HEADER ANTIVIRAL PROTEIN 19-APR-21 7OAP TITLE NANOBODY H3 AND C1 BOUND TO RBD COMPND MOL_ID: 1; COMPND 2 MOLECULE: C1 NANOBODY; 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 MOL_ID: 3; COMPND 10 MOLECULE: H3 NANOBODY; COMPND 11 CHAIN: FFF; COMPND 12 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. 1.90 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) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.25 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 50645 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) : 0.180 REMARK 3 FREE R VALUE : 0.204 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.244 REMARK 3 FREE R VALUE TEST SET COUNT : 2656 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3478 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.67 REMARK 3 BIN R VALUE (WORKING SET) : 0.3290 REMARK 3 BIN FREE R VALUE SET COUNT : 181 REMARK 3 BIN FREE R VALUE : 0.3070 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3507 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 28 REMARK 3 SOLVENT ATOMS : 235 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.25 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.75900 REMARK 3 B22 (A**2) : 0.75900 REMARK 3 B33 (A**2) : -1.51800 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): 0.119 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.111 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.099 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.988 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3667 ; 0.010 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 3267 ; 0.001 ; 0.018 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4999 ; 1.528 ; 1.655 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7513 ; 1.342 ; 1.583 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 459 ; 7.375 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 196 ;28.989 ;21.684 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 552 ;13.460 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;14.764 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 464 ; 0.068 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4275 ; 0.008 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 947 ; 0.002 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 542 ; 0.192 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 36 ; 0.220 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1763 ; 0.175 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 192 ; 0.146 ; 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): 1803 ; 2.040 ; 2.033 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1802 ; 2.036 ; 2.031 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2252 ; 2.937 ; 3.033 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2253 ; 2.938 ; 3.035 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1864 ; 3.370 ; 2.399 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1861 ; 3.194 ; 2.390 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2740 ; 4.978 ; 3.469 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2741 ; 4.977 ; 3.473 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): NULL ; NULL ; NULL 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 : 12 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 27 REMARK 3 ORIGIN FOR THE GROUP (A): 19.4470 -15.5020 17.3320 REMARK 3 T TENSOR REMARK 3 T11: 0.7076 T22: 0.7091 REMARK 3 T33: 0.2006 T12: -0.0873 REMARK 3 T13: -0.1278 T23: -0.0139 REMARK 3 L TENSOR REMARK 3 L11: 9.6235 L22: 3.6658 REMARK 3 L33: 6.1886 L12: -0.6203 REMARK 3 L13: -5.7949 L23: 1.2379 REMARK 3 S TENSOR REMARK 3 S11: 0.1661 S12: -0.7571 S13: 0.1197 REMARK 3 S21: 0.4970 S22: -0.0418 S23: -0.4532 REMARK 3 S31: -0.1371 S32: 0.4740 S33: -0.1244 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 28 AA 64 REMARK 3 ORIGIN FOR THE GROUP (A): 15.0170 -14.8940 6.4290 REMARK 3 T TENSOR REMARK 3 T11: 0.5082 T22: 0.4210 REMARK 3 T33: 0.0836 T12: -0.0658 REMARK 3 T13: -0.0430 T23: -0.0722 REMARK 3 L TENSOR REMARK 3 L11: 6.7188 L22: 4.6618 REMARK 3 L33: 4.8892 L12: 0.7238 REMARK 3 L13: -1.2712 L23: -0.3295 REMARK 3 S TENSOR REMARK 3 S11: 0.0778 S12: -0.5581 S13: -0.0074 REMARK 3 S21: 0.3728 S22: -0.0438 S23: 0.1771 REMARK 3 S31: -0.0934 S32: 0.0374 S33: -0.0341 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 : AA 65 AA 89 REMARK 3 ORIGIN FOR THE GROUP (A): 14.0630 -8.4830 13.9860 REMARK 3 T TENSOR REMARK 3 T11: 0.6883 T22: 0.5300 REMARK 3 T33: 0.2076 T12: -0.0447 REMARK 3 T13: -0.0353 T23: -0.1135 REMARK 3 L TENSOR REMARK 3 L11: 11.2775 L22: 5.7656 REMARK 3 L33: 3.6114 L12: 0.3835 REMARK 3 L13: -1.9916 L23: -1.0252 REMARK 3 S TENSOR REMARK 3 S11: 0.0581 S12: -0.4716 S13: 0.5480 REMARK 3 S21: 0.3191 S22: -0.0362 S23: 0.1585 REMARK 3 S31: -0.3715 S32: 0.1461 S33: -0.0219 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 : AA 90 AA 124 REMARK 3 ORIGIN FOR THE GROUP (A): 15.4910 -20.0510 9.2620 REMARK 3 T TENSOR REMARK 3 T11: 0.5001 T22: 0.4583 REMARK 3 T33: 0.1294 T12: -0.0648 REMARK 3 T13: -0.0346 T23: -0.0048 REMARK 3 L TENSOR REMARK 3 L11: 2.6789 L22: 2.0920 REMARK 3 L33: 5.7778 L12: 0.6240 REMARK 3 L13: -0.7966 L23: 0.2242 REMARK 3 S TENSOR REMARK 3 S11: -0.0009 S12: -0.7372 S13: -0.1751 REMARK 3 S21: 0.5542 S22: -0.0515 S23: -0.1395 REMARK 3 S31: 0.1579 S32: 0.3609 S33: 0.0524 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 334 EE 346 REMARK 3 ORIGIN FOR THE GROUP (A): 7.5740 -9.5450 -19.8410 REMARK 3 T TENSOR REMARK 3 T11: 0.3066 T22: 0.3246 REMARK 3 T33: 0.2621 T12: 0.0369 REMARK 3 T13: 0.0023 T23: 0.0120 REMARK 3 L TENSOR REMARK 3 L11: 5.8985 L22: 15.2056 REMARK 3 L33: 2.2483 L12: 4.9213 REMARK 3 L13: -2.2155 L23: -1.9432 REMARK 3 S TENSOR REMARK 3 S11: -0.1067 S12: 0.2879 S13: 0.4003 REMARK 3 S21: -0.3772 S22: 0.1490 S23: 0.2018 REMARK 3 S31: -0.2356 S32: -0.0232 S33: -0.0423 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 347 EE 457 REMARK 3 ORIGIN FOR THE GROUP (A): 14.7910 -19.5470 -14.0640 REMARK 3 T TENSOR REMARK 3 T11: 0.1802 T22: 0.1907 REMARK 3 T33: 0.0683 T12: -0.0433 REMARK 3 T13: -0.0003 T23: -0.0215 REMARK 3 L TENSOR REMARK 3 L11: 1.3444 L22: 2.8423 REMARK 3 L33: 1.5433 L12: 0.5242 REMARK 3 L13: -0.3995 L23: 0.2463 REMARK 3 S TENSOR REMARK 3 S11: 0.0827 S12: -0.1467 S13: 0.1353 REMARK 3 S21: 0.1948 S22: -0.0300 S23: -0.0439 REMARK 3 S31: -0.1476 S32: 0.1089 S33: -0.0527 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 458 EE 473 REMARK 3 ORIGIN FOR THE GROUP (A): 20.4690 -33.4650 -23.4330 REMARK 3 T TENSOR REMARK 3 T11: 0.1613 T22: 0.2367 REMARK 3 T33: 0.1268 T12: -0.0110 REMARK 3 T13: 0.0243 T23: -0.0192 REMARK 3 L TENSOR REMARK 3 L11: 1.2948 L22: 7.1322 REMARK 3 L33: 1.7780 L12: 1.5512 REMARK 3 L13: 0.4788 L23: -0.0111 REMARK 3 S TENSOR REMARK 3 S11: -0.0205 S12: 0.1092 S13: -0.1924 REMARK 3 S21: -0.2929 S22: 0.1513 S23: -0.5349 REMARK 3 S31: -0.0124 S32: 0.4454 S33: -0.1308 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 : EE 474 EE 530 REMARK 3 ORIGIN FOR THE GROUP (A): 14.3850 -26.0120 -17.4990 REMARK 3 T TENSOR REMARK 3 T11: 0.1732 T22: 0.2230 REMARK 3 T33: 0.0235 T12: -0.0135 REMARK 3 T13: -0.0219 T23: 0.0056 REMARK 3 L TENSOR REMARK 3 L11: 1.4145 L22: 1.6996 REMARK 3 L33: 0.8624 L12: 0.5632 REMARK 3 L13: -0.4729 L23: 0.0064 REMARK 3 S TENSOR REMARK 3 S11: 0.0906 S12: -0.1140 S13: 0.1258 REMARK 3 S21: 0.1525 S22: -0.0435 S23: 0.1026 REMARK 3 S31: -0.0933 S32: 0.1446 S33: -0.0472 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 1 FF 36 REMARK 3 ORIGIN FOR THE GROUP (A): -5.2060 -49.5290 -35.7400 REMARK 3 T TENSOR REMARK 3 T11: 0.1682 T22: 0.1938 REMARK 3 T33: 0.0589 T12: -0.0187 REMARK 3 T13: 0.0014 T23: -0.0076 REMARK 3 L TENSOR REMARK 3 L11: 3.2324 L22: 3.7659 REMARK 3 L33: 3.0104 L12: 1.0084 REMARK 3 L13: 1.0750 L23: -0.6787 REMARK 3 S TENSOR REMARK 3 S11: -0.0667 S12: 0.1821 S13: -0.0831 REMARK 3 S21: -0.2031 S22: 0.1582 S23: 0.1241 REMARK 3 S31: 0.1647 S32: -0.1495 S33: -0.0915 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 46 REMARK 3 ORIGIN FOR THE GROUP (A): -10.2540 -55.8620 -21.8490 REMARK 3 T TENSOR REMARK 3 T11: 0.3154 T22: 0.2956 REMARK 3 T33: 0.2489 T12: -0.0268 REMARK 3 T13: 0.0110 T23: 0.0221 REMARK 3 L TENSOR REMARK 3 L11: 9.1759 L22: 0.0686 REMARK 3 L33: 6.1908 L12: 0.7657 REMARK 3 L13: -1.8248 L23: -0.0119 REMARK 3 S TENSOR REMARK 3 S11: -0.0177 S12: -0.4966 S13: -0.1154 REMARK 3 S21: 0.0110 S22: -0.0377 S23: -0.0032 REMARK 3 S31: 0.4665 S32: -0.4874 S33: 0.0554 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 47 FF 88 REMARK 3 ORIGIN FOR THE GROUP (A): 2.7290 -52.6200 -31.5850 REMARK 3 T TENSOR REMARK 3 T11: 0.1783 T22: 0.1524 REMARK 3 T33: 0.0800 T12: 0.0098 REMARK 3 T13: -0.0127 T23: -0.0082 REMARK 3 L TENSOR REMARK 3 L11: 1.5807 L22: 0.8395 REMARK 3 L33: 2.1164 L12: -0.0923 REMARK 3 L13: 0.8231 L23: -0.3515 REMARK 3 S TENSOR REMARK 3 S11: 0.0292 S12: 0.0629 S13: -0.2153 REMARK 3 S21: -0.0758 S22: 0.0172 S23: -0.0343 REMARK 3 S31: 0.2489 S32: 0.0679 S33: -0.0463 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : FF 89 FF 127 REMARK 3 ORIGIN FOR THE GROUP (A): -5.0880 -50.2010 -25.2990 REMARK 3 T TENSOR REMARK 3 T11: 0.1583 T22: 0.1342 REMARK 3 T33: 0.0434 T12: 0.0095 REMARK 3 T13: 0.0003 T23: 0.0197 REMARK 3 L TENSOR REMARK 3 L11: 3.1082 L22: 1.3456 REMARK 3 L33: 2.2849 L12: 0.5095 REMARK 3 L13: 0.8147 L23: 0.6097 REMARK 3 S TENSOR REMARK 3 S11: -0.0097 S12: -0.1015 S13: -0.1381 REMARK 3 S21: 0.0152 S22: -0.0123 S23: 0.1442 REMARK 3 S31: 0.1503 S32: -0.1777 S33: 0.0219 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 : 1.00 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 7OAP 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_1292115384. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-SEP-20 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 : I03 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 : 50645 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 62.254 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 25.40 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.4000 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) : 1.95 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 22.10 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.700 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: 6ZBP REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.18 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94 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 56.26950 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 52.84150 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 52.84150 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 84.40425 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 52.84150 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 52.84150 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 28.13475 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 52.84150 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.84150 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 84.40425 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 52.84150 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.84150 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 28.13475 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 56.26950 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: 3330 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21210 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 A 218 LIES ON A SPECIAL POSITION. REMARK 375 HOH E 701 LIES ON A SPECIAL POSITION. REMARK 375 HOH E 765 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 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 739 O HOHEE 811 2.01 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 HOHEE 810 O HOHEE 810 8554 1.80 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 ARGFF 19 CG - CD - NE ANGL. DEV. = 12.8 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 SERAA 25 -98.53 -92.67 REMARK 500 METAA 85 48.99 38.12 REMARK 500 ALAAA 92 167.91 179.87 REMARK 500 ASNEE 422 -52.37 -126.73 REMARK 500 LYSEE 529 67.69 -100.86 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 SERAA 25 GLYAA 26 -149.19 REMARK 500 REMARK 500 REMARK: NULL DBREF 7OAPAA 1 131 PDB 7OAP 7OAP 1 131 DBREF 7OAPEE 331 532 UNP P0DTC2 SPIKE_SARS2 331 532 DBREF 7OAPFF -1 134 PDB 7OAP 7OAP -1 134 SEQADV 7OAP LYSEE 533 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAP HISEE 534 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAP HISEE 535 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAP HISEE 536 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAP HISEE 537 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAP HISEE 538 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAP 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 209 ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN SEQRES 2EE 209 ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS SEQRES 3EE 209 ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR SEQRES 4EE 209 ASN SER ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SEQRES 5EE 209 SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL SEQRES 6EE 209 TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG SEQRES 7EE 209 GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR SEQRES 8EE 209 ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE SEQRES 9EE 209 ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY SEQRES 10EE 209 ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN SEQRES 11EE 209 LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR SEQRES 12EE 209 GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE SEQRES 13EE 209 ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO SEQRES 14EE 209 THR ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL SEQRES 15EE 209 LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS SEQRES 16EE 209 GLY PRO LYS LYS SER THR ASN LYS HIS HIS HIS HIS HIS SEQRES 17EE 209 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 *235(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 ARGFF 27 TYRFF 32 1 6 HELIX 13 AB4 LYSFF 87 THRFF 91 5 5 HELIX 14 AB5 TYRFF 105 TYRFF 109 5 5 HELIX 15 AB6 THRFF 110 PHEFF 114 5 5 SHEET 1 AA1 4 LEUAA 4 SERAA 7 0 SHEET 2 AA1 4 LEUAA 18 ALAAA 24 -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 GLYAA 10 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 SERAA 49 N TRPAA 36 SHEET 6 AA2 6 THRAA 57 TYRAA 60 -1 O THRAA 59 N TRPAA 50 SHEET 1 AA3 4 GLYAA 10 VALAA 12 0 SHEET 2 AA3 4 THRAA 118 VALAA 122 1 O THRAA 121 N GLYAA 10 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 VALEE 433 N LYSEE 378 SHEET 4 AA4 6 PROEE 507 GLUEE 516 -1 O VALEE 511 N ILEEE 434 SHEET 5 AA4 6 ASNEE 394 ARGEE 403 -1 N ASPEE 398 O VALEE 512 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 SERFF 7 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 SERFF 71 O TYRFF 80 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 2.13 SSBOND 2 CYSEE 336 CYSEE 361 1555 1555 2.07 SSBOND 3 CYSEE 379 CYSEE 432 1555 1555 2.20 SSBOND 4 CYSEE 391 CYSEE 525 1555 1555 2.14 SSBOND 5 CYSEE 480 CYSEE 488 1555 1555 2.12 SSBOND 6 CYSFF 22 CYSFF 96 1555 1555 2.20 LINK ND2 ASNEE 343 C1 NAGEE 601 1555 1555 1.45 CRYST1 105.683 105.683 112.539 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 0.009462 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009462 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008886 0.00000