HEADER VIRAL PROTEIN 06-MAY-23 8JAP TITLE CRYO-EM STRUCTURE OF SARS-COV-2 WT 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 W328-6H2 FAB REGION; COMPND 8 CHAIN: H; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: L CHAIN OF W328-6H2 FAB REGION; COMPND 12 CHAIN: L; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_TAXID: 2697049; 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-2, 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 8JAP 0 JRNL AUTH X.Y.NAN,Y.J.LI JRNL TITL CRYO-EM STRUCTURE OF SARS-COV-2 WT RBD IN COMPLEX WITH JRNL TITL 2 W328-6H2 (LOCAL REFINEMENT) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.81 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) : 3.810 REMARK 3 NUMBER OF PARTICLES : 146713 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 8JAP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAY-23. REMARK 100 THE DEPOSITION ID IS D_1300037535. 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-2 REMARK 245 WT IN COMPLEX WITH W328-6H2; REMARK 245 SARS-COV-2 WT 6P; W328-6H2 IGG REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : CRYO-EM STRUCTURE OF SARS-COV-2 REMARK 245 WT IN COMPLEX WITH W328-6H2; SARS-COV-2 WT 6P; 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 : BRIGHT 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A -317 REMARK 465 PHE A -316 REMARK 465 VAL A -315 REMARK 465 PHE A -314 REMARK 465 LEU A -313 REMARK 465 VAL A -312 REMARK 465 LEU A -311 REMARK 465 LEU A -310 REMARK 465 PRO A -309 REMARK 465 LEU A -308 REMARK 465 VAL A -307 REMARK 465 SER A -306 REMARK 465 SER A -305 REMARK 465 GLN A -304 REMARK 465 CYS A -303 REMARK 465 VAL A -302 REMARK 465 ASN A -301 REMARK 465 LEU A -300 REMARK 465 THR A -299 REMARK 465 THR A -298 REMARK 465 ARG A -297 REMARK 465 THR A -296 REMARK 465 GLN A -295 REMARK 465 LEU A -294 REMARK 465 PRO A -293 REMARK 465 PRO A -292 REMARK 465 ALA A -291 REMARK 465 TYR A -290 REMARK 465 THR A -289 REMARK 465 ASN A -288 REMARK 465 SER A -287 REMARK 465 PHE A -286 REMARK 465 THR A -285 REMARK 465 ARG A -284 REMARK 465 GLY A -283 REMARK 465 VAL A -282 REMARK 465 TYR A -281 REMARK 465 TYR A -280 REMARK 465 PRO A -279 REMARK 465 ASP A -278 REMARK 465 LYS A -277 REMARK 465 VAL A -276 REMARK 465 PHE A -275 REMARK 465 ARG A -274 REMARK 465 SER A -273 REMARK 465 SER A -272 REMARK 465 VAL A -271 REMARK 465 LEU A -270 REMARK 465 HIS A -269 REMARK 465 SER A -268 REMARK 465 THR A -267 REMARK 465 GLN A -266 REMARK 465 ASP A -265 REMARK 465 LEU A -264 REMARK 465 PHE A -263 REMARK 465 LEU A -262 REMARK 465 PRO A -261 REMARK 465 PHE A -260 REMARK 465 PHE A -259 REMARK 465 SER A -258 REMARK 465 ASN A -257 REMARK 465 VAL A -256 REMARK 465 THR A -255 REMARK 465 TRP A -254 REMARK 465 PHE A -253 REMARK 465 HIS A -252 REMARK 465 ALA A -251 REMARK 465 ILE A -250 REMARK 465 HIS A -249 REMARK 465 VAL A -248 REMARK 465 SER A -247 REMARK 465 GLY A -246 REMARK 465 THR A -245 REMARK 465 ASN A -244 REMARK 465 GLY A -243 REMARK 465 THR A -242 REMARK 465 LYS A -241 REMARK 465 ARG A -240 REMARK 465 PHE A -239 REMARK 465 ASP A -238 REMARK 465 ASN A -237 REMARK 465 PRO A -236 REMARK 465 VAL A -235 REMARK 465 LEU A -234 REMARK 465 PRO A -233 REMARK 465 PHE A -232 REMARK 465 ASN A -231 REMARK 465 ASP A -230 REMARK 465 GLY A -229 REMARK 465 VAL A -228 REMARK 465 TYR A -227 REMARK 465 PHE A -226 REMARK 465 ALA A -225 REMARK 465 SER A -224 REMARK 465 THR A -223 REMARK 465 GLU A -222 REMARK 465 LYS A -221 REMARK 465 SER A -220 REMARK 465 ASN A -219 REMARK 465 ILE A -218 REMARK 465 ILE A -217 REMARK 465 ARG A -216 REMARK 465 GLY A -215 REMARK 465 TRP A -214 REMARK 465 ILE A -213 REMARK 465 PHE A -212 REMARK 465 GLY A -211 REMARK 465 THR A -210 REMARK 465 THR A -209 REMARK 465 LEU A -208 REMARK 465 ASP A -207 REMARK 465 SER A -206 REMARK 465 LYS A -205 REMARK 465 THR A -204 REMARK 465 GLN A -203 REMARK 465 SER A -202 REMARK 465 LEU A -201 REMARK 465 LEU A -200 REMARK 465 ILE A -199 REMARK 465 VAL A -198 REMARK 465 ASN A -197 REMARK 465 ASN A -196 REMARK 465 ALA A -195 REMARK 465 THR A -194 REMARK 465 ASN A -193 REMARK 465 VAL A -192 REMARK 465 VAL A -191 REMARK 465 ILE A -190 REMARK 465 LYS A -189 REMARK 465 VAL A -188 REMARK 465 CYS A -187 REMARK 465 GLU A -186 REMARK 465 PHE A -185 REMARK 465 GLN A -184 REMARK 465 PHE A -183 REMARK 465 CYS A -182 REMARK 465 ASN A -181 REMARK 465 ASP A -180 REMARK 465 PRO A -179 REMARK 465 PHE A -178 REMARK 465 LEU A -177 REMARK 465 GLY A -176 REMARK 465 VAL A -175 REMARK 465 TYR A -174 REMARK 465 TYR A -173 REMARK 465 HIS A -172 REMARK 465 LYS A -171 REMARK 465 ASN A -170 REMARK 465 ASN A -169 REMARK 465 LYS A -168 REMARK 465 SER A -167 REMARK 465 TRP A -166 REMARK 465 MET A -165 REMARK 465 GLU A -164 REMARK 465 SER A -163 REMARK 465 GLU A -162 REMARK 465 PHE A -161 REMARK 465 ARG A -160 REMARK 465 VAL A -159 REMARK 465 TYR A -158 REMARK 465 SER A -157 REMARK 465 SER A -156 REMARK 465 ALA A -155 REMARK 465 ASN A -154 REMARK 465 ASN A -153 REMARK 465 CYS A -152 REMARK 465 THR A -151 REMARK 465 PHE A -150 REMARK 465 GLU A -149 REMARK 465 TYR A -148 REMARK 465 VAL A -147 REMARK 465 SER A -146 REMARK 465 GLN A -145 REMARK 465 PRO A -144 REMARK 465 PHE A -143 REMARK 465 LEU A -142 REMARK 465 MET A -141 REMARK 465 ASP A -140 REMARK 465 LEU A -139 REMARK 465 GLU A -138 REMARK 465 GLY A -137 REMARK 465 LYS A -136 REMARK 465 GLN A -135 REMARK 465 GLY A -134 REMARK 465 ASN A -133 REMARK 465 PHE A -132 REMARK 465 LYS A -131 REMARK 465 ASN A -130 REMARK 465 LEU A -129 REMARK 465 ARG A -128 REMARK 465 GLU A -127 REMARK 465 PHE A -126 REMARK 465 VAL A -125 REMARK 465 PHE A -124 REMARK 465 LYS A -123 REMARK 465 ASN A -122 REMARK 465 ILE A -121 REMARK 465 ASP A -120 REMARK 465 GLY A -119 REMARK 465 TYR A -118 REMARK 465 PHE A -117 REMARK 465 LYS A -116 REMARK 465 ILE A -115 REMARK 465 TYR A -114 REMARK 465 SER A -113 REMARK 465 LYS A -112 REMARK 465 HIS A -111 REMARK 465 THR A -110 REMARK 465 PRO A -109 REMARK 465 ILE A -108 REMARK 465 ASN A -107 REMARK 465 LEU A -106 REMARK 465 VAL A -105 REMARK 465 ARG A -104 REMARK 465 ASP A -103 REMARK 465 LEU A -102 REMARK 465 PRO A -101 REMARK 465 GLN A -100 REMARK 465 GLY A -99 REMARK 465 PHE A -98 REMARK 465 SER A -97 REMARK 465 ALA A -96 REMARK 465 LEU A -95 REMARK 465 GLU A -94 REMARK 465 PRO A -93 REMARK 465 LEU A -92 REMARK 465 VAL A -91 REMARK 465 ASP A -90 REMARK 465 LEU A -89 REMARK 465 PRO A -88 REMARK 465 ILE A -87 REMARK 465 GLY A -86 REMARK 465 ILE A -85 REMARK 465 ASN A -84 REMARK 465 ILE A -83 REMARK 465 THR A -82 REMARK 465 ARG A -81 REMARK 465 PHE A -80 REMARK 465 GLN A -79 REMARK 465 THR A -78 REMARK 465 LEU A -77 REMARK 465 LEU A -76 REMARK 465 ALA A -75 REMARK 465 LEU A -74 REMARK 465 HIS A -73 REMARK 465 ARG A -72 REMARK 465 SER A -71 REMARK 465 TYR A -70 REMARK 465 LEU A -69 REMARK 465 THR A -68 REMARK 465 PRO A -67 REMARK 465 GLY A -66 REMARK 465 ASP A -65 REMARK 465 SER A -64 REMARK 465 SER A -63 REMARK 465 SER A -62 REMARK 465 GLY A -61 REMARK 465 TRP A -60 REMARK 465 THR A -59 REMARK 465 ALA A -58 REMARK 465 GLY A -57 REMARK 465 ALA A -56 REMARK 465 ALA A -55 REMARK 465 ALA A -54 REMARK 465 TYR A -53 REMARK 465 TYR A -52 REMARK 465 VAL A -51 REMARK 465 GLY A -50 REMARK 465 TYR A -49 REMARK 465 LEU A -48 REMARK 465 GLN A -47 REMARK 465 PRO A -46 REMARK 465 ARG A -45 REMARK 465 THR A -44 REMARK 465 PHE A -43 REMARK 465 LEU A -42 REMARK 465 LEU A -41 REMARK 465 LYS A -40 REMARK 465 TYR A -39 REMARK 465 ASN A -38 REMARK 465 GLU A -37 REMARK 465 ASN A -36 REMARK 465 GLY A -35 REMARK 465 THR A -34 REMARK 465 ILE A -33 REMARK 465 THR A -32 REMARK 465 ASP A -31 REMARK 465 ALA A -30 REMARK 465 VAL A -29 REMARK 465 ASP A -28 REMARK 465 CYS A -27 REMARK 465 ALA A -26 REMARK 465 LEU A -25 REMARK 465 ASP A -24 REMARK 465 PRO A -23 REMARK 465 LEU A -22 REMARK 465 SER A -21 REMARK 465 GLU A -20 REMARK 465 THR A -19 REMARK 465 LYS A -18 REMARK 465 CYS A -17 REMARK 465 THR A -16 REMARK 465 LEU A -15 REMARK 465 LYS A -14 REMARK 465 SER A -13 REMARK 465 PHE A -12 REMARK 465 THR A -11 REMARK 465 VAL A -10 REMARK 465 GLU A -9 REMARK 465 LYS A -8 REMARK 465 GLY A -7 REMARK 465 ILE A -6 REMARK 465 TYR A -5 REMARK 465 GLN A -4 REMARK 465 THR A -3 REMARK 465 SER A -2 REMARK 465 ASN A -1 REMARK 465 PHE A 0 REMARK 465 GLY A 167 REMARK 465 ASN A 183 REMARK 465 GLY A 184 REMARK 465 LEU H 74 REMARK 465 THR H 101 REMARK 465 ASP L 0 REMARK 465 PHE L 98 REMARK 465 THR L 106 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 TYR A 33 CD1 TYR A 33 CE1 -0.099 REMARK 500 TYR A 135 CB TYR A 135 CG -0.096 REMARK 500 PHE A 168 CG PHE A 168 CD2 0.092 REMARK 500 PHE A 168 CG PHE A 168 CD1 0.093 REMARK 500 VAL H 37 CB VAL H 37 CG1 -0.300 REMARK 500 PHE H 63 CB PHE H 63 CG -0.118 REMARK 500 TYR H 73 CG TYR H 73 CD2 0.088 REMARK 500 TYR H 73 CG TYR H 73 CD1 0.105 REMARK 500 TYR H 73 CE1 TYR H 73 CZ 0.086 REMARK 500 TYR H 73 CZ TYR H 73 CE2 0.095 REMARK 500 VAL L 89 CB VAL L 89 CG1 -0.140 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 139 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 PRO L 17 C - N - CA ANGL. DEV. = 10.0 DEGREES REMARK 500 ARG L 58 NE - CZ - NH2 ANGL. DEV. = -3.3 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 CYS A 18 82.83 69.01 REMARK 500 VAL A 32 -7.89 -59.83 REMARK 500 LYS A 68 -112.35 -107.30 REMARK 500 LEU A 69 -55.62 63.99 REMARK 500 ASN A 104 -150.35 -122.26 REMARK 500 TYR A 131 -153.92 -143.21 REMARK 500 LEU A 134 -162.07 -113.74 REMARK 500 ARG A 139 -31.57 -146.10 REMARK 500 SER A 141 -21.02 -156.47 REMARK 500 LEU A 143 160.22 63.25 REMARK 500 PHE A 179 -29.17 -163.64 REMARK 500 GLN A 180 114.92 -34.11 REMARK 500 PRO A 181 94.83 -40.26 REMARK 500 TYR A 187 8.83 -161.92 REMARK 500 ARG A 191 71.17 41.70 REMARK 500 LYS A 211 138.51 -174.15 REMARK 500 SER A 212 87.40 -175.66 REMARK 500 LYS A 217 11.61 57.72 REMARK 500 VAL H 2 48.90 35.72 REMARK 500 SER H 7 -164.46 -109.17 REMARK 500 TRP H 50 -92.43 -143.93 REMARK 500 SER H 68 -128.28 50.43 REMARK 500 SER H 78 -32.15 -137.47 REMARK 500 ASP H 82 80.55 51.67 REMARK 500 ALA H 85 70.79 52.12 REMARK 500 LEU H 95 13.90 55.32 REMARK 500 SER L 9 -88.98 -121.69 REMARK 500 ALA L 84 -119.07 48.78 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-36121 RELATED DB: EMDB DBREF 8JAP A -317 222 UNP P0DTC2 SPIKE_SARS2 1 540 DBREF 8JAP H 1 107 PDB 8JAP 8JAP 1 107 DBREF 8JAP L 0 111 PDB 8JAP 8JAP 0 111 SEQRES 1 A 540 MET PHE VAL PHE LEU VAL LEU LEU PRO LEU VAL SER SER SEQRES 2 A 540 GLN CYS VAL ASN LEU THR THR ARG THR GLN LEU PRO PRO SEQRES 3 A 540 ALA TYR THR ASN SER PHE THR ARG GLY VAL TYR TYR PRO SEQRES 4 A 540 ASP LYS VAL PHE ARG SER SER VAL LEU HIS SER THR GLN SEQRES 5 A 540 ASP LEU PHE LEU PRO PHE PHE SER ASN VAL THR TRP PHE SEQRES 6 A 540 HIS ALA ILE HIS VAL SER GLY THR ASN GLY THR LYS ARG SEQRES 7 A 540 PHE ASP ASN PRO VAL LEU PRO PHE ASN ASP GLY VAL TYR SEQRES 8 A 540 PHE ALA SER THR GLU LYS SER ASN ILE ILE ARG GLY TRP SEQRES 9 A 540 ILE PHE GLY THR THR LEU ASP SER LYS THR GLN SER LEU SEQRES 10 A 540 LEU ILE VAL ASN ASN ALA THR ASN VAL VAL ILE LYS VAL SEQRES 11 A 540 CYS GLU PHE GLN PHE CYS ASN ASP PRO PHE LEU GLY VAL SEQRES 12 A 540 TYR TYR HIS LYS ASN ASN LYS SER TRP MET GLU SER GLU SEQRES 13 A 540 PHE ARG VAL TYR SER SER ALA ASN ASN CYS THR PHE GLU SEQRES 14 A 540 TYR VAL SER GLN PRO PHE LEU MET ASP LEU GLU GLY LYS SEQRES 15 A 540 GLN GLY ASN PHE LYS ASN LEU ARG GLU PHE VAL PHE LYS SEQRES 16 A 540 ASN ILE ASP GLY TYR PHE LYS ILE TYR SER LYS HIS THR SEQRES 17 A 540 PRO ILE ASN LEU VAL ARG ASP LEU PRO GLN GLY PHE SER SEQRES 18 A 540 ALA LEU GLU PRO LEU VAL ASP LEU PRO ILE GLY ILE ASN SEQRES 19 A 540 ILE THR ARG PHE GLN THR LEU LEU ALA LEU HIS ARG SER SEQRES 20 A 540 TYR LEU THR PRO GLY ASP SER SER SER GLY TRP THR ALA SEQRES 21 A 540 GLY ALA ALA ALA TYR TYR VAL GLY TYR LEU GLN PRO ARG SEQRES 22 A 540 THR PHE LEU LEU LYS TYR ASN GLU ASN GLY THR ILE THR SEQRES 23 A 540 ASP ALA VAL ASP CYS ALA LEU ASP PRO LEU SER GLU THR SEQRES 24 A 540 LYS CYS THR LEU LYS SER PHE THR VAL GLU LYS GLY ILE SEQRES 25 A 540 TYR GLN THR SER ASN PHE ARG VAL GLN PRO THR GLU SER SEQRES 26 A 540 ILE VAL ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE SEQRES 27 A 540 GLY GLU VAL PHE ASN ALA THR ARG PHE ALA SER VAL TYR SEQRES 28 A 540 ALA TRP ASN ARG LYS ARG ILE SER ASN CYS VAL ALA ASP SEQRES 29 A 540 TYR SER VAL LEU TYR ASN SER ALA SER PHE SER THR PHE SEQRES 30 A 540 LYS CYS TYR GLY VAL SER PRO THR LYS LEU ASN ASP LEU SEQRES 31 A 540 CYS PHE THR ASN VAL TYR ALA ASP SER PHE VAL ILE ARG SEQRES 32 A 540 GLY ASP GLU VAL ARG GLN ILE ALA PRO GLY GLN THR GLY SEQRES 33 A 540 LYS ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE SEQRES 34 A 540 THR GLY CYS VAL ILE ALA TRP ASN SER ASN ASN LEU ASP SEQRES 35 A 540 SER LYS VAL GLY GLY ASN TYR ASN TYR LEU TYR ARG LEU SEQRES 36 A 540 PHE ARG LYS SER ASN LEU LYS PRO PHE GLU ARG ASP ILE SEQRES 37 A 540 SER THR GLU ILE TYR GLN ALA GLY SER THR PRO CYS ASN SEQRES 38 A 540 GLY VAL GLU GLY PHE ASN CYS TYR PHE PRO LEU GLN SER SEQRES 39 A 540 TYR GLY PHE GLN PRO THR ASN GLY VAL GLY TYR GLN PRO SEQRES 40 A 540 TYR ARG VAL VAL VAL LEU SER PHE GLU LEU LEU HIS ALA SEQRES 41 A 540 PRO ALA THR VAL CYS GLY PRO LYS LYS SER THR ASN LEU SEQRES 42 A 540 VAL LYS ASN LYS CYS VAL ASN 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 A 301 28 HET NAG A 302 28 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 2(C8 H15 N O6) HELIX 1 AA1 PHE A 20 ASN A 25 1 6 HELIX 2 AA2 TYR A 47 ASN A 52 1 6 HELIX 3 AA3 ARG A 85 VAL A 89 5 5 SHEET 1 AA1 2 GLU A 6 SER A 7 0 SHEET 2 AA1 2 VAL A 221 ASN A 222 1 O ASN A 222 N GLU A 6 SHEET 1 AA2 3 ALA A 30 SER A 31 0 SHEET 2 AA2 3 VAL A 77 VAL A 83 1 O VAL A 83 N ALA A 30 SHEET 3 AA2 3 LYS A 38 ILE A 40 -1 N ILE A 40 O VAL A 77 SHEET 1 AA3 5 ALA A 30 SER A 31 0 SHEET 2 AA3 5 VAL A 77 VAL A 83 1 O VAL A 83 N ALA A 30 SHEET 3 AA3 5 VAL A 192 PHE A 197 -1 O VAL A 194 N ASP A 80 SHEET 4 AA3 5 CYS A 114 ALA A 117 -1 N ILE A 116 O VAL A 193 SHEET 5 AA3 5 THR A 58 CYS A 61 -1 N LYS A 60 O VAL A 115 SHEET 1 AA4 2 GLU H 10 LEU H 11 0 SHEET 2 AA4 2 VAL H 103 THR H 104 1 O THR H 104 N GLU H 10 SHEET 1 AA5 3 ALA H 72 TYR H 73 0 SHEET 2 AA5 3 VAL H 18 CYS H 22 -1 N CYS H 22 O ALA H 72 SHEET 3 AA5 3 ILE H 76 ILE H 76 -1 O ILE H 76 N VAL H 18 SHEET 1 AA6 4 LEU H 45 GLY H 49 0 SHEET 2 AA6 4 MET H 34 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 3 AA6 4 TYR H 88 ARG H 91 -1 O TYR H 88 N VAL H 37 SHEET 4 AA6 4 PHE H 98 GLN H 99 -1 O GLN H 99 N CYS H 89 SHEET 1 AA7 3 THR L 4 GLN L 5 0 SHEET 2 AA7 3 ALA L 18 LYS L 23 -1 O LYS L 23 N THR L 4 SHEET 3 AA7 3 ASP L 74 ILE L 79 -1 O ILE L 79 N ALA L 18 SHEET 1 AA8 4 LEU L 50 TYR L 53 0 SHEET 2 AA8 4 PHE L 37 GLN L 42 -1 N PHE L 37 O TYR L 53 SHEET 3 AA8 4 VAL L 89 MET L 93 -1 O MET L 93 N TYR L 38 SHEET 4 AA8 4 THR L 101 GLY L 105 -1 O GLY L 105 N TYR L 90 SSBOND 1 CYS A 18 CYS A 43 1555 1555 2.13 SSBOND 2 CYS A 61 CYS A 114 1555 1555 2.04 SSBOND 3 CYS A 73 CYS A 207 1555 1555 2.10 SSBOND 4 CYS A 162 CYS A 170 1555 1555 2.02 SSBOND 5 CYS H 22 CYS H 89 1555 1555 2.04 SSBOND 6 CYS L 22 CYS L 92 1555 1555 2.11 LINK ND2 ASN A 13 C1 NAG A 302 1555 1555 1.53 LINK ND2 ASN A 25 C1 NAG A 301 1555 1555 1.51 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