HEADER VIRAL PROTEIN/IMMUNE SYSTEM 22-OCT-24 9K6J TITLE CRYSTAL STRUCTURE OF SARS-COV-2 WT RBD BOUND WITH P5-1C8 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE PROTEIN S1; COMPND 3 CHAIN: C; COMPND 4 FRAGMENT: RECEPTOR-BINDING DOMAIN (RBD); COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: H CHAIN OF P5-1C8 FAB; COMPND 8 CHAIN: A; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: L CHAIN OF P5-1C8 FAB; COMPND 12 CHAIN: B; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_TAXID: 2697049; SOURCE 5 GENE: S, 2; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS CRYSTAL, SARS-COV-2, RBD, ANTIBODY, VIRAL PROTEIN/IMMUNE SYSTEM, KEYWDS 2 VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR N.N.LV,R.Y.YANG REVDAT 1 07-JAN-26 9K6J 0 JRNL AUTH N.LV,P.CHEN,X.DAI,H.XU,Z.LI,Z.SHAN,J.LI,F.GUO,Y.CHEN,J.LI, JRNL AUTH 2 Y.HUANG,G.DONG,Y.JIANG,L.CHEN,X.NAN,H.ZHAO,K.ZHANG,S.FAN, JRNL AUTH 3 Y.DONG,D.LIU,X.WANG,D.HUANG,X.PAN,C.CHEN,Z.LIU,L.T.YAN, JRNL AUTH 4 Q.ZHANG,L.ZHANG,Y.ZHAO,Y.R.YANG JRNL TITL IGG-BRIDGING-SEEDED SYNERGISTIC AGGREGATION OF SARS-COV-2 JRNL TITL 2 SPIKES UNDERLIES POTENT NEUTRALIZATION BY A LOW-AFFINITY JRNL TITL 3 ANTIBODY. JRNL REF ADV SCI 17192 2025 JRNL REFN ESSN 2198-3844 JRNL PMID 41355083 JRNL DOI 10.1002/ADVS.202517192 REMARK 2 REMARK 2 RESOLUTION. 2.39 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.39 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.44 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 91.2 REMARK 3 NUMBER OF REFLECTIONS : 34149 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.238 REMARK 3 R VALUE (WORKING SET) : 0.236 REMARK 3 FREE R VALUE : 0.283 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940 REMARK 3 FREE R VALUE TEST SET COUNT : 1686 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 53.4400 - 5.4600 1.00 3167 165 0.2032 0.2443 REMARK 3 2 5.4600 - 4.3400 0.96 2922 146 0.1620 0.2038 REMARK 3 3 4.3400 - 3.8200 0.82 2267 134 0.2039 0.2554 REMARK 3 4 3.5600 - 3.4400 0.74 820 46 0.2512 0.3576 REMARK 3 5 3.4400 - 3.2000 0.97 2882 140 0.2413 0.2768 REMARK 3 6 3.2000 - 3.0100 1.00 2946 170 0.2268 0.2513 REMARK 3 7 3.0100 - 2.8600 1.00 2944 143 0.2514 0.3087 REMARK 3 8 2.8600 - 2.7300 1.00 2931 162 0.2713 0.3393 REMARK 3 9 2.7300 - 2.6300 1.00 2912 133 0.2954 0.3511 REMARK 3 10 2.6300 - 2.5400 1.00 2927 147 0.2904 0.3531 REMARK 3 11 2.5400 - 2.4600 1.00 2917 155 0.2984 0.3431 REMARK 3 12 2.4600 - 2.3900 0.97 2828 145 0.3595 0.3970 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.620 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 4738 REMARK 3 ANGLE : 0.777 6448 REMARK 3 CHIRALITY : 0.056 712 REMARK 3 PLANARITY : 0.004 833 REMARK 3 DIHEDRAL : 16.530 1673 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 23 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 336 THROUGH 353 ) REMARK 3 ORIGIN FOR THE GROUP (A): 31.0038 12.6529 59.1863 REMARK 3 T TENSOR REMARK 3 T11: 0.1749 T22: 0.2446 REMARK 3 T33: 0.2891 T12: -0.0867 REMARK 3 T13: -0.0292 T23: 0.0028 REMARK 3 L TENSOR REMARK 3 L11: 2.5409 L22: 1.4170 REMARK 3 L33: 1.7854 L12: 0.0361 REMARK 3 L13: 1.2183 L23: -0.0432 REMARK 3 S TENSOR REMARK 3 S11: 0.2104 S12: -0.4133 S13: 0.1527 REMARK 3 S21: 0.1663 S22: -0.3074 S23: -0.2387 REMARK 3 S31: 0.1646 S32: 0.2238 S33: 0.0352 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 354 THROUGH 364 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.6350 8.6494 70.7683 REMARK 3 T TENSOR REMARK 3 T11: 0.4268 T22: 0.3830 REMARK 3 T33: 0.2309 T12: -0.0476 REMARK 3 T13: -0.1590 T23: 0.0927 REMARK 3 L TENSOR REMARK 3 L11: 2.6694 L22: 0.7649 REMARK 3 L33: 2.8514 L12: 0.3135 REMARK 3 L13: 1.5234 L23: 1.3953 REMARK 3 S TENSOR REMARK 3 S11: -0.1517 S12: -0.3354 S13: -0.0600 REMARK 3 S21: 0.8496 S22: -0.2417 S23: -0.6693 REMARK 3 S31: 0.1086 S32: 0.3547 S33: -0.6278 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 365 THROUGH 375 ) REMARK 3 ORIGIN FOR THE GROUP (A): 31.9263 24.9854 68.8982 REMARK 3 T TENSOR REMARK 3 T11: 0.7777 T22: 0.4629 REMARK 3 T33: -0.3349 T12: -0.2399 REMARK 3 T13: -0.2833 T23: -0.0693 REMARK 3 L TENSOR REMARK 3 L11: 0.6870 L22: 0.0071 REMARK 3 L33: 1.0515 L12: 0.0860 REMARK 3 L13: 0.8474 L23: 0.1010 REMARK 3 S TENSOR REMARK 3 S11: -0.1382 S12: -0.2693 S13: 0.2945 REMARK 3 S21: 0.3038 S22: 0.0303 S23: -0.1776 REMARK 3 S31: -0.2996 S32: 0.2727 S33: 0.0651 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 376 THROUGH 393 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.6661 20.3183 74.8030 REMARK 3 T TENSOR REMARK 3 T11: 0.7117 T22: 0.3955 REMARK 3 T33: -0.0902 T12: -0.0935 REMARK 3 T13: -0.0823 T23: -0.0231 REMARK 3 L TENSOR REMARK 3 L11: 0.5522 L22: 1.1353 REMARK 3 L33: 2.3435 L12: -0.5485 REMARK 3 L13: 0.5079 L23: -1.4863 REMARK 3 S TENSOR REMARK 3 S11: -0.1357 S12: -0.6102 S13: 0.2479 REMARK 3 S21: 1.0296 S22: 0.0871 S23: -0.2042 REMARK 3 S31: -0.0919 S32: -0.4235 S33: 0.0296 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 394 THROUGH 421 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.4036 17.5035 57.6719 REMARK 3 T TENSOR REMARK 3 T11: 0.1953 T22: 0.2323 REMARK 3 T33: 0.1741 T12: -0.0416 REMARK 3 T13: -0.0005 T23: 0.0396 REMARK 3 L TENSOR REMARK 3 L11: 1.5803 L22: 0.9613 REMARK 3 L33: 1.3723 L12: -0.4925 REMARK 3 L13: 0.5228 L23: -0.0636 REMARK 3 S TENSOR REMARK 3 S11: -0.1057 S12: -0.0444 S13: 0.0496 REMARK 3 S21: 0.2028 S22: -0.0744 S23: 0.1876 REMARK 3 S31: -0.0182 S32: -0.1293 S33: -0.1255 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 422 THROUGH 469 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.0321 14.4042 54.1642 REMARK 3 T TENSOR REMARK 3 T11: 0.1673 T22: 0.1430 REMARK 3 T33: 0.1829 T12: -0.0367 REMARK 3 T13: -0.0239 T23: 0.0486 REMARK 3 L TENSOR REMARK 3 L11: 1.1529 L22: 1.3328 REMARK 3 L33: 1.8549 L12: -0.4558 REMARK 3 L13: 0.6127 L23: -0.3243 REMARK 3 S TENSOR REMARK 3 S11: 0.1140 S12: -0.2293 S13: 0.0468 REMARK 3 S21: 0.0340 S22: -0.0283 S23: 0.0440 REMARK 3 S31: 0.1253 S32: 0.0578 S33: 0.0076 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 470 THROUGH 494 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.2135 4.5835 38.0985 REMARK 3 T TENSOR REMARK 3 T11: 0.2938 T22: 0.2233 REMARK 3 T33: 0.2815 T12: -0.0189 REMARK 3 T13: -0.0555 T23: -0.0062 REMARK 3 L TENSOR REMARK 3 L11: 2.5642 L22: 1.1936 REMARK 3 L33: 1.6563 L12: -0.0544 REMARK 3 L13: 0.9235 L23: -0.1653 REMARK 3 S TENSOR REMARK 3 S11: 0.1786 S12: 0.3207 S13: -0.3337 REMARK 3 S21: -0.4438 S22: -0.0853 S23: 0.2410 REMARK 3 S31: 0.3440 S32: -0.1510 S33: -0.2087 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 495 THROUGH 516 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.5198 21.9290 53.1017 REMARK 3 T TENSOR REMARK 3 T11: 0.2713 T22: 0.2030 REMARK 3 T33: 0.2390 T12: -0.0744 REMARK 3 T13: -0.0056 T23: 0.0278 REMARK 3 L TENSOR REMARK 3 L11: 1.3535 L22: 1.2442 REMARK 3 L33: 1.7574 L12: -0.3363 REMARK 3 L13: 0.8629 L23: -0.5891 REMARK 3 S TENSOR REMARK 3 S11: 0.0365 S12: 0.1084 S13: 0.2864 REMARK 3 S21: 0.1932 S22: -0.0221 S23: 0.1449 REMARK 3 S31: -0.0161 S32: -0.1538 S33: 0.1208 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.5778 23.5682 37.6244 REMARK 3 T TENSOR REMARK 3 T11: 0.1217 T22: 0.3184 REMARK 3 T33: 0.2273 T12: -0.0655 REMARK 3 T13: -0.0091 T23: 0.0630 REMARK 3 L TENSOR REMARK 3 L11: 1.9866 L22: 1.6199 REMARK 3 L33: 1.0395 L12: -0.9011 REMARK 3 L13: 0.9294 L23: -1.1770 REMARK 3 S TENSOR REMARK 3 S11: 0.0131 S12: -0.1311 S13: -0.3894 REMARK 3 S21: -0.1700 S22: 0.1591 S23: 0.2623 REMARK 3 S31: 0.1553 S32: -0.5878 S33: -0.1369 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 18 THROUGH 82 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.3606 20.7865 43.3816 REMARK 3 T TENSOR REMARK 3 T11: 0.1580 T22: 0.2066 REMARK 3 T33: 0.1917 T12: -0.0379 REMARK 3 T13: 0.0278 T23: 0.0366 REMARK 3 L TENSOR REMARK 3 L11: 1.5906 L22: 0.6816 REMARK 3 L33: 1.4349 L12: -0.9930 REMARK 3 L13: 0.5554 L23: -0.2728 REMARK 3 S TENSOR REMARK 3 S11: 0.1133 S12: -0.1297 S13: -0.1647 REMARK 3 S21: 0.0516 S22: 0.0354 S23: 0.1368 REMARK 3 S31: 0.1439 S32: -0.1464 S33: -0.1305 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 83 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.0807 24.8170 37.8948 REMARK 3 T TENSOR REMARK 3 T11: 0.1408 T22: 0.1916 REMARK 3 T33: 0.1739 T12: -0.0538 REMARK 3 T13: 0.0006 T23: 0.0270 REMARK 3 L TENSOR REMARK 3 L11: 1.7429 L22: 1.1551 REMARK 3 L33: 0.9891 L12: -1.0031 REMARK 3 L13: 0.4812 L23: -0.6773 REMARK 3 S TENSOR REMARK 3 S11: 0.0700 S12: -0.0198 S13: -0.2130 REMARK 3 S21: 0.1238 S22: -0.0191 S23: 0.1242 REMARK 3 S31: -0.0199 S32: -0.0543 S33: -0.0831 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 114 THROUGH 138 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.8115 36.8667 20.5120 REMARK 3 T TENSOR REMARK 3 T11: 0.1729 T22: 0.3040 REMARK 3 T33: 0.2504 T12: -0.0879 REMARK 3 T13: -0.0214 T23: 0.0334 REMARK 3 L TENSOR REMARK 3 L11: 1.3085 L22: 0.8357 REMARK 3 L33: 0.9825 L12: -0.5081 REMARK 3 L13: 0.7752 L23: -0.1644 REMARK 3 S TENSOR REMARK 3 S11: -0.0590 S12: -0.1552 S13: -0.0403 REMARK 3 S21: -0.1117 S22: 0.0521 S23: 0.1887 REMARK 3 S31: 0.2665 S32: -0.4726 S33: -0.1240 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 139 THROUGH 194 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.6916 34.0136 15.4918 REMARK 3 T TENSOR REMARK 3 T11: 0.1626 T22: 0.1532 REMARK 3 T33: 0.2015 T12: -0.0572 REMARK 3 T13: 0.0217 T23: -0.0217 REMARK 3 L TENSOR REMARK 3 L11: 1.6175 L22: 0.6977 REMARK 3 L33: 1.8176 L12: -0.3612 REMARK 3 L13: 0.5915 L23: -0.6934 REMARK 3 S TENSOR REMARK 3 S11: 0.0328 S12: -0.0520 S13: -0.2398 REMARK 3 S21: -0.0295 S22: 0.0674 S23: -0.0324 REMARK 3 S31: 0.2268 S32: -0.2970 S33: -0.1026 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 195 THROUGH 217 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.9538 28.0240 14.8910 REMARK 3 T TENSOR REMARK 3 T11: 0.2985 T22: 0.3515 REMARK 3 T33: 0.3255 T12: -0.1652 REMARK 3 T13: -0.0506 T23: 0.0766 REMARK 3 L TENSOR REMARK 3 L11: 0.9518 L22: 0.7026 REMARK 3 L33: 3.8118 L12: -0.5993 REMARK 3 L13: 0.4006 L23: -0.0391 REMARK 3 S TENSOR REMARK 3 S11: 0.0428 S12: -0.3212 S13: -0.7329 REMARK 3 S21: 0.1772 S22: -0.0895 S23: -0.0706 REMARK 3 S31: 0.5956 S32: -0.2641 S33: -0.2616 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.4169 37.4691 24.2341 REMARK 3 T TENSOR REMARK 3 T11: 0.2724 T22: 0.2246 REMARK 3 T33: 0.2612 T12: -0.0163 REMARK 3 T13: 0.0391 T23: 0.0246 REMARK 3 L TENSOR REMARK 3 L11: 0.9799 L22: 0.9827 REMARK 3 L33: 1.7871 L12: -0.2430 REMARK 3 L13: 0.8028 L23: -0.7060 REMARK 3 S TENSOR REMARK 3 S11: 0.2603 S12: 0.0991 S13: 0.2675 REMARK 3 S21: 0.1823 S22: -0.0826 S23: -0.1728 REMARK 3 S31: -0.1743 S32: 0.0548 S33: 0.1906 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 19 THROUGH 30 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.8104 35.0926 34.1122 REMARK 3 T TENSOR REMARK 3 T11: 0.0863 T22: 0.3479 REMARK 3 T33: 0.1010 T12: -0.0175 REMARK 3 T13: 0.0062 T23: 0.0169 REMARK 3 L TENSOR REMARK 3 L11: 0.5139 L22: 3.0991 REMARK 3 L33: 4.9371 L12: -0.1461 REMARK 3 L13: 1.5438 L23: -1.2507 REMARK 3 S TENSOR REMARK 3 S11: 0.1051 S12: 0.3875 S13: -0.0291 REMARK 3 S21: 0.4562 S22: -0.2529 S23: -0.4674 REMARK 3 S31: -0.4719 S32: 0.2130 S33: 0.2297 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 31 THROUGH 49 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.6637 25.8397 28.6781 REMARK 3 T TENSOR REMARK 3 T11: 0.1003 T22: 0.2111 REMARK 3 T33: 0.1702 T12: 0.0532 REMARK 3 T13: 0.0024 T23: 0.0061 REMARK 3 L TENSOR REMARK 3 L11: 2.3846 L22: 1.1405 REMARK 3 L33: 1.7573 L12: -1.2222 REMARK 3 L13: 1.2378 L23: -1.3007 REMARK 3 S TENSOR REMARK 3 S11: 0.3166 S12: 0.2873 S13: -0.3997 REMARK 3 S21: -0.1792 S22: 0.0260 S23: 0.0037 REMARK 3 S31: 0.3959 S32: -0.1411 S33: 0.1283 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 50 THROUGH 76 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.9728 25.3163 25.9292 REMARK 3 T TENSOR REMARK 3 T11: 0.2083 T22: 0.2231 REMARK 3 T33: 0.2173 T12: 0.0119 REMARK 3 T13: 0.0205 T23: -0.0088 REMARK 3 L TENSOR REMARK 3 L11: 1.7269 L22: 1.3230 REMARK 3 L33: 1.9253 L12: -0.6539 REMARK 3 L13: 0.4862 L23: -1.4420 REMARK 3 S TENSOR REMARK 3 S11: 0.0890 S12: 0.3613 S13: -0.1472 REMARK 3 S21: -0.2447 S22: -0.0525 S23: -0.2912 REMARK 3 S31: 0.0290 S32: 0.4294 S33: 0.0905 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 77 THROUGH 98 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.7341 29.8369 27.6765 REMARK 3 T TENSOR REMARK 3 T11: 0.1345 T22: 0.1470 REMARK 3 T33: 0.2233 T12: 0.0125 REMARK 3 T13: 0.0182 T23: 0.0202 REMARK 3 L TENSOR REMARK 3 L11: 0.9750 L22: 0.6370 REMARK 3 L33: 2.1840 L12: -0.5651 REMARK 3 L13: 0.5523 L23: -1.1376 REMARK 3 S TENSOR REMARK 3 S11: 0.1378 S12: 0.0897 S13: 0.0343 REMARK 3 S21: -0.0438 S22: 0.0437 S23: -0.1082 REMARK 3 S31: 0.0597 S32: -0.0703 S33: 0.0728 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 99 THROUGH 137 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.5163 41.7105 12.3203 REMARK 3 T TENSOR REMARK 3 T11: 0.1380 T22: 0.1370 REMARK 3 T33: 0.1800 T12: -0.0305 REMARK 3 T13: 0.0111 T23: -0.0562 REMARK 3 L TENSOR REMARK 3 L11: 1.2412 L22: 0.7549 REMARK 3 L33: 1.3595 L12: -0.6861 REMARK 3 L13: 0.8232 L23: -0.1897 REMARK 3 S TENSOR REMARK 3 S11: 0.1221 S12: -0.0355 S13: -0.1058 REMARK 3 S21: 0.0062 S22: -0.0659 S23: 0.0382 REMARK 3 S31: -0.0684 S32: -0.0510 S33: 0.0234 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 138 THROUGH 150 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.2028 48.2680 9.9313 REMARK 3 T TENSOR REMARK 3 T11: 0.1629 T22: 0.1587 REMARK 3 T33: 0.1366 T12: 0.0117 REMARK 3 T13: 0.0030 T23: -0.0304 REMARK 3 L TENSOR REMARK 3 L11: 2.3214 L22: 3.4330 REMARK 3 L33: 1.2841 L12: -2.0172 REMARK 3 L13: -0.1589 L23: -0.9473 REMARK 3 S TENSOR REMARK 3 S11: -0.0088 S12: -0.2771 S13: 0.2840 REMARK 3 S21: -0.1496 S22: -0.1399 S23: -0.4181 REMARK 3 S31: -0.0198 S32: 0.1629 S33: -0.4559 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 151 THROUGH 163 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.1318 53.6353 14.2018 REMARK 3 T TENSOR REMARK 3 T11: 0.2459 T22: 0.1410 REMARK 3 T33: 0.1713 T12: 0.0108 REMARK 3 T13: -0.0246 T23: -0.0438 REMARK 3 L TENSOR REMARK 3 L11: 0.9497 L22: 2.0514 REMARK 3 L33: 1.2361 L12: -1.0865 REMARK 3 L13: 0.7908 L23: -1.2546 REMARK 3 S TENSOR REMARK 3 S11: -0.0535 S12: -0.0269 S13: 0.0527 REMARK 3 S21: 0.1964 S22: -0.1678 S23: 0.0714 REMARK 3 S31: -0.0874 S32: -0.2780 S33: 0.1033 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 164 THROUGH 211 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.8730 47.5109 8.7242 REMARK 3 T TENSOR REMARK 3 T11: 0.1507 T22: 0.1800 REMARK 3 T33: 0.1779 T12: 0.0182 REMARK 3 T13: -0.0095 T23: -0.0246 REMARK 3 L TENSOR REMARK 3 L11: 1.8182 L22: 0.8671 REMARK 3 L33: 1.8414 L12: -0.2916 REMARK 3 L13: 0.7685 L23: -0.6715 REMARK 3 S TENSOR REMARK 3 S11: 0.0290 S12: 0.0081 S13: 0.1589 REMARK 3 S21: -0.1061 S22: -0.0473 S23: 0.0015 REMARK 3 S31: -0.2166 S32: -0.0639 S33: 0.0569 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9K6J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 01-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1300052804. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-SEP-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL02U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34150 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.390 REMARK 200 RESOLUTION RANGE LOW (A) : 89.940 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 9.000 REMARK 200 R MERGE (I) : 0.08600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.39 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 7.55 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 7CDI REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 64.08 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM PHOSPHATE DIBASIC,28% REMARK 280 W/V POLYETHYLENE GLYCOL 3,350, PH 8.0, VAPOR DIFFUSION, HANGING REMARK 280 DROP, TEMPERATURE 291.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 27.65300 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.06750 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.54600 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.06750 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.65300 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.54600 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, A, B 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 MET C 300 REMARK 465 GLY C 301 REMARK 465 TRP C 302 REMARK 465 SER C 303 REMARK 465 CYS C 304 REMARK 465 ILE C 305 REMARK 465 ILE C 306 REMARK 465 LEU C 307 REMARK 465 PHE C 308 REMARK 465 LEU C 309 REMARK 465 VAL C 310 REMARK 465 ALA C 311 REMARK 465 THR C 312 REMARK 465 ALA C 313 REMARK 465 THR C 314 REMARK 465 GLY C 315 REMARK 465 VAL C 316 REMARK 465 HIS C 317 REMARK 465 SER C 318 REMARK 465 ARG C 319 REMARK 465 VAL C 320 REMARK 465 GLN C 321 REMARK 465 PRO C 322 REMARK 465 THR C 323 REMARK 465 GLU C 324 REMARK 465 SER C 325 REMARK 465 ILE C 326 REMARK 465 VAL C 327 REMARK 465 ARG C 328 REMARK 465 PHE C 329 REMARK 465 PRO C 330 REMARK 465 ASN C 331 REMARK 465 ILE C 332 REMARK 465 THR C 333 REMARK 465 ASN C 334 REMARK 465 LEU C 335 REMARK 465 LEU C 517 REMARK 465 HIS C 518 REMARK 465 ALA C 519 REMARK 465 PRO C 520 REMARK 465 ALA C 521 REMARK 465 THR C 522 REMARK 465 VAL C 523 REMARK 465 CYS C 524 REMARK 465 GLY C 525 REMARK 465 PRO C 526 REMARK 465 LYS C 527 REMARK 465 LYS C 528 REMARK 465 SER C 529 REMARK 465 THR C 530 REMARK 465 ASN C 531 REMARK 465 LEU C 532 REMARK 465 VAL C 533 REMARK 465 LYS C 534 REMARK 465 ASN C 535 REMARK 465 LYS C 536 REMARK 465 HIS C 537 REMARK 465 HIS C 538 REMARK 465 HIS C 539 REMARK 465 HIS C 540 REMARK 465 HIS C 541 REMARK 465 HIS C 542 REMARK 465 HIS C 543 REMARK 465 HIS C 544 REMARK 465 GLN C 545 REMARK 465 PRO C 546 REMARK 465 ARG C 547 REMARK 465 PHE C 548 REMARK 465 ALA C 549 REMARK 465 ALA C 550 REMARK 465 ALA C 551 REMARK 465 ALA C 552 REMARK 465 SER C 553 REMARK 465 SER C 554 REMARK 465 ALA C 555 REMARK 465 GLY C 556 REMARK 465 LEU C 557 REMARK 465 ASN C 558 REMARK 465 ASP C 559 REMARK 465 ILE C 560 REMARK 465 PHE C 561 REMARK 465 GLU C 562 REMARK 465 ALA C 563 REMARK 465 GLN C 564 REMARK 465 LYS C 565 REMARK 465 ILE C 566 REMARK 465 GLU C 567 REMARK 465 TRP C 568 REMARK 465 HIS C 569 REMARK 465 GLU C 570 REMARK 465 LYS A 133 REMARK 465 SER A 134 REMARK 465 THR A 135 REMARK 465 SER A 136 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU C 340 CG CD OE1 OE2 REMARK 470 SER C 359 OG REMARK 470 ASP C 364 CG OD1 OD2 REMARK 470 TYR C 369 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASN C 370 CG OD1 ND2 REMARK 470 THR C 385 OG1 CG2 REMARK 470 LYS C 386 CG CD CE NZ REMARK 470 LEU C 387 CG CD1 CD2 REMARK 470 ASP C 389 CG OD1 OD2 REMARK 470 GLU C 516 CG CD OE1 OE2 REMARK 470 GLU A 1 CG CD OE1 OE2 REMARK 470 GLU A 26 CG CD OE1 OE2 REMARK 470 ARG A 109 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 210 CG CD CE NZ REMARK 470 GLU B 1 CG CD OE1 OE2 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 ALA C 352 51.49 -115.68 REMARK 500 ASN C 370 60.74 -105.60 REMARK 500 ALA C 372 10.08 59.94 REMARK 500 PHE C 377 76.15 -151.24 REMARK 500 ASN C 422 -57.71 -135.11 REMARK 500 ASP C 428 39.37 -88.83 REMARK 500 GLU A 26 -58.96 75.90 REMARK 500 ASP A 148 74.38 57.33 REMARK 500 ALA B 52 -46.60 76.28 REMARK 500 ASN B 138 70.04 58.85 REMARK 500 ASN B 158 36.00 -143.36 REMARK 500 LYS B 169 -61.47 -99.01 REMARK 500 LYS B 190 -50.17 -122.34 REMARK 500 ASN B 210 91.37 66.83 REMARK 500 REMARK 500 REMARK: NULL DBREF 9K6J C 319 536 UNP P0DTC2 SPIKE_SARS2 319 537 DBREF 9K6J A 1 217 PDB 9K6J 9K6J 1 217 DBREF 9K6J B 1 211 PDB 9K6J 9K6J 1 211 SEQADV 9K6J MET C 300 UNP P0DTC2 INITIATING METHIONINE SEQADV 9K6J GLY C 301 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J TRP C 302 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J SER C 303 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J CYS C 304 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J ILE C 305 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J ILE C 306 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J LEU C 307 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J PHE C 308 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J LEU C 309 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J VAL C 310 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J ALA C 311 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J THR C 312 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J ALA C 313 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J THR C 314 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J GLY C 315 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J VAL C 316 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J HIS C 317 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J SER C 318 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J C UNP P0DTC2 LEU 517 DELETION SEQADV 9K6J HIS C 537 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J HIS C 538 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J HIS C 539 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J HIS C 540 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J HIS C 541 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J HIS C 542 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J HIS C 543 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J HIS C 544 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J GLN C 545 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J PRO C 546 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J ARG C 547 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J PHE C 548 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J ALA C 549 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J ALA C 550 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J ALA C 551 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J ALA C 552 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J SER C 553 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J SER C 554 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J ALA C 555 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J GLY C 556 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J LEU C 557 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J ASN C 558 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J ASP C 559 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J ILE C 560 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J PHE C 561 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J GLU C 562 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J ALA C 563 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J GLN C 564 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J LYS C 565 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J ILE C 566 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J GLU C 567 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J TRP C 568 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J HIS C 569 UNP P0DTC2 EXPRESSION TAG SEQADV 9K6J GLU C 570 UNP P0DTC2 EXPRESSION TAG SEQRES 1 C 271 MET GLY TRP SER CYS ILE ILE LEU PHE LEU VAL ALA THR SEQRES 2 C 271 ALA THR GLY VAL HIS SER ARG VAL GLN PRO THR GLU SER SEQRES 3 C 271 ILE VAL ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE SEQRES 4 C 271 GLY GLU VAL PHE ASN ALA THR ARG PHE ALA SER VAL TYR SEQRES 5 C 271 ALA TRP ASN ARG LYS ARG ILE SER ASN CYS VAL ALA ASP SEQRES 6 C 271 TYR SER VAL LEU TYR ASN SER ALA SER PHE SER THR PHE SEQRES 7 C 271 LYS CYS TYR GLY VAL SER PRO THR LYS LEU ASN ASP LEU SEQRES 8 C 271 CYS PHE THR ASN VAL TYR ALA ASP SER PHE VAL ILE ARG SEQRES 9 C 271 GLY ASP GLU VAL ARG GLN ILE ALA PRO GLY GLN THR GLY SEQRES 10 C 271 LYS ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE SEQRES 11 C 271 THR GLY CYS VAL ILE ALA TRP ASN SER ASN ASN LEU ASP SEQRES 12 C 271 SER LYS VAL GLY GLY ASN TYR ASN TYR LEU TYR ARG LEU SEQRES 13 C 271 PHE ARG LYS SER ASN LEU LYS PRO PHE GLU ARG ASP ILE SEQRES 14 C 271 SER THR GLU ILE TYR GLN ALA GLY SER THR PRO CYS ASN SEQRES 15 C 271 GLY VAL GLU GLY PHE ASN CYS TYR PHE PRO LEU GLN SER SEQRES 16 C 271 TYR GLY PHE GLN PRO THR ASN GLY VAL GLY TYR GLN PRO SEQRES 17 C 271 TYR ARG VAL VAL VAL LEU SER PHE GLU LEU HIS ALA PRO SEQRES 18 C 271 ALA THR VAL CYS GLY PRO LYS LYS SER THR ASN LEU VAL SEQRES 19 C 271 LYS ASN LYS HIS HIS HIS HIS HIS HIS HIS HIS GLN PRO SEQRES 20 C 271 ARG PHE ALA ALA ALA ALA SER SER ALA GLY LEU ASN ASP SEQRES 21 C 271 ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS GLU SEQRES 1 A 217 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU ILE GLN SEQRES 2 A 217 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLU SEQRES 3 A 217 ILE ILE VAL SER ARG ASN TYR MET ASN TRP VAL ARG GLN SEQRES 4 A 217 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER VAL ILE TYR SEQRES 5 A 217 SER GLY GLY SER THR PHE TYR ALA ASP SER VAL LYS GLY SEQRES 6 A 217 ARG PHE THR ILE SER ARG ASP ASN SER GLU ASN THR LEU SEQRES 7 A 217 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 A 217 VAL TYR TYR CYS ALA ARG GLY TYR GLY ASP TYR TYR PHE SEQRES 9 A 217 ASP TYR TRP GLY ARG GLY THR LEU VAL THR VAL SER SER SEQRES 10 A 217 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11 A 217 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12 A 217 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 A 217 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14 A 217 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15 A 217 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16 A 217 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17 A 217 THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 1 B 211 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 B 211 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 B 211 GLN SER VAL SER SER SER TYR LEU ALA TRP TYR GLN GLN SEQRES 4 B 211 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 B 211 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 B 211 SER GLY SER GLY ALA ASP PHE THR LEU THR ILE SER ARG SEQRES 7 B 211 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8 B 211 TYR GLY SER SER PRO LEU PHE GLY GLN GLY THR LYS LEU SEQRES 9 B 211 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 B 211 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 B 211 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 B 211 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 B 211 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 B 211 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 B 211 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 B 211 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 B 211 PHE ASN ARG HET NAG C 601 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 4 NAG C8 H15 N O6 FORMUL 5 HOH *157(H2 O) HELIX 1 AA1 PHE C 338 ASN C 343 1 6 HELIX 2 AA2 ASP C 364 ASN C 370 1 7 HELIX 3 AA3 THR C 385 LEU C 390 5 6 HELIX 4 AA4 ASP C 405 ILE C 410 5 6 HELIX 5 AA5 GLY C 416 ASN C 422 1 7 HELIX 6 AA6 SER C 438 SER C 443 1 6 HELIX 7 AA7 GLY C 502 TYR C 505 5 4 HELIX 8 AA8 ASP A 61 LYS A 64 5 4 HELIX 9 AA9 ARG A 86 THR A 90 5 5 HELIX 10 AB1 SER A 160 ALA A 162 5 3 HELIX 11 AB2 SER A 191 THR A 195 5 5 HELIX 12 AB3 SER B 30 LEU B 34 5 5 HELIX 13 AB4 GLU B 80 PHE B 84 5 5 HELIX 14 AB5 SER B 121 LYS B 126 1 6 HELIX 15 AB6 LYS B 183 HIS B 189 1 7 SHEET 1 AA1 5 ASN C 354 ILE C 358 0 SHEET 2 AA1 5 ASN C 394 ARG C 403 -1 O ALA C 397 N LYS C 356 SHEET 3 AA1 5 PRO C 507 GLU C 516 -1 O VAL C 510 N PHE C 400 SHEET 4 AA1 5 GLY C 431 ASN C 437 -1 N CYS C 432 O LEU C 513 SHEET 5 AA1 5 THR C 376 TYR C 380 -1 N THR C 376 O ALA C 435 SHEET 1 AA2 2 LEU C 452 ARG C 454 0 SHEET 2 AA2 2 LEU C 492 SER C 494 -1 O GLN C 493 N TYR C 453 SHEET 1 AA3 2 TYR C 473 GLN C 474 0 SHEET 2 AA3 2 CYS C 488 TYR C 489 -1 O TYR C 489 N TYR C 473 SHEET 1 AA4 4 GLN A 3 SER A 7 0 SHEET 2 AA4 4 LEU A 18 SER A 25 -1 O SER A 21 N SER A 7 SHEET 3 AA4 4 THR A 77 MET A 82 -1 O MET A 82 N LEU A 18 SHEET 4 AA4 4 PHE A 67 ASP A 72 -1 N THR A 68 O GLN A 81 SHEET 1 AA5 6 LEU A 11 ILE A 12 0 SHEET 2 AA5 6 THR A 111 VAL A 115 1 O THR A 114 N ILE A 12 SHEET 3 AA5 6 ALA A 91 GLY A 98 -1 N TYR A 93 O THR A 111 SHEET 4 AA5 6 TYR A 33 GLN A 39 -1 N VAL A 37 O TYR A 94 SHEET 5 AA5 6 LEU A 45 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA5 6 THR A 57 TYR A 59 -1 O PHE A 58 N VAL A 50 SHEET 1 AA6 4 LEU A 11 ILE A 12 0 SHEET 2 AA6 4 THR A 111 VAL A 115 1 O THR A 114 N ILE A 12 SHEET 3 AA6 4 ALA A 91 GLY A 98 -1 N TYR A 93 O THR A 111 SHEET 4 AA6 4 PHE A 104 TRP A 107 -1 O TYR A 106 N ARG A 97 SHEET 1 AA7 4 SER A 124 LEU A 128 0 SHEET 2 AA7 4 THR A 139 TYR A 149 -1 O LYS A 147 N SER A 124 SHEET 3 AA7 4 TYR A 180 PRO A 189 -1 O TYR A 180 N TYR A 149 SHEET 4 AA7 4 VAL A 167 THR A 169 -1 N HIS A 168 O VAL A 185 SHEET 1 AA8 4 SER A 124 LEU A 128 0 SHEET 2 AA8 4 THR A 139 TYR A 149 -1 O LYS A 147 N SER A 124 SHEET 3 AA8 4 TYR A 180 PRO A 189 -1 O TYR A 180 N TYR A 149 SHEET 4 AA8 4 VAL A 173 LEU A 174 -1 N VAL A 173 O SER A 181 SHEET 1 AA9 3 THR A 155 TRP A 158 0 SHEET 2 AA9 3 TYR A 198 HIS A 204 -1 O ASN A 201 N SER A 157 SHEET 3 AA9 3 THR A 209 VAL A 215 -1 O VAL A 211 N VAL A 202 SHEET 1 AB1 4 LEU B 4 SER B 7 0 SHEET 2 AB1 4 ALA B 19 ALA B 25 -1 O SER B 22 N SER B 7 SHEET 3 AB1 4 ASP B 71 ILE B 76 -1 O LEU B 74 N LEU B 21 SHEET 4 AB1 4 PHE B 63 SER B 68 -1 N SER B 64 O THR B 75 SHEET 1 AB2 6 THR B 10 LEU B 13 0 SHEET 2 AB2 6 THR B 102 ILE B 106 1 O LYS B 103 N LEU B 11 SHEET 3 AB2 6 ALA B 85 TYR B 92 -1 N ALA B 85 O LEU B 104 SHEET 4 AB2 6 ALA B 35 GLN B 39 -1 N GLN B 39 O VAL B 86 SHEET 5 AB2 6 ARG B 46 TYR B 50 -1 O ARG B 46 N GLN B 38 SHEET 6 AB2 6 SER B 54 ARG B 55 -1 O SER B 54 N TYR B 50 SHEET 1 AB3 4 THR B 10 LEU B 13 0 SHEET 2 AB3 4 THR B 102 ILE B 106 1 O LYS B 103 N LEU B 11 SHEET 3 AB3 4 ALA B 85 TYR B 92 -1 N ALA B 85 O LEU B 104 SHEET 4 AB3 4 PRO B 96 PHE B 98 -1 O LEU B 97 N GLN B 91 SHEET 1 AB4 4 SER B 114 PHE B 118 0 SHEET 2 AB4 4 THR B 129 PHE B 139 -1 O LEU B 135 N PHE B 116 SHEET 3 AB4 4 TYR B 173 SER B 182 -1 O LEU B 175 N LEU B 136 SHEET 4 AB4 4 SER B 159 VAL B 163 -1 N GLN B 160 O THR B 178 SHEET 1 AB5 4 ALA B 153 LEU B 154 0 SHEET 2 AB5 4 LYS B 145 VAL B 150 -1 N VAL B 150 O ALA B 153 SHEET 3 AB5 4 TYR B 192 THR B 197 -1 O THR B 197 N LYS B 145 SHEET 4 AB5 4 VAL B 205 SER B 208 -1 O VAL B 205 N VAL B 196 SSBOND 1 CYS C 336 CYS C 361 1555 1555 2.03 SSBOND 2 CYS C 379 CYS C 432 1555 1555 2.04 SSBOND 3 CYS C 480 CYS C 488 1555 1555 2.03 SSBOND 4 CYS A 22 CYS A 95 1555 1555 2.04 SSBOND 5 CYS A 144 CYS A 200 1555 1555 2.04 SSBOND 6 CYS B 23 CYS B 89 1555 1555 2.04 SSBOND 7 CYS B 134 CYS B 194 1555 1555 2.04 LINK ND2 ASN C 343 C1 NAG C 601 1555 1555 1.44 CISPEP 1 PHE A 150 PRO A 151 0 -0.98 CISPEP 2 GLU A 152 PRO A 153 0 -1.07 CISPEP 3 SER B 7 PRO B 8 0 -10.92 CISPEP 4 TYR B 140 PRO B 141 0 6.03 CRYST1 55.306 115.092 144.135 90.00 90.00 90.00 P 21 21 21 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 0.018081 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008689 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006938 0.00000