLY ILE SEQRES 8 A 216 TYR GLY ASP GLY ALA ASP ASP GLY ILE ALA PHE GLY GLY SEQRES 9 A 216 GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SEQRES 10 A 216 SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SEQRES 11 A 216 SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE SEQRES 12 A 216 TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN SEQRES 13 A 216 ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU SEQRES 14 A 216 GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER THR SEQRES 15 A 216 LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL SEQRES 16 A 216 TYR ALA CYS GLU VAL THR GLN GLY THR THR SER VAL THR SEQRES 17 A 216 LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 B 230 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 230 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 230 PHE SER LEU SER SER TYR TYR MET THR TRP VAL ARG GLN SEQRES 4 B 230 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER VAL ILE ASN SEQRES 5 B 230 VAL TYR GLY GLY THR TYR TYR ALA SER TRP ALA LYS GLY SEQRES 6 B 230 ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR LEU SEQRES 7 B 230 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 B 230 VAL TYR TYR CYS ALA ARG GLU ASP VAL ALA VAL TYR MET SEQRES 9 B 230 ALA ILE ASP LEU TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10 B 230 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 B 230 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 B 230 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 B 230 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 B 230 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 B 230 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 B 230 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 B 230 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 18 B 230 CYS GLY GLY HIS HIS HIS HIS HIS HIS SEQRES 1 C 216 ALA ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 C 216 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 C 216 GLN SER ILE SER ASN GLN LEU SER TRP TYR GLN GLN LYS SEQRES 4 C 216 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP ALA SER SEQRES 5 C 216 SER LEU ALA SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 C 216 ARG SER GLY THR LYS PHE THR LEU THR ILE SER SER LEU SEQRES 7 C 216 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS LEU GLY ILE SEQRES 8 C 216 TYR GLY ASP GLY ALA ASP ASP GLY ILE ALA PHE GLY GLY SEQRES 9 C 216 GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SEQRES 10 C 216 SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SEQRES 11 C 216 SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE SEQRES 12 C 216 TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN SEQRES 13 C 216 ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU SEQRES 14 C 216 GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER THR SEQRES 15 C 216 LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL SEQRES 16 C 216 TYR ALA CYS GLU VAL THR GLN GLY THR THR SER VAL THR SEQRES 17 C 216 LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 D 230 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 230 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 D 230 PHE SER LEU SER SER TYR TYR MET THR TRP VAL ARG GLN SEQRES 4 D 230 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER VAL ILE ASN SEQRES 5 D 230 VAL TYR GLY GLY THR TYR TYR ALA SER TRP ALA LYS GLY SEQRES 6 D 230 ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR LEU SEQRES 7 D 230 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 D 230 VAL TYR TYR CYS ALA ARG GLU ASP VAL ALA VAL TYR MET SEQRES 9 D 230 ALA ILE ASP LEU TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10 D 230 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 D 230 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 D 230 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 D 230 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 D 230 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 D 230 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 D 230 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 D 230 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 18 D 230 CYS GLY GLY HIS HIS HIS HIS HIS HIS SEQRES 1 E 346 MET MET VAL VAL LEU LEU GLY ALA THR THR LEU VAL LEU SEQRES 2 E 346 VAL ALA VAL ALA PRO TRP VAL LEU SER ALA ALA ALA GLY SEQRES 3 E 346 GLY LYS ASN LEU LYS SER PRO GLN LYS VAL GLU VAL ASP SEQRES 4 E 346 ILE ILE ASP ASP ASN PHE ILE LEU ARG TRP ASN ARG SER SEQRES 5 E 346 ASP GLU SER VAL GLY ASN VAL THR PHE SER PHE ASP TYR SEQRES 6 E 346 GLN LYS THR GLY MET ASP ASN TRP ILE LYS LEU SER GLY SEQRES 7 E 346 CYS GLN ASN ILE THR SER THR LYS CYS ASN PHE SER SER SEQRES 8 E 346 LEU LYS LEU ASN VAL TYR GLU GLU ILE LYS LEU ARG ILE SEQRES 9 E 346 ARG ALA GLU LYS GLU ASN THR SER SER TRP TYR GLU VAL SEQRES 10 E 346 ASP SER PHE THR PRO PHE ARG LYS ALA GLN ILE GLY PRO SEQRES 11 E 346 PRO GLU VAL HIS LEU GLU ALA GLU ASP LYS ALA ILE VAL SEQRES 12 E 346 ILE HIS ILE SER PRO GLY THR LYS ASP SER VAL MET TRP SEQRES 13 E 346 ALA LEU ASP GLY LEU SER PHE THR TYR SER LEU VAL ILE SEQRES 14 E 346 TRP LYS ASN SER SER GLY VAL GLU GLU ARG ILE GLU ASN SEQRES 15 E 346 ILE TYR SER ARG HIS LYS ILE TYR LYS LEU SER PRO GLU SEQRES 16 E 346 THR THR TYR CYS LEU LYS VAL LYS ALA ALA LEU LEU THR SEQRES 17 E 346 SER TRP LYS ILE GLY VAL TYR SER PRO VAL HIS CYS ILE SEQRES 18 E 346 LYS THR THR VAL GLU ASN GLU LEU PRO PRO PRO GLU ASN SEQRES 19 E 346 ILE GLU VAL SER VAL GLN ASN GLN ASN TYR VAL LEU LYS SEQRES 20 E 346 TRP ASP TYR THR TYR ALA ASN MET THR PHE GLN VAL GLN SEQRES 21 E 346 TRP LEU HIS ALA PHE LEU LYS ARG ASN PRO GLY ASN HIS SEQRES 22 E 346 LEU TYR LYS TRP LYS GLN ILE PRO ASP CYS GLU ASN VAL SEQRES 23 E 346 LYS THR THR GLN CYS VAL PHE PRO GLN ASN VAL PHE GLN SEQRES 24 E 346 LYS GLY ILE TYR LEU LEU ARG VAL GLN ALA SER ASP GLY SEQRES 25 E 346 ASN ASN THR SER PHE TRP SER GLU GLU ILE LYS PHE ASP SEQRES 26 E 346 THR GLU ILE GLN ALA PHE LEU LEU GLU VAL LEU PHE GLN SEQRES 27 E 346 GLY PRO HIS HIS HIS HIS HIS HIS SEQRES 1 F 346 MET MET VAL VAL LEU LEU GLY ALA THR THR LEU VAL LEU SEQRES 2 F 346 VAL ALA VAL ALA PRO TRP VAL LEU SER ALA ALA ALA GLY SEQRES 3 F 346 GLY LYS ASN LEU LYS SER PRO GLN LYS VAL GLU VAL ASP SEQRES 4 F 346 ILE ILE ASP ASP ASN PHE ILE LEU ARG TRP ASN ARG SER SEQRES 5 F 346 ASP GLU SER VAL GLY ASN VAL THR PHE SER PHE ASP TYR SEQRES 6 F 346 GLN LYS THR GLY MET ASP ASN TRP ILE LYS LEU SER GLY SEQRES 7 F 346 CYS GLN ASN ILE THR SER THR LYS CYS ASN PHE SER SER SEQRES 8 F 346 LEU LYS LEU ASN VAL TYR GLU GLU ILE LYS LEU ARG ILE SEQRES 9 F 346 ARG ALA GLU LYS GLU ASN THR SER SER TRP TYR GLU VAL SEQRES 10 F 346 ASP SER PHE THR PRO PHE ARG LYS ALA GLN ILE GLY PRO SEQRES 11 F 346 PRO GLU VAL HIS LEU GLU ALA GLU ASP LYS ALA ILE VAL SEQRES 12 F 346 ILE HIS ILE SER PRO GLY THR LYS ASP SER VAL MET TRP SEQRES 13 F 346 ALA LEU ASP GLY LEU SER PHE THR TYR SER LEU VAL ILE SEQRES 14 F 346 TRP LYS ASN SER SER GLY VAL GLU GLU ARG ILE GLU ASN SEQRES 15 F 346 ILE TYR SER ARG HIS LYS ILE TYR LYS LEU SER PRO GLU SEQRES 16 F 346 THR THR TYR CYS LEU LYS VAL LYS ALA ALA LEU LEU THR SEQRES 17 F 346 SER TRP LYS ILE GLY VAL TYR SER PRO VAL HIS CYS ILE SEQRES 18 F 346 LYS THR THR VAL GLU ASN GLU LEU PRO PRO PRO GLU ASN SEQRES 19 F 346 ILE GLU VAL SER VAL GLN ASN GLN ASN TYR VAL LEU LYS SEQRES 20 F 346 TRP ASP TYR THR TYR ALA ASN MET THR PHE GLN VAL GLN SEQRES 21 F 346 TRP LEU HIS ALA PHE LEU LYS ARG ASN PRO GLY ASN HIS SEQRES 22 F 346 LEU TYR LYS TRP LYS GLN ILE PRO ASP CYS GLU ASN VAL SEQRES 23 F 346 LYS THR THR GLN CYS VAL PHE PRO GLN ASN VAL PHE GLN SEQRES 24 F 346 LYS GLY ILE TYR LEU LEU ARG VAL GLN ALA SER ASP GLY SEQRES 25 F 346 ASN ASN THR SER PHE TRP SER GLU GLU ILE LYS PHE ASP SEQRES 26 F 346 THR GLU ILE GLN ALA PHE LEU LEU GLU VAL LEU PHE GLN SEQRES 27 F 346 GLY PRO HIS HIS HIS HIS HIS HIS FORMUL 7 HOH *68(H2 O) HELIX 1 AA1 GLN A 79 PHE A 83 5 5 HELIX 2 AA2 SER A 125 GLY A 132 1 8 HELIX 3 AA3 LYS A 187 LYS A 192 1 6 HELIX 4 AA4 SER B 28 TYR B 32 5 5 HELIX 5 AA5 ALA B 60 GLY B 65 1 6 HELIX 6 AA6 ARG B 86 THR B 90 5 5 HELIX 7 AA7 SER B 162 ALA B 164 5 3 HELIX 8 AA8 SER B 193 LEU B 195 5 3 HELIX 9 AA9 LYS B 207 ASN B 210 5 4 HELIX 10 AB1 GLN C 79 PHE C 83 5 5 HELIX 11 AB2 SER C 125 GLY C 132 1 8 HELIX 12 AB3 LYS C 187 LYS C 192 1 6 HELIX 13 AB4 SER D 28 TYR D 32 5 5 HELIX 14 AB5 SER D 61 LYS D 64 5 4 HELIX 15 AB6 ARG D 86 THR D 90 5 5 HELIX 16 AB7 SER D 162 ALA D 164 5 3 HELIX 17 AB8 SER D 193 LEU D 195 5 3 HELIX 18 AB9 LYS D 207 ASN D 210 5 4 HELIX 19 AC1 PHE E 265 ARG E 268 5 4 HELIX 20 AC2 ASN E 296 PHE E 298 5 3 HELIX 21 AC3 PHE F 265 ARG F 268 5 4 HELIX 22 AC4 ASN F 296 PHE F 298 5 3 SHEET 1 AA1 4 MET A 4 SER A 7 0 SHEET 2 AA1 4 VAL A 19 ALA A 25 -1 O THR A 22 N SER A 7 SHEET 3 AA1 4 LYS A 70 ILE A 75 -1 O LEU A 73 N ILE A 21 SHEET 4 AA1 4 PHE A 62 SER A 67 -1 N SER A 63 O THR A 74 SHEET 1 AA2 6 SER A 10 SER A 14 0 SHEET 2 AA2 6 THR A 106 LYS A 111 1 O LYS A 111 N ALA A 13 SHEET 3 AA2 6 ALA A 84 ILE A 91 -1 N ALA A 84 O VAL A 108 SHEET 4 AA2 6 LEU A 33 GLN A 38 -1 N TYR A 36 O TYR A 87 SHEET 5 AA2 6 LYS A 45 TYR A 49 -1 O LEU A 47 N TRP A 35 SHEET 6 AA2 6 SER A 53 LEU A 54 -1 O SER A 53 N TYR A 49 SHEET 1 AA3 4 SER A 10 SER A 14 0 SHEET 2 AA3 4 THR A 106 LYS A 111 1 O LYS A 111 N ALA A 13 SHEET 3 AA3 4 ALA A 84 ILE A 91 -1 N ALA A 84 O VAL A 108 SHEET 4 AA3 4 ILE A 100 PHE A 102 -1 O ALA A 101 N GLY A 90 SHEET 1 AA4 4 SER A 118 PHE A 122 0 SHEET 2 AA4 4 THR A 133 PHE A 143 -1 O VAL A 137 N PHE A 122 SHEET 3 AA4 4 TYR A 177 SER A 186 -1 O LEU A 179 N LEU A 140 SHEET 4 AA4 4 SER A 163 VAL A 167 -1 N GLN A 164 O THR A 182 SHEET 1 AA5 4 ALA A 157 LEU A 158 0 SHEET 2 AA5 4 LYS A 149 VAL A 154 -1 N VAL A 154 O ALA A 157 SHEET 3 AA5 4 VAL A 195 GLN A 202 -1 O ALA A 197 N LYS A 153 SHEET 4 AA5 4 THR A 205 ASN A 212 -1 O VAL A 207 N VAL A 200 SHEET 1 AA6 4 GLN B 3 SER B 7 0 SHEET 2 AA6 4 LEU B 18 SER B 25 -1 O ALA B 23 N VAL B 5 SHEET 3 AA6 4 THR B 77 MET B 82 -1 O MET B 82 N LEU B 18 SHEET 4 AA6 4 PHE B 67 ASP B 72 -1 N SER B 70 O TYR B 79 SHEET 1 AA7 6 LEU B 11 VAL B 12 0 SHEET 2 AA7 6 THR B 113 VAL B 117 1 O THR B 116 N VAL B 12 SHEET 3 AA7 6 ALA B 91 GLU B 98 -1 N TYR B 93 O THR B 113 SHEET 4 AA7 6 TYR B 33 GLN B 39 -1 N VAL B 37 O TYR B 94 SHEET 5 AA7 6 LEU B 45 ILE B 51 -1 O GLU B 46 N ARG B 38 SHEET 6 AA7 6 THR B 57 TYR B 59 -1 O TYR B 58 N VAL B 50 SHEET 1 AA8 4 LEU B 11 VAL B 12 0 SHEET 2 AA8 4 THR B 113 VAL B 117 1 O THR B 116 N VAL B 12 SHEET 3 AA8 4 ALA B 91 GLU B 98 -1 N TYR B 93 O THR B 113 SHEET 4 AA8 4 ILE B 106 TRP B 109 -1 O LEU B 108 N ARG B 97 SHEET 1 AA9 4 SER B 126 LEU B 130 0 SHEET 2 AA9 4 THR B 141 TYR B 151 -1 O GLY B 145 N LEU B 130 SHEET 3 AA9 4 TYR B 182 PRO B 191 -1 O TYR B 182 N TYR B 151 SHEET 4 AA9 4 VAL B 169 THR B 171 -1 N HIS B 170 O VAL B 187 SHEET 1 AB1 4 SER B 126 LEU B 130 0 SHEET 2 AB1 4 THR B 141 TYR B 151 -1 O GLY B 145 N LEU B 130 SHEET 3 AB1 4 TYR B 182 PRO B 191 -1 O TYR B 182 N TYR B 151 SHEET 4 AB1 4 VAL B 175 LEU B 176 -1 N VAL B 175 O SER B 183 SHEET 1 AB2 3 THR B 157 TRP B 160 0 SHEET 2 AB2 3 TYR B 200 HIS B 206 -1 O ASN B 203 N SER B 159 SHEET 3 AB2 3 THR B 211 VAL B 217 -1 O THR B 211 N HIS B 206 SHEET 1 AB3 4 MET C 4 SER C 7 0 SHEET 2 AB3 4 VAL C 19 ALA C 25 -1 O THR C 22 N SER C 7 SHEET 3 AB3 4 LYS C 70 ILE C 75 -1 O PHE C 71 N CYS C 23 SHEET 4 AB3 4 PHE C 62 SER C 67 -1 N SER C 63 O THR C 74 SHEET 1 AB4 6 SER C 10 SER C 14 0 SHEET 2 AB4 6 THR C 106 LYS C 111 1 O LYS C 111 N ALA C 13 SHEET 3 AB4 6 ALA C 84 ILE C 91 -1 N ALA C 84 O VAL C 108 SHEET 4 AB4 6 LEU C 33 GLN C 38 -1 N TYR C 36 O TYR C 87 SHEET 5 AB4 6 LYS C 45 TYR C 49 -1 O LEU C 47 N TRP C 35 SHEET 6 AB4 6 SER C 53 LEU C 54 -1 O SER C 53 N TYR C 49 SHEET 1 AB5 4 SER C 10 SER C 14 0 SHEET 2 AB5 4 THR C 106 LYS C 111 1 O LYS C 111 N ALA C 13 SHEET 3 AB5 4 ALA C 84 ILE C 91 -1 N ALA C 84 O VAL C 108 SHEET 4 AB5 4 ILE C 100 PHE C 102 -1 O ALA C 101 N GLY C 90 SHEET 1 AB6 4 SER C 118 PHE C 122 0 SHEET 2 AB6 4 THR C 133 PHE C 143 -1 O VAL C 137 N PHE C 122 SHEET 3 AB6 4 TYR C 177 SER C 186 -1 O LEU C 179 N LEU C 140 SHEET 4 AB6 4 SER C 163 VAL C 167 -1 N SER C 166 O SER C 180 SHEET 1 AB7 4 ALA C 157 LEU C 158 0 SHEET 2 AB7 4 LYS C 149 VAL C 154 -1 N VAL C 154 O ALA C 157 SHEET 3 AB7 4 VAL C 195 GLN C 202 -1 O GLU C 199 N GLN C 151 SHEET 4 AB7 4 THR C 205 ASN C 212 -1 O VAL C 207 N VAL C 200 SHEET 1 AB8 4 GLN D 3 SER D 7 0 SHEET 2 AB8 4 LEU D 18 SER D 25 -1 O SER D 25 N GLN D 3 SHEET 3 AB8 4 THR D 77 MET D 82 -1 O MET D 82 N LEU D 18 SHEET 4 AB8 4 PHE D 67 ASP D 72 -1 N SER D 70 O TYR D 79 SHEET 1 AB9 6 LEU D 11 VAL D 12 0 SHEET 2 AB9 6 THR D 113 VAL D 117 1 O THR D 116 N VAL D 12 SHEET 3 AB9 6 ALA D 91 GLU D 98 -1 N TYR D 93 O THR D 113 SHEET 4 AB9 6 TYR D 33 GLN D 39 -1 N VAL D 37 O TYR D 94 SHEET 5 AB9 6 LEU D 45 ILE D 51 -1 O GLU D 46 N ARG D 38 SHEET 6 AB9 6 THR D 57 TYR D 59 -1 O TYR D 58 N VAL D 50 SHEET 1 AC1 4 LEU D 11 VAL D 12 0 SHEET 2 AC1 4 THR D 113 VAL D 117 1 O THR D 116 N VAL D 12 SHEET 3 AC1 4 ALA D 91 GLU D 98 -1 N TYR D 93 O THR D 113 SHEET 4 AC1 4 ILE D 106 TRP D 109 -1 O LEU D 108 N ARG D 97 SHEET 1 AC2 4 SER D 126 LEU D 130 0 SHEET 2 AC2 4 THR D 141 TYR D 151 -1 O LYS D 149 N SER D 126 SHEET 3 AC2 4 TYR D 182 PRO D 191 -1 O TYR D 182 N TYR D 151 SHEET 4 AC2 4 VAL D 169 THR D 171 -1 N HIS D 170 O VAL D 187 SHEET 1 AC3 4 THR D 137 SER D 138 0 SHEET 2 AC3 4 THR D 141 TYR D 151 -1 O THR D 141 N SER D 138 SHEET 3 AC3 4 TYR D 182 PRO D 191 -1 O TYR D 182 N TYR D 151 SHEET 4 AC3 4 VAL D 175 LEU D 176 -1 N VAL D 175 O SER D 183 SHEET 1 AC4 3 THR D 157 TRP D 160 0 SHEET 2 AC4 3 TYR D 200 HIS D 206 -1 O ASN D 203 N SER D 159 SHEET 3 AC4 3 THR D 211 VAL D 217 -1 O THR D 211 N HIS D 206 SHEET 1 AC5 3 GLU E 233 GLN E 240 0 SHEET 2 AC5 3 ASN E 243 ASP E 249 -1 O ASP E 249 N GLU E 233 SHEET 3 AC5 3 GLN E 290 PRO E 294 -1 O PHE E 293 N TYR E 244 SHEET 1 AC6 4 LYS E 278 GLN E 279 0 SHEET 2 AC6 4 THR E 256 HIS E 263 -1 N TRP E 261 O LYS E 278 SHEET 3 AC6 4 ILE E 302 SER E 310 -1 O ARG E 306 N GLN E 260 SHEET 4 AC6 4 ILE E 322 ASP E 325 -1 O PHE E 324 N TYR E 303 SHEET 1 AC7 3 GLU F 233 GLN F 240 0 SHEET 2 AC7 3 ASN F 243 ASP F 249 -1 O LYS F 247 N GLU F 236 SHEET 3 AC7 3 GLN F 290 PRO F 294 -1 O CYS F 291 N LEU F 246 SHEET 1 AC8 4 LYS F 278 GLN F 279 0 SHEET 2 AC8 4 THR F 256 HIS F 263 -1 N TRP F 261 O LYS F 278 SHEET 3 AC8 4 ILE F 302 SER F 310 -1 O LEU F 304 N LEU F 262 SHEET 4 AC8 4 ILE F 322 ASP F 325 -1 O PHE F 324 N TYR F 303 SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.05 SSBOND 2 CYS A 138 CYS A 198 1555 1555 2.05 SSBOND 3 CYS B 22 CYS B 95 1555 1555 2.04 SSBOND 4 CYS B 146 CYS B 202 1555 1555 2.03 SSBOND 5 CYS C 23 CYS C 88 1555 1555 2.05 SSBOND 6 CYS C 138 CYS C 198 1555 1555 2.04 SSBOND 7 CYS D 22 CYS D 95 1555 1555 2.04 SSBOND 8 CYS D 146 CYS D 202 1555 1555 2.04 SSBOND 9 CYS E 283 CYS E 291 1555 1555 2.04 SSBOND 10 CYS F 283 CYS F 291 1555 1555 2.03 CISPEP 1 SER A 7 PRO A 8 0 -4.26 CISPEP 2 TYR A 144 PRO A 145 0 6.22 CISPEP 3 PHE B 152 PRO B 153 0 -3.33 CISPEP 4 GLU B 154 PRO B 155 0 0.57 CISPEP 5 SER C 7 PRO C 8 0 -4.69 CISPEP 6 TYR C 144 PRO C 145 0 6.51 CISPEP 7 PHE D 152 PRO D 153 0 -4.25 CISPEP 8 GLU D 154 PRO D 155 0 2.31 CRYST1 73.155 121.031 79.738 90.00 111.51 90.00 P 1 21 1 4 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 0.013670 0.000000 0.005387 0.00000 SCALE2 0.000000 0.008262 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013480 0.00000