HEADER VIRAL PROTEIN/IMMUNE SYSTEM 10-JUN-24 9C6Y TITLE CRYSTAL STRUCTURE OF SARS-COV-2 XBB.1.5 RBD BOUND TO COV2-3906 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN OF COV2-3906 FAB; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: LIGHT CHAIN OF COV2-3906 FAB; COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: SPIKE PROTEIN S2'; COMPND 11 CHAIN: E, F; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS; SOURCE 15 ORGANISM_TAXID: 2901879; SOURCE 16 GENE: S, 2; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS CORONAVIRUS, ANTIBODY, FAB, IMMUNE SYSTEM, VIRAL PROTEIN-IMMUNE KEYWDS 2 SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR C.D.BUCHMAN,J.E.CROWE REVDAT 1 08-OCT-25 9C6Y 0 JRNL AUTH S.J.ZOST,C.D.BUCHMAN,J.E.CROWE JRNL TITL EPITOPE-FOCUSED DISCOVERY OF SARS-COV-2 ANTIBODIES THAT JRNL TITL 2 POTENTLY NEUTRALIZE OMICRON VARIANTS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.68 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.68 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.50 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 75515 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.208 REMARK 3 R VALUE (WORKING SET) : 0.207 REMARK 3 FREE R VALUE : 0.242 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.650 REMARK 3 FREE R VALUE TEST SET COUNT : 1999 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 48.5000 - 6.4500 1.00 5598 152 0.1914 0.1807 REMARK 3 2 6.4500 - 5.1200 1.00 5345 145 0.1708 0.1970 REMARK 3 3 5.1200 - 4.4800 1.00 5291 143 0.1374 0.1818 REMARK 3 4 4.4800 - 4.0700 1.00 5302 144 0.1514 0.1840 REMARK 3 5 4.0700 - 3.7800 0.99 5190 142 0.1882 0.2262 REMARK 3 6 3.7800 - 3.5500 1.00 5220 142 0.1985 0.2553 REMARK 3 7 3.5500 - 3.3800 1.00 5252 142 0.2190 0.3040 REMARK 3 8 3.3800 - 3.2300 1.00 5215 142 0.2957 0.3475 REMARK 3 9 3.2300 - 3.1100 1.00 5200 142 0.2784 0.3409 REMARK 3 10 3.1100 - 3.0000 1.00 5204 142 0.2761 0.3274 REMARK 3 11 3.0000 - 2.9000 1.00 5165 140 0.2821 0.3171 REMARK 3 12 2.9000 - 2.8200 1.00 5220 142 0.3242 0.3694 REMARK 3 13 2.8200 - 2.7500 1.00 5192 142 0.3990 0.4330 REMARK 3 14 2.7500 - 2.6800 1.00 5122 139 0.4728 0.4812 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) : 0.464 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.456 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 69.31 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 67.73 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 : 0.010 10268 REMARK 3 ANGLE : 1.067 14057 REMARK 3 CHIRALITY : 0.058 1613 REMARK 3 PLANARITY : 0.009 1786 REMARK 3 DIHEDRAL : 7.157 1479 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 25 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.4228 43.9258 25.4144 REMARK 3 T TENSOR REMARK 3 T11: 0.4265 T22: 0.5537 REMARK 3 T33: 0.5403 T12: -0.0143 REMARK 3 T13: 0.0558 T23: 0.0383 REMARK 3 L TENSOR REMARK 3 L11: 0.6454 L22: 4.4522 REMARK 3 L33: 4.5154 L12: -0.0296 REMARK 3 L13: -1.3631 L23: 2.6128 REMARK 3 S TENSOR REMARK 3 S11: 0.2981 S12: 0.1662 S13: 0.3734 REMARK 3 S21: -0.6581 S22: 0.0250 S23: -0.3752 REMARK 3 S31: -0.4467 S32: 0.4615 S33: -0.3511 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 18 THROUGH 73 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.9549 44.7846 37.5711 REMARK 3 T TENSOR REMARK 3 T11: 0.2509 T22: 0.4664 REMARK 3 T33: 0.4249 T12: -0.0036 REMARK 3 T13: -0.0596 T23: -0.0418 REMARK 3 L TENSOR REMARK 3 L11: 0.4502 L22: 4.2510 REMARK 3 L33: 3.3575 L12: 0.5266 REMARK 3 L13: -1.1640 L23: 0.8276 REMARK 3 S TENSOR REMARK 3 S11: 0.1248 S12: -0.0503 S13: -0.0280 REMARK 3 S21: 0.3411 S22: -0.0406 S23: -0.3462 REMARK 3 S31: 0.0213 S32: 0.4827 S33: -0.0779 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 74 THROUGH 118 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.7491 45.3369 34.6153 REMARK 3 T TENSOR REMARK 3 T11: 0.2558 T22: 0.4260 REMARK 3 T33: 0.4233 T12: -0.0094 REMARK 3 T13: -0.0087 T23: 0.0050 REMARK 3 L TENSOR REMARK 3 L11: 0.1847 L22: 2.8905 REMARK 3 L33: 4.5477 L12: -0.6446 REMARK 3 L13: 0.0134 L23: 1.5278 REMARK 3 S TENSOR REMARK 3 S11: 0.1559 S12: 0.2645 S13: -0.0496 REMARK 3 S21: 0.0028 S22: -0.2198 S23: -0.2761 REMARK 3 S31: -0.2608 S32: 0.0964 S33: 0.0875 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 119 THROUGH 143 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.7934 42.4675 3.2524 REMARK 3 T TENSOR REMARK 3 T11: 0.2486 T22: 0.5657 REMARK 3 T33: 0.6138 T12: 0.0425 REMARK 3 T13: -0.0778 T23: -0.1407 REMARK 3 L TENSOR REMARK 3 L11: 0.8568 L22: 3.0863 REMARK 3 L33: 4.5338 L12: 1.1811 REMARK 3 L13: -1.4209 L23: 0.5563 REMARK 3 S TENSOR REMARK 3 S11: 0.0957 S12: 0.4815 S13: 0.1113 REMARK 3 S21: -0.4411 S22: -0.3881 S23: 0.9112 REMARK 3 S31: -0.0984 S32: -0.3235 S33: 0.3154 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 144 THROUGH 166 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.4142 45.6437 6.5412 REMARK 3 T TENSOR REMARK 3 T11: 0.2561 T22: 0.6137 REMARK 3 T33: 0.5564 T12: 0.0424 REMARK 3 T13: 0.0419 T23: -0.0538 REMARK 3 L TENSOR REMARK 3 L11: 0.4053 L22: 3.8954 REMARK 3 L33: 2.8685 L12: 1.2324 REMARK 3 L13: 0.0500 L23: -0.0517 REMARK 3 S TENSOR REMARK 3 S11: -0.2226 S12: 0.1575 S13: 0.0137 REMARK 3 S21: 0.0475 S22: -0.0227 S23: 0.3130 REMARK 3 S31: -0.1711 S32: 0.0922 S33: 0.1801 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 167 THROUGH 223 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.0285 48.0749 4.4312 REMARK 3 T TENSOR REMARK 3 T11: 0.2244 T22: 0.5545 REMARK 3 T33: 0.4825 T12: 0.0718 REMARK 3 T13: -0.0178 T23: -0.0159 REMARK 3 L TENSOR REMARK 3 L11: 0.3694 L22: 6.1346 REMARK 3 L33: 3.0531 L12: 1.4408 REMARK 3 L13: 0.1774 L23: -0.4473 REMARK 3 S TENSOR REMARK 3 S11: -0.1618 S12: -0.0241 S13: 0.2145 REMARK 3 S21: -0.0076 S22: 0.1279 S23: 0.4855 REMARK 3 S31: -0.3360 S32: -0.2493 S33: 0.0226 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 94 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.5819 41.1338 39.0199 REMARK 3 T TENSOR REMARK 3 T11: 0.2677 T22: 0.4597 REMARK 3 T33: 0.4094 T12: -0.0087 REMARK 3 T13: 0.0334 T23: -0.0144 REMARK 3 L TENSOR REMARK 3 L11: 4.0949 L22: 4.8915 REMARK 3 L33: 6.7215 L12: 0.6756 REMARK 3 L13: 1.3244 L23: 0.0520 REMARK 3 S TENSOR REMARK 3 S11: 0.1603 S12: 0.2087 S13: -0.0959 REMARK 3 S21: -0.0095 S22: 0.0788 S23: 0.5389 REMARK 3 S31: 0.2811 S32: -0.7198 S33: -0.2215 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 95 THROUGH 133 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.1607 38.2407 14.4959 REMARK 3 T TENSOR REMARK 3 T11: 0.2084 T22: 0.4839 REMARK 3 T33: 0.4907 T12: 0.0260 REMARK 3 T13: -0.0177 T23: -0.0220 REMARK 3 L TENSOR REMARK 3 L11: 0.2335 L22: 0.8381 REMARK 3 L33: 4.1256 L12: 0.1944 REMARK 3 L13: 0.3173 L23: -0.1012 REMARK 3 S TENSOR REMARK 3 S11: -0.0258 S12: 0.1015 S13: 0.0034 REMARK 3 S21: -0.0245 S22: 0.0259 S23: 0.1397 REMARK 3 S31: 0.3794 S32: -0.4382 S33: -0.0152 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 134 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.1168 33.5388 -0.5997 REMARK 3 T TENSOR REMARK 3 T11: 0.2476 T22: 0.5350 REMARK 3 T33: 0.4807 T12: 0.0620 REMARK 3 T13: -0.0186 T23: 0.0137 REMARK 3 L TENSOR REMARK 3 L11: 5.2547 L22: 2.2588 REMARK 3 L33: 5.2198 L12: -0.0973 REMARK 3 L13: -2.1717 L23: 0.7879 REMARK 3 S TENSOR REMARK 3 S11: -0.1081 S12: -0.0017 S13: -0.0766 REMARK 3 S21: -0.0182 S22: 0.1036 S23: 0.0400 REMARK 3 S31: 0.1437 S32: 0.1490 S33: -0.0340 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 118 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.7670 6.9143 55.4320 REMARK 3 T TENSOR REMARK 3 T11: 0.6413 T22: 0.4882 REMARK 3 T33: 0.5642 T12: 0.1310 REMARK 3 T13: 0.0406 T23: 0.1080 REMARK 3 L TENSOR REMARK 3 L11: 4.9606 L22: 1.6831 REMARK 3 L33: 2.8075 L12: 0.1118 REMARK 3 L13: 1.6656 L23: -0.5798 REMARK 3 S TENSOR REMARK 3 S11: 0.0495 S12: -0.0579 S13: 0.1413 REMARK 3 S21: 0.1251 S22: -0.0284 S23: 0.3203 REMARK 3 S31: -0.2279 S32: -0.3281 S33: -0.0208 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 119 THROUGH 184 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.1917 7.9479 30.2153 REMARK 3 T TENSOR REMARK 3 T11: 0.7476 T22: 0.6481 REMARK 3 T33: 0.9265 T12: 0.1561 REMARK 3 T13: 0.1194 T23: 0.2099 REMARK 3 L TENSOR REMARK 3 L11: 3.6920 L22: 0.6723 REMARK 3 L33: 6.2042 L12: 0.4301 REMARK 3 L13: 1.3329 L23: -1.7921 REMARK 3 S TENSOR REMARK 3 S11: -0.4136 S12: -0.5420 S13: -0.7298 REMARK 3 S21: -0.0293 S22: 0.3200 S23: 0.0311 REMARK 3 S31: 1.3507 S32: 0.1864 S33: 0.1184 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 185 THROUGH 200 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.0502 2.4645 20.2949 REMARK 3 T TENSOR REMARK 3 T11: 1.3020 T22: 0.8145 REMARK 3 T33: 1.0261 T12: 0.1634 REMARK 3 T13: 0.1333 T23: 0.0370 REMARK 3 L TENSOR REMARK 3 L11: 5.4573 L22: 6.0994 REMARK 3 L33: 7.1440 L12: 0.8095 REMARK 3 L13: 0.3709 L23: 4.9012 REMARK 3 S TENSOR REMARK 3 S11: 0.1001 S12: 0.2943 S13: -1.3247 REMARK 3 S21: -0.3686 S22: 0.4005 S23: -0.8346 REMARK 3 S31: 1.5324 S32: 0.3496 S33: -0.5306 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 201 THROUGH 224 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.8697 0.0422 28.9776 REMARK 3 T TENSOR REMARK 3 T11: 1.2838 T22: 0.7351 REMARK 3 T33: 1.1481 T12: 0.1303 REMARK 3 T13: 0.3039 T23: 0.2348 REMARK 3 L TENSOR REMARK 3 L11: 2.6197 L22: 4.7261 REMARK 3 L33: 1.8395 L12: 0.3338 REMARK 3 L13: 0.1114 L23: 2.9815 REMARK 3 S TENSOR REMARK 3 S11: -0.4314 S12: -0.5996 S13: -0.8447 REMARK 3 S21: 0.5762 S22: -0.0804 S23: 0.5812 REMARK 3 S31: 2.3512 S32: -0.0628 S33: 0.5053 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 110 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.0578 14.9554 43.2901 REMARK 3 T TENSOR REMARK 3 T11: 0.6524 T22: 0.4634 REMARK 3 T33: 0.5863 T12: 0.0585 REMARK 3 T13: -0.0032 T23: 0.1268 REMARK 3 L TENSOR REMARK 3 L11: 2.3124 L22: 2.3738 REMARK 3 L33: 7.3591 L12: 0.6403 REMARK 3 L13: 0.5444 L23: -1.1328 REMARK 3 S TENSOR REMARK 3 S11: -0.0437 S12: 0.3940 S13: 0.4580 REMARK 3 S21: -0.2465 S22: 0.0477 S23: 0.0504 REMARK 3 S31: -0.8641 S32: 0.0318 S33: 0.0195 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 111 THROUGH 177 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.5344 17.2064 20.5645 REMARK 3 T TENSOR REMARK 3 T11: 0.4680 T22: 0.3650 REMARK 3 T33: 0.5101 T12: 0.0756 REMARK 3 T13: -0.0088 T23: 0.0137 REMARK 3 L TENSOR REMARK 3 L11: 5.6256 L22: 3.6162 REMARK 3 L33: 4.9787 L12: -0.0158 REMARK 3 L13: 0.6527 L23: -0.5825 REMARK 3 S TENSOR REMARK 3 S11: 0.2105 S12: -0.3186 S13: -0.9482 REMARK 3 S21: 0.1098 S22: -0.1190 S23: -0.0955 REMARK 3 S31: 0.6906 S32: 0.2358 S33: -0.0711 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 178 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.4829 20.3719 15.2116 REMARK 3 T TENSOR REMARK 3 T11: 0.3886 T22: 0.3608 REMARK 3 T33: 0.5336 T12: -0.0004 REMARK 3 T13: -0.0315 T23: -0.0684 REMARK 3 L TENSOR REMARK 3 L11: 5.2156 L22: 6.3294 REMARK 3 L33: 8.8747 L12: 0.0097 REMARK 3 L13: -0.3469 L23: -0.4649 REMARK 3 S TENSOR REMARK 3 S11: 0.1867 S12: 0.1416 S13: 0.3584 REMARK 3 S21: -0.4117 S22: -0.0569 S23: 0.8068 REMARK 3 S31: 0.4093 S32: -0.6230 S33: -0.0819 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 321 THROUGH 358 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.9494 56.1735 64.9494 REMARK 3 T TENSOR REMARK 3 T11: 0.7098 T22: 0.5508 REMARK 3 T33: 0.4251 T12: -0.1256 REMARK 3 T13: -0.0808 T23: -0.0583 REMARK 3 L TENSOR REMARK 3 L11: 1.0291 L22: 6.7418 REMARK 3 L33: 3.2383 L12: 0.9610 REMARK 3 L13: 0.0106 L23: -2.7460 REMARK 3 S TENSOR REMARK 3 S11: 0.2112 S12: -0.4111 S13: 0.1406 REMARK 3 S21: 1.4277 S22: -0.3675 S23: -0.4180 REMARK 3 S31: -0.1797 S32: -0.0680 S33: 0.1231 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 359 THROUGH 442 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.8637 46.8352 62.1527 REMARK 3 T TENSOR REMARK 3 T11: 0.5864 T22: 0.4501 REMARK 3 T33: 0.3804 T12: -0.0949 REMARK 3 T13: -0.0686 T23: -0.0498 REMARK 3 L TENSOR REMARK 3 L11: 1.1453 L22: 2.9906 REMARK 3 L33: 2.3986 L12: -0.0265 REMARK 3 L13: -0.4043 L23: -0.6610 REMARK 3 S TENSOR REMARK 3 S11: 0.1521 S12: -0.1911 S13: 0.0041 REMARK 3 S21: 0.7997 S22: -0.1344 S23: -0.0781 REMARK 3 S31: -0.0367 S32: -0.0772 S33: -0.0297 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 443 THROUGH 479 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.3929 38.3252 81.3853 REMARK 3 T TENSOR REMARK 3 T11: 1.1303 T22: 0.7510 REMARK 3 T33: 0.4583 T12: -0.1950 REMARK 3 T13: -0.0561 T23: -0.0657 REMARK 3 L TENSOR REMARK 3 L11: 4.8565 L22: 3.1884 REMARK 3 L33: 2.6517 L12: -1.0436 REMARK 3 L13: 0.1261 L23: -1.0032 REMARK 3 S TENSOR REMARK 3 S11: 0.0988 S12: -1.1332 S13: 0.2963 REMARK 3 S21: 0.9414 S22: -0.0460 S23: 0.0418 REMARK 3 S31: 0.0465 S32: 0.2042 S33: -0.0011 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 480 THROUGH 523 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.2114 39.4662 73.1271 REMARK 3 T TENSOR REMARK 3 T11: 0.8019 T22: 0.6291 REMARK 3 T33: 0.4174 T12: -0.1008 REMARK 3 T13: -0.1136 T23: -0.0180 REMARK 3 L TENSOR REMARK 3 L11: 1.3063 L22: 3.1253 REMARK 3 L33: 2.2856 L12: 0.4036 REMARK 3 L13: -0.0209 L23: -0.3854 REMARK 3 S TENSOR REMARK 3 S11: 0.1694 S12: -0.4786 S13: -0.1527 REMARK 3 S21: 0.5908 S22: -0.0831 S23: 0.1991 REMARK 3 S31: 0.3393 S32: -0.1049 S33: -0.0222 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 524 THROUGH 534 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.8520 64.1964 49.0536 REMARK 3 T TENSOR REMARK 3 T11: 0.6522 T22: 0.4691 REMARK 3 T33: 0.6299 T12: -0.1191 REMARK 3 T13: -0.0365 T23: -0.0138 REMARK 3 L TENSOR REMARK 3 L11: 5.9685 L22: 9.8719 REMARK 3 L33: 2.0079 L12: -2.8561 REMARK 3 L13: 6.3639 L23: 3.6767 REMARK 3 S TENSOR REMARK 3 S11: -0.0346 S12: 0.6487 S13: 0.4696 REMARK 3 S21: -0.4245 S22: 0.0306 S23: -0.9622 REMARK 3 S31: -0.3904 S32: 0.6298 S33: -0.1051 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 321 THROUGH 373 ) REMARK 3 ORIGIN FOR THE GROUP (A): 53.0793 0.2454 72.1679 REMARK 3 T TENSOR REMARK 3 T11: 0.8375 T22: 0.5120 REMARK 3 T33: 0.4955 T12: -0.0186 REMARK 3 T13: -0.0175 T23: 0.0547 REMARK 3 L TENSOR REMARK 3 L11: 0.8346 L22: 4.2279 REMARK 3 L33: 0.8557 L12: 1.9336 REMARK 3 L13: -0.0037 L23: 0.3459 REMARK 3 S TENSOR REMARK 3 S11: 0.2267 S12: -0.2867 S13: -0.1266 REMARK 3 S21: 1.0933 S22: -0.2780 S23: -0.2784 REMARK 3 S31: 0.0912 S32: 0.0105 S33: 0.0450 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 374 THROUGH 459 ) REMARK 3 ORIGIN FOR THE GROUP (A): 61.0448 13.1777 68.3515 REMARK 3 T TENSOR REMARK 3 T11: 0.8709 T22: 0.4736 REMARK 3 T33: 0.4977 T12: -0.0389 REMARK 3 T13: -0.0615 T23: 0.0642 REMARK 3 L TENSOR REMARK 3 L11: 2.0229 L22: 1.9090 REMARK 3 L33: 1.3249 L12: 1.2104 REMARK 3 L13: 0.3198 L23: 0.2010 REMARK 3 S TENSOR REMARK 3 S11: 0.0658 S12: -0.1371 S13: 0.0349 REMARK 3 S21: 0.1959 S22: -0.0210 S23: -0.0253 REMARK 3 S31: -0.3521 S32: 0.1021 S33: -0.0727 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 460 THROUGH 494 ) REMARK 3 ORIGIN FOR THE GROUP (A): 77.2343 20.5052 82.1446 REMARK 3 T TENSOR REMARK 3 T11: 1.2102 T22: 0.7925 REMARK 3 T33: 0.5974 T12: -0.2001 REMARK 3 T13: -0.2520 T23: 0.1617 REMARK 3 L TENSOR REMARK 3 L11: 3.3715 L22: 5.3914 REMARK 3 L33: 1.1715 L12: 3.0558 REMARK 3 L13: 0.7454 L23: 2.2442 REMARK 3 S TENSOR REMARK 3 S11: 0.4540 S12: -1.0121 S13: -0.5426 REMARK 3 S21: 1.1671 S22: -0.2759 S23: -0.8955 REMARK 3 S31: -0.3542 S32: 0.0754 S33: -0.1975 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 495 THROUGH 534 ) REMARK 3 ORIGIN FOR THE GROUP (A): 54.7525 7.2135 68.7455 REMARK 3 T TENSOR REMARK 3 T11: 0.6317 T22: 0.4779 REMARK 3 T33: 0.4277 T12: 0.0363 REMARK 3 T13: -0.0214 T23: 0.0634 REMARK 3 L TENSOR REMARK 3 L11: 1.1472 L22: 4.2601 REMARK 3 L33: 2.3786 L12: 1.4555 REMARK 3 L13: 0.2162 L23: 1.5124 REMARK 3 S TENSOR REMARK 3 S11: 0.1136 S12: -0.1365 S13: 0.1183 REMARK 3 S21: 0.2778 S22: -0.2545 S23: 0.1877 REMARK 3 S31: -0.0453 S32: 0.0202 S33: 0.0960 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 9C6Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1000284886. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-APR-24 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 : ESRF REMARK 200 BEAMLINE : MASSIF-3 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.961 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75613 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.680 REMARK 200 RESOLUTION RANGE LOW (A) : 48.500 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 13.80 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.68 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.77 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 14.50 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 73.44 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.63 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M AMMONIUM SULFATE, 0.1 M SODIUM REMARK 280 ACETATE PH 5.1, 2 MM DL-PANTHENOL, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K 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 33.48550 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 115.77150 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 85.42550 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 115.77150 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.48550 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 85.42550 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7560 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 29810 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, G REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7570 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 30060 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F, H 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 SER A 224 REMARK 465 CYS A 225 REMARK 465 GLU B 214 REMARK 465 CYS B 215 REMARK 465 SER B 216 REMARK 465 SER C 137 REMARK 465 LYS C 138 REMARK 465 SER C 139 REMARK 465 THR C 140 REMARK 465 SER C 141 REMARK 465 CYS C 225 REMARK 465 GLU D 214 REMARK 465 CYS D 215 REMARK 465 SER D 216 REMARK 465 ARG E 319 REMARK 465 VAL E 320 REMARK 465 ARG F 319 REMARK 465 VAL F 320 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 GLN A 1 CG CD OE1 NE2 REMARK 470 GLN A 114 CG CD OE1 NE2 REMARK 470 LYS A 223 CG CD CE NZ REMARK 470 LYS B 170 CG CD CE NZ REMARK 470 GLN C 1 CG CD OE1 NE2 REMARK 470 LYS C 45 CG CD CE NZ REMARK 470 LEU C 198 CG CD1 CD2 REMARK 470 THR C 200 OG1 CG2 REMARK 470 GLN C 201 CG CD OE1 NE2 REMARK 470 THR C 202 OG1 CG2 REMARK 470 ILE C 204 CG1 CG2 CD1 REMARK 470 LYS C 210 CG CD CE NZ REMARK 470 ASN C 213 CG OD1 ND2 REMARK 470 LYS C 215 CG CD CE NZ REMARK 470 LYS C 219 CG CD CE NZ REMARK 470 VAL C 220 CG1 CG2 REMARK 470 GLU C 221 CG CD OE1 OE2 REMARK 470 LYS C 223 CG CD CE NZ REMARK 470 SER C 224 OG REMARK 470 LYS D 16 CG CD CE NZ REMARK 470 GLU D 84 CG CD OE1 OE2 REMARK 470 LYS D 190 CG CD CE NZ REMARK 470 GLN E 321 CG CD OE1 NE2 REMARK 470 LYS E 440 CG CD CE NZ REMARK 470 LYS E 444 CG CD CE NZ REMARK 470 LYS E 458 CG CD CE NZ REMARK 470 LYS E 478 CG CD CE NZ REMARK 470 ASN E 481 CG OD1 ND2 REMARK 470 VAL E 483 CG1 CG2 REMARK 470 PHE E 533 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLN F 321 CG CD OE1 NE2 REMARK 470 LYS F 444 CG CD CE NZ REMARK 470 LYS F 458 CG CD CE NZ REMARK 470 LYS F 478 CG CD CE NZ REMARK 470 ASN F 481 CG OD1 ND2 REMARK 470 VAL F 483 CG1 CG2 REMARK 470 PHE F 533 CG CD1 CD2 CE1 CE2 CZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 GLU D 51 CD GLU D 51 OE2 0.070 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 CYS D 22 CA - CB - SG ANGL. DEV. = 8.7 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 SER A 15 -0.51 82.02 REMARK 500 ILE A 104 -104.06 49.58 REMARK 500 ASP A 110 126.45 179.96 REMARK 500 PRO A 135 131.12 -26.25 REMARK 500 SER A 139 -3.71 -145.44 REMARK 500 SER A 141 -35.22 -26.64 REMARK 500 ASP A 153 48.75 72.37 REMARK 500 THR A 169 -39.71 -135.52 REMARK 500 PRO B 41 126.45 -38.99 REMARK 500 ASP B 52 -50.47 72.18 REMARK 500 ASN B 53 14.51 -148.92 REMARK 500 SER B 93 -150.14 -161.25 REMARK 500 ASP B 155 -108.50 52.45 REMARK 500 SER C 64 20.94 -79.17 REMARK 500 LEU C 65 -36.44 -152.94 REMARK 500 ASN C 66 -55.49 -22.05 REMARK 500 SER C 67 -49.18 -25.87 REMARK 500 ALA C 90 0.73 -68.46 REMARK 500 ILE C 104 -103.78 53.25 REMARK 500 ASP C 110 125.90 -172.05 REMARK 500 ASP C 153 70.90 66.68 REMARK 500 THR C 169 -41.92 -136.33 REMARK 500 THR C 200 -79.93 -96.22 REMARK 500 SER D 26 78.21 54.30 REMARK 500 ASP D 52 -52.69 67.87 REMARK 500 ASN D 53 16.50 -145.60 REMARK 500 SER D 93 -145.92 -152.65 REMARK 500 ASP D 155 -122.17 49.87 REMARK 500 ASN E 422 -49.84 -130.63 REMARK 500 PRO E 479 155.08 -46.71 REMARK 500 ALA F 352 45.54 -109.43 REMARK 500 PRO F 373 79.92 -65.44 REMARK 500 PRO F 384 -35.78 -39.83 REMARK 500 ASN F 422 -61.43 -135.35 REMARK 500 ASP F 428 35.79 -87.55 REMARK 500 ASN F 481 -74.11 54.09 REMARK 500 ASN F 487 17.18 58.87 REMARK 500 PHE F 497 105.56 -54.30 REMARK 500 REMARK 500 REMARK: NULL DBREF 9C6Y A 1 225 PDB 9C6Y 9C6Y 1 225 DBREF 9C6Y B 1 216 PDB 9C6Y 9C6Y 1 216 DBREF 9C6Y C 1 225 PDB 9C6Y 9C6Y 1 225 DBREF 9C6Y D 1 216 PDB 9C6Y 9C6Y 1 216 DBREF 9C6Y E 319 534 UNP P0DTC2 SPIKE_SARS2 319 534 DBREF 9C6Y F 319 534 UNP P0DTC2 SPIKE_SARS2 319 534 SEQADV 9C6Y HIS E 339 UNP P0DTC2 GLY 339 CONFLICT SEQADV 9C6Y THR E 346 UNP P0DTC2 ARG 346 CONFLICT SEQADV 9C6Y PHE E 365 UNP P0DTC2 TYR 365 CONFLICT SEQADV 9C6Y ILE E 368 UNP P0DTC2 LEU 368 CONFLICT SEQADV 9C6Y PHE E 371 UNP P0DTC2 SER 371 CONFLICT SEQADV 9C6Y PRO E 373 UNP P0DTC2 SER 373 CONFLICT SEQADV 9C6Y PHE E 375 UNP P0DTC2 SER 375 CONFLICT SEQADV 9C6Y ALA E 376 UNP P0DTC2 THR 376 CONFLICT SEQADV 9C6Y TRP E 392 UNP P0DTC2 PHE 392 CONFLICT SEQADV 9C6Y ILE E 395 UNP P0DTC2 VAL 395 CONFLICT SEQADV 9C6Y ASN E 405 UNP P0DTC2 ASP 405 CONFLICT SEQADV 9C6Y SER E 408 UNP P0DTC2 ARG 408 CONFLICT SEQADV 9C6Y ASN E 417 UNP P0DTC2 LYS 417 CONFLICT SEQADV 9C6Y LYS E 440 UNP P0DTC2 ASN 440 CONFLICT SEQADV 9C6Y PRO E 445 UNP P0DTC2 VAL 445 CONFLICT SEQADV 9C6Y SER E 446 UNP P0DTC2 GLY 446 CONFLICT SEQADV 9C6Y LYS E 460 UNP P0DTC2 ASN 460 CONFLICT SEQADV 9C6Y ASN E 477 UNP P0DTC2 SER 477 CONFLICT SEQADV 9C6Y LYS E 478 UNP P0DTC2 THR 478 CONFLICT SEQADV 9C6Y ALA E 484 UNP P0DTC2 GLU 484 CONFLICT SEQADV 9C6Y PRO E 486 UNP P0DTC2 PHE 486 CONFLICT SEQADV 9C6Y SER E 490 UNP P0DTC2 PHE 490 CONFLICT SEQADV 9C6Y ARG E 498 UNP P0DTC2 GLN 498 CONFLICT SEQADV 9C6Y TYR E 501 UNP P0DTC2 ASN 501 CONFLICT SEQADV 9C6Y HIS E 505 UNP P0DTC2 TYR 505 CONFLICT SEQADV 9C6Y LEU E 529 UNP P0DTC2 LYS 529 CONFLICT SEQADV 9C6Y GLU E 530 UNP P0DTC2 SER 530 CONFLICT SEQADV 9C6Y VAL E 531 UNP P0DTC2 THR 531 CONFLICT SEQADV 9C6Y LEU E 532 UNP P0DTC2 ASN 532 CONFLICT SEQADV 9C6Y PHE E 533 UNP P0DTC2 LEU 533 CONFLICT SEQADV 9C6Y GLN E 534 UNP P0DTC2 VAL 534 CONFLICT SEQADV 9C6Y HIS F 339 UNP P0DTC2 GLY 339 CONFLICT SEQADV 9C6Y THR F 346 UNP P0DTC2 ARG 346 CONFLICT SEQADV 9C6Y PHE F 365 UNP P0DTC2 TYR 365 CONFLICT SEQADV 9C6Y ILE F 368 UNP P0DTC2 LEU 368 CONFLICT SEQADV 9C6Y PHE F 371 UNP P0DTC2 SER 371 CONFLICT SEQADV 9C6Y PRO F 373 UNP P0DTC2 SER 373 CONFLICT SEQADV 9C6Y PHE F 375 UNP P0DTC2 SER 375 CONFLICT SEQADV 9C6Y ALA F 376 UNP P0DTC2 THR 376 CONFLICT SEQADV 9C6Y TRP F 392 UNP P0DTC2 PHE 392 CONFLICT SEQADV 9C6Y ILE F 395 UNP P0DTC2 VAL 395 CONFLICT SEQADV 9C6Y ASN F 405 UNP P0DTC2 ASP 405 CONFLICT SEQADV 9C6Y SER F 408 UNP P0DTC2 ARG 408 CONFLICT SEQADV 9C6Y ASN F 417 UNP P0DTC2 LYS 417 CONFLICT SEQADV 9C6Y LYS F 440 UNP P0DTC2 ASN 440 CONFLICT SEQADV 9C6Y PRO F 445 UNP P0DTC2 VAL 445 CONFLICT SEQADV 9C6Y SER F 446 UNP P0DTC2 GLY 446 CONFLICT SEQADV 9C6Y LYS F 460 UNP P0DTC2 ASN 460 CONFLICT SEQADV 9C6Y ASN F 477 UNP P0DTC2 SER 477 CONFLICT SEQADV 9C6Y LYS F 478 UNP P0DTC2 THR 478 CONFLICT SEQADV 9C6Y ALA F 484 UNP P0DTC2 GLU 484 CONFLICT SEQADV 9C6Y PRO F 486 UNP P0DTC2 PHE 486 CONFLICT SEQADV 9C6Y SER F 490 UNP P0DTC2 PHE 490 CONFLICT SEQADV 9C6Y ARG F 498 UNP P0DTC2 GLN 498 CONFLICT SEQADV 9C6Y TYR F 501 UNP P0DTC2 ASN 501 CONFLICT SEQADV 9C6Y HIS F 505 UNP P0DTC2 TYR 505 CONFLICT SEQADV 9C6Y LEU F 529 UNP P0DTC2 LYS 529 CONFLICT SEQADV 9C6Y GLU F 530 UNP P0DTC2 SER 530 CONFLICT SEQADV 9C6Y VAL F 531 UNP P0DTC2 THR 531 CONFLICT SEQADV 9C6Y LEU F 532 UNP P0DTC2 ASN 532 CONFLICT SEQADV 9C6Y PHE F 533 UNP P0DTC2 LEU 533 CONFLICT SEQADV 9C6Y GLN F 534 UNP P0DTC2 VAL 534 CONFLICT SEQRES 1 A 225 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 A 225 PRO SER GLN THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 A 225 ASP SER ILE SER SER ASP GLY TYR TYR TRP SER TRP LEU SEQRES 4 A 225 ARG GLN ARG PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR SEQRES 5 A 225 ILE TYR ASN SER GLY SER THR HIS TYR ASN PRO SER LEU SEQRES 6 A 225 ASN SER ARG VAL SER ILE SER ILE ASP THR SER LYS THR SEQRES 7 A 225 GLN PHE SER LEU LYS LEU SER SER VAL THR ALA ALA ASP SEQRES 8 A 225 THR ALA VAL TYR TYR CYS ALA ARG ALA LEU VAL LEU ILE SEQRES 9 A 225 THR TYR VAL TRP PHE ASP PRO TRP GLY GLN GLY THR LEU SEQRES 10 A 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 A 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 A 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 A 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 A 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 A 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 A 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 A 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 A 225 PRO LYS SER CYS SEQRES 1 B 216 ASN PHE MET LEU THR GLN PRO HIS SER VAL SER GLU SER SEQRES 2 B 216 PRO GLY LYS THR VAL THR ILE SER CYS THR GLY SER SER SEQRES 3 B 216 GLY SER VAL ALA SER ASN TYR VAL GLN TRP TYR GLN HIS SEQRES 4 B 216 ARG PRO GLY SER ALA PRO THR THR VAL ILE TYR GLU ASP SEQRES 5 B 216 ASN GLN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY SEQRES 6 B 216 SER ILE ASP SER SER SER ASN SER ALA SER LEU THR ILE SEQRES 7 B 216 SER GLU LEU LYS PRO GLU ASP GLU ALA ASP TYR TYR CYS SEQRES 8 B 216 GLN SER TYR GLY ASP ARG ASN VAL VAL PHE GLY GLY GLY SEQRES 9 B 216 THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 B 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 B 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 B 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 B 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 14 B 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 B 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 B 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 B 216 THR VAL ALA PRO THR GLU CYS SER SEQRES 1 C 225 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 C 225 PRO SER GLN THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 C 225 ASP SER ILE SER SER ASP GLY TYR TYR TRP SER TRP LEU SEQRES 4 C 225 ARG GLN ARG PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR SEQRES 5 C 225 ILE TYR ASN SER GLY SER THR HIS TYR ASN PRO SER LEU SEQRES 6 C 225 ASN SER ARG VAL SER ILE SER ILE ASP THR SER LYS THR SEQRES 7 C 225 GLN PHE SER LEU LYS LEU SER SER VAL THR ALA ALA ASP SEQRES 8 C 225 THR ALA VAL TYR TYR CYS ALA ARG ALA LEU VAL LEU ILE SEQRES 9 C 225 THR TYR VAL TRP PHE ASP PRO TRP GLY GLN GLY THR LEU SEQRES 10 C 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 C 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 C 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 C 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 C 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 C 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 C 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 C 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 C 225 PRO LYS SER CYS SEQRES 1 D 216 ASN PHE MET LEU THR GLN PRO HIS SER VAL SER GLU SER SEQRES 2 D 216 PRO GLY LYS THR VAL THR ILE SER CYS THR GLY SER SER SEQRES 3 D 216 GLY SER VAL ALA SER ASN TYR VAL GLN TRP TYR GLN HIS SEQRES 4 D 216 ARG PRO GLY SER ALA PRO THR THR VAL ILE TYR GLU ASP SEQRES 5 D 216 ASN GLN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY SEQRES 6 D 216 SER ILE ASP SER SER SER ASN SER ALA SER LEU THR ILE SEQRES 7 D 216 SER GLU LEU LYS PRO GLU ASP GLU ALA ASP TYR TYR CYS SEQRES 8 D 216 GLN SER TYR GLY ASP ARG ASN VAL VAL PHE GLY GLY GLY SEQRES 9 D 216 THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 D 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 D 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 D 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 D 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 14 D 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 D 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 D 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 D 216 THR VAL ALA PRO THR GLU CYS SER SEQRES 1 E 216 ARG VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN SEQRES 2 E 216 ILE THR ASN LEU CYS PRO PHE HIS GLU VAL PHE ASN ALA SEQRES 3 E 216 THR THR PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG SEQRES 4 E 216 ILE SER ASN CYS VAL ALA ASP PHE SER VAL ILE TYR ASN SEQRES 5 E 216 PHE ALA PRO PHE PHE ALA PHE LYS CYS TYR GLY VAL SER SEQRES 6 E 216 PRO THR LYS LEU ASN ASP LEU CYS TRP THR ASN ILE TYR SEQRES 7 E 216 ALA ASP SER PHE VAL ILE ARG GLY ASN GLU VAL SER GLN SEQRES 8 E 216 ILE ALA PRO GLY GLN THR GLY ASN ILE ALA ASP TYR ASN SEQRES 9 E 216 TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA SEQRES 10 E 216 TRP ASN SER ASN LYS LEU ASP SER LYS PRO SER GLY ASN SEQRES 11 E 216 TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER LYS LEU SEQRES 12 E 216 LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN SEQRES 13 E 216 ALA GLY ASN LYS PRO CYS ASN GLY VAL ALA GLY PRO ASN SEQRES 14 E 216 CYS TYR SER PRO LEU GLN SER TYR GLY PHE ARG PRO THR SEQRES 15 E 216 TYR GLY VAL GLY HIS GLN PRO TYR ARG VAL VAL VAL LEU SEQRES 16 E 216 SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY SEQRES 17 E 216 PRO LYS LEU GLU VAL LEU PHE GLN SEQRES 1 F 216 ARG VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN SEQRES 2 F 216 ILE THR ASN LEU CYS PRO PHE HIS GLU VAL PHE ASN ALA SEQRES 3 F 216 THR THR PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG SEQRES 4 F 216 ILE SER ASN CYS VAL ALA ASP PHE SER VAL ILE TYR ASN SEQRES 5 F 216 PHE ALA PRO PHE PHE ALA PHE LYS CYS TYR GLY VAL SER SEQRES 6 F 216 PRO THR LYS LEU ASN ASP LEU CYS TRP THR ASN ILE TYR SEQRES 7 F 216 ALA ASP SER PHE VAL ILE ARG GLY ASN GLU VAL SER GLN SEQRES 8 F 216 ILE ALA PRO GLY GLN THR GLY ASN ILE ALA ASP TYR ASN SEQRES 9 F 216 TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA SEQRES 10 F 216 TRP ASN SER ASN LYS LEU ASP SER LYS PRO SER GLY ASN SEQRES 11 F 216 TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER LYS LEU SEQRES 12 F 216 LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN SEQRES 13 F 216 ALA GLY ASN LYS PRO CYS ASN GLY VAL ALA GLY PRO ASN SEQRES 14 F 216 CYS TYR SER PRO LEU GLN SER TYR GLY PHE ARG PRO THR SEQRES 15 F 216 TYR GLY VAL GLY HIS GLN PRO TYR ARG VAL VAL VAL LEU SEQRES 16 F 216 SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY SEQRES 17 F 216 PRO LYS LEU GLU VAL LEU PHE GLN HET NAG G 1 14 HET NAG G 2 14 HET BMA G 3 11 HET FUC G 4 10 HET NAG H 1 14 HET NAG H 2 14 HET BMA H 3 11 HET MAN H 4 11 HET FUC H 5 10 HET SO4 B 301 5 HET SO4 B 302 5 HET CL B 303 1 HET CL D 301 1 HET NAG E 601 14 HET A2G E 602 14 HET SO4 E 603 5 HET SO4 E 604 5 HET NAG F 601 14 HET A2G F 602 14 HET SO4 F 603 5 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM SO4 SULFATE ION HETNAM CL CHLORIDE ION HETNAM A2G 2-ACETAMIDO-2-DEOXY-ALPHA-D-GALACTOPYRANOSE 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 HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN A2G N-ACETYL-ALPHA-D-GALACTOSAMINE; 2-ACETAMIDO-2-DEOXY- HETSYN 2 A2G ALPHA-D-GALACTOSE; 2-ACETAMIDO-2-DEOXY-D-GALACTOSE; 2- HETSYN 3 A2G ACETAMIDO-2-DEOXY-GALACTOSE; N-ACETYL-2-DEOXY-2-AMINO- HETSYN 4 A2G GALACTOSE FORMUL 7 NAG 6(C8 H15 N O6) FORMUL 7 BMA 2(C6 H12 O6) FORMUL 7 FUC 2(C6 H12 O5) FORMUL 8 MAN C6 H12 O6 FORMUL 9 SO4 5(O4 S 2-) FORMUL 11 CL 2(CL 1-) FORMUL 14 A2G 2(C8 H15 N O6) FORMUL 20 HOH *94(H2 O) HELIX 1 AA1 LEU A 65 SER A 67 5 3 HELIX 2 AA2 THR A 88 THR A 92 5 5 HELIX 3 AA3 SER A 165 ALA A 167 5 3 HELIX 4 AA4 SER A 196 GLY A 199 5 4 HELIX 5 AA5 LYS A 210 ASN A 213 5 4 HELIX 6 AA6 SER B 28 ASN B 32 5 5 HELIX 7 AA7 LYS B 82 GLU B 86 5 5 HELIX 8 AA8 SER B 125 ALA B 131 1 7 HELIX 9 AA9 THR B 185 HIS B 192 1 8 HELIX 10 AB1 LEU C 65 SER C 67 5 3 HELIX 11 AB2 THR C 88 THR C 92 5 5 HELIX 12 AB3 SER C 165 ALA C 167 5 3 HELIX 13 AB4 SER C 195 GLN C 201 1 7 HELIX 14 AB5 PRO C 211 ASN C 213 5 3 HELIX 15 AB6 SER D 28 ASN D 32 5 5 HELIX 16 AB7 LYS D 82 GLU D 86 5 5 HELIX 17 AB8 SER D 125 ALA D 131 1 7 HELIX 18 AB9 THR D 185 HIS D 192 1 8 HELIX 19 AC1 PRO E 337 ASN E 343 1 7 HELIX 20 AC2 SER E 349 TRP E 353 5 5 HELIX 21 AC3 ASP E 364 TYR E 369 5 6 HELIX 22 AC4 SER E 383 ASN E 388 1 6 HELIX 23 AC5 ASN E 405 ILE E 410 5 6 HELIX 24 AC6 GLY E 416 ASN E 422 1 7 HELIX 25 AC7 SER E 438 SER E 443 1 6 HELIX 26 AC8 GLY E 502 HIS E 505 5 4 HELIX 27 AC9 PRO E 527 PHE E 533 5 7 HELIX 28 AD1 PRO F 337 ASN F 343 1 7 HELIX 29 AD2 SER F 349 TRP F 353 5 5 HELIX 30 AD3 ASP F 364 TYR F 369 5 6 HELIX 31 AD4 SER F 383 ASN F 388 1 6 HELIX 32 AD5 ASN F 405 ILE F 410 5 6 HELIX 33 AD6 GLY F 416 ASN F 422 1 7 HELIX 34 AD7 SER F 438 SER F 443 1 6 HELIX 35 AD8 GLY F 502 HIS F 505 5 4 HELIX 36 AD9 PRO F 527 LEU F 532 5 6 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O SER A 25 N GLN A 3 SHEET 3 AA1 4 GLN A 79 LEU A 84 -1 O PHE A 80 N CYS A 22 SHEET 4 AA1 4 VAL A 69 ILE A 73 -1 N SER A 72 O SER A 81 SHEET 1 AA2 6 LEU A 11 VAL A 12 0 SHEET 2 AA2 6 THR A 116 VAL A 120 1 O THR A 119 N VAL A 12 SHEET 3 AA2 6 ALA A 93 LEU A 103 -1 N ALA A 93 O VAL A 118 SHEET 4 AA2 6 TYR A 34 GLN A 41 -1 N TYR A 35 O ALA A 100 SHEET 5 AA2 6 LEU A 47 ILE A 53 -1 O GLY A 51 N TRP A 38 SHEET 6 AA2 6 THR A 59 TYR A 61 -1 O HIS A 60 N TYR A 52 SHEET 1 AA3 4 LEU A 11 VAL A 12 0 SHEET 2 AA3 4 THR A 116 VAL A 120 1 O THR A 119 N VAL A 12 SHEET 3 AA3 4 ALA A 93 LEU A 103 -1 N ALA A 93 O VAL A 118 SHEET 4 AA3 4 TYR A 106 TRP A 112 -1 O TYR A 106 N LEU A 103 SHEET 1 AA4 4 SER A 129 SER A 136 0 SHEET 2 AA4 4 THR A 144 TYR A 154 -1 O LYS A 152 N SER A 129 SHEET 3 AA4 4 TYR A 185 PRO A 194 -1 O LEU A 187 N VAL A 151 SHEET 4 AA4 4 HIS A 173 THR A 174 -1 N HIS A 173 O VAL A 190 SHEET 1 AA5 4 SER A 129 SER A 136 0 SHEET 2 AA5 4 THR A 144 TYR A 154 -1 O LYS A 152 N SER A 129 SHEET 3 AA5 4 TYR A 185 PRO A 194 -1 O LEU A 187 N VAL A 151 SHEET 4 AA5 4 VAL A 178 LEU A 179 -1 N VAL A 178 O SER A 186 SHEET 1 AA6 3 THR A 160 TRP A 163 0 SHEET 2 AA6 3 ILE A 204 HIS A 209 -1 O ASN A 206 N SER A 162 SHEET 3 AA6 3 THR A 214 LYS A 219 -1 O VAL A 216 N VAL A 207 SHEET 1 AA7 4 MET B 3 THR B 5 0 SHEET 2 AA7 4 VAL B 18 SER B 25 -1 O THR B 23 N THR B 5 SHEET 3 AA7 4 SER B 73 ILE B 78 -1 O LEU B 76 N ILE B 20 SHEET 4 AA7 4 PHE B 63 ASP B 68 -1 N SER B 66 O SER B 75 SHEET 1 AA8 5 SER B 9 GLU B 12 0 SHEET 2 AA8 5 THR B 105 VAL B 109 1 O LYS B 106 N VAL B 10 SHEET 3 AA8 5 ASP B 88 TYR B 94 -1 N TYR B 89 O THR B 105 SHEET 4 AA8 5 GLN B 35 HIS B 39 -1 N GLN B 35 O GLN B 92 SHEET 5 AA8 5 THR B 46 ILE B 49 -1 O ILE B 49 N TRP B 36 SHEET 1 AA9 4 SER B 9 GLU B 12 0 SHEET 2 AA9 4 THR B 105 VAL B 109 1 O LYS B 106 N VAL B 10 SHEET 3 AA9 4 ASP B 88 TYR B 94 -1 N TYR B 89 O THR B 105 SHEET 4 AA9 4 VAL B 99 PHE B 101 -1 O VAL B 100 N SER B 93 SHEET 1 AB1 4 SER B 118 PHE B 122 0 SHEET 2 AB1 4 ALA B 134 PHE B 143 -1 O VAL B 137 N PHE B 122 SHEET 3 AB1 4 TYR B 176 LEU B 184 -1 O TYR B 176 N PHE B 143 SHEET 4 AB1 4 VAL B 163 THR B 165 -1 N GLU B 164 O TYR B 181 SHEET 1 AB2 4 SER B 118 PHE B 122 0 SHEET 2 AB2 4 ALA B 134 PHE B 143 -1 O VAL B 137 N PHE B 122 SHEET 3 AB2 4 TYR B 176 LEU B 184 -1 O TYR B 176 N PHE B 143 SHEET 4 AB2 4 SER B 169 LYS B 170 -1 N SER B 169 O ALA B 177 SHEET 1 AB3 4 SER B 157 VAL B 159 0 SHEET 2 AB3 4 THR B 149 ALA B 154 -1 N ALA B 154 O SER B 157 SHEET 3 AB3 4 TYR B 195 HIS B 201 -1 O THR B 200 N THR B 149 SHEET 4 AB3 4 SER B 204 VAL B 210 -1 O VAL B 206 N VAL B 199 SHEET 1 AB4 4 GLU C 6 SER C 7 0 SHEET 2 AB4 4 LEU C 18 THR C 23 -1 O THR C 21 N SER C 7 SHEET 3 AB4 4 GLN C 79 LEU C 84 -1 O LEU C 84 N LEU C 18 SHEET 4 AB4 4 VAL C 69 ILE C 73 -1 N SER C 72 O SER C 81 SHEET 1 AB5 6 LEU C 11 VAL C 12 0 SHEET 2 AB5 6 THR C 116 VAL C 120 1 O THR C 119 N VAL C 12 SHEET 3 AB5 6 ALA C 93 LEU C 103 -1 N TYR C 95 O THR C 116 SHEET 4 AB5 6 TYR C 34 GLN C 41 -1 N TYR C 35 O ALA C 100 SHEET 5 AB5 6 LEU C 47 ILE C 53 -1 O ILE C 50 N TRP C 38 SHEET 6 AB5 6 THR C 59 TYR C 61 -1 O HIS C 60 N TYR C 52 SHEET 1 AB6 4 LEU C 11 VAL C 12 0 SHEET 2 AB6 4 THR C 116 VAL C 120 1 O THR C 119 N VAL C 12 SHEET 3 AB6 4 ALA C 93 LEU C 103 -1 N TYR C 95 O THR C 116 SHEET 4 AB6 4 TYR C 106 TRP C 112 -1 O TYR C 106 N LEU C 103 SHEET 1 AB7 4 SER C 129 LEU C 133 0 SHEET 2 AB7 4 THR C 144 TYR C 154 -1 O GLY C 148 N LEU C 133 SHEET 3 AB7 4 TYR C 185 PRO C 194 -1 O VAL C 191 N LEU C 147 SHEET 4 AB7 4 VAL C 172 THR C 174 -1 N HIS C 173 O VAL C 190 SHEET 1 AB8 4 SER C 129 LEU C 133 0 SHEET 2 AB8 4 THR C 144 TYR C 154 -1 O GLY C 148 N LEU C 133 SHEET 3 AB8 4 TYR C 185 PRO C 194 -1 O VAL C 191 N LEU C 147 SHEET 4 AB8 4 VAL C 178 LEU C 179 -1 N VAL C 178 O SER C 186 SHEET 1 AB9 3 VAL C 159 TRP C 163 0 SHEET 2 AB9 3 ILE C 204 HIS C 209 -1 O ASN C 206 N SER C 162 SHEET 3 AB9 3 THR C 214 LYS C 219 -1 O VAL C 216 N VAL C 207 SHEET 1 AC1 4 MET D 3 THR D 5 0 SHEET 2 AC1 4 VAL D 18 SER D 25 -1 O SER D 25 N MET D 3 SHEET 3 AC1 4 SER D 73 ILE D 78 -1 O LEU D 76 N ILE D 20 SHEET 4 AC1 4 PHE D 63 ASP D 68 -1 N ASP D 68 O SER D 73 SHEET 1 AC2 5 SER D 9 GLU D 12 0 SHEET 2 AC2 5 THR D 105 VAL D 109 1 O THR D 108 N VAL D 10 SHEET 3 AC2 5 ALA D 87 TYR D 94 -1 N TYR D 89 O THR D 105 SHEET 4 AC2 5 GLN D 35 HIS D 39 -1 N GLN D 35 O GLN D 92 SHEET 5 AC2 5 THR D 46 ILE D 49 -1 O ILE D 49 N TRP D 36 SHEET 1 AC3 4 SER D 9 GLU D 12 0 SHEET 2 AC3 4 THR D 105 VAL D 109 1 O THR D 108 N VAL D 10 SHEET 3 AC3 4 ALA D 87 TYR D 94 -1 N TYR D 89 O THR D 105 SHEET 4 AC3 4 VAL D 99 PHE D 101 -1 O VAL D 100 N SER D 93 SHEET 1 AC4 4 SER D 118 PHE D 122 0 SHEET 2 AC4 4 ALA D 134 PHE D 143 -1 O LEU D 139 N THR D 120 SHEET 3 AC4 4 TYR D 176 LEU D 184 -1 O SER D 180 N CYS D 138 SHEET 4 AC4 4 VAL D 163 THR D 165 -1 N GLU D 164 O TYR D 181 SHEET 1 AC5 4 SER D 118 PHE D 122 0 SHEET 2 AC5 4 ALA D 134 PHE D 143 -1 O LEU D 139 N THR D 120 SHEET 3 AC5 4 TYR D 176 LEU D 184 -1 O SER D 180 N CYS D 138 SHEET 4 AC5 4 SER D 169 LYS D 170 -1 N SER D 169 O ALA D 177 SHEET 1 AC6 4 SER D 157 VAL D 159 0 SHEET 2 AC6 4 THR D 149 ALA D 154 -1 N TRP D 152 O VAL D 159 SHEET 3 AC6 4 TYR D 195 HIS D 201 -1 O GLN D 198 N ALA D 151 SHEET 4 AC6 4 SER D 204 VAL D 210 -1 O VAL D 206 N VAL D 199 SHEET 1 AC7 5 ASN E 354 ILE E 358 0 SHEET 2 AC7 5 ASN E 394 ARG E 403 -1 O ILE E 395 N ILE E 358 SHEET 3 AC7 5 PRO E 507 GLU E 516 -1 O VAL E 512 N ASP E 398 SHEET 4 AC7 5 GLY E 431 ASN E 437 -1 N ILE E 434 O VAL E 511 SHEET 5 AC7 5 PHE E 374 TYR E 380 -1 N PHE E 375 O ALA E 435 SHEET 1 AC8 3 CYS E 361 VAL E 362 0 SHEET 2 AC8 3 VAL E 524 CYS E 525 1 O CYS E 525 N CYS E 361 SHEET 3 AC8 3 CYS E 391 TRP E 392 -1 N TRP E 392 O VAL E 524 SHEET 1 AC9 2 LEU E 452 ARG E 454 0 SHEET 2 AC9 2 LEU E 492 SER E 494 -1 O GLN E 493 N TYR E 453 SHEET 1 AD1 2 TYR E 473 GLN E 474 0 SHEET 2 AD1 2 CYS E 488 TYR E 489 -1 O TYR E 489 N TYR E 473 SHEET 1 AD2 5 ASN F 354 ILE F 358 0 SHEET 2 AD2 5 ASN F 394 ARG F 403 -1 O ALA F 397 N LYS F 356 SHEET 3 AD2 5 PRO F 507 GLU F 516 -1 O SER F 514 N TYR F 396 SHEET 4 AD2 5 GLY F 431 ASN F 437 -1 N ILE F 434 O VAL F 511 SHEET 5 AD2 5 PHE F 374 TYR F 380 -1 N TYR F 380 O GLY F 431 SHEET 1 AD3 3 CYS F 361 VAL F 362 0 SHEET 2 AD3 3 VAL F 524 CYS F 525 1 O CYS F 525 N CYS F 361 SHEET 3 AD3 3 CYS F 391 TRP F 392 -1 N TRP F 392 O VAL F 524 SHEET 1 AD4 2 LEU F 452 ARG F 454 0 SHEET 2 AD4 2 LEU F 492 SER F 494 -1 O GLN F 493 N TYR F 453 SHEET 1 AD5 2 TYR F 473 GLN F 474 0 SHEET 2 AD5 2 CYS F 488 TYR F 489 -1 O TYR F 489 N TYR F 473 SSBOND 1 CYS A 22 CYS A 97 1555 1555 2.12 SSBOND 2 CYS A 149 CYS A 205 1555 1555 2.04 SSBOND 3 CYS B 22 CYS B 91 1555 1555 2.04 SSBOND 4 CYS B 138 CYS B 197 1555 1555 2.04 SSBOND 5 CYS C 22 CYS C 97 1555 1555 2.12 SSBOND 6 CYS C 149 CYS C 205 1555 1555 2.04 SSBOND 7 CYS D 22 CYS D 91 1555 1555 2.05 SSBOND 8 CYS D 138 CYS D 197 1555 1555 2.06 SSBOND 9 CYS E 336 CYS E 361 1555 1555 2.09 SSBOND 10 CYS E 379 CYS E 432 1555 1555 2.07 SSBOND 11 CYS E 391 CYS E 525 1555 1555 2.05 SSBOND 12 CYS E 480 CYS E 488 1555 1555 2.05 SSBOND 13 CYS F 336 CYS F 361 1555 1555 2.09 SSBOND 14 CYS F 379 CYS F 432 1555 1555 2.07 SSBOND 15 CYS F 391 CYS F 525 1555 1555 2.05 SSBOND 16 CYS F 480 CYS F 488 1555 1555 2.07 LINK OG1 THR E 323 C1 A2G E 602 1555 1555 1.37 LINK ND2 ASN E 331 C1 NAG G 1 1555 1555 1.45 LINK ND2 ASN E 343 C1 NAG E 601 1555 1555 1.46 LINK OG1 THR F 323 C1 A2G F 602 1555 1555 1.37 LINK ND2 ASN F 331 C1 NAG H 1 1555 1555 1.45 LINK ND2 ASN F 343 C1 NAG F 601 1555 1555 1.46 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.46 LINK O6 NAG G 1 C1 FUC G 4 1555 1555 1.46 LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.46 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.47 LINK O6 NAG H 1 C1 FUC H 5 1555 1555 1.45 LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.45 LINK O6 BMA H 3 C1 MAN H 4 1555 1555 1.46 CISPEP 1 ASP A 110 PRO A 111 0 -3.99 CISPEP 2 PHE A 155 PRO A 156 0 -2.40 CISPEP 3 GLU A 157 PRO A 158 0 -2.17 CISPEP 4 TYR B 144 PRO B 145 0 -2.15 CISPEP 5 ASP C 110 PRO C 111 0 -8.87 CISPEP 6 PHE C 155 PRO C 156 0 -3.58 CISPEP 7 GLU C 157 PRO C 158 0 4.39 CISPEP 8 TYR D 144 PRO D 145 0 2.66 CRYST1 66.971 170.851 231.543 90.00 90.00 90.00 P 21 21 21 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 0.014932 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005853 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004319 0.00000