HEADER ANTIVIRAL PROTEIN 20-APR-21 7OAU TITLE NANOBODY C5 BOUND TO KENT VARIANT RBD (N501Y) COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE PROTEIN S1; COMPND 3 CHAIN: AAA, EEE; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: C5; COMPND 8 CHAIN: BBB, FFF; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_COMMON: 2019-NCOV, SARS-COV-2; SOURCE 5 ORGANISM_TAXID: 2697049; SOURCE 6 GENE: S, 2; SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 11 ORGANISM_TAXID: 9844; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 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. 1.65 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) : 1.65 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.46 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 77679 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) : 0.175 REMARK 3 FREE R VALUE : 0.199 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.861 REMARK 3 FREE R VALUE TEST SET COUNT : 3776 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) : 1.65 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69 REMARK 3 REFLECTION IN BIN (WORKING SET) : 5545 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.95 REMARK 3 BIN R VALUE (WORKING SET) : 0.3160 REMARK 3 BIN FREE R VALUE SET COUNT : 274 REMARK 3 BIN FREE R VALUE : 0.3290 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4892 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 34 REMARK 3 SOLVENT ATOMS : 470 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.12 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.02000 REMARK 3 B22 (A**2) : -2.16300 REMARK 3 B33 (A**2) : 1.76800 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.70700 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.096 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.091 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.078 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.776 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5183 ; 0.007 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 4667 ; 0.001 ; 0.018 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7089 ; 1.337 ; 1.654 REMARK 3 BOND ANGLES OTHERS (DEGREES): 10739 ; 1.323 ; 1.581 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 664 ; 6.913 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 268 ;31.749 ;22.052 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 775 ;11.560 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;16.287 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 670 ; 0.060 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6048 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1328 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 790 ; 0.180 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 92 ; 0.159 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2510 ; 0.168 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 353 ; 0.152 ; 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): 2564 ; 1.314 ; 1.658 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2563 ; 1.314 ; 1.657 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3210 ; 1.893 ; 2.480 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3211 ; 1.892 ; 2.481 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2619 ; 2.179 ; 1.947 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2620 ; 2.179 ; 1.948 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3862 ; 3.356 ; 2.823 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3863 ; 3.355 ; 2.824 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 : 2 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : AAA EEE REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 AA 334 AA 527 NULL REMARK 3 1 EE 334 EE 527 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : BBB FFF REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 2 BB 1 BB 120 NULL REMARK 3 2 FF 1 FF 120 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 18 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 334 AA 340 REMARK 3 ORIGIN FOR THE GROUP (A): 11.4230 -1.1390 -25.5300 REMARK 3 T TENSOR REMARK 3 T11: 0.2311 T22: 0.1540 REMARK 3 T33: 0.1361 T12: 0.0112 REMARK 3 T13: -0.0078 T23: 0.0140 REMARK 3 L TENSOR REMARK 3 L11: 0.8453 L22: 18.9204 REMARK 3 L33: 2.3672 L12: 0.0506 REMARK 3 L13: 1.2185 L23: 3.4616 REMARK 3 S TENSOR REMARK 3 S11: -0.0263 S12: -0.0179 S13: -0.0024 REMARK 3 S21: 0.4218 S22: 0.0568 S23: -0.2744 REMARK 3 S31: 0.0210 S32: 0.0001 S33: -0.0305 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 341 AA 362 REMARK 3 ORIGIN FOR THE GROUP (A): 13.0590 8.7750 -31.4660 REMARK 3 T TENSOR REMARK 3 T11: 0.1737 T22: 0.0882 REMARK 3 T33: 0.0862 T12: 0.0161 REMARK 3 T13: -0.0376 T23: 0.0031 REMARK 3 L TENSOR REMARK 3 L11: 1.0441 L22: 6.5546 REMARK 3 L33: 1.8768 L12: 1.0786 REMARK 3 L13: -0.2402 L23: -2.1966 REMARK 3 S TENSOR REMARK 3 S11: 0.0389 S12: -0.1718 S13: -0.1541 REMARK 3 S21: 0.5111 S22: -0.0841 S23: -0.4401 REMARK 3 S31: 0.1525 S32: 0.0649 S33: 0.0452 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 363 AA 395 REMARK 3 ORIGIN FOR THE GROUP (A): 1.4740 -1.5720 -35.5790 REMARK 3 T TENSOR REMARK 3 T11: 0.2290 T22: 0.1439 REMARK 3 T33: 0.2828 T12: -0.0505 REMARK 3 T13: 0.0539 T23: -0.0143 REMARK 3 L TENSOR REMARK 3 L11: 2.3148 L22: 4.9801 REMARK 3 L33: 0.9402 L12: -1.3651 REMARK 3 L13: -0.7598 L23: -0.0078 REMARK 3 S TENSOR REMARK 3 S11: -0.1953 S12: 0.0388 S13: -0.2127 REMARK 3 S21: 0.3955 S22: 0.0590 S23: 0.5409 REMARK 3 S31: 0.2448 S32: -0.1001 S33: 0.1363 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 396 AA 513 REMARK 3 ORIGIN FOR THE GROUP (A): 8.5110 21.3490 -40.1270 REMARK 3 T TENSOR REMARK 3 T11: 0.0262 T22: 0.0566 REMARK 3 T33: 0.0273 T12: 0.0075 REMARK 3 T13: 0.0028 T23: -0.0150 REMARK 3 L TENSOR REMARK 3 L11: 1.4888 L22: 3.1578 REMARK 3 L33: 1.3008 L12: 1.0192 REMARK 3 L13: -0.5221 L23: -1.0980 REMARK 3 S TENSOR REMARK 3 S11: -0.0320 S12: 0.0251 S13: -0.1020 REMARK 3 S21: -0.0075 S22: 0.0395 S23: 0.1292 REMARK 3 S31: 0.0594 S32: -0.0802 S33: -0.0075 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 : AA 514 AA 527 REMARK 3 ORIGIN FOR THE GROUP (A): 12.9780 -6.9820 -39.5200 REMARK 3 T TENSOR REMARK 3 T11: 0.1586 T22: 0.0837 REMARK 3 T33: 0.2044 T12: -0.0176 REMARK 3 T13: -0.0194 T23: -0.0027 REMARK 3 L TENSOR REMARK 3 L11: 3.9086 L22: 6.5954 REMARK 3 L33: 6.2282 L12: -4.4325 REMARK 3 L13: -3.7229 L23: 3.5869 REMARK 3 S TENSOR REMARK 3 S11: -0.1684 S12: -0.0646 S13: 0.0129 REMARK 3 S21: -0.0008 S22: -0.0694 S23: -0.0629 REMARK 3 S31: 0.1400 S32: -0.0768 S33: 0.2377 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 : BB 1 BB 36 REMARK 3 ORIGIN FOR THE GROUP (A): 0.1440 45.4780 -36.3320 REMARK 3 T TENSOR REMARK 3 T11: 0.1320 T22: 0.0913 REMARK 3 T33: 0.0661 T12: 0.0022 REMARK 3 T13: 0.0351 T23: 0.0003 REMARK 3 L TENSOR REMARK 3 L11: 2.2830 L22: 1.7754 REMARK 3 L33: 0.1136 L12: -0.6084 REMARK 3 L13: 0.3031 L23: 0.1855 REMARK 3 S TENSOR REMARK 3 S11: 0.0685 S12: 0.1128 S13: 0.0805 REMARK 3 S21: 0.0520 S22: -0.0806 S23: 0.1470 REMARK 3 S31: -0.0231 S32: -0.0185 S33: 0.0121 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 : BB 37 BB 52 REMARK 3 ORIGIN FOR THE GROUP (A): 7.7220 54.3440 -31.4700 REMARK 3 T TENSOR REMARK 3 T11: 0.1221 T22: 0.0930 REMARK 3 T33: 0.0849 T12: -0.0053 REMARK 3 T13: 0.0243 T23: -0.0205 REMARK 3 L TENSOR REMARK 3 L11: 0.8369 L22: 9.8954 REMARK 3 L33: 0.3504 L12: -1.3073 REMARK 3 L13: 0.3183 L23: -0.9445 REMARK 3 S TENSOR REMARK 3 S11: -0.0220 S12: -0.0350 S13: 0.1574 REMARK 3 S21: 0.0145 S22: 0.0138 S23: -0.2263 REMARK 3 S31: -0.0194 S32: 0.0380 S33: 0.0082 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 : BB 53 BB 106 REMARK 3 ORIGIN FOR THE GROUP (A): 4.2530 46.5550 -29.1540 REMARK 3 T TENSOR REMARK 3 T11: 0.1689 T22: 0.1035 REMARK 3 T33: 0.0359 T12: -0.0226 REMARK 3 T13: 0.0334 T23: -0.0279 REMARK 3 L TENSOR REMARK 3 L11: 0.9918 L22: 2.4688 REMARK 3 L33: 0.4421 L12: -1.1759 REMARK 3 L13: -0.2073 L23: 0.7186 REMARK 3 S TENSOR REMARK 3 S11: -0.0059 S12: -0.1253 S13: 0.0523 REMARK 3 S21: 0.2300 S22: 0.0248 S23: -0.0079 REMARK 3 S31: -0.0273 S32: 0.0063 S33: -0.0190 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 : BB 107 BB 122 REMARK 3 ORIGIN FOR THE GROUP (A): 1.2310 54.5100 -35.2530 REMARK 3 T TENSOR REMARK 3 T11: 0.1133 T22: 0.0467 REMARK 3 T33: 0.0767 T12: -0.0239 REMARK 3 T13: 0.0417 T23: -0.0207 REMARK 3 L TENSOR REMARK 3 L11: 6.0567 L22: 4.2113 REMARK 3 L33: 3.8326 L12: -4.1822 REMARK 3 L13: -4.0092 L23: 2.7640 REMARK 3 S TENSOR REMARK 3 S11: 0.0859 S12: -0.1260 S13: 0.1302 REMARK 3 S21: -0.0575 S22: -0.0674 S23: -0.0041 REMARK 3 S31: -0.1401 S32: 0.0288 S33: -0.0185 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 : EE 334 EE 346 REMARK 3 ORIGIN FOR THE GROUP (A): 11.3170 -11.6470 12.4400 REMARK 3 T TENSOR REMARK 3 T11: 0.1550 T22: 0.1450 REMARK 3 T33: 0.2329 T12: 0.0092 REMARK 3 T13: 0.0668 T23: -0.0360 REMARK 3 L TENSOR REMARK 3 L11: 2.7966 L22: 11.4563 REMARK 3 L33: 3.5881 L12: -4.1620 REMARK 3 L13: 1.3130 L23: -1.4796 REMARK 3 S TENSOR REMARK 3 S11: -0.1648 S12: -0.1810 S13: 0.0987 REMARK 3 S21: 0.3907 S22: 0.1671 S23: 0.4051 REMARK 3 S31: -0.1941 S32: -0.1982 S33: -0.0023 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 : EE 347 EE 395 REMARK 3 ORIGIN FOR THE GROUP (A): 15.5400 -8.0520 2.9560 REMARK 3 T TENSOR REMARK 3 T11: 0.0996 T22: 0.0700 REMARK 3 T33: 0.1545 T12: -0.0103 REMARK 3 T13: 0.0021 T23: 0.0090 REMARK 3 L TENSOR REMARK 3 L11: 0.6999 L22: 3.5491 REMARK 3 L33: 0.5483 L12: -0.1439 REMARK 3 L13: 0.2113 L23: 0.0907 REMARK 3 S TENSOR REMARK 3 S11: -0.0250 S12: 0.0066 S13: 0.2924 REMARK 3 S21: 0.1433 S22: -0.0501 S23: -0.0614 REMARK 3 S31: -0.1532 S32: 0.0703 S33: 0.0751 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 : EE 396 EE 470 REMARK 3 ORIGIN FOR THE GROUP (A): 14.1540 -23.7290 -2.8380 REMARK 3 T TENSOR REMARK 3 T11: 0.0280 T22: 0.0384 REMARK 3 T33: 0.0225 T12: -0.0020 REMARK 3 T13: 0.0046 T23: 0.0105 REMARK 3 L TENSOR REMARK 3 L11: 1.7106 L22: 2.5459 REMARK 3 L33: 1.3626 L12: 0.9464 REMARK 3 L13: 0.6864 L23: 0.8710 REMARK 3 S TENSOR REMARK 3 S11: -0.0544 S12: 0.1479 S13: 0.1167 REMARK 3 S21: -0.1569 S22: 0.0549 S23: 0.1198 REMARK 3 S31: -0.0386 S32: 0.0858 S33: -0.0005 REMARK 3 REMARK 3 TLS GROUP : 13 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : EE 471 EE 509 REMARK 3 ORIGIN FOR THE GROUP (A): 11.7760 -36.7350 -3.6270 REMARK 3 T TENSOR REMARK 3 T11: 0.0472 T22: 0.0666 REMARK 3 T33: 0.0135 T12: 0.0255 REMARK 3 T13: 0.0027 T23: 0.0004 REMARK 3 L TENSOR REMARK 3 L11: 2.9046 L22: 3.0524 REMARK 3 L33: 2.6816 L12: 2.6610 REMARK 3 L13: 2.1338 L23: 2.2793 REMARK 3 S TENSOR REMARK 3 S11: 0.0872 S12: 0.1592 S13: -0.1185 REMARK 3 S21: 0.0857 S22: 0.0643 S23: -0.1227 REMARK 3 S31: 0.1562 S32: 0.1011 S33: -0.1515 REMARK 3 REMARK 3 TLS GROUP : 14 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : EE 510 EE 527 REMARK 3 ORIGIN FOR THE GROUP (A): 10.0440 -3.1630 -0.4070 REMARK 3 T TENSOR REMARK 3 T11: 0.1495 T22: 0.0862 REMARK 3 T33: 0.2933 T12: 0.0001 REMARK 3 T13: 0.0026 T23: 0.0080 REMARK 3 L TENSOR REMARK 3 L11: 1.6990 L22: 8.1834 REMARK 3 L33: 0.7897 L12: -3.5108 REMARK 3 L13: 1.0699 L23: -1.8834 REMARK 3 S TENSOR REMARK 3 S11: 0.0589 S12: 0.0279 S13: -0.0099 REMARK 3 S21: -0.2043 S22: -0.1214 S23: 0.1942 REMARK 3 S31: 0.0144 S32: -0.0019 S33: 0.0625 REMARK 3 REMARK 3 TLS GROUP : 15 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : FF 1 FF 37 REMARK 3 ORIGIN FOR THE GROUP (A): 21.6280 -52.1160 0.1330 REMARK 3 T TENSOR REMARK 3 T11: 0.1723 T22: 0.1004 REMARK 3 T33: 0.1257 T12: -0.0008 REMARK 3 T13: -0.0585 T23: -0.0230 REMARK 3 L TENSOR REMARK 3 L11: 2.5359 L22: 3.5600 REMARK 3 L33: 0.1159 L12: -0.4957 REMARK 3 L13: -0.5159 L23: -0.0584 REMARK 3 S TENSOR REMARK 3 S11: 0.1094 S12: 0.0845 S13: -0.2635 REMARK 3 S21: 0.0739 S22: -0.1632 S23: -0.3146 REMARK 3 S31: -0.0105 S32: -0.0046 S33: 0.0538 REMARK 3 REMARK 3 TLS GROUP : 16 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : FF 38 FF 49 REMARK 3 ORIGIN FOR THE GROUP (A): 14.8630 -64.6610 4.9290 REMARK 3 T TENSOR REMARK 3 T11: 0.1291 T22: 0.0853 REMARK 3 T33: 0.1093 T12: -0.0002 REMARK 3 T13: -0.0214 T23: 0.0201 REMARK 3 L TENSOR REMARK 3 L11: 2.0849 L22: 12.9858 REMARK 3 L33: 3.5387 L12: 0.2817 REMARK 3 L13: -0.4941 L23: 4.3775 REMARK 3 S TENSOR REMARK 3 S11: -0.1084 S12: -0.0529 S13: -0.1930 REMARK 3 S21: 0.2333 S22: -0.0256 S23: 0.4357 REMARK 3 S31: -0.0763 S32: -0.1298 S33: 0.1340 REMARK 3 REMARK 3 TLS GROUP : 17 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : FF 50 FF 111 REMARK 3 ORIGIN FOR THE GROUP (A): 16.8250 -52.8280 6.0300 REMARK 3 T TENSOR REMARK 3 T11: 0.2962 T22: 0.1507 REMARK 3 T33: 0.0969 T12: -0.0565 REMARK 3 T13: -0.0722 T23: 0.0345 REMARK 3 L TENSOR REMARK 3 L11: 1.4621 L22: 4.0083 REMARK 3 L33: 0.1561 L12: -1.4051 REMARK 3 L13: 0.0974 L23: -0.2780 REMARK 3 S TENSOR REMARK 3 S11: 0.0523 S12: -0.1837 S13: -0.1720 REMARK 3 S21: 0.4920 S22: -0.0220 S23: 0.0039 REMARK 3 S31: 0.0904 S32: -0.0229 S33: -0.0303 REMARK 3 REMARK 3 TLS GROUP : 18 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : FF 112 FF 121 REMARK 3 ORIGIN FOR THE GROUP (A): 26.4170 -64.1890 3.2870 REMARK 3 T TENSOR REMARK 3 T11: 0.1171 T22: 0.1909 REMARK 3 T33: 0.3400 T12: -0.0013 REMARK 3 T13: -0.0098 T23: 0.1542 REMARK 3 L TENSOR REMARK 3 L11: 11.3730 L22: 14.1367 REMARK 3 L33: 8.4650 L12: -10.0100 REMARK 3 L13: 7.3904 L23: -5.9343 REMARK 3 S TENSOR REMARK 3 S11: 0.1324 S12: 0.3381 S13: -0.1892 REMARK 3 S21: 0.2501 S22: -0.4261 S23: -0.6179 REMARK 3 S31: 0.1651 S32: 0.6447 S33: 0.2937 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 : 1.30 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 7OAU 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_1292115388. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-MAR-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 : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9999 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 : 77705 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650 REMARK 200 RESOLUTION RANGE LOW (A) : 39.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 6.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 6.00 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.200 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: 7OAO REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.92 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM FLUORIDE AND 20 % PEG REMARK 280 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 76.86500 REMARK 290 SMTRY3 2 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2010 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15000 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: AAA, BBB 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1680 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15160 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 PRO A 330 REMARK 465 ASN A 331 REMARK 465 ILE A 332 REMARK 465 THR A 333 REMARK 465 LYS A 528 REMARK 465 LYS A 529 REMARK 465 SER A 530 REMARK 465 THR A 531 REMARK 465 ASN A 532 REMARK 465 LYS A 533 REMARK 465 HIS A 534 REMARK 465 HIS A 535 REMARK 465 HIS A 536 REMARK 465 HIS A 537 REMARK 465 HIS A 538 REMARK 465 HIS A 539 REMARK 465 MET B -1 REMARK 465 ALA B 0 REMARK 465 HIS B 123 REMARK 465 HIS B 124 REMARK 465 HIS B 125 REMARK 465 HIS B 126 REMARK 465 HIS B 127 REMARK 465 PRO E 330 REMARK 465 ASN E 331 REMARK 465 ILE E 332 REMARK 465 THR E 333 REMARK 465 LYS E 528 REMARK 465 LYS E 529 REMARK 465 SER E 530 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 HIS F 122 REMARK 465 HIS F 123 REMARK 465 HIS F 124 REMARK 465 HIS F 125 REMARK 465 HIS F 126 REMARK 465 HIS F 127 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 HOHBB 352 O HOHBB 377 1.90 REMARK 500 O HOHFF 208 O HOHFF 257 1.91 REMARK 500 OG SERBB 7 OG SERBB 21 2.07 REMARK 500 O HOHEE 779 O HOHFF 257 2.16 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 TYREE 501 CB - CG - CD1 ANGL. DEV. = 4.4 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 ALAAA 352 41.81 -108.00 REMARK 500 PHEAA 377 85.81 -151.61 REMARK 500 ASNAA 422 -54.87 -126.03 REMARK 500 ALAEE 352 42.87 -108.59 REMARK 500 ASNEE 422 -56.00 -125.65 REMARK 500 REMARK 500 REMARK: NULL DBREF 7OAUAA 330 532 UNP P0DTC2 SPIKE_SARS2 330 532 DBREF 7OAUBB -1 127 PDB 7OAU 7OAU -1 127 DBREF 7OAUEE 330 532 UNP P0DTC2 SPIKE_SARS2 330 532 DBREF 7OAUFF -1 127 PDB 7OAU 7OAU -1 127 SEQADV 7OAU TYRAA 501 UNP P0DTC2 ASN 501 ENGINEERED MUTATION SEQADV 7OAU LYSAA 533 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAU HISAA 534 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAU HISAA 535 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAU HISAA 536 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAU HISAA 537 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAU HISAA 538 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAU HISAA 539 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAU TYREE 501 UNP P0DTC2 ASN 501 ENGINEERED MUTATION SEQADV 7OAU LYSEE 533 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAU HISEE 534 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAU HISEE 535 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAU HISEE 536 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAU HISEE 537 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAU HISEE 538 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAU HISEE 539 UNP P0DTC2 EXPRESSION TAG SEQRES 1AA 210 PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE SEQRES 2AA 210 ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG SEQRES 3AA 210 LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU SEQRES 4AA 210 TYR ASN SER ALA SER PHE SER THR PHE LYS CYS TYR GLY SEQRES 5AA 210 VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN SEQRES 6AA 210 VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL SEQRES 7AA 210 ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP SEQRES 8AA 210 TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL SEQRES 9AA 210 ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY SEQRES 10AA 210 GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER SEQRES 11AA 210 ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE SEQRES 12AA 210 TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY SEQRES 13AA 210 PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN SEQRES 14AA 210 PRO THR TYR GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL SEQRES 15AA 210 VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL SEQRES 16AA 210 CYS GLY PRO LYS LYS SER THR ASN LYS HIS HIS HIS HIS SEQRES 17AA 210 HIS HIS SEQRES 1BB 129 MET ALA GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER SEQRES 2BB 129 VAL GLN ALA GLY GLY SER LEU THR LEU SER CYS VAL ALA SEQRES 3BB 129 SER GLY VAL THR LEU GLY ARG HIS ALA ILE GLY TRP PHE SEQRES 4BB 129 ARG GLN ALA PRO GLY LYS GLU ARG GLU ARG VAL SER CYS SEQRES 5BB 129 ILE ARG THR PHE ASP GLY ILE THR SER TYR VAL GLU SER SEQRES 6BB 129 THR LYS GLY ARG PHE THR ILE SER SER ASN ASN ALA MET SEQRES 7BB 129 ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8BB 129 ASP THR ALA VAL TYR PHE CYS ALA LEU GLY VAL THR ALA SEQRES 9BB 129 ALA CYS SER ASP ASN PRO TYR PHE TRP GLY GLN GLY THR SEQRES 10BB 129 GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS 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 129 MET ALA GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER SEQRES 2FF 129 VAL GLN ALA GLY GLY SER LEU THR LEU SER CYS VAL ALA SEQRES 3FF 129 SER GLY VAL THR LEU GLY ARG HIS ALA ILE GLY TRP PHE SEQRES 4FF 129 ARG GLN ALA PRO GLY LYS GLU ARG GLU ARG VAL SER CYS SEQRES 5FF 129 ILE ARG THR PHE ASP GLY ILE THR SER TYR VAL GLU SER SEQRES 6FF 129 THR LYS GLY ARG PHE THR ILE SER SER ASN ASN ALA MET SEQRES 7FF 129 ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8FF 129 ASP THR ALA VAL TYR PHE CYS ALA LEU GLY VAL THR ALA SEQRES 9FF 129 ALA CYS SER ASP ASN PRO TYR PHE TRP GLY GLN GLY THR SEQRES 10FF 129 GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS HET NAG AA 601 14 HET GOL BB 201 6 HET NAG EE 601 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 5 NAG 2(C8 H15 N O6) FORMUL 6 GOL C3 H8 O3 FORMUL 8 HOH *470(H2 O) HELIX 1 AA1 PROAA 337 ASNAA 343 1 7 HELIX 2 AA2 SERAA 349 TRPAA 353 5 5 HELIX 3 AA3 ASPAA 364 ASNAA 370 1 7 HELIX 4 AA4 SERAA 383 ASPAA 389 5 7 HELIX 5 AA5 ASPAA 405 ILEAA 410 5 6 HELIX 6 AA6 GLYAA 416 ASNAA 422 1 7 HELIX 7 AA7 SERAA 438 SERAA 443 1 6 HELIX 8 AA8 GLYAA 502 TYRAA 505 5 4 HELIX 9 AA9 ASNBB 74 METBB 76 5 3 HELIX 10 AB1 LYSBB 87 THRBB 91 5 5 HELIX 11 AB2 PROEE 337 ASNEE 343 1 7 HELIX 12 AB3 SEREE 349 TRPEE 353 5 5 HELIX 13 AB4 ASPEE 364 ASNEE 370 1 7 HELIX 14 AB5 SEREE 383 ASPEE 389 5 7 HELIX 15 AB6 ASPEE 405 ILEEE 410 5 6 HELIX 16 AB7 GLYEE 416 ASNEE 422 1 7 HELIX 17 AB8 SEREE 438 SEREE 443 1 6 HELIX 18 AB9 GLYEE 502 TYREE 505 5 4 HELIX 19 AC1 ASNFF 74 METFF 76 5 3 HELIX 20 AC2 LYSFF 87 THRFF 91 5 5 SHEET 1 AA1 5 ASNAA 354 ILEAA 358 0 SHEET 2 AA1 5 ASNAA 394 ARGAA 403 -1 O VALAA 395 N ILEAA 358 SHEET 3 AA1 5 PROAA 507 GLUAA 516 -1 O TYRAA 508 N ILEAA 402 SHEET 4 AA1 5 GLYAA 431 ASNAA 437 -1 N ILEAA 434 O VALAA 511 SHEET 5 AA1 5 THRAA 376 TYRAA 380 -1 N TYRAA 380 O GLYAA 431 SHEET 1 AA2 3 CYSAA 361 VALAA 362 0 SHEET 2 AA2 3 VALAA 524 CYSAA 525 1 O CYSAA 525 N CYSAA 361 SHEET 3 AA2 3 CYSAA 391 PHEAA 392 -1 N PHEAA 392 O VALAA 524 SHEET 1 AA3 2 LEUAA 452 ARGAA 454 0 SHEET 2 AA3 2 LEUAA 492 SERAA 494 -1 O GLNAA 493 N TYRAA 453 SHEET 1 AA4 2 TYRAA 473 GLNAA 474 0 SHEET 2 AA4 2 CYSAA 488 TYRAA 489 -1 O TYRAA 489 N TYRAA 473 SHEET 1 AA5 4 GLNBB 3 SERBB 7 0 SHEET 2 AA5 4 LEUBB 18 SERBB 25 -1 O VALBB 23 N VALBB 5 SHEET 3 AA5 4 THRBB 78 METBB 83 -1 O METBB 83 N LEUBB 18 SHEET 4 AA5 4 PHEBB 68 ASNBB 73 -1 N THRBB 69 O GLNBB 82 SHEET 1 AA6 6 GLYBB 10 GLNBB 13 0 SHEET 2 AA6 6 THRBB 115 SERBB 120 1 O THRBB 118 N GLYBB 10 SHEET 3 AA6 6 ALABB 92 LEUBB 98 -1 N TYRBB 94 O THRBB 115 SHEET 4 AA6 6 ALABB 33 GLNBB 39 -1 N PHEBB 37 O PHEBB 95 SHEET 5 AA6 6 GLUBB 46 ARGBB 52 -1 O ILEBB 51 N ILEBB 34 SHEET 6 AA6 6 THRBB 58 TYRBB 60 -1 O SERBB 59 N CYSBB 50 SHEET 1 AA7 4 GLYBB 10 GLNBB 13 0 SHEET 2 AA7 4 THRBB 115 SERBB 120 1 O THRBB 118 N GLYBB 10 SHEET 3 AA7 4 ALABB 92 LEUBB 98 -1 N TYRBB 94 O THRBB 115 SHEET 4 AA7 4 PHEBB 110 TRPBB 111 -1 O PHEBB 110 N LEUBB 98 SHEET 1 AA8 5 ASNEE 354 ILEEE 358 0 SHEET 2 AA8 5 ASNEE 394 ARGEE 403 -1 O VALEE 395 N ILEEE 358 SHEET 3 AA8 5 PROEE 507 GLUEE 516 -1 O TYREE 508 N ILEEE 402 SHEET 4 AA8 5 GLYEE 431 ASNEE 437 -1 N ILEEE 434 O VALEE 511 SHEET 5 AA8 5 THREE 376 TYREE 380 -1 N TYREE 380 O GLYEE 431 SHEET 1 AA9 3 CYSEE 361 VALEE 362 0 SHEET 2 AA9 3 VALEE 524 CYSEE 525 1 O CYSEE 525 N CYSEE 361 SHEET 3 AA9 3 CYSEE 391 PHEEE 392 -1 N PHEEE 392 O VALEE 524 SHEET 1 AB1 2 LEUEE 452 ARGEE 454 0 SHEET 2 AB1 2 LEUEE 492 SEREE 494 -1 O GLNEE 493 N TYREE 453 SHEET 1 AB2 2 TYREE 473 GLNEE 474 0 SHEET 2 AB2 2 CYSEE 488 TYREE 489 -1 O TYREE 489 N TYREE 473 SHEET 1 AB3 4 GLNFF 3 SERFF 7 0 SHEET 2 AB3 4 LEUFF 18 SERFF 25 -1 O VALFF 23 N VALFF 5 SHEET 3 AB3 4 THRFF 78 METFF 83 -1 O METFF 83 N LEUFF 18 SHEET 4 AB3 4 PHEFF 68 ASNFF 73 -1 N THRFF 69 O GLNFF 82 SHEET 1 AB4 6 GLYFF 10 GLNFF 13 0 SHEET 2 AB4 6 THRFF 115 SERFF 120 1 O THRFF 118 N GLYFF 10 SHEET 3 AB4 6 ALAFF 92 LEUFF 98 -1 N TYRFF 94 O THRFF 115 SHEET 4 AB4 6 ALAFF 33 GLNFF 39 -1 N GLYFF 35 O ALAFF 97 SHEET 5 AB4 6 GLUFF 46 ARGFF 52 -1 O ILEFF 51 N ILEFF 34 SHEET 6 AB4 6 THRFF 58 TYRFF 60 -1 O SERFF 59 N CYSFF 50 SHEET 1 AB5 4 GLYFF 10 GLNFF 13 0 SHEET 2 AB5 4 THRFF 115 SERFF 120 1 O THRFF 118 N GLYFF 10 SHEET 3 AB5 4 ALAFF 92 LEUFF 98 -1 N TYRFF 94 O THRFF 115 SHEET 4 AB5 4 PHEFF 110 TRPFF 111 -1 O PHEFF 110 N LEUFF 98 SSBOND 1 CYSAA 336 CYSAA 361 1555 1555 2.04 SSBOND 2 CYSAA 379 CYSAA 432 1555 1555 2.07 SSBOND 3 CYSAA 391 CYSAA 525 1555 1555 2.07 SSBOND 4 CYSAA 480 CYSAA 488 1555 1555 2.11 SSBOND 5 CYSBB 22 CYSBB 96 1555 1555 2.04 SSBOND 6 CYSBB 50 CYSBB 104 1555 1555 2.05 SSBOND 7 CYSEE 336 CYSEE 361 1555 1555 2.05 SSBOND 8 CYSEE 379 CYSEE 432 1555 1555 2.08 SSBOND 9 CYSEE 391 CYSEE 525 1555 1555 2.07 SSBOND 10 CYSEE 480 CYSEE 488 1555 1555 2.11 SSBOND 11 CYSFF 22 CYSFF 96 1555 1555 2.03 SSBOND 12 CYSFF 50 CYSFF 104 1555 1555 2.08 LINK ND2 ASNAA 343 C1 NAGAA 601 1555 1555 1.44 LINK ND2 ASNEE 343 C1 NAGEE 601 1555 1555 1.44 CRYST1 28.810 153.730 75.850 90.00 100.33 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.034710 0.000000 0.006327 0.00000 SCALE2 0.000000 0.006505 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013401 0.00000