HEADER VIRAL PROTEIN/IMMUNE SYSTEM 07-SEP-21 7S3N TITLE SARS-COV-2 S STEM HELIX PEPTIDE BOUND TO FAB22 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB22 HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB22 LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: SPIKE GLYCOPROTEIN; COMPND 11 CHAIN: A; COMPND 12 FRAGMENT: STEM HELIX PEPTIDE (UNP RESIDUES 1146-1164); COMPND 13 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_COMMON: MOUSE; SOURCE 11 ORGANISM_TAXID: 10090; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 SYNTHETIC: YES; SOURCE 17 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 18 2; SOURCE 19 ORGANISM_COMMON: 2019-NCOV, SARS-COV-2; SOURCE 20 ORGANISM_TAXID: 2697049 KEYWDS SPIKE, FUSION, ANTIBODY, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR J.A.GOLDSMITH,J.S.MCLELLAN REVDAT 1 27-OCT-21 7S3N 0 JRNL AUTH C.-L.HSIEH,J.S.MCLELLAN JRNL TITL STABILIZED CORONAVIRUS SPIKE STEM ELICITS A BROADLY JRNL TITL 2 PROTECTIVE ANTIBODY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.1_4122+SVN 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.78 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.400 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 3 NUMBER OF REFLECTIONS : 38919 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.184 REMARK 3 R VALUE (WORKING SET) : 0.182 REMARK 3 FREE R VALUE : 0.221 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980 REMARK 3 FREE R VALUE TEST SET COUNT : 1937 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 43.7800 - 4.5800 0.98 2729 149 0.1703 0.1924 REMARK 3 2 4.5800 - 3.6300 0.99 2662 166 0.1483 0.2091 REMARK 3 3 3.6300 - 3.1700 0.99 2724 123 0.1715 0.2068 REMARK 3 4 3.1700 - 2.8800 0.99 2692 132 0.1955 0.2062 REMARK 3 5 2.8800 - 2.6800 0.99 2692 153 0.1894 0.2279 REMARK 3 6 2.6800 - 2.5200 0.99 2677 128 0.1990 0.2519 REMARK 3 7 2.5200 - 2.3900 0.97 2659 142 0.2048 0.2515 REMARK 3 8 2.3900 - 2.2900 0.99 2651 140 0.1983 0.2520 REMARK 3 9 2.2900 - 2.2000 0.99 2685 146 0.1946 0.2321 REMARK 3 10 2.2000 - 2.1300 0.98 2605 137 0.2001 0.2305 REMARK 3 11 2.1300 - 2.0600 0.96 2610 125 0.1936 0.2367 REMARK 3 12 2.0600 - 2.0000 0.92 2471 134 0.2051 0.2473 REMARK 3 13 2.0000 - 1.9500 0.96 2567 138 0.2141 0.2637 REMARK 3 14 1.9500 - 1.9000 0.94 2558 124 0.2379 0.2659 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) : 0.194 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.841 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 25.51 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.87 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 : 0.015 3504 REMARK 3 ANGLE : 1.501 4773 REMARK 3 CHIRALITY : 0.090 542 REMARK 3 PLANARITY : 0.012 610 REMARK 3 DIHEDRAL : 7.326 487 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 5 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN H AND RESID :117 REMARK 3 ORIGIN FOR THE GROUP (A): 1.4587 30.1361 28.1281 REMARK 3 T TENSOR REMARK 3 T11: 0.6270 T22: 0.2843 REMARK 3 T33: 0.1625 T12: -0.0385 REMARK 3 T13: -0.0044 T23: -0.0494 REMARK 3 L TENSOR REMARK 3 L11: 1.7292 L22: 2.0209 REMARK 3 L33: 4.1657 L12: 0.0810 REMARK 3 L13: -0.1859 L23: -0.2598 REMARK 3 S TENSOR REMARK 3 S11: 0.1795 S12: -0.2765 S13: -0.0110 REMARK 3 S21: 1.0018 S22: -0.0390 S23: -0.0595 REMARK 3 S31: 0.1361 S32: 0.3243 S33: -0.1138 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN H AND RESID 118: REMARK 3 ORIGIN FOR THE GROUP (A): -18.8303 20.6761 5.3146 REMARK 3 T TENSOR REMARK 3 T11: 0.1923 T22: 0.1623 REMARK 3 T33: 0.2066 T12: -0.0365 REMARK 3 T13: 0.0607 T23: 0.0000 REMARK 3 L TENSOR REMARK 3 L11: 2.6590 L22: 2.4368 REMARK 3 L33: 1.2214 L12: 0.5579 REMARK 3 L13: -0.4934 L23: 0.3704 REMARK 3 S TENSOR REMARK 3 S11: -0.1321 S12: 0.0507 S13: -0.1326 REMARK 3 S21: 0.1890 S22: -0.0428 S23: 0.4845 REMARK 3 S31: 0.2085 S32: -0.1246 S33: 0.1194 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN L AND RESID :113 REMARK 3 ORIGIN FOR THE GROUP (A): 1.6809 9.0655 31.9823 REMARK 3 T TENSOR REMARK 3 T11: 0.9830 T22: 0.3734 REMARK 3 T33: 0.2369 T12: 0.1089 REMARK 3 T13: -0.0941 T23: 0.0311 REMARK 3 L TENSOR REMARK 3 L11: 1.1492 L22: 1.5188 REMARK 3 L33: 2.7495 L12: -0.0213 REMARK 3 L13: 0.1022 L23: -0.5511 REMARK 3 S TENSOR REMARK 3 S11: 0.1035 S12: -0.2529 S13: -0.0889 REMARK 3 S21: 0.6447 S22: -0.0987 S23: -0.2009 REMARK 3 S31: 0.7470 S32: 0.2187 S33: 0.0236 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN L AND RESID 114: REMARK 3 ORIGIN FOR THE GROUP (A): -13.8547 6.2627 -2.2423 REMARK 3 T TENSOR REMARK 3 T11: 0.2154 T22: 0.1568 REMARK 3 T33: 0.1732 T12: -0.0070 REMARK 3 T13: 0.0552 T23: 0.0194 REMARK 3 L TENSOR REMARK 3 L11: 1.5975 L22: 4.0080 REMARK 3 L33: 4.1322 L12: 0.2112 REMARK 3 L13: 0.7502 L23: -0.1812 REMARK 3 S TENSOR REMARK 3 S11: 0.0522 S12: 0.0547 S13: -0.1716 REMARK 3 S21: 0.2793 S22: -0.0428 S23: 0.1041 REMARK 3 S31: 0.0113 S32: 0.1369 S33: -0.0078 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN A REMARK 3 ORIGIN FOR THE GROUP (A): 15.3624 26.2372 40.0275 REMARK 3 T TENSOR REMARK 3 T11: 0.8528 T22: 0.7866 REMARK 3 T33: 0.4265 T12: -0.0256 REMARK 3 T13: -0.6517 T23: -0.1072 REMARK 3 L TENSOR REMARK 3 L11: 6.3648 L22: 7.7456 REMARK 3 L33: 3.0503 L12: 2.0165 REMARK 3 L13: -1.3364 L23: 2.0468 REMARK 3 S TENSOR REMARK 3 S11: 0.3747 S12: -0.2287 S13: -0.7388 REMARK 3 S21: 0.7790 S22: 0.0486 S23: -1.3001 REMARK 3 S31: 0.6025 S32: 1.7734 S33: -0.8072 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 7S3N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-SEP-21. REMARK 100 THE DEPOSITION ID IS D_1000259569. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-JUN-21 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 19-ID 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 : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38944 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 87.550 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 200 DATA REDUNDANCY : 3.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94 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: PDB ENTRY 7M53 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.07 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE, PH 5.5, 23% REMARK 280 PEG8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 40.12300 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.54000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 40.12300 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.54000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL 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 TOTAL BURIED SURFACE AREA: 4880 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19580 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, A 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 SER H 138 REMARK 465 SER H 139 REMARK 465 LYS H 140 REMARK 465 SER H 141 REMARK 465 THR H 142 REMARK 465 SER H 143 REMARK 465 ASP L 36 REMARK 465 GLY L 37 REMARK 465 CYS L 219 REMARK 465 ASP A 1146 REMARK 465 LYS A 1157 REMARK 465 ASN A 1158 REMARK 465 HIS A 1159 REMARK 465 THR A 1160 REMARK 465 SER A 1161 REMARK 465 PRO A 1162 REMARK 465 ASP A 1163 REMARK 465 VAL A 1164 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLN H 7 CG CD OE1 NE2 REMARK 470 LYS L 133 CG CD CE NZ 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 O HOH H 452 O HOH L 407 1.84 REMARK 500 ND2 ASN L 61 O HOH L 301 1.85 REMARK 500 O HOH H 462 O HOH H 481 1.86 REMARK 500 O HOH L 330 O HOH L 413 1.86 REMARK 500 O HOH L 417 O HOH L 425 1.95 REMARK 500 O HOH H 443 O HOH L 353 1.96 REMARK 500 O HOH L 389 O HOH L 416 1.96 REMARK 500 O HOH H 431 O HOH H 455 1.97 REMARK 500 O HOH H 482 O HOH H 487 1.97 REMARK 500 OE1 GLU L 112 O HOH L 302 2.00 REMARK 500 O HOH H 463 O HOH L 410 2.01 REMARK 500 O HOH H 474 O HOH H 479 2.01 REMARK 500 O HOH H 311 O HOH H 442 2.02 REMARK 500 O ALA H 136 O HOH H 301 2.03 REMARK 500 OE2 GLU H 91 O HOH H 302 2.04 REMARK 500 O HOH H 378 O HOH H 473 2.06 REMARK 500 O HOH H 443 O HOH L 418 2.07 REMARK 500 O HOH H 369 O HOH H 466 2.09 REMARK 500 O HOH H 383 O HOH H 482 2.10 REMARK 500 NZ LYS H 212 O HOH H 303 2.12 REMARK 500 OH TYR L 95 O HOH L 303 2.13 REMARK 500 O HOH L 380 O HOH L 423 2.13 REMARK 500 NZ LYS H 128 O HOH H 304 2.14 REMARK 500 O HOH H 425 O HOH H 445 2.15 REMARK 500 O HOH H 412 O HOH H 456 2.15 REMARK 500 O LYS H 225 O HOH H 305 2.15 REMARK 500 O HOH H 305 O HOH H 383 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH H 466 O HOH H 466 2555 1.46 REMARK 500 O HOH H 481 O HOH L 426 4455 2.03 REMARK 500 O HOH H 324 O HOH H 324 2455 2.09 REMARK 500 O HOH H 467 O HOH L 321 4455 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 LEU H 181 CG LEU H 181 CD1 -0.224 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 ASN H 215 C - N - CA ANGL. DEV. = -20.0 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 LYS H 45 -64.80 -123.12 REMARK 500 ASP H 105 -111.86 60.36 REMARK 500 LEU L 58 -108.76 56.06 REMARK 500 SER L 75 -83.70 -124.95 REMARK 500 TYR L 101 -167.13 -115.17 REMARK 500 LEU L 102 120.64 -35.16 REMARK 500 ASN L 145 71.14 51.81 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH H 487 DISTANCE = 5.84 ANGSTROMS REMARK 525 HOH H 488 DISTANCE = 5.86 ANGSTROMS REMARK 525 HOH H 489 DISTANCE = 6.29 ANGSTROMS DBREF 7S3N H 3 225 PDB 7S3N 7S3N 3 225 DBREF 7S3N L 3 219 PDB 7S3N 7S3N 3 219 DBREF1 7S3N A 1146 1164 UNP A0A7L8JV80_SARS2 DBREF2 7S3N A A0A7L8JV80 1146 1164 SEQRES 1 H 223 GLU VAL GLN LEU GLN GLN PRO GLY PRO VAL LEU VAL LYS SEQRES 2 H 223 PRO GLY ALA SER VAL ARG MET SER CYS LYS ALA SER GLY SEQRES 3 H 223 TYR ARG ILE THR ASP ASN PHE MET ASN TRP VAL LYS GLN SEQRES 4 H 223 SER HIS GLY LYS SER LEU GLU TRP ILE GLY ILE ILE ASN SEQRES 5 H 223 PRO TYR ASN GLY GLY THR LYS TYR ASN GLN LYS PHE LYS SEQRES 6 H 223 GLY LYS ALA THR LEU THR VAL ASP THR SER SER SER THR SEQRES 7 H 223 ALA TYR MET GLU LEU ASN SER LEU THR SER GLU ASP SER SEQRES 8 H 223 ALA VAL TYR TYR CYS THR ARG VAL ARG GLY ASN ASP TYR SEQRES 9 H 223 HIS GLY ARG ALA MET ASP TYR TRP GLY GLN GLY THR SER SEQRES 10 H 223 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 H 223 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 H 223 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 H 223 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 H 223 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 H 223 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 H 223 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 H 223 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 H 223 PRO LYS SEQRES 1 L 215 ASP VAL VAL LEU THR GLN THR PRO LEU SER LEU PRO VAL SEQRES 2 L 215 ASN ILE GLY ASP GLN ALA SER ILE SER CYS LYS SER THR SEQRES 3 L 215 LYS SER LEU LEU ASN ARG ASP GLY PHE THR PHE LEU ASP SEQRES 4 L 215 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 L 215 ILE TYR LEU SER ASN ARG PHE SER GLY VAL PRO ASP ARG SEQRES 6 L 215 PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU LYS SEQRES 7 L 215 ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR TYR SEQRES 8 L 215 CYS PHE GLN SER ASN TYR LEU PHE THR PHE GLY SER GLY SEQRES 9 L 215 THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER SEQRES 10 L 215 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 L 215 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 L 215 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 L 215 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 L 215 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 L 215 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 L 215 ALA CYS GLU VAL THR GLN GLY THR THR SER VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 A 19 ASP SER PHE LYS GLU GLU LEU ASP LYS TYR PHE LYS ASN SEQRES 2 A 19 HIS THR SER PRO ASP VAL FORMUL 4 HOH *318(H2 O) HELIX 1 AA1 ARG H 30 ASN H 34 5 5 HELIX 2 AA2 GLN H 64 LYS H 67 5 4 HELIX 3 AA3 THR H 76 SER H 78 5 3 HELIX 4 AA4 THR H 89 SER H 93 5 5 HELIX 5 AA5 ASN H 104 GLY H 108 5 5 HELIX 6 AA6 SER H 167 ALA H 169 5 3 HELIX 7 AA7 SER H 198 LEU H 200 5 3 HELIX 8 AA8 GLU L 87 LEU L 91 5 5 HELIX 9 AA9 SER L 128 LYS L 133 1 6 HELIX 10 AB1 LYS L 190 GLU L 194 1 5 HELIX 11 AB2 PHE A 1148 PHE A 1156 1 9 SHEET 1 AA1 4 GLN H 5 GLN H 7 0 SHEET 2 AA1 4 VAL H 20 SER H 27 -1 O LYS H 25 N GLN H 7 SHEET 3 AA1 4 THR H 80 LEU H 85 -1 O MET H 83 N MET H 22 SHEET 4 AA1 4 ALA H 70 ASP H 75 -1 N THR H 73 O TYR H 82 SHEET 1 AA2 6 VAL H 12 VAL H 14 0 SHEET 2 AA2 6 THR H 118 VAL H 122 1 O THR H 121 N VAL H 12 SHEET 3 AA2 6 ALA H 94 VAL H 101 -1 N ALA H 94 O VAL H 120 SHEET 4 AA2 6 PHE H 35 SER H 42 -1 N VAL H 39 O TYR H 97 SHEET 5 AA2 6 SER H 46 ILE H 53 -1 O ILE H 50 N TRP H 38 SHEET 6 AA2 6 THR H 60 TYR H 62 -1 O LYS H 61 N ILE H 52 SHEET 1 AA3 4 VAL H 12 VAL H 14 0 SHEET 2 AA3 4 THR H 118 VAL H 122 1 O THR H 121 N VAL H 12 SHEET 3 AA3 4 ALA H 94 VAL H 101 -1 N ALA H 94 O VAL H 120 SHEET 4 AA3 4 MET H 111 TRP H 114 -1 O TYR H 113 N ARG H 100 SHEET 1 AA4 4 SER H 131 LEU H 135 0 SHEET 2 AA4 4 THR H 146 TYR H 156 -1 O LEU H 152 N PHE H 133 SHEET 3 AA4 4 TYR H 187 PRO H 196 -1 O LEU H 189 N VAL H 153 SHEET 4 AA4 4 VAL H 174 THR H 176 -1 N HIS H 175 O VAL H 192 SHEET 1 AA5 4 SER H 131 LEU H 135 0 SHEET 2 AA5 4 THR H 146 TYR H 156 -1 O LEU H 152 N PHE H 133 SHEET 3 AA5 4 TYR H 187 PRO H 196 -1 O LEU H 189 N VAL H 153 SHEET 4 AA5 4 VAL H 180 LEU H 181 -1 N VAL H 180 O SER H 188 SHEET 1 AA6 3 THR H 162 TRP H 165 0 SHEET 2 AA6 3 ILE H 206 HIS H 211 -1 O ASN H 208 N SER H 164 SHEET 3 AA6 3 THR H 216 LYS H 221 -1 O VAL H 218 N VAL H 209 SHEET 1 AA7 4 LEU L 6 THR L 9 0 SHEET 2 AA7 4 ALA L 21 SER L 27 -1 O SER L 24 N THR L 9 SHEET 3 AA7 4 ASP L 78 ILE L 83 -1 O ILE L 83 N ALA L 21 SHEET 4 AA7 4 PHE L 70 GLY L 74 -1 N SER L 71 O LYS L 82 SHEET 1 AA8 6 SER L 12 ASN L 16 0 SHEET 2 AA8 6 THR L 109 LYS L 114 1 O LYS L 110 N LEU L 13 SHEET 3 AA8 6 GLY L 92 GLN L 98 -1 N GLY L 92 O LEU L 111 SHEET 4 AA8 6 LEU L 41 GLN L 46 -1 N ASP L 42 O PHE L 97 SHEET 5 AA8 6 GLN L 53 TYR L 57 -1 O LEU L 55 N TRP L 43 SHEET 6 AA8 6 ASN L 61 ARG L 62 -1 O ASN L 61 N TYR L 57 SHEET 1 AA9 4 SER L 12 ASN L 16 0 SHEET 2 AA9 4 THR L 109 LYS L 114 1 O LYS L 110 N LEU L 13 SHEET 3 AA9 4 GLY L 92 GLN L 98 -1 N GLY L 92 O LEU L 111 SHEET 4 AA9 4 THR L 104 PHE L 105 -1 O THR L 104 N GLN L 98 SHEET 1 AB1 4 SER L 121 PHE L 125 0 SHEET 2 AB1 4 THR L 136 PHE L 146 -1 O LEU L 142 N PHE L 123 SHEET 3 AB1 4 TYR L 180 SER L 189 -1 O LEU L 182 N LEU L 143 SHEET 4 AB1 4 SER L 166 VAL L 170 -1 N SER L 169 O SER L 183 SHEET 1 AB2 4 ALA L 160 LEU L 161 0 SHEET 2 AB2 4 LYS L 152 VAL L 157 -1 N VAL L 157 O ALA L 160 SHEET 3 AB2 4 VAL L 198 GLN L 205 -1 O GLU L 202 N GLN L 154 SHEET 4 AB2 4 THR L 208 ASN L 215 -1 O VAL L 210 N VAL L 203 SSBOND 1 CYS H 24 CYS H 98 1555 1555 2.06 SSBOND 2 CYS H 151 CYS H 207 1555 1555 2.05 SSBOND 3 CYS L 25 CYS L 96 1555 1555 2.09 SSBOND 4 CYS L 141 CYS L 201 1555 1555 2.04 CISPEP 1 PHE H 157 PRO H 158 0 -9.71 CISPEP 2 GLU H 159 PRO H 160 0 -0.02 CISPEP 3 THR L 9 PRO L 10 0 -1.04 CISPEP 4 TYR L 147 PRO L 148 0 -1.73 CRYST1 80.246 73.080 89.043 90.00 100.50 90.00 C 1 2 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 0.012462 0.000000 0.002309 0.00000 SCALE2 0.000000 0.013684 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011422 0.00000