HEADER PROTEIN BINDING 23-JAN-24 8RRN TITLE CRYSTAL STRUCTURE OF THE SARS-COV-2 S RBD IN COMPLEX WITH PT1616 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE PROTEIN S1; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: PT1616 FAB HEAVY CHAIN; COMPND 7 CHAIN: H, C; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: PT1616 FAB LIGHT CHAIN; COMPND 11 CHAIN: L, D; COMPND 12 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 EXPRESSION_SYSTEM_CELL_LINE: HEK293EXPI; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: HEK293EXPI; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 17 2; SOURCE 18 ORGANISM_TAXID: 2697049; SOURCE 19 GENE: S, 2; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 EXPRESSION_SYSTEM_CELL_LINE: HEK293EXPI KEYWDS PROTEIN BINDING/IMMUNE SYSTEM, PROTEIN BINDING EXPDTA X-RAY DIFFRACTION AUTHOR G.HANSEN,T.KREY REVDAT 1 30-OCT-24 8RRN 0 JRNL AUTH C.S.STEIN,G.HANSEN,L.STROEH,O.OCHULOR,E.HEROLD,B.SCHWARZLOH, JRNL AUTH 2 D.MUTSCHALL,J.ZISCHKE,A.K.CORDES,T.SCHNEIDER,I.HINRICHS, JRNL AUTH 3 R.BLASCZYK,H.KLEINE-WEBER,M.HOFFMANN,K.KLEIN,M.M.HOEPER, JRNL AUTH 4 F.K.KAISER,M.GONZALEZ-HERNANDEZ,F.ARMANDO,M.CIURKIEWICZ, JRNL AUTH 5 G.BEYTHIEN,S.POEHLMANN,W.BAUMGAERTNER,A.OSTERHAUS, JRNL AUTH 6 T.F.SCHULZ,T.KREY JRNL TITL A HUMAN MONOCLONAL ANTIBODY NEUTRALIZING SARS-COV-2 OMICRON JRNL TITL 2 VARIANTS CONTAINING THE L452R MUTATION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.11 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 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) : 3.11 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.62 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 27710 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.246 REMARK 3 R VALUE (WORKING SET) : 0.243 REMARK 3 FREE R VALUE : 0.291 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 1384 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 45.6200 - 6.7100 1.00 2753 145 0.2273 0.2635 REMARK 3 2 6.7000 - 5.3200 1.00 2655 137 0.2365 0.2597 REMARK 3 3 5.3200 - 4.6500 1.00 2679 142 0.2143 0.2857 REMARK 3 4 4.6500 - 4.2300 1.00 2622 138 0.2038 0.2461 REMARK 3 5 4.2300 - 3.9200 1.00 2625 138 0.2272 0.2579 REMARK 3 6 3.9200 - 3.6900 1.00 2609 137 0.2757 0.3638 REMARK 3 7 3.6900 - 3.5100 1.00 2644 139 0.2787 0.3598 REMARK 3 8 3.5100 - 3.3600 1.00 2589 137 0.3053 0.3770 REMARK 3 9 3.3600 - 3.2300 0.99 2622 138 0.3346 0.3665 REMARK 3 10 3.2300 - 3.1100 0.98 2528 133 0.3688 0.4171 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 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) : 0.554 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.386 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 97.24 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 108.9 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 : 0.007 9757 REMARK 3 ANGLE : 0.823 13304 REMARK 3 CHIRALITY : 0.053 1482 REMARK 3 PLANARITY : 0.007 1721 REMARK 3 DIHEDRAL : 4.572 1365 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 335 THROUGH 527) REMARK 3 ORIGIN FOR THE GROUP (A): -24.3707 -5.6468 56.1342 REMARK 3 T TENSOR REMARK 3 T11: 0.9374 T22: 0.7521 REMARK 3 T33: 0.4270 T12: 0.0353 REMARK 3 T13: -0.0276 T23: -0.1463 REMARK 3 L TENSOR REMARK 3 L11: 4.4075 L22: 3.8246 REMARK 3 L33: 3.7217 L12: 0.5480 REMARK 3 L13: -1.2886 L23: -0.5887 REMARK 3 S TENSOR REMARK 3 S11: -0.3787 S12: 0.0993 S13: -0.1098 REMARK 3 S21: -0.0963 S22: 0.2287 S23: -0.3167 REMARK 3 S31: 0.5789 S32: 0.4144 S33: 0.1451 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'B' AND RESID 334 THROUGH 528) REMARK 3 ORIGIN FOR THE GROUP (A): -21.1383 -8.2802 24.0187 REMARK 3 T TENSOR REMARK 3 T11: 0.7879 T22: 0.6516 REMARK 3 T33: 0.4328 T12: -0.0620 REMARK 3 T13: 0.0676 T23: -0.1295 REMARK 3 L TENSOR REMARK 3 L11: 4.1289 L22: 2.8201 REMARK 3 L33: 7.3683 L12: -0.8325 REMARK 3 L13: 1.5816 L23: -0.2258 REMARK 3 S TENSOR REMARK 3 S11: -0.1715 S12: -0.1462 S13: 0.1606 REMARK 3 S21: 0.0330 S22: 0.3025 S23: -0.3751 REMARK 3 S31: -0.7172 S32: 0.3824 S33: -0.1125 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN 'H' AND RESID 2 THROUGH 125) REMARK 3 ORIGIN FOR THE GROUP (A): -34.1290 4.6232 81.1796 REMARK 3 T TENSOR REMARK 3 T11: 1.0538 T22: 0.7351 REMARK 3 T33: 0.5541 T12: 0.0505 REMARK 3 T13: 0.0832 T23: -0.0577 REMARK 3 L TENSOR REMARK 3 L11: 1.5964 L22: 3.5665 REMARK 3 L33: 9.3618 L12: -0.3459 REMARK 3 L13: 2.8154 L23: -0.4193 REMARK 3 S TENSOR REMARK 3 S11: -0.0701 S12: -0.4349 S13: -0.0358 REMARK 3 S21: 0.6223 S22: 0.0700 S23: 0.0162 REMARK 3 S31: 0.7254 S32: 0.0546 S33: 0.0075 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN 'H' AND RESID 126 THROUGH 225) REMARK 3 ORIGIN FOR THE GROUP (A): -40.0328 31.6120 106.3102 REMARK 3 T TENSOR REMARK 3 T11: 0.8505 T22: 0.8922 REMARK 3 T33: 0.6328 T12: -0.0999 REMARK 3 T13: 0.0209 T23: -0.0649 REMARK 3 L TENSOR REMARK 3 L11: 6.3376 L22: 9.0434 REMARK 3 L33: 7.6784 L12: -3.9582 REMARK 3 L13: -0.5484 L23: 1.7870 REMARK 3 S TENSOR REMARK 3 S11: 0.0589 S12: 0.1374 S13: 0.1455 REMARK 3 S21: -0.1281 S22: 0.1208 S23: 0.5359 REMARK 3 S31: -0.3921 S32: -0.3420 S33: -0.0290 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN 'C' AND RESID 3 THROUGH 125) REMARK 3 ORIGIN FOR THE GROUP (A): -25.9840 -17.4260 -2.9415 REMARK 3 T TENSOR REMARK 3 T11: 0.8748 T22: 0.8083 REMARK 3 T33: 0.5423 T12: -0.1707 REMARK 3 T13: 0.0014 T23: -0.1226 REMARK 3 L TENSOR REMARK 3 L11: 0.7084 L22: 4.6628 REMARK 3 L33: 7.2948 L12: -1.3118 REMARK 3 L13: -1.4714 L23: 0.3597 REMARK 3 S TENSOR REMARK 3 S11: 0.0750 S12: 0.2766 S13: 0.0530 REMARK 3 S21: -1.0477 S22: 0.2291 S23: -0.2421 REMARK 3 S31: -0.6075 S32: 0.3331 S33: -0.2758 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN 'C' AND RESID 126 THROUGH 225) REMARK 3 ORIGIN FOR THE GROUP (A): -25.9148 -44.3777 -28.8092 REMARK 3 T TENSOR REMARK 3 T11: 1.1573 T22: 0.8999 REMARK 3 T33: 0.6712 T12: 0.0903 REMARK 3 T13: 0.1584 T23: -0.0605 REMARK 3 L TENSOR REMARK 3 L11: 5.4236 L22: 2.9110 REMARK 3 L33: 5.9153 L12: 2.3307 REMARK 3 L13: -0.8872 L23: -1.4548 REMARK 3 S TENSOR REMARK 3 S11: -0.3197 S12: -0.0041 S13: -0.6365 REMARK 3 S21: -0.8441 S22: 0.3202 S23: -0.2277 REMARK 3 S31: 0.9711 S32: -0.0905 S33: -0.0748 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN 'L' AND RESID 2 THROUGH 112) REMARK 3 ORIGIN FOR THE GROUP (A): -33.5948 20.7556 66.9513 REMARK 3 T TENSOR REMARK 3 T11: 0.9939 T22: 0.6332 REMARK 3 T33: 0.5282 T12: -0.1000 REMARK 3 T13: 0.0674 T23: 0.0543 REMARK 3 L TENSOR REMARK 3 L11: 3.9819 L22: 6.1753 REMARK 3 L33: 3.8679 L12: -1.8198 REMARK 3 L13: -0.0465 L23: 2.2096 REMARK 3 S TENSOR REMARK 3 S11: 0.1585 S12: 0.3857 S13: 0.6641 REMARK 3 S21: -1.1879 S22: 0.0120 S23: -0.3575 REMARK 3 S31: -1.1068 S32: 0.2524 S33: -0.1503 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: (CHAIN 'L' AND RESID 113 THROUGH 213) REMARK 3 ORIGIN FOR THE GROUP (A): -27.8891 39.8191 99.5054 REMARK 3 T TENSOR REMARK 3 T11: 1.1761 T22: 0.8899 REMARK 3 T33: 0.6105 T12: -0.1203 REMARK 3 T13: -0.0530 T23: -0.0949 REMARK 3 L TENSOR REMARK 3 L11: 4.3584 L22: 5.8649 REMARK 3 L33: 5.9702 L12: -0.4746 REMARK 3 L13: 0.9536 L23: -0.2296 REMARK 3 S TENSOR REMARK 3 S11: 0.2693 S12: 0.1445 S13: 0.2427 REMARK 3 S21: -0.2693 S22: -0.3500 S23: 0.2090 REMARK 3 S31: 0.2840 S32: 0.8459 S33: 0.1272 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: (CHAIN 'D' AND RESID 2 THROUGH 112) REMARK 3 ORIGIN FOR THE GROUP (A): -27.9636 -34.1120 10.6237 REMARK 3 T TENSOR REMARK 3 T11: 0.8884 T22: 0.5945 REMARK 3 T33: 0.5397 T12: 0.1033 REMARK 3 T13: -0.0583 T23: 0.0392 REMARK 3 L TENSOR REMARK 3 L11: 4.7210 L22: 2.6852 REMARK 3 L33: 4.3948 L12: 0.4151 REMARK 3 L13: 0.9209 L23: 1.6091 REMARK 3 S TENSOR REMARK 3 S11: 0.3093 S12: -0.1732 S13: -0.7655 REMARK 3 S21: 0.6512 S22: 0.0545 S23: -0.1461 REMARK 3 S31: 0.9485 S32: 0.2232 S33: -0.3603 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: (CHAIN 'D' AND RESID 113 THROUGH 213) REMARK 3 ORIGIN FOR THE GROUP (A): -14.0547 -51.0655 -20.2332 REMARK 3 T TENSOR REMARK 3 T11: 1.7657 T22: 1.0226 REMARK 3 T33: 0.8280 T12: 0.4043 REMARK 3 T13: -0.1065 T23: -0.0795 REMARK 3 L TENSOR REMARK 3 L11: 3.5732 L22: 3.8724 REMARK 3 L33: 7.7494 L12: 2.4332 REMARK 3 L13: -1.5239 L23: -0.5612 REMARK 3 S TENSOR REMARK 3 S11: 0.3461 S12: -0.0179 S13: -0.6471 REMARK 3 S21: 0.9401 S22: -0.3128 S23: -0.2422 REMARK 3 S31: 1.1778 S32: 1.0738 S33: -0.0948 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 3 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "A" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "B" and resid 335 through 527) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "C" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "H" and resid 3 through 225) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "D" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "L" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8RRN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-JAN-24. REMARK 100 THE DEPOSITION ID IS D_1292136086. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-JUN-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27745 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.110 REMARK 200 RESOLUTION RANGE LOW (A) : 45.620 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 6.600 REMARK 200 R MERGE (I) : 0.40930 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.1700 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.11 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.23 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6 REMARK 200 DATA REDUNDANCY IN SHELL : 6.50 REMARK 200 R MERGE FOR SHELL (I) : 2.74100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.020 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 (%): 59.48 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 3000, 200 MM NACL, 100 MM TRIS REMARK 280 PH 7.0, 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 86.55000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.53000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 86.55000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.53000 REMARK 290 SMTRY3 4 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, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D 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 ASN A 334 REMARK 465 ASP A 528 REMARK 465 ASP A 529 REMARK 465 ASP A 530 REMARK 465 ASP A 531 REMARK 465 LYS A 532 REMARK 465 ASP B 529 REMARK 465 ASP B 530 REMARK 465 ASP B 531 REMARK 465 LYS B 532 REMARK 465 GLN H 1 REMARK 465 SER H 226 REMARK 465 CYS H 227 REMARK 465 ASP H 228 REMARK 465 LYS H 229 REMARK 465 THR H 230 REMARK 465 ASP H 231 REMARK 465 ASP H 232 REMARK 465 ASP H 233 REMARK 465 ASP H 234 REMARK 465 LYS H 235 REMARK 465 GLN L 1 REMARK 465 GLU L 215 REMARK 465 CYS L 216 REMARK 465 SER L 217 REMARK 465 GLN C 1 REMARK 465 VAL C 2 REMARK 465 SER C 226 REMARK 465 CYS C 227 REMARK 465 ASP C 228 REMARK 465 LYS C 229 REMARK 465 THR C 230 REMARK 465 ASP C 231 REMARK 465 ASP C 232 REMARK 465 ASP C 233 REMARK 465 ASP C 234 REMARK 465 LYS C 235 REMARK 465 GLN D 1 REMARK 465 GLU D 215 REMARK 465 CYS D 216 REMARK 465 SER D 217 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 ASN A 343 40.77 -90.54 REMARK 500 ASP A 389 56.16 -115.04 REMARK 500 PHE A 400 -177.66 -174.99 REMARK 500 ASP A 428 33.48 -98.84 REMARK 500 ASP A 442 34.32 -94.51 REMARK 500 THR A 470 48.47 -92.15 REMARK 500 SER A 477 58.54 -116.74 REMARK 500 ASN B 343 42.69 -90.18 REMARK 500 SER B 373 43.38 -81.71 REMARK 500 ASP B 389 54.14 -111.62 REMARK 500 PHE B 400 -177.03 -177.23 REMARK 500 ASP B 428 33.28 -98.64 REMARK 500 ASP B 442 31.63 -93.41 REMARK 500 THR B 470 49.43 -92.83 REMARK 500 SER B 477 50.75 -110.78 REMARK 500 PHE H 29 25.43 45.56 REMARK 500 SER H 31 16.07 53.47 REMARK 500 GLN H 65 -165.28 -119.66 REMARK 500 ALA H 72 139.02 -170.91 REMARK 500 SER H 77 11.27 85.30 REMARK 500 THR H 142 -163.80 -109.19 REMARK 500 ASP H 155 72.07 49.87 REMARK 500 PRO H 158 -162.42 -78.34 REMARK 500 THR H 171 -41.93 -130.53 REMARK 500 THR H 202 -60.51 -106.59 REMARK 500 ASN L 28 -94.10 -122.57 REMARK 500 ASN L 53 -50.32 75.27 REMARK 500 THR L 78 -70.29 -72.46 REMARK 500 LYS L 161 -62.34 -135.60 REMARK 500 ASN L 175 -2.51 69.62 REMARK 500 PHE C 29 30.77 -145.36 REMARK 500 SER C 30 -55.01 -143.11 REMARK 500 SER C 77 12.12 85.66 REMARK 500 THR C 142 -164.07 -110.94 REMARK 500 ASP C 155 70.39 53.19 REMARK 500 THR C 171 -41.63 -131.70 REMARK 500 THR C 202 -60.05 -107.13 REMARK 500 ASN D 28 -97.96 -126.10 REMARK 500 ASN D 53 -56.18 79.06 REMARK 500 THR D 78 -71.52 -72.62 REMARK 500 PRO D 146 -178.60 -69.60 REMARK 500 ASP D 156 -123.80 58.20 REMARK 500 LYS D 161 -53.28 -135.41 REMARK 500 REMARK 500 REMARK: NULL DBREF 8RRN A 334 527 UNP P0DTC2 SPIKE_SARS2 334 527 DBREF 8RRN B 334 527 UNP P0DTC2 SPIKE_SARS2 334 527 DBREF 8RRN H 1 235 PDB 8RRN 8RRN 1 235 DBREF 8RRN L 1 217 PDB 8RRN 8RRN 1 217 DBREF 8RRN C 1 235 PDB 8RRN 8RRN 1 235 DBREF 8RRN D 1 217 PDB 8RRN 8RRN 1 217 SEQADV 8RRN ASP A 528 UNP P0DTC2 EXPRESSION TAG SEQADV 8RRN ASP A 529 UNP P0DTC2 EXPRESSION TAG SEQADV 8RRN ASP A 530 UNP P0DTC2 EXPRESSION TAG SEQADV 8RRN ASP A 531 UNP P0DTC2 EXPRESSION TAG SEQADV 8RRN LYS A 532 UNP P0DTC2 EXPRESSION TAG SEQADV 8RRN ASP B 528 UNP P0DTC2 EXPRESSION TAG SEQADV 8RRN ASP B 529 UNP P0DTC2 EXPRESSION TAG SEQADV 8RRN ASP B 530 UNP P0DTC2 EXPRESSION TAG SEQADV 8RRN ASP B 531 UNP P0DTC2 EXPRESSION TAG SEQADV 8RRN LYS B 532 UNP P0DTC2 EXPRESSION TAG SEQRES 1 A 199 ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR ARG SEQRES 2 A 199 PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE SER SEQRES 3 A 199 ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER ALA SEQRES 4 A 199 SER PHE SER THR PHE LYS CYS TYR GLY VAL SER PRO THR SEQRES 5 A 199 LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA ASP SEQRES 6 A 199 SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN ILE ALA SEQRES 7 A 199 PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN TYR LYS SEQRES 8 A 199 LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP ASN SEQRES 9 A 199 SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN TYR ASN SEQRES 10 A 199 TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU LYS PRO SEQRES 11 A 199 PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA GLY SEQRES 12 A 199 SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN CYS TYR SEQRES 13 A 199 PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR ASN GLY SEQRES 14 A 199 VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER PHE SEQRES 15 A 199 GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO ASP SEQRES 16 A 199 ASP ASP ASP LYS SEQRES 1 B 199 ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR ARG SEQRES 2 B 199 PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE SER SEQRES 3 B 199 ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER ALA SEQRES 4 B 199 SER PHE SER THR PHE LYS CYS TYR GLY VAL SER PRO THR SEQRES 5 B 199 LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA ASP SEQRES 6 B 199 SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN ILE ALA SEQRES 7 B 199 PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN TYR LYS SEQRES 8 B 199 LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP ASN SEQRES 9 B 199 SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN TYR ASN SEQRES 10 B 199 TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU LYS PRO SEQRES 11 B 199 PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA GLY SEQRES 12 B 199 SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN CYS TYR SEQRES 13 B 199 PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR ASN GLY SEQRES 14 B 199 VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER PHE SEQRES 15 B 199 GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO ASP SEQRES 16 B 199 ASP ASP ASP LYS SEQRES 1 H 235 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 235 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 235 GLY THR PHE SER SER TYR THR ILE SER TRP VAL ARG GLN SEQRES 4 H 235 ALA PRO GLY GLN GLY LEU GLU CYS MET GLY ARG ILE ILE SEQRES 5 H 235 PRO ILE LEU GLY ILE ALA ASN TYR ALA GLN LYS PHE GLN SEQRES 6 H 235 GLY ARG VAL THR ILE THR ALA ASP LYS SER THR SER ILE SEQRES 7 H 235 ALA TYR MET GLU VAL SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 235 ALA VAL TYR TYR CYS ALA THR GLU VAL GLY TYR SER GLY SEQRES 9 H 235 TYR GLY SER ALA GLU TYR PHE ASN HIS TRP GLY GLN GLY SEQRES 10 H 235 THR PRO VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 H 235 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 H 235 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 H 235 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 H 235 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 H 235 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 H 235 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 H 235 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG SEQRES 18 H 235 VAL GLU PRO LYS SER CYS ASP LYS THR ASP ASP ASP ASP SEQRES 19 H 235 LYS SEQRES 1 L 217 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 L 217 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY SER ASN SEQRES 3 L 217 SER ASN ILE GLY ALA GLY TYR ASP VAL HIS TRP TYR GLN SEQRES 4 L 217 GLN LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR ALA SEQRES 5 L 217 ASN ASN ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 L 217 GLY SER ARG SER GLY THR SER ALA SER LEU VAL ILE THR SEQRES 7 L 217 GLY LEU GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 L 217 SER TYR ASP SER SER LEU THR GLY SER LEU PHE GLY GLY SEQRES 9 L 217 GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA SEQRES 10 L 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 L 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 L 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 L 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 L 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 L 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 L 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 L 217 LYS THR VAL ALA PRO THR GLU CYS SER SEQRES 1 C 235 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 C 235 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 C 235 GLY THR PHE SER SER TYR THR ILE SER TRP VAL ARG GLN SEQRES 4 C 235 ALA PRO GLY GLN GLY LEU GLU CYS MET GLY ARG ILE ILE SEQRES 5 C 235 PRO ILE LEU GLY ILE ALA ASN TYR ALA GLN LYS PHE GLN SEQRES 6 C 235 GLY ARG VAL THR ILE THR ALA ASP LYS SER THR SER ILE SEQRES 7 C 235 ALA TYR MET GLU VAL SER SER LEU ARG SER GLU ASP THR SEQRES 8 C 235 ALA VAL TYR TYR CYS ALA THR GLU VAL GLY TYR SER GLY SEQRES 9 C 235 TYR GLY SER ALA GLU TYR PHE ASN HIS TRP GLY GLN GLY SEQRES 10 C 235 THR PRO VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 C 235 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 C 235 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 C 235 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 C 235 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 C 235 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 C 235 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 C 235 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG SEQRES 18 C 235 VAL GLU PRO LYS SER CYS ASP LYS THR ASP ASP ASP ASP SEQRES 19 C 235 LYS SEQRES 1 D 217 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 D 217 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY SER ASN SEQRES 3 D 217 SER ASN ILE GLY ALA GLY TYR ASP VAL HIS TRP TYR GLN SEQRES 4 D 217 GLN LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR ALA SEQRES 5 D 217 ASN ASN ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 D 217 GLY SER ARG SER GLY THR SER ALA SER LEU VAL ILE THR SEQRES 7 D 217 GLY LEU GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 D 217 SER TYR ASP SER SER LEU THR GLY SER LEU PHE GLY GLY SEQRES 9 D 217 GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA SEQRES 10 D 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 D 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 D 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 D 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 D 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 D 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 D 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 D 217 LYS THR VAL ALA PRO THR GLU CYS SER HELIX 1 AA1 PHE A 338 ASN A 343 1 6 HELIX 2 AA2 SER A 349 TRP A 353 5 5 HELIX 3 AA3 ASP A 364 LEU A 368 5 5 HELIX 4 AA4 ASP A 405 ILE A 410 5 6 HELIX 5 AA5 GLY A 416 ASN A 422 1 7 HELIX 6 AA6 PHE B 338 ASN B 343 1 6 HELIX 7 AA7 ASP B 364 LEU B 368 5 5 HELIX 8 AA8 ASP B 405 ILE B 410 5 6 HELIX 9 AA9 GLY B 416 ASN B 422 1 7 HELIX 10 AB1 SER B 438 SER B 443 1 6 HELIX 11 AB2 GLY B 502 TYR B 505 5 4 HELIX 12 AB3 SER H 198 LEU H 200 5 3 HELIX 13 AB4 GLN L 81 GLU L 85 5 5 HELIX 14 AB5 SER L 126 GLN L 131 1 6 HELIX 15 AB6 THR L 186 HIS L 193 1 8 HELIX 16 AB7 SER C 198 LEU C 200 5 3 HELIX 17 AB8 GLN D 81 GLU D 85 5 5 HELIX 18 AB9 SER D 126 ALA D 132 1 7 HELIX 19 AC1 THR D 186 HIS D 193 1 8 SHEET 1 AA110 ASN A 354 ARG A 357 0 SHEET 2 AA110 ASN A 394 ARG A 403 -1 O SER A 399 N ASN A 354 SHEET 3 AA110 PRO A 507 GLU A 516 -1 O TYR A 508 N ILE A 402 SHEET 4 AA110 GLY A 431 ASN A 437 -1 N ILE A 434 O VAL A 511 SHEET 5 AA110 THR A 376 VAL A 382 -1 N LYS A 378 O VAL A 433 SHEET 6 AA110 THR B 376 VAL B 382 -1 O CYS B 379 N GLY A 381 SHEET 7 AA110 GLY B 431 ASN B 437 -1 O VAL B 433 N LYS B 378 SHEET 8 AA110 PRO B 507 VAL B 511 -1 O VAL B 511 N ILE B 434 SHEET 9 AA110 ASN B 394 ARG B 403 -1 N PHE B 400 O VAL B 510 SHEET 10 AA110 ASN B 354 ARG B 357 -1 N ASN B 354 O SER B 399 SHEET 1 AA210 ASN A 354 ARG A 357 0 SHEET 2 AA210 ASN A 394 ARG A 403 -1 O SER A 399 N ASN A 354 SHEET 3 AA210 PRO A 507 GLU A 516 -1 O TYR A 508 N ILE A 402 SHEET 4 AA210 GLY A 431 ASN A 437 -1 N ILE A 434 O VAL A 511 SHEET 5 AA210 THR A 376 VAL A 382 -1 N LYS A 378 O VAL A 433 SHEET 6 AA210 THR B 376 VAL B 382 -1 O CYS B 379 N GLY A 381 SHEET 7 AA210 GLY B 431 ASN B 437 -1 O VAL B 433 N LYS B 378 SHEET 8 AA210 PRO B 507 VAL B 511 -1 O VAL B 511 N ILE B 434 SHEET 9 AA210 ASN B 394 ARG B 403 -1 N PHE B 400 O VAL B 510 SHEET 10 AA210 SER B 514 GLU B 516 -1 O GLU B 516 N ASN B 394 SHEET 1 AA3 3 CYS A 361 VAL A 362 0 SHEET 2 AA3 3 VAL A 524 CYS A 525 1 O CYS A 525 N CYS A 361 SHEET 3 AA3 3 CYS A 391 PHE A 392 -1 N PHE A 392 O VAL A 524 SHEET 1 AA4 2 LEU A 452 ARG A 454 0 SHEET 2 AA4 2 LEU A 492 SER A 494 -1 O GLN A 493 N TYR A 453 SHEET 1 AA5 2 ARG A 466 ASP A 467 0 SHEET 2 AA5 2 SER H 103 GLY H 104 -1 O GLY H 104 N ARG A 466 SHEET 1 AA6 2 TYR A 473 GLN A 474 0 SHEET 2 AA6 2 CYS A 488 TYR A 489 -1 O TYR A 489 N TYR A 473 SHEET 1 AA7 3 CYS B 361 VAL B 362 0 SHEET 2 AA7 3 VAL B 524 CYS B 525 1 O CYS B 525 N CYS B 361 SHEET 3 AA7 3 CYS B 391 PHE B 392 -1 N PHE B 392 O VAL B 524 SHEET 1 AA8 2 LEU B 452 ARG B 454 0 SHEET 2 AA8 2 LEU B 492 SER B 494 -1 O GLN B 493 N TYR B 453 SHEET 1 AA9 2 ARG B 466 ASP B 467 0 SHEET 2 AA9 2 SER C 103 GLY C 104 -1 O GLY C 104 N ARG B 466 SHEET 1 AB1 2 TYR B 473 GLN B 474 0 SHEET 2 AB1 2 CYS B 488 TYR B 489 -1 O TYR B 489 N TYR B 473 SHEET 1 AB2 4 LEU H 4 GLN H 6 0 SHEET 2 AB2 4 VAL H 18 ALA H 24 -1 O LYS H 23 N VAL H 5 SHEET 3 AB2 4 ALA H 79 VAL H 83 -1 O ALA H 79 N CYS H 22 SHEET 4 AB2 4 THR H 69 ALA H 72 -1 N THR H 71 O TYR H 80 SHEET 1 AB3 6 GLU H 10 LYS H 12 0 SHEET 2 AB3 6 THR H 118 VAL H 122 1 O THR H 121 N LYS H 12 SHEET 3 AB3 6 ALA H 92 VAL H 100 -1 N ALA H 92 O VAL H 120 SHEET 4 AB3 6 ILE H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AB3 6 LEU H 45 ILE H 52 -1 O GLU H 46 N ARG H 38 SHEET 6 AB3 6 ILE H 57 TYR H 60 -1 O ILE H 57 N ILE H 52 SHEET 1 AB4 4 GLU H 10 LYS H 12 0 SHEET 2 AB4 4 THR H 118 VAL H 122 1 O THR H 121 N LYS H 12 SHEET 3 AB4 4 ALA H 92 VAL H 100 -1 N ALA H 92 O VAL H 120 SHEET 4 AB4 4 TYR H 110 TRP H 114 -1 O HIS H 113 N THR H 98 SHEET 1 AB5 4 SER H 131 LEU H 135 0 SHEET 2 AB5 4 THR H 146 TYR H 156 -1 O GLY H 150 N LEU H 135 SHEET 3 AB5 4 TYR H 187 PRO H 196 -1 O VAL H 195 N ALA H 147 SHEET 4 AB5 4 HIS H 175 THR H 176 -1 N HIS H 175 O VAL H 192 SHEET 1 AB6 4 SER H 131 LEU H 135 0 SHEET 2 AB6 4 THR H 146 TYR H 156 -1 O GLY H 150 N LEU H 135 SHEET 3 AB6 4 TYR H 187 PRO H 196 -1 O VAL H 195 N ALA H 147 SHEET 4 AB6 4 VAL H 180 LEU H 181 -1 N VAL H 180 O SER H 188 SHEET 1 AB7 3 THR H 162 TRP H 165 0 SHEET 2 AB7 3 ILE H 206 HIS H 211 -1 O ASN H 208 N SER H 164 SHEET 3 AB7 3 THR H 216 ARG H 221 -1 O THR H 216 N HIS H 211 SHEET 1 AB8 4 LEU L 4 THR L 5 0 SHEET 2 AB8 4 VAL L 18 GLY L 24 -1 O THR L 23 N THR L 5 SHEET 3 AB8 4 SER L 72 ILE L 77 -1 O LEU L 75 N ILE L 20 SHEET 4 AB8 4 PHE L 64 ARG L 68 -1 N SER L 67 O SER L 74 SHEET 1 AB9 5 SER L 9 GLY L 12 0 SHEET 2 AB9 5 THR L 106 VAL L 110 1 O LYS L 107 N VAL L 10 SHEET 3 AB9 5 ALA L 86 ASP L 94 -1 N ALA L 86 O LEU L 108 SHEET 4 AB9 5 HIS L 36 GLN L 40 -1 N GLN L 40 O ASP L 87 SHEET 5 AB9 5 LYS L 47 ILE L 50 -1 O LEU L 49 N TRP L 37 SHEET 1 AC1 4 SER L 9 GLY L 12 0 SHEET 2 AC1 4 THR L 106 VAL L 110 1 O LYS L 107 N VAL L 10 SHEET 3 AC1 4 ALA L 86 ASP L 94 -1 N ALA L 86 O LEU L 108 SHEET 4 AC1 4 GLY L 99 PHE L 102 -1 O LEU L 101 N SER L 92 SHEET 1 AC2 4 SER L 119 PHE L 123 0 SHEET 2 AC2 4 ALA L 135 PHE L 144 -1 O LEU L 140 N THR L 121 SHEET 3 AC2 4 TYR L 177 LEU L 185 -1 O LEU L 185 N ALA L 135 SHEET 4 AC2 4 VAL L 164 THR L 166 -1 N GLU L 165 O TYR L 182 SHEET 1 AC3 4 SER L 119 PHE L 123 0 SHEET 2 AC3 4 ALA L 135 PHE L 144 -1 O LEU L 140 N THR L 121 SHEET 3 AC3 4 TYR L 177 LEU L 185 -1 O LEU L 185 N ALA L 135 SHEET 4 AC3 4 SER L 170 LYS L 171 -1 N SER L 170 O ALA L 178 SHEET 1 AC4 4 SER L 158 PRO L 159 0 SHEET 2 AC4 4 THR L 150 ALA L 155 -1 N ALA L 155 O SER L 158 SHEET 3 AC4 4 TYR L 196 HIS L 202 -1 O GLN L 199 N ALA L 152 SHEET 4 AC4 4 SER L 205 VAL L 211 -1 O SER L 205 N HIS L 202 SHEET 1 AC5 4 VAL C 5 GLN C 6 0 SHEET 2 AC5 4 VAL C 18 LYS C 23 -1 O LYS C 23 N VAL C 5 SHEET 3 AC5 4 ALA C 79 VAL C 83 -1 O ALA C 79 N CYS C 22 SHEET 4 AC5 4 VAL C 68 ALA C 72 -1 N THR C 71 O TYR C 80 SHEET 1 AC6 6 GLU C 10 LYS C 12 0 SHEET 2 AC6 6 THR C 118 VAL C 122 1 O THR C 121 N LYS C 12 SHEET 3 AC6 6 ALA C 92 VAL C 100 -1 N ALA C 92 O VAL C 120 SHEET 4 AC6 6 ILE C 34 GLN C 39 -1 N VAL C 37 O TYR C 95 SHEET 5 AC6 6 LEU C 45 ILE C 51 -1 O MET C 48 N TRP C 36 SHEET 6 AC6 6 ALA C 58 TYR C 60 -1 O ASN C 59 N ARG C 50 SHEET 1 AC7 4 GLU C 10 LYS C 12 0 SHEET 2 AC7 4 THR C 118 VAL C 122 1 O THR C 121 N LYS C 12 SHEET 3 AC7 4 ALA C 92 VAL C 100 -1 N ALA C 92 O VAL C 120 SHEET 4 AC7 4 TYR C 110 TRP C 114 -1 O TYR C 110 N VAL C 100 SHEET 1 AC8 4 SER C 131 LEU C 135 0 SHEET 2 AC8 4 THR C 146 TYR C 156 -1 O LYS C 154 N SER C 131 SHEET 3 AC8 4 TYR C 187 PRO C 196 -1 O VAL C 195 N ALA C 147 SHEET 4 AC8 4 VAL C 174 THR C 176 -1 N HIS C 175 O VAL C 192 SHEET 1 AC9 4 SER C 131 LEU C 135 0 SHEET 2 AC9 4 THR C 146 TYR C 156 -1 O LYS C 154 N SER C 131 SHEET 3 AC9 4 TYR C 187 PRO C 196 -1 O VAL C 195 N ALA C 147 SHEET 4 AC9 4 VAL C 180 LEU C 181 -1 N VAL C 180 O SER C 188 SHEET 1 AD1 3 THR C 162 TRP C 165 0 SHEET 2 AD1 3 ILE C 206 HIS C 211 -1 O ASN C 208 N SER C 164 SHEET 3 AD1 3 THR C 216 ARG C 221 -1 O THR C 216 N HIS C 211 SHEET 1 AD2 4 LEU D 4 THR D 5 0 SHEET 2 AD2 4 VAL D 18 GLY D 24 -1 O THR D 23 N THR D 5 SHEET 3 AD2 4 SER D 72 ILE D 77 -1 O LEU D 75 N ILE D 20 SHEET 4 AD2 4 PHE D 64 ARG D 68 -1 N SER D 65 O VAL D 76 SHEET 1 AD3 5 SER D 9 GLY D 12 0 SHEET 2 AD3 5 THR D 106 VAL D 110 1 O THR D 109 N GLY D 12 SHEET 3 AD3 5 ASP D 87 TYR D 93 -1 N TYR D 88 O THR D 106 SHEET 4 AD3 5 HIS D 36 GLN D 40 -1 N GLN D 40 O ASP D 87 SHEET 5 AD3 5 LYS D 47 ILE D 50 -1 O LEU D 49 N TRP D 37 SHEET 1 AD4 4 SER D 9 GLY D 12 0 SHEET 2 AD4 4 THR D 106 VAL D 110 1 O THR D 109 N GLY D 12 SHEET 3 AD4 4 ASP D 87 TYR D 93 -1 N TYR D 88 O THR D 106 SHEET 4 AD4 4 SER D 100 PHE D 102 -1 O LEU D 101 N SER D 92 SHEET 1 AD5 4 SER D 119 PHE D 123 0 SHEET 2 AD5 4 ALA D 135 PHE D 144 -1 O LEU D 140 N THR D 121 SHEET 3 AD5 4 TYR D 177 LEU D 185 -1 O LEU D 185 N ALA D 135 SHEET 4 AD5 4 VAL D 164 THR D 166 -1 N GLU D 165 O TYR D 182 SHEET 1 AD6 4 SER D 119 PHE D 123 0 SHEET 2 AD6 4 ALA D 135 PHE D 144 -1 O LEU D 140 N THR D 121 SHEET 3 AD6 4 TYR D 177 LEU D 185 -1 O LEU D 185 N ALA D 135 SHEET 4 AD6 4 SER D 170 LYS D 171 -1 N SER D 170 O ALA D 178 SHEET 1 AD7 4 SER D 158 PRO D 159 0 SHEET 2 AD7 4 THR D 150 ALA D 155 -1 N ALA D 155 O SER D 158 SHEET 3 AD7 4 TYR D 196 HIS D 202 -1 O GLN D 199 N ALA D 152 SHEET 4 AD7 4 SER D 205 VAL D 211 -1 O SER D 205 N HIS D 202 SSBOND 1 CYS A 336 CYS A 361 1555 1555 2.03 SSBOND 2 CYS A 379 CYS A 432 1555 1555 2.04 SSBOND 3 CYS A 391 CYS A 525 1555 1555 2.04 SSBOND 4 CYS A 480 CYS A 488 1555 1555 2.04 SSBOND 5 CYS B 336 CYS B 361 1555 1555 2.04 SSBOND 6 CYS B 379 CYS B 432 1555 1555 2.06 SSBOND 7 CYS B 391 CYS B 525 1555 1555 2.04 SSBOND 8 CYS B 480 CYS B 488 1555 1555 2.04 SSBOND 9 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 10 CYS H 151 CYS H 207 1555 1555 2.03 SSBOND 11 CYS L 22 CYS L 90 1555 1555 2.04 SSBOND 12 CYS L 139 CYS L 198 1555 1555 2.03 SSBOND 13 CYS C 22 CYS C 96 1555 1555 2.03 SSBOND 14 CYS C 151 CYS C 207 1555 1555 2.02 SSBOND 15 CYS D 22 CYS D 90 1555 1555 2.03 SSBOND 16 CYS D 139 CYS D 198 1555 1555 2.04 CISPEP 1 PHE H 157 PRO H 158 0 -3.80 CISPEP 2 TYR L 145 PRO L 146 0 5.53 CISPEP 3 PHE C 157 PRO C 158 0 -6.76 CISPEP 4 TYR D 145 PRO D 146 0 2.32 CRYST1 173.100 59.060 152.030 90.00 95.45 90.00 C 1 2 1 8 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 0.005777 0.000000 0.000551 0.00000 SCALE2 0.000000 0.016932 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006608 0.00000 MTRIX1 1 0.980810 -0.009756 0.194723 -8.41801 1 MTRIX2 1 -0.012941 -0.999802 0.015094 -14.91716 1 MTRIX3 1 0.194537 -0.017325 -0.980742 83.58831 1 MTRIX1 2 0.983522 0.063461 0.169285 -6.86569 1 MTRIX2 2 0.065342 -0.997848 -0.005554 -11.14705 1 MTRIX3 2 0.168568 0.016524 -0.985552 82.98487 1 MTRIX1 3 0.975996 0.076750 0.203815 -5.98404 1 MTRIX2 3 0.084075 -0.996079 -0.027515 -10.50239 1 MTRIX3 3 0.200904 0.043990 -0.978623 84.61722 1