HEADER ANTIVIRAL PROTEIN 20-APR-21 7OAQ TITLE NANOBODY H3 AND C1 BOUND TO RBD WITH KENT MUTATION COMPND MOL_ID: 1; COMPND 2 MOLECULE: H3; COMPND 3 CHAIN: AAA; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SPIKE PROTEIN S1; COMPND 7 CHAIN: EEE; COMPND 8 ENGINEERED: YES; COMPND 9 MUTATION: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: H3; COMPND 12 CHAIN: FFF; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 3 ORGANISM_TAXID: 9844; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 8 2; SOURCE 9 ORGANISM_COMMON: 2019-NCOV, SARS-COV-2; SOURCE 10 ORGANISM_TAXID: 2697049; SOURCE 11 GENE: S, 2; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 16 ORGANISM_TAXID: 9844; SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS RBD, NANOBODY, HIGH AFFINITY, ANTIVIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.H.NAISMITH,H.MIKOLAJEK JRNL AUTH J.HUO,H.MIKOLAJEK,A.LE BAS,J.CLARK,P.SHARMA,A.KIPAR, JRNL AUTH 2 J.DORMON,C.NORMAN,M.WECKENER,D.CLARE,P.HARRISON,J.TREE, JRNL AUTH 3 K.BUTTIGIEG,F.SALGUERO,R.WATSON,D.KNOTT,O.CARNELL,D.NGABO, JRNL AUTH 4 M.ELMORE,S.FOTHERINGHAM,A.HARDING,P.WARD,L.MOYNIE,M.DUMOUX, JRNL AUTH 5 Y.HALL,J.HISCOX,A.OWEN,W.JAMES,M.CARROLL,J.STEWART, JRNL AUTH 6 J.NAISMITH,R.OWENS JRNL TITL A POTENT SARS-COV-2 NEUTRALISING NANOBODY SHOWS THERAPEUTIC JRNL TITL 2 EFFICACY IN THE SYRIAN GOLDEN HAMSTER MODEL OF COVID-19 JRNL REF RES SQ 2021 JRNL REFN ISSN 2693-5015 JRNL DOI 10.21203/RS.3.RS-548968/V1 REMARK 2 REMARK 2 RESOLUTION. 1.55 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0267 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.98 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 92354 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.155 REMARK 3 FREE R VALUE : 0.178 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.113 REMARK 3 FREE R VALUE TEST SET COUNT : 4722 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.55 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59 REMARK 3 REFLECTION IN BIN (WORKING SET) : 6366 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.39 REMARK 3 BIN R VALUE (WORKING SET) : 0.3890 REMARK 3 BIN FREE R VALUE SET COUNT : 313 REMARK 3 BIN FREE R VALUE : 0.3960 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3511 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 28 REMARK 3 SOLVENT ATOMS : 375 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.16 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.21100 REMARK 3 B22 (A**2) : -1.21100 REMARK 3 B33 (A**2) : 2.42200 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.068 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.060 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.056 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.859 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.974 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.966 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3734 ; 0.008 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 3333 ; 0.003 ; 0.018 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5110 ; 1.398 ; 1.655 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7683 ; 1.340 ; 1.581 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 481 ; 6.728 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 198 ;29.114 ;21.667 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 567 ;12.225 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;14.157 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 478 ; 0.069 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4366 ; 0.007 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 964 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 557 ; 0.210 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 48 ; 0.142 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1765 ; 0.173 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 255 ; 0.174 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1825 ; 2.317 ; 1.126 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1824 ; 2.276 ; 1.125 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2285 ; 2.774 ; 1.701 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2286 ; 2.776 ; 1.703 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1909 ; 3.102 ; 1.395 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1906 ; 3.022 ; 1.389 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2807 ; 3.642 ; 2.007 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2808 ; 3.642 ; 2.009 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 7067 ; 8.608 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 11 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : AA 1 AA 64 REMARK 3 ORIGIN FOR THE GROUP (A): 16.9190 -15.2670 10.6360 REMARK 3 T TENSOR REMARK 3 T11: 0.6369 T22: 0.5405 REMARK 3 T33: 0.1125 T12: -0.1282 REMARK 3 T13: -0.0258 T23: -0.0928 REMARK 3 L TENSOR REMARK 3 L11: 4.1991 L22: 4.6212 REMARK 3 L33: 5.6984 L12: 0.9967 REMARK 3 L13: -1.2366 L23: -0.5286 REMARK 3 S TENSOR REMARK 3 S11: 0.1564 S12: -0.9005 S13: -0.0635 REMARK 3 S21: 0.8081 S22: -0.1031 S23: -0.0449 REMARK 3 S31: -0.0984 S32: 0.3673 S33: -0.0533 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : AA 65 AA 124 REMARK 3 ORIGIN FOR THE GROUP (A): 14.9160 -14.9380 11.4300 REMARK 3 T TENSOR REMARK 3 T11: 0.6387 T22: 0.5447 REMARK 3 T33: 0.1191 T12: -0.1129 REMARK 3 T13: -0.0088 T23: -0.1060 REMARK 3 L TENSOR REMARK 3 L11: 3.4048 L22: 3.8798 REMARK 3 L33: 5.5278 L12: 0.7335 REMARK 3 L13: -0.4104 L23: 0.0517 REMARK 3 S TENSOR REMARK 3 S11: 0.1652 S12: -0.9563 S13: 0.3617 REMARK 3 S21: 0.9783 S22: -0.0710 S23: 0.0457 REMARK 3 S31: -0.4062 S32: 0.2191 S33: -0.0942 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : EE 334 EE 346 REMARK 3 ORIGIN FOR THE GROUP (A): 7.5620 -9.3840 -19.9790 REMARK 3 T TENSOR REMARK 3 T11: 0.2876 T22: 0.2504 REMARK 3 T33: 0.2220 T12: 0.0345 REMARK 3 T13: 0.0232 T23: 0.0164 REMARK 3 L TENSOR REMARK 3 L11: 7.5222 L22: 11.2447 REMARK 3 L33: 1.5734 L12: 5.6725 REMARK 3 L13: -0.8310 L23: -0.3782 REMARK 3 S TENSOR REMARK 3 S11: -0.0338 S12: 0.3370 S13: 0.4751 REMARK 3 S21: -0.3110 S22: 0.1793 S23: 0.3915 REMARK 3 S31: -0.2514 S32: -0.0217 S33: -0.1455 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : EE 347 EE 457 REMARK 3 ORIGIN FOR THE GROUP (A): 14.6550 -19.3950 -14.1080 REMARK 3 T TENSOR REMARK 3 T11: 0.1973 T22: 0.1823 REMARK 3 T33: 0.0259 T12: -0.0339 REMARK 3 T13: 0.0062 T23: -0.0252 REMARK 3 L TENSOR REMARK 3 L11: 1.3974 L22: 2.8087 REMARK 3 L33: 1.4508 L12: 0.6187 REMARK 3 L13: -0.5455 L23: 0.2228 REMARK 3 S TENSOR REMARK 3 S11: 0.1320 S12: -0.1528 S13: 0.1772 REMARK 3 S21: 0.2330 S22: -0.0535 S23: -0.0101 REMARK 3 S31: -0.1717 S32: 0.1325 S33: -0.0785 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : EE 458 EE 473 REMARK 3 ORIGIN FOR THE GROUP (A): 20.3660 -33.2700 -23.4050 REMARK 3 T TENSOR REMARK 3 T11: 0.1535 T22: 0.2082 REMARK 3 T33: 0.1083 T12: 0.0022 REMARK 3 T13: 0.0186 T23: -0.0178 REMARK 3 L TENSOR REMARK 3 L11: 0.6925 L22: 6.7499 REMARK 3 L33: 1.4181 L12: 1.6782 REMARK 3 L13: 0.3926 L23: -0.1091 REMARK 3 S TENSOR REMARK 3 S11: -0.0015 S12: 0.1036 S13: -0.1801 REMARK 3 S21: -0.0667 S22: 0.1260 S23: -0.5159 REMARK 3 S31: 0.0294 S32: 0.3680 S33: -0.1246 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : EE 474 EE 515 REMARK 3 ORIGIN FOR THE GROUP (A): 10.2860 -34.8610 -16.1490 REMARK 3 T TENSOR REMARK 3 T11: 0.1558 T22: 0.1689 REMARK 3 T33: 0.0053 T12: -0.0030 REMARK 3 T13: -0.0066 T23: 0.0096 REMARK 3 L TENSOR REMARK 3 L11: 0.6111 L22: 2.5967 REMARK 3 L33: 0.8115 L12: 0.4650 REMARK 3 L13: 0.0283 L23: 0.5228 REMARK 3 S TENSOR REMARK 3 S11: 0.0270 S12: -0.0764 S13: -0.0137 REMARK 3 S21: 0.1636 S22: -0.0046 S23: 0.0481 REMARK 3 S31: 0.0294 S32: 0.1284 S33: -0.0224 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : EE 516 EE 530 REMARK 3 ORIGIN FOR THE GROUP (A): 25.0000 -1.5380 -21.1170 REMARK 3 T TENSOR REMARK 3 T11: 0.5515 T22: 0.4368 REMARK 3 T33: 0.3444 T12: 0.0664 REMARK 3 T13: 0.1365 T23: -0.1676 REMARK 3 L TENSOR REMARK 3 L11: 9.1567 L22: 4.7740 REMARK 3 L33: 11.0153 L12: -5.9370 REMARK 3 L13: -9.8607 L23: 5.8855 REMARK 3 S TENSOR REMARK 3 S11: 0.4839 S12: -0.2334 S13: 1.0507 REMARK 3 S21: 0.2235 S22: 0.5469 S23: -0.6736 REMARK 3 S31: -0.6990 S32: 0.0259 S33: -1.0308 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : FF 1 FF 12 REMARK 3 ORIGIN FOR THE GROUP (A): -10.2930 -49.6620 -35.7650 REMARK 3 T TENSOR REMARK 3 T11: 0.1676 T22: 0.2424 REMARK 3 T33: 0.0325 T12: -0.0257 REMARK 3 T13: -0.0174 T23: -0.0034 REMARK 3 L TENSOR REMARK 3 L11: 4.1113 L22: 11.0520 REMARK 3 L33: 2.8007 L12: 1.1374 REMARK 3 L13: 0.6521 L23: -2.4583 REMARK 3 S TENSOR REMARK 3 S11: -0.0056 S12: -0.0157 S13: 0.0472 REMARK 3 S21: 0.1384 S22: -0.0576 S23: 0.2260 REMARK 3 S31: 0.0705 S32: -0.2334 S33: 0.0632 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : FF 13 FF 36 REMARK 3 ORIGIN FOR THE GROUP (A): -2.8620 -49.4640 -35.6160 REMARK 3 T TENSOR REMARK 3 T11: 0.1731 T22: 0.1809 REMARK 3 T33: 0.0106 T12: -0.0004 REMARK 3 T13: -0.0132 T23: -0.0164 REMARK 3 L TENSOR REMARK 3 L11: 2.8876 L22: 2.0772 REMARK 3 L33: 2.8532 L12: -0.1222 REMARK 3 L13: 0.8739 L23: 0.2678 REMARK 3 S TENSOR REMARK 3 S11: 0.0342 S12: 0.2656 S13: -0.0814 REMARK 3 S21: -0.0732 S22: -0.0267 S23: 0.1285 REMARK 3 S31: 0.1386 S32: 0.0098 S33: -0.0075 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : FF 37 FF 47 REMARK 3 ORIGIN FOR THE GROUP (A): -9.3170 -55.3110 -21.8180 REMARK 3 T TENSOR REMARK 3 T11: 0.3509 T22: 0.2717 REMARK 3 T33: 0.2320 T12: 0.0022 REMARK 3 T13: 0.0872 T23: 0.0594 REMARK 3 L TENSOR REMARK 3 L11: 11.6513 L22: 0.4816 REMARK 3 L33: 6.2377 L12: 2.1912 REMARK 3 L13: -3.1713 L23: -0.1484 REMARK 3 S TENSOR REMARK 3 S11: 0.1910 S12: -0.6731 S13: -0.0359 REMARK 3 S21: 0.1337 S22: -0.1349 S23: 0.0566 REMARK 3 S31: 0.3264 S32: -0.5174 S33: -0.0560 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : FF 48 FF 127 REMARK 3 ORIGIN FOR THE GROUP (A): -0.9780 -51.4620 -28.8150 REMARK 3 T TENSOR REMARK 3 T11: 0.1687 T22: 0.1334 REMARK 3 T33: 0.0261 T12: -0.0017 REMARK 3 T13: -0.0135 T23: 0.0020 REMARK 3 L TENSOR REMARK 3 L11: 1.7353 L22: 0.7892 REMARK 3 L33: 2.0528 L12: 0.1149 REMARK 3 L13: 0.7317 L23: 0.0942 REMARK 3 S TENSOR REMARK 3 S11: 0.0407 S12: 0.0002 S13: -0.1809 REMARK 3 S21: -0.0070 S22: -0.0097 S23: 0.0497 REMARK 3 S31: 0.2115 S32: -0.0529 S33: -0.0310 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK BULK SOLVENT REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.10 REMARK 3 ION PROBE RADIUS : 0.70 REMARK 3 SHRINKAGE RADIUS : 0.70 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 7OAQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292115387. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-FEB-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I04 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93033 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550 REMARK 200 RESOLUTION RANGE LOW (A) : 53.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 26.80 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0 REMARK 200 DATA REDUNDANCY IN SHELL : 27.60 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.600 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: 7OAP REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.27 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M LITHIUM CHLORIDE, 0.1 M CITRATE REMARK 280 PH 4, 20 % PEG 6000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 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 56.35450 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 52.92850 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 52.92850 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 84.53175 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 52.92850 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 52.92850 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 28.17725 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 52.92850 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.92850 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 84.53175 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 52.92850 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.92850 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 28.17725 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 56.35450 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: 3450 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21020 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: AAA, EEE, FFF 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH E 801 LIES ON A SPECIAL POSITION. 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 LYS A 125 REMARK 465 HIS A 126 REMARK 465 HIS A 127 REMARK 465 HIS A 128 REMARK 465 HIS A 129 REMARK 465 HIS A 130 REMARK 465 HIS A 131 REMARK 465 PRO E 330 REMARK 465 ASN E 331 REMARK 465 ILE E 332 REMARK 465 THR E 333 REMARK 465 THR E 531 REMARK 465 ASN E 532 REMARK 465 LYS E 533 REMARK 465 HIS E 534 REMARK 465 HIS E 535 REMARK 465 HIS E 536 REMARK 465 HIS E 537 REMARK 465 HIS E 538 REMARK 465 HIS E 539 REMARK 465 MET F -1 REMARK 465 ALA F 0 REMARK 465 LYS F 128 REMARK 465 HIS F 129 REMARK 465 HIS F 130 REMARK 465 HIS F 131 REMARK 465 HIS F 132 REMARK 465 HIS F 133 REMARK 465 HIS F 134 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 HOHEE 721 O HOHFF 364 1.89 REMARK 500 O6 CITEE 602 O HOHEE 701 1.97 REMARK 500 O4 CITEE 602 O HOHEE 702 2.01 REMARK 500 O3 CITEE 602 O HOHEE 703 2.01 REMARK 500 O HOHFF 394 O HOHFF 400 2.09 REMARK 500 O HOHEE 767 O HOHEE 868 2.17 REMARK 500 OE2 GLUEE 406 O5 CITEE 602 2.19 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 METAA 85 49.68 39.43 REMARK 500 ALAAA 92 166.96 173.87 REMARK 500 ASNEE 422 -55.45 -125.79 REMARK 500 ALAFF 92 168.98 179.85 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 E 906 DISTANCE = 6.57 ANGSTROMS DBREF 7OAQAA 1 131 PDB 7OAQ 7OAQ 1 131 DBREF 7OAQEE 330 532 UNP P0DTC2 SPIKE_SARS2 330 532 DBREF 7OAQFF -1 134 PDB 7OAQ 7OAQ -1 134 SEQADV 7OAQ TYREE 501 UNP P0DTC2 ASN 501 ENGINEERED MUTATION SEQADV 7OAQ LYSEE 533 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAQ HISEE 534 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAQ HISEE 535 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAQ HISEE 536 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAQ HISEE 537 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAQ HISEE 538 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAQ HISEE 539 UNP P0DTC2 EXPRESSION TAG SEQRES 1AA 131 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2AA 131 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3AA 131 PHE THR ASN ASP PHE TYR SER ILE ALA TRP PHE ARG GLN SEQRES 4AA 131 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER TRP LEU SER SEQRES 5AA 131 VAL SER ASP ASN THR PRO THR TYR VAL ASP SER VAL LYS SEQRES 6AA 131 ASP ARG PHE THR ILE SER ARG HIS ASN ALA ASN ASN THR SEQRES 7AA 131 VAL TYR LEU GLN MET ASN MET LEU LYS PRO GLU ASP THR SEQRES 8AA 131 ALA ILE TYR TYR CYS ALA ALA GLY ARG PHE ALA GLY ARG SEQRES 9AA 131 ASP THR TRP PRO SER SER TYR ASP TYR TRP GLY GLN GLY SEQRES 10AA 131 THR GLN VAL THR VAL SER SER LYS HIS HIS HIS HIS HIS SEQRES 11AA 131 HIS SEQRES 1EE 210 PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE SEQRES 2EE 210 ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG SEQRES 3EE 210 LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU SEQRES 4EE 210 TYR ASN SER ALA SER PHE SER THR PHE LYS CYS TYR GLY SEQRES 5EE 210 VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN SEQRES 6EE 210 VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL SEQRES 7EE 210 ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP SEQRES 8EE 210 TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL SEQRES 9EE 210 ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY SEQRES 10EE 210 GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER SEQRES 11EE 210 ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE SEQRES 12EE 210 TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY SEQRES 13EE 210 PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN SEQRES 14EE 210 PRO THR TYR GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL SEQRES 15EE 210 VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL SEQRES 16EE 210 CYS GLY PRO LYS LYS SER THR ASN LYS HIS HIS HIS HIS SEQRES 17EE 210 HIS HIS SEQRES 1FF 136 MET ALA GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2FF 136 VAL LYS THR GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3FF 136 SER GLY ARG THR PHE SER THR TYR SER MET GLY TRP PHE SEQRES 4FF 136 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA GLY SEQRES 5FF 136 MET ARG TRP THR GLY SER SER THR PHE TYR SER ASP SER SEQRES 6FF 136 VAL LYS GLY ARG PHE THR VAL SER ARG ASN ASN ALA LYS SEQRES 7FF 136 ASP THR VAL TYR LEU HIS MET ASN SER LEU LYS PRO GLU SEQRES 8FF 136 ASP THR ALA VAL TYR TYR CYS ALA ILE THR THR ILE VAL SEQRES 9FF 136 ARG ALA TYR TYR THR GLU TYR THR GLU ALA ASP PHE GLY SEQRES 10FF 136 SER TRP GLY GLN GLY THR GLN VAL THR VAL SER SER LYS SEQRES 11FF 136 HIS HIS HIS HIS HIS HIS HET NAG EE 601 14 HET CIT EE 602 13 HET CL FF 201 1 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM CIT CITRIC ACID HETNAM CL CHLORIDE ION FORMUL 4 NAG C8 H15 N O6 FORMUL 5 CIT C6 H8 O7 FORMUL 6 CL CL 1- FORMUL 7 HOH *375(H2 O) HELIX 1 AA1 ASPAA 62 LYSAA 65 5 4 HELIX 2 AA2 LYSAA 87 THRAA 91 5 5 HELIX 3 AA3 TRPAA 107 TYRAA 111 5 5 HELIX 4 AA4 PHEEE 338 ASNEE 343 1 6 HELIX 5 AA5 SEREE 349 TRPEE 353 5 5 HELIX 6 AA6 ASPEE 364 ASNEE 370 1 7 HELIX 7 AA7 SEREE 383 ASNEE 388 1 6 HELIX 8 AA8 ASPEE 405 ILEEE 410 5 6 HELIX 9 AA9 GLYEE 416 ASNEE 422 1 7 HELIX 10 AB1 SEREE 438 SEREE 443 1 6 HELIX 11 AB2 GLYEE 502 TYREE 505 5 4 HELIX 12 AB3 PROEE 527 SEREE 530 5 4 HELIX 13 AB4 ARGFF 27 TYRFF 32 1 6 HELIX 14 AB5 LYSFF 87 THRFF 91 5 5 HELIX 15 AB6 TYRFF 105 TYRFF 109 5 5 HELIX 16 AB7 THRFF 110 PHEFF 114 5 5 SHEET 1 AA1 4 GLNAA 3 SERAA 7 0 SHEET 2 AA1 4 LEUAA 18 SERAA 25 -1 O ALAAA 23 N VALAA 5 SHEET 3 AA1 4 THRAA 78 METAA 83 -1 O METAA 83 N LEUAA 18 SHEET 4 AA1 4 PHEAA 68 HISAA 73 -1 N THRAA 69 O GLNAA 82 SHEET 1 AA2 6 GLYAA 10 VALAA 12 0 SHEET 2 AA2 6 THRAA 118 VALAA 122 1 O THRAA 121 N VALAA 12 SHEET 3 AA2 6 ALAAA 92 GLYAA 99 -1 N TYRAA 94 O THRAA 118 SHEET 4 AA2 6 SERAA 33 GLNAA 39 -1 N PHEAA 37 O TYRAA 95 SHEET 5 AA2 6 GLUAA 46 SERAA 52 -1 O VALAA 48 N TRPAA 36 SHEET 6 AA2 6 THRAA 57 TYRAA 60 -1 O THRAA 57 N SERAA 52 SHEET 1 AA3 4 GLYAA 10 VALAA 12 0 SHEET 2 AA3 4 THRAA 118 VALAA 122 1 O THRAA 121 N VALAA 12 SHEET 3 AA3 4 ALAAA 92 GLYAA 99 -1 N TYRAA 94 O THRAA 118 SHEET 4 AA3 4 TYRAA 113 TRPAA 114 -1 O TYRAA 113 N ALAAA 98 SHEET 1 AA4 6 ALAAA 102 ASPAA 105 0 SHEET 2 AA4 6 THREE 376 TYREE 380 -1 O CYSEE 379 N ALAAA 102 SHEET 3 AA4 6 GLYEE 431 ASNEE 437 -1 O GLYEE 431 N TYREE 380 SHEET 4 AA4 6 PROEE 507 GLUEE 516 -1 O LEUEE 513 N CYSEE 432 SHEET 5 AA4 6 ASNEE 394 ARGEE 403 -1 N ILEEE 402 O TYREE 508 SHEET 6 AA4 6 ASNEE 354 ILEEE 358 -1 N ILEEE 358 O VALEE 395 SHEET 1 AA5 3 CYSEE 361 VALEE 362 0 SHEET 2 AA5 3 VALEE 524 CYSEE 525 1 O CYSEE 525 N CYSEE 361 SHEET 3 AA5 3 CYSEE 391 PHEEE 392 -1 N PHEEE 392 O VALEE 524 SHEET 1 AA6 2 LEUEE 452 ARGEE 454 0 SHEET 2 AA6 2 LEUEE 492 SEREE 494 -1 O GLNEE 493 N TYREE 453 SHEET 1 AA7 2 TYREE 473 GLNEE 474 0 SHEET 2 AA7 2 CYSEE 488 TYREE 489 -1 O TYREE 489 N TYREE 473 SHEET 1 AA8 4 VALFF 5 GLYFF 8 0 SHEET 2 AA8 4 LEUFF 18 ALAFF 23 -1 O ALAFF 23 N VALFF 5 SHEET 3 AA8 4 THRFF 78 METFF 83 -1 O METFF 83 N LEUFF 18 SHEET 4 AA8 4 PHEFF 68 ARGFF 72 -1 N THRFF 69 O HISFF 82 SHEET 1 AA9 6 GLYFF 10 LYSFF 13 0 SHEET 2 AA9 6 THRFF 121 SERFF 126 1 O THRFF 124 N GLYFF 10 SHEET 3 AA9 6 ALAFF 92 THRFF 99 -1 N TYRFF 94 O THRFF 121 SHEET 4 AA9 6 SERFF 33 GLNFF 39 -1 N PHEFF 37 O TYRFF 95 SHEET 5 AA9 6 GLUFF 46 METFF 51 -1 O ALAFF 49 N TRPFF 36 SHEET 6 AA9 6 THRFF 58 TYRFF 60 -1 O PHEFF 59 N GLYFF 50 SSBOND 1 CYSAA 22 CYSAA 96 1555 1555 2.08 SSBOND 2 CYSEE 336 CYSEE 361 1555 1555 2.06 SSBOND 3 CYSEE 379 CYSEE 432 1555 1555 2.11 SSBOND 4 CYSEE 391 CYSEE 525 1555 1555 2.07 SSBOND 5 CYSEE 480 CYSEE 488 1555 1555 2.08 SSBOND 6 CYSFF 22 CYSFF 96 1555 1555 2.14 LINK ND2 ASNEE 343 C1 NAGEE 601 1555 1555 1.45 CRYST1 105.857 105.857 112.709 90.00 90.00 90.00 P 43 21 2 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 0.009447 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009447 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008872 0.00000