HEADER VIRAL PROTEIN 06-MAY-23 8JAG TITLE CRYO-EM STRUCTURE OF SARS-COV-1 RBD IN COMPLEX WITH W328-6H2 (LOCAL TITLE 2 REFINEMENT) COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE GLYCOPROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: H CHAIN OF 6H2 FAB REGION; COMPND 8 CHAIN: H; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: L CHAIN OF 6H2 FAB REGION; COMPND 12 CHAIN: L; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME-RELATED SOURCE 3 CORONAVIRUS; SOURCE 4 ORGANISM_TAXID: 694009; SOURCE 5 GENE: S, 2; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; 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_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS CRYO-EM, COMPLEX, SARS-COV-1, ANTIBODY, HOMO SAPIENS, IGG, RBD, LOCAL KEYWDS 2 REFINEMENT, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR X.Y.NAN,Y.J.LI REVDAT 1 18-DEC-24 8JAG 0 JRNL AUTH X.Y.NAN,Y.J.LI JRNL TITL CRYO-EM STRUCTURE OF SARS-COV-1 2P RBD IN COMPLEX WITH JRNL TITL 2 W328-6H2 ( LOCAL REFINEMENT) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.55 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : GCTF 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) : 3.550 REMARK 3 NUMBER OF PARTICLES : 110546 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 8JAG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-MAY-23. REMARK 100 THE DEPOSITION ID IS D_1300037511. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : CRYO-EM STRUCTURE OF SARS-COV-1 REMARK 245 RBD IN COMPLEX WITH W328-6H2 REMARK 245 (LOCAL REFINEMENT); SEVERE REMARK 245 ACUTE RESPIRATORY SYNDROME REMARK 245 CORONAVIRUS 1 2P; W328-6H2 IGG REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.30 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : CRYO-EM STRUCTURE OF SARS-COV-1 REMARK 245 RBD IN COMPLEX WITH W328-6H2 (LOCAL REFINEMENT); SEVERE ACUTE REMARK 245 RESPIRATORY SYNDROME CORONAVIRUS 1 2P; W328-6H2 IGG REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1600.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : DARK FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 PHE A 2 REMARK 465 ILE A 3 REMARK 465 PHE A 4 REMARK 465 LEU A 5 REMARK 465 LEU A 6 REMARK 465 PHE A 7 REMARK 465 LEU A 8 REMARK 465 THR A 9 REMARK 465 LEU A 10 REMARK 465 THR A 11 REMARK 465 SER A 12 REMARK 465 GLY A 13 REMARK 465 SER A 14 REMARK 465 ASP A 15 REMARK 465 LEU A 16 REMARK 465 ASP A 17 REMARK 465 PHE A 22 REMARK 465 ASP A 23 REMARK 465 ASP A 24 REMARK 465 VAL A 25 REMARK 465 GLN A 26 REMARK 465 ALA A 27 REMARK 465 PRO A 28 REMARK 465 ASN A 29 REMARK 465 TYR A 30 REMARK 465 ASN A 73 REMARK 465 HIS A 74 REMARK 465 THR A 75 REMARK 465 VAL A 140 REMARK 465 SER A 141 REMARK 465 LYS A 142 REMARK 465 PRO A 143 REMARK 465 MET A 144 REMARK 465 GLY A 145 REMARK 465 THR A 146 REMARK 465 GLN A 147 REMARK 465 THR A 148 REMARK 465 SER A 169 REMARK 465 LEU A 170 REMARK 465 ASP A 171 REMARK 465 VAL A 172 REMARK 465 SER A 173 REMARK 465 GLU A 174 REMARK 465 LYS A 175 REMARK 465 SER A 176 REMARK 465 GLY A 177 REMARK 465 ASN A 178 REMARK 465 PHE A 179 REMARK 465 VAL A 206 REMARK 465 ARG A 207 REMARK 465 ASP A 208 REMARK 465 PHE A 238 REMARK 465 SER A 239 REMARK 465 PRO A 240 REMARK 465 ALA A 241 REMARK 465 GLN A 242 REMARK 465 ASP A 243 REMARK 465 ILE A 244 REMARK 465 TRP A 245 REMARK 465 GLY A 246 REMARK 465 THR A 247 REMARK 465 SER A 248 REMARK 465 ALA A 249 REMARK 465 LYS A 465 REMARK 465 PRO A 466 REMARK 465 CYS A 467 REMARK 465 THR A 468 REMARK 465 PRO A 469 REMARK 465 PRO A 470 REMARK 465 SER A 664 REMARK 465 LEU A 665 REMARK 465 LEU A 666 REMARK 465 ARG A 667 REMARK 465 SER A 668 REMARK 465 THR A 669 REMARK 465 SER A 670 REMARK 465 THR A 809 REMARK 465 LEU A 810 REMARK 465 ALA A 811 REMARK 465 ASP A 812 REMARK 465 ALA A 813 REMARK 465 GLY A 814 REMARK 465 PHE A 815 REMARK 465 MET A 816 REMARK 465 LYS A 817 REMARK 465 CYS A 822 REMARK 465 LEU A 823 REMARK 465 GLY A 824 REMARK 465 ASP A 825 REMARK 465 ILE A 826 REMARK 465 ASN A 827 REMARK 465 ALA A 828 REMARK 465 ARG A 829 REMARK 465 ASP A 830 REMARK 465 LEU A 831 REMARK 465 ILE A 832 REMARK 465 CYS A 833 REMARK 465 ALA A 834 REMARK 465 ASP A 1128 REMARK 465 SER A 1129 REMARK 465 PHE A 1130 REMARK 465 LYS A 1131 REMARK 465 GLU A 1132 REMARK 465 GLU A 1133 REMARK 465 LEU A 1134 REMARK 465 ASP A 1135 REMARK 465 LYS A 1136 REMARK 465 TYR A 1137 REMARK 465 PHE A 1138 REMARK 465 LYS A 1139 REMARK 465 ASN A 1140 REMARK 465 HIS A 1141 REMARK 465 THR A 1142 REMARK 465 SER A 1143 REMARK 465 PRO A 1144 REMARK 465 ASP A 1145 REMARK 465 VAL A 1146 REMARK 465 ASP A 1147 REMARK 465 LEU A 1148 REMARK 465 GLY A 1149 REMARK 465 ASP A 1150 REMARK 465 ILE A 1151 REMARK 465 SER A 1152 REMARK 465 GLY A 1153 REMARK 465 ILE A 1154 REMARK 465 ASN A 1155 REMARK 465 ALA A 1156 REMARK 465 SER A 1157 REMARK 465 VAL A 1158 REMARK 465 VAL A 1159 REMARK 465 ASN A 1160 REMARK 465 ILE A 1161 REMARK 465 GLN A 1162 REMARK 465 LYS A 1163 REMARK 465 GLU A 1164 REMARK 465 ILE A 1165 REMARK 465 ASP A 1166 REMARK 465 ARG A 1167 REMARK 465 LEU A 1168 REMARK 465 ASN A 1169 REMARK 465 GLU A 1170 REMARK 465 VAL A 1171 REMARK 465 ALA A 1172 REMARK 465 LYS A 1173 REMARK 465 ASN A 1174 REMARK 465 LEU A 1175 REMARK 465 ASN A 1176 REMARK 465 GLU A 1177 REMARK 465 SER A 1178 REMARK 465 LEU A 1179 REMARK 465 ILE A 1180 REMARK 465 ASP A 1181 REMARK 465 LEU A 1182 REMARK 465 GLN A 1183 REMARK 465 GLU A 1184 REMARK 465 LEU A 1185 REMARK 465 GLY A 1186 REMARK 465 LYS A 1187 REMARK 465 TYR A 1188 REMARK 465 GLU A 1189 REMARK 465 GLN A 1190 REMARK 465 TYR A 1191 REMARK 465 ILE A 1192 REMARK 465 LYS A 1193 REMARK 465 TRP A 1194 REMARK 465 PRO A 1195 REMARK 465 TRP A 1196 REMARK 465 TYR A 1197 REMARK 465 VAL A 1198 REMARK 465 TRP A 1199 REMARK 465 LEU A 1200 REMARK 465 GLY A 1201 REMARK 465 PHE A 1202 REMARK 465 ILE A 1203 REMARK 465 ALA A 1204 REMARK 465 GLY A 1205 REMARK 465 LEU A 1206 REMARK 465 ILE A 1207 REMARK 465 ALA A 1208 REMARK 465 ILE A 1209 REMARK 465 VAL A 1210 REMARK 465 MET A 1211 REMARK 465 VAL A 1212 REMARK 465 THR A 1213 REMARK 465 ILE A 1214 REMARK 465 LEU A 1215 REMARK 465 LEU A 1216 REMARK 465 CYS A 1217 REMARK 465 CYS A 1218 REMARK 465 MET A 1219 REMARK 465 THR A 1220 REMARK 465 SER A 1221 REMARK 465 CYS A 1222 REMARK 465 CYS A 1223 REMARK 465 SER A 1224 REMARK 465 CYS A 1225 REMARK 465 LEU A 1226 REMARK 465 LYS A 1227 REMARK 465 GLY A 1228 REMARK 465 ALA A 1229 REMARK 465 CYS A 1230 REMARK 465 SER A 1231 REMARK 465 CYS A 1232 REMARK 465 GLY A 1233 REMARK 465 SER A 1234 REMARK 465 CYS A 1235 REMARK 465 CYS A 1236 REMARK 465 LYS A 1237 REMARK 465 PHE A 1238 REMARK 465 ASP A 1239 REMARK 465 GLU A 1240 REMARK 465 ASP A 1241 REMARK 465 ASP A 1242 REMARK 465 SER A 1243 REMARK 465 GLU A 1244 REMARK 465 PRO A 1245 REMARK 465 VAL A 1246 REMARK 465 LEU A 1247 REMARK 465 LYS A 1248 REMARK 465 GLY A 1249 REMARK 465 VAL A 1250 REMARK 465 LYS A 1251 REMARK 465 LEU A 1252 REMARK 465 HIS A 1253 REMARK 465 TYR A 1254 REMARK 465 THR A 1255 REMARK 465 THR H 67 REMARK 465 SER H 68 REMARK 465 ASP L 0 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 CA GLY A 368 CE1 PHE A 416 1.64 REMARK 500 O TYR A 367 CZ PHE A 416 2.14 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 SER A1033 CB SER A1033 OG -0.078 REMARK 500 REMARK 500 REMARK: NULL 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 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 TYR A 88 CB - CG - CD1 ANGL. DEV. = -5.2 DEGREES REMARK 500 TYR A 197 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES REMARK 500 TYR A 300 CB - CG - CD2 ANGL. DEV. = -5.3 DEGREES REMARK 500 ARG A 444 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES REMARK 500 ARG A 563 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES REMARK 500 CYS A 635 CA - CB - SG ANGL. DEV. = 6.9 DEGREES REMARK 500 TYR A 660 CB - CG - CD1 ANGL. DEV. = -4.0 DEGREES REMARK 500 ARG A 758 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 TYR A 899 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 ARG A 982 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 ARG A1073 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES REMARK 500 TYR L 38 CB - CG - CD2 ANGL. DEV. = -5.7 DEGREES REMARK 500 TYR L 53 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES REMARK 500 ARG L 58 NE - CZ - NH2 ANGL. DEV. = -4.3 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 SER A 36 -130.24 56.50 REMARK 500 LYS A 94 -17.12 -148.01 REMARK 500 SER A 95 29.91 -141.52 REMARK 500 SER A 105 -66.14 -135.41 REMARK 500 LYS A 297 152.25 177.84 REMARK 500 SER A 303 -155.83 -159.70 REMARK 500 SER A 310 -88.69 -96.27 REMARK 500 PHE A 451 19.30 59.16 REMARK 500 PHE A 529 -136.81 -93.47 REMARK 500 ASP A 613 103.31 -53.49 REMARK 500 ASP A 649 -74.47 -102.37 REMARK 500 ASN A 692 23.61 -141.20 REMARK 500 HIS A1040 18.39 58.67 REMARK 500 SER A1052 -138.92 -115.19 REMARK 500 THR A1082 39.73 38.51 REMARK 500 SER A1093 76.07 -150.72 REMARK 500 ALA H 16 -142.85 49.42 REMARK 500 SER H 28 -145.64 59.61 REMARK 500 HIS H 32 -143.58 47.08 REMARK 500 PRO H 52 68.82 -69.72 REMARK 500 ALA H 55 -124.68 -138.54 REMARK 500 VAL H 94 -71.27 68.26 REMARK 500 GLU H 96 140.28 72.27 REMARK 500 GLN L 5 119.47 82.95 REMARK 500 SER L 24 -158.69 -134.24 REMARK 500 ILE L 55 43.45 29.51 REMARK 500 SER L 56 -50.21 -150.70 REMARK 500 ALA L 84 -53.12 65.99 REMARK 500 THR L 96 -143.69 -131.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ILE H 51 PRO H 52 -56.50 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-36113 RELATED DB: EMDB DBREF 8JAG A 1 1255 UNP P59594 SPIKE_SARS 1 1255 DBREF 8JAG H 1 107 PDB 8JAG 8JAG 1 107 DBREF 8JAG L 0 111 PDB 8JAG 8JAG 0 111 SEQRES 1 A 1255 MET PHE ILE PHE LEU LEU PHE LEU THR LEU THR SER GLY SEQRES 2 A 1255 SER ASP LEU ASP ARG CYS THR THR PHE ASP ASP VAL GLN SEQRES 3 A 1255 ALA PRO ASN TYR THR GLN HIS THR SER SER MET ARG GLY SEQRES 4 A 1255 VAL TYR TYR PRO ASP GLU ILE PHE ARG SER ASP THR LEU SEQRES 5 A 1255 TYR LEU THR GLN ASP LEU PHE LEU PRO PHE TYR SER ASN SEQRES 6 A 1255 VAL THR GLY PHE HIS THR ILE ASN HIS THR PHE GLY ASN SEQRES 7 A 1255 PRO VAL ILE PRO PHE LYS ASP GLY ILE TYR PHE ALA ALA SEQRES 8 A 1255 THR GLU LYS SER ASN VAL VAL ARG GLY TRP VAL PHE GLY SEQRES 9 A 1255 SER THR MET ASN ASN LYS SER GLN SER VAL ILE ILE ILE SEQRES 10 A 1255 ASN ASN SER THR ASN VAL VAL ILE ARG ALA CYS ASN PHE SEQRES 11 A 1255 GLU LEU CYS ASP ASN PRO PHE PHE ALA VAL SER LYS PRO SEQRES 12 A 1255 MET GLY THR GLN THR HIS THR MET ILE PHE ASP ASN ALA SEQRES 13 A 1255 PHE ASN CYS THR PHE GLU TYR ILE SER ASP ALA PHE SER SEQRES 14 A 1255 LEU ASP VAL SER GLU LYS SER GLY ASN PHE LYS HIS LEU SEQRES 15 A 1255 ARG GLU PHE VAL PHE LYS ASN LYS ASP GLY PHE LEU TYR SEQRES 16 A 1255 VAL TYR LYS GLY TYR GLN PRO ILE ASP VAL VAL ARG ASP SEQRES 17 A 1255 LEU PRO SER GLY PHE ASN THR LEU LYS PRO ILE PHE LYS SEQRES 18 A 1255 LEU PRO LEU GLY ILE ASN ILE THR ASN PHE ARG ALA ILE SEQRES 19 A 1255 LEU THR ALA PHE SER PRO ALA GLN ASP ILE TRP GLY THR SEQRES 20 A 1255 SER ALA ALA ALA TYR PHE VAL GLY TYR LEU LYS PRO THR SEQRES 21 A 1255 THR PHE MET LEU LYS TYR ASP GLU ASN GLY THR ILE THR SEQRES 22 A 1255 ASP ALA VAL ASP CYS SER GLN ASN PRO LEU ALA GLU LEU SEQRES 23 A 1255 LYS CYS SER VAL LYS SER PHE GLU ILE ASP LYS GLY ILE SEQRES 24 A 1255 TYR GLN THR SER ASN PHE ARG VAL VAL PRO SER GLY ASP SEQRES 25 A 1255 VAL VAL ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE SEQRES 26 A 1255 GLY GLU VAL PHE ASN ALA THR LYS PHE PRO SER VAL TYR SEQRES 27 A 1255 ALA TRP GLU ARG LYS LYS ILE SER ASN CYS VAL ALA ASP SEQRES 28 A 1255 TYR SER VAL LEU TYR ASN SER THR PHE PHE SER THR PHE SEQRES 29 A 1255 LYS CYS TYR GLY VAL SER ALA THR LYS LEU ASN ASP LEU SEQRES 30 A 1255 CYS PHE SER ASN VAL TYR ALA ASP SER PHE VAL VAL LYS SEQRES 31 A 1255 GLY ASP ASP VAL ARG GLN ILE ALA PRO GLY GLN THR GLY SEQRES 32 A 1255 VAL ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE SEQRES 33 A 1255 MET GLY CYS VAL LEU ALA TRP ASN THR ARG ASN ILE ASP SEQRES 34 A 1255 ALA THR SER THR GLY ASN TYR ASN TYR LYS TYR ARG TYR SEQRES 35 A 1255 LEU ARG HIS GLY LYS LEU ARG PRO PHE GLU ARG ASP ILE SEQRES 36 A 1255 SER ASN VAL PRO PHE SER PRO ASP GLY LYS PRO CYS THR SEQRES 37 A 1255 PRO PRO ALA LEU ASN CYS TYR TRP PRO LEU ASN ASP TYR SEQRES 38 A 1255 GLY PHE TYR THR THR THR GLY ILE GLY TYR GLN PRO TYR SEQRES 39 A 1255 ARG VAL VAL VAL LEU SER PHE GLU LEU LEU ASN ALA PRO SEQRES 40 A 1255 ALA THR VAL CYS GLY PRO LYS LEU SER THR ASP LEU ILE SEQRES 41 A 1255 LYS ASN GLN CYS VAL ASN PHE ASN PHE ASN GLY LEU THR SEQRES 42 A 1255 GLY THR GLY VAL LEU THR PRO SER SER LYS ARG PHE GLN SEQRES 43 A 1255 PRO PHE GLN GLN PHE GLY ARG ASP VAL SER ASP PHE THR SEQRES 44 A 1255 ASP SER VAL ARG ASP PRO LYS THR SER GLU ILE LEU ASP SEQRES 45 A 1255 ILE SER PRO CYS SER PHE GLY GLY VAL SER VAL ILE THR SEQRES 46 A 1255 PRO GLY THR ASN ALA SER SER GLU VAL ALA VAL LEU TYR SEQRES 47 A 1255 GLN ASP VAL ASN CYS THR ASP VAL SER THR ALA ILE HIS SEQRES 48 A 1255 ALA ASP GLN LEU THR PRO ALA TRP ARG ILE TYR SER THR SEQRES 49 A 1255 GLY ASN ASN VAL PHE GLN THR GLN ALA GLY CYS LEU ILE SEQRES 50 A 1255 GLY ALA GLU HIS VAL ASP THR SER TYR GLU CYS ASP ILE SEQRES 51 A 1255 PRO ILE GLY ALA GLY ILE CYS ALA SER TYR HIS THR VAL SEQRES 52 A 1255 SER LEU LEU ARG SER THR SER GLN LYS SER ILE VAL ALA SEQRES 53 A 1255 TYR THR MET SER LEU GLY ALA ASP SER SER ILE ALA TYR SEQRES 54 A 1255 SER ASN ASN THR ILE ALA ILE PRO THR ASN PHE SER ILE SEQRES 55 A 1255 SER ILE THR THR GLU VAL MET PRO VAL SER MET ALA LYS SEQRES 56 A 1255 THR SER VAL ASP CYS ASN MET TYR ILE CYS GLY ASP SER SEQRES 57 A 1255 THR GLU CYS ALA ASN LEU LEU LEU GLN TYR GLY SER PHE SEQRES 58 A 1255 CYS THR GLN LEU ASN ARG ALA LEU SER GLY ILE ALA ALA SEQRES 59 A 1255 GLU GLN ASP ARG ASN THR ARG GLU VAL PHE ALA GLN VAL SEQRES 60 A 1255 LYS GLN MET TYR LYS THR PRO THR LEU LYS TYR PHE GLY SEQRES 61 A 1255 GLY PHE ASN PHE SER GLN ILE LEU PRO ASP PRO LEU LYS SEQRES 62 A 1255 PRO THR LYS ARG SER PHE ILE GLU ASP LEU LEU PHE ASN SEQRES 63 A 1255 LYS VAL THR LEU ALA ASP ALA GLY PHE MET LYS GLN TYR SEQRES 64 A 1255 GLY GLU CYS LEU GLY ASP ILE ASN ALA ARG ASP LEU ILE SEQRES 65 A 1255 CYS ALA GLN LYS PHE ASN GLY LEU THR VAL LEU PRO PRO SEQRES 66 A 1255 LEU LEU THR ASP ASP MET ILE ALA ALA TYR THR ALA ALA SEQRES 67 A 1255 LEU VAL SER GLY THR ALA THR ALA GLY TRP THR PHE GLY SEQRES 68 A 1255 ALA GLY ALA ALA LEU GLN ILE PRO PHE ALA MET GLN MET SEQRES 69 A 1255 ALA TYR ARG PHE ASN GLY ILE GLY VAL THR GLN ASN VAL SEQRES 70 A 1255 LEU TYR GLU ASN GLN LYS GLN ILE ALA ASN GLN PHE ASN SEQRES 71 A 1255 LYS ALA ILE SER GLN ILE GLN GLU SER LEU THR THR THR SEQRES 72 A 1255 SER THR ALA LEU GLY LYS LEU GLN ASP VAL VAL ASN GLN SEQRES 73 A 1255 ASN ALA GLN ALA LEU ASN THR LEU VAL LYS GLN LEU SER SEQRES 74 A 1255 SER ASN PHE GLY ALA ILE SER SER VAL LEU ASN ASP ILE SEQRES 75 A 1255 LEU SER ARG LEU ASP LYS VAL GLU ALA GLU VAL GLN ILE SEQRES 76 A 1255 ASP ARG LEU ILE THR GLY ARG LEU GLN SER LEU GLN THR SEQRES 77 A 1255 TYR VAL THR GLN GLN LEU ILE ARG ALA ALA GLU ILE ARG SEQRES 78 A 1255 ALA SER ALA ASN LEU ALA ALA THR LYS MET SER GLU CYS SEQRES 79 A 1255 VAL LEU GLY GLN SER LYS ARG VAL ASP PHE CYS GLY LYS SEQRES 80 A 1255 GLY TYR HIS LEU MET SER PHE PRO GLN ALA ALA PRO HIS SEQRES 81 A 1255 GLY VAL VAL PHE LEU HIS VAL THR TYR VAL PRO SER GLN SEQRES 82 A 1255 GLU ARG ASN PHE THR THR ALA PRO ALA ILE CYS HIS GLU SEQRES 83 A 1255 GLY LYS ALA TYR PHE PRO ARG GLU GLY VAL PHE VAL PHE SEQRES 84 A 1255 ASN GLY THR SER TRP PHE ILE THR GLN ARG ASN PHE PHE SEQRES 85 A 1255 SER PRO GLN ILE ILE THR THR ASP ASN THR PHE VAL SER SEQRES 86 A 1255 GLY ASN CYS ASP VAL VAL ILE GLY ILE ILE ASN ASN THR SEQRES 87 A 1255 VAL TYR ASP PRO LEU GLN PRO GLU LEU ASP SER PHE LYS SEQRES 88 A 1255 GLU GLU LEU ASP LYS TYR PHE LYS ASN HIS THR SER PRO SEQRES 89 A 1255 ASP VAL ASP LEU GLY ASP ILE SER GLY ILE ASN ALA SER SEQRES 90 A 1255 VAL VAL ASN ILE GLN LYS GLU ILE ASP ARG LEU ASN GLU SEQRES 91 A 1255 VAL ALA LYS ASN LEU ASN GLU SER LEU ILE ASP LEU GLN SEQRES 92 A 1255 GLU LEU GLY LYS TYR GLU GLN TYR ILE LYS TRP PRO TRP SEQRES 93 A 1255 TYR VAL TRP LEU GLY PHE ILE ALA GLY LEU ILE ALA ILE SEQRES 94 A 1255 VAL MET VAL THR ILE LEU LEU CYS CYS MET THR SER CYS SEQRES 95 A 1255 CYS SER CYS LEU LYS GLY ALA CYS SER CYS GLY SER CYS SEQRES 96 A 1255 CYS LYS PHE ASP GLU ASP ASP SER GLU PRO VAL LEU LYS SEQRES 97 A 1255 GLY VAL LYS LEU HIS TYR THR SEQRES 1 H 107 GLN VAL GLN LEU VAL GLN SER GLY SER GLU LEU LYS LYS SEQRES 2 H 107 PRO GLY ALA SER VAL THR VAL SER CYS LYS ALA SER GLY SEQRES 3 H 107 TYR SER PHE PRO THR HIS ALA MET ASN TRP VAL ARG GLN SEQRES 4 H 107 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE PRO SEQRES 5 H 107 THR TYR ALA GLY PHE THR GLY ARG PHE VAL PHE SER LEU SEQRES 6 H 107 ASP THR SER VAL SER THR ALA TYR LEU GLN ILE SER SER SEQRES 7 H 107 LEU LYS ALA ASP ASP THR ALA VAL TYR TYR CYS ALA ARG SEQRES 8 H 107 GLY HIS VAL LEU GLU TRP PHE GLN GLY THR LEU VAL THR SEQRES 9 H 107 VAL SER SER SEQRES 1 L 112 ASP VAL VAL MET THR GLN SER PRO LEU SER LEU SER VAL SEQRES 2 L 112 THR PRO GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3 L 112 GLN THR LEU LEU HIS SER ASP GLY GLN THR SER PHE TYR SEQRES 4 L 112 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 L 112 ILE TYR ASP ILE SER SER ARG PHE SER GLY VAL PRO ASP SEQRES 6 L 112 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 112 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 L 112 TYR CYS MET GLN GLY THR GLN PHE PRO TRP THR PHE GLY SEQRES 9 L 112 GLN GLY THR LYS VAL GLU ILE LYS HET NAG A1301 14 HET NAG A1302 14 HET NAG A1303 14 HET NAG A1304 14 HET NAG A1305 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 4 NAG 5(C8 H15 N O6) HELIX 1 AA1 ASN A 281 VAL A 290 1 10 HELIX 2 AA2 PHE A 325 ASN A 330 1 6 HELIX 3 AA3 SER A 336 TRP A 340 5 5 HELIX 4 AA4 TYR A 352 ASN A 357 1 6 HELIX 5 AA5 SER A 370 LEU A 377 5 8 HELIX 6 AA6 GLY A 391 ARG A 395 1 5 HELIX 7 AA7 GLY A 403 ASN A 409 1 7 HELIX 8 AA8 GLY A 488 TYR A 491 5 4 HELIX 9 AA9 ASN A 602 ALA A 612 1 11 HELIX 10 AB1 ASP A 719 GLY A 726 1 8 HELIX 11 AB2 SER A 728 LEU A 736 1 9 HELIX 12 AB3 GLN A 737 GLY A 739 5 3 HELIX 13 AB4 SER A 740 ALA A 765 1 26 HELIX 14 AB5 SER A 798 VAL A 808 1 11 HELIX 15 AB6 THR A 848 GLY A 867 1 20 HELIX 16 AB7 TRP A 868 PHE A 870 5 3 HELIX 17 AB8 PRO A 879 GLY A 890 1 12 HELIX 18 AB9 GLN A 895 ASN A 901 1 7 HELIX 19 AC1 ASN A 901 THR A 923 1 23 HELIX 20 AC2 LEU A 927 GLN A 947 1 21 HELIX 21 AC3 LEU A 948 SER A 950 5 3 HELIX 22 AC4 LEU A 959 SER A 964 1 6 HELIX 23 AC5 ASP A 967 VAL A 1015 1 49 HELIX 24 AC6 PRO A 1122 LEU A 1127 1 6 SHEET 1 AA1 7 GLN A 32 THR A 34 0 SHEET 2 AA1 7 ASN A 65 HIS A 70 -1 O VAL A 66 N HIS A 33 SHEET 3 AA1 7 ALA A 251 TYR A 256 -1 O TYR A 252 N PHE A 69 SHEET 4 AA1 7 GLY A 86 GLU A 93 -1 N ALA A 90 O PHE A 253 SHEET 5 AA1 7 HIS A 181 LYS A 190 -1 O PHE A 185 N PHE A 89 SHEET 6 AA1 7 PHE A 193 PRO A 202 -1 O TYR A 195 N LYS A 188 SHEET 7 AA1 7 LYS A 217 PRO A 223 -1 O LYS A 217 N LYS A 198 SHEET 1 AA2 3 THR A 51 PHE A 59 0 SHEET 2 AA2 3 LYS A 258 TYR A 266 -1 O LEU A 264 N TYR A 53 SHEET 3 AA2 3 ILE A 272 ASP A 277 -1 O THR A 273 N LYS A 265 SHEET 1 AA3 6 ILE A 81 PRO A 82 0 SHEET 2 AA3 6 ASN A 230 LEU A 235 -1 O PHE A 231 N ILE A 81 SHEET 3 AA3 6 VAL A 98 GLY A 104 -1 N GLY A 100 O ILE A 234 SHEET 4 AA3 6 SER A 113 ASN A 118 -1 O ILE A 116 N TRP A 101 SHEET 5 AA3 6 ASN A 122 CYS A 128 -1 O VAL A 124 N ILE A 117 SHEET 6 AA3 6 PHE A 161 ALA A 167 -1 O PHE A 161 N ALA A 127 SHEET 1 AA4 2 LEU A 132 PHE A 137 0 SHEET 2 AA4 2 MET A 151 PHE A 153 -1 O MET A 151 N PHE A 137 SHEET 1 AA5 6 LEU A 615 THR A 616 0 SHEET 2 AA5 6 GLY A 298 VAL A 307 -1 N ARG A 306 O THR A 616 SHEET 3 AA5 6 PHE A 578 THR A 585 -1 O VAL A 583 N TYR A 300 SHEET 4 AA5 6 ALA A 595 TYR A 598 -1 O LEU A 597 N SER A 582 SHEET 5 AA5 6 GLY A 634 ILE A 637 -1 O CYS A 635 N TYR A 598 SHEET 6 AA5 6 VAL A 628 THR A 631 -1 N PHE A 629 O LEU A 636 SHEET 1 AA6 6 ASP A 312 VAL A 314 0 SHEET 2 AA6 6 CYS A 524 ASN A 528 1 O ASN A 526 N VAL A 313 SHEET 3 AA6 6 THR A 533 PRO A 540 -1 O GLY A 534 N PHE A 527 SHEET 4 AA6 6 ILE A 570 SER A 574 -1 O SER A 574 N VAL A 537 SHEET 5 AA6 6 THR A 559 ARG A 563 -1 N ASP A 560 O ILE A 573 SHEET 6 AA6 6 PHE A 551 ARG A 553 -1 N GLY A 552 O SER A 561 SHEET 1 AA7 5 GLU A 341 ILE A 345 0 SHEET 2 AA7 5 VAL A 382 LYS A 390 -1 O VAL A 382 N ILE A 345 SHEET 3 AA7 5 PRO A 493 PHE A 501 -1 O TYR A 494 N VAL A 389 SHEET 4 AA7 5 CYS A 419 ASN A 424 -1 N CYS A 419 O LEU A 499 SHEET 5 AA7 5 THR A 363 CYS A 366 -1 N LYS A 365 O VAL A 420 SHEET 1 AA8 2 CYS A 348 VAL A 349 0 SHEET 2 AA8 2 VAL A 510 CYS A 511 1 O CYS A 511 N CYS A 348 SHEET 1 AA9 2 LYS A 439 ARG A 441 0 SHEET 2 AA9 2 LEU A 478 ASP A 480 -1 O ASN A 479 N TYR A 440 SHEET 1 AB1 4 GLU A 640 TYR A 646 0 SHEET 2 AB1 4 SER A 673 MET A 679 1 O ALA A 676 N GLU A 640 SHEET 3 AB1 4 ILE A 656 HIS A 661 -1 N CYS A 657 O TYR A 677 SHEET 4 AB1 4 ILE A 650 GLY A 653 -1 N ILE A 650 O ALA A 658 SHEET 1 AB2 5 THR A 693 PRO A 697 0 SHEET 2 AB2 5 GLU A1054 THR A1059 -1 O PHE A1057 N ILE A 694 SHEET 3 AB2 5 VAL A1076 ASN A1080 -1 O PHE A1079 N THR A1058 SHEET 4 AB2 5 SER A1083 GLN A1088 -1 O PHE A1085 N VAL A1078 SHEET 5 AB2 5 PHE A1091 ILE A1096 -1 O GLN A1095 N ILE A1086 SHEET 1 AB3 3 PHE A 700 PRO A 710 0 SHEET 2 AB3 3 GLY A1041 PRO A1051 -1 O PHE A1044 N GLU A 707 SHEET 3 AB3 3 TYR A1029 ALA A1038 -1 N MET A1032 O VAL A1047 SHEET 1 AB4 2 LYS A 715 VAL A 718 0 SHEET 2 AB4 2 LEU A 840 LEU A 843 -1 O LEU A 843 N LYS A 715 SHEET 1 AB5 2 TYR A 778 PHE A 779 0 SHEET 2 AB5 2 PHE A 782 ASN A 783 -1 O PHE A 782 N PHE A 779 SHEET 1 AB6 4 THR A1102 ASN A1107 0 SHEET 2 AB6 4 LYS A1068 PRO A1072 -1 N PHE A1071 O PHE A1103 SHEET 3 AB6 4 ILE A1063 HIS A1065 -1 N ILE A1063 O TYR A1070 SHEET 4 AB6 4 ILE A1115 ASN A1116 1 O ILE A1115 N CYS A1064 SHEET 1 AB7 4 LEU H 4 GLN H 6 0 SHEET 2 AB7 4 VAL H 18 ALA H 24 -1 O LYS H 23 N VAL H 5 SHEET 3 AB7 4 THR H 71 ILE H 76 -1 O ILE H 76 N VAL H 18 SHEET 4 AB7 4 PHE H 61 ASP H 66 -1 N SER H 64 O TYR H 73 SHEET 1 AB8 2 GLU H 10 LYS H 12 0 SHEET 2 AB8 2 VAL H 103 VAL H 105 1 O THR H 104 N GLU H 10 SHEET 1 AB9 4 LEU H 45 TRP H 47 0 SHEET 2 AB9 4 MET H 34 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 3 AB9 4 TYR H 88 ARG H 91 -1 O ALA H 90 N ASN H 35 SHEET 4 AB9 4 TRP H 97 PHE H 98 -1 O TRP H 97 N ARG H 91 SHEET 1 AC1 3 ALA L 18 LYS L 23 0 SHEET 2 AC1 3 ASP L 74 ILE L 79 -1 O ILE L 79 N ALA L 18 SHEET 3 AC1 3 PHE L 66 SER L 71 -1 N SER L 67 O LYS L 78 SHEET 1 AC2 5 SER L 57 ARG L 58 0 SHEET 2 AC2 5 PRO L 48 TYR L 53 -1 N TYR L 53 O SER L 57 SHEET 3 AC2 5 TYR L 38 GLN L 42 -1 N TRP L 39 O LEU L 51 SHEET 4 AC2 5 GLY L 88 MET L 93 -1 O VAL L 89 N GLN L 42 SHEET 5 AC2 5 THR L 106 VAL L 108 -1 O VAL L 108 N GLY L 88 SSBOND 1 CYS A 19 CYS A 133 1555 1555 2.02 SSBOND 2 CYS A 128 CYS A 159 1555 1555 2.03 SSBOND 3 CYS A 278 CYS A 288 1555 1555 2.04 SSBOND 4 CYS A 323 CYS A 348 1555 1555 2.04 SSBOND 5 CYS A 366 CYS A 419 1555 1555 2.08 SSBOND 6 CYS A 378 CYS A 511 1555 1555 2.11 SSBOND 7 CYS A 524 CYS A 576 1555 1555 2.03 SSBOND 8 CYS A 603 CYS A 635 1555 1555 2.07 SSBOND 9 CYS A 648 CYS A 657 1555 1555 2.03 SSBOND 10 CYS A 720 CYS A 742 1555 1555 2.04 SSBOND 11 CYS A 725 CYS A 731 1555 1555 2.03 SSBOND 12 CYS A 1014 CYS A 1025 1555 1555 2.02 SSBOND 13 CYS A 1064 CYS A 1108 1555 1555 2.02 SSBOND 14 CYS H 22 CYS H 89 1555 1555 2.07 SSBOND 15 CYS L 22 CYS L 92 1555 1555 2.05 LINK ND2 ASN A 65 C1 NAG A1305 1555 1555 1.42 LINK ND2 ASN A 227 C1 NAG A1302 1555 1555 1.43 LINK ND2 ASN A 269 C1 NAG A1303 1555 1555 1.45 LINK ND2 ASN A 330 C1 NAG A1301 1555 1555 1.42 LINK ND2 ASN A 783 C1 NAG A1304 1555 1555 1.45 CISPEP 1 THR A 616 PRO A 617 0 -5.17 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