HEADER VIRAL PROTEIN, IMMUNE SYSTEM 07-MAR-21 7EAM TITLE IMMUNE COMPLEX OF SARS-COV-2 RBD AND CROSS-NEUTRALIZING ANTIBODY 7D6 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE PROTEIN S1; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: UNP RESIDUES 319-541; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: THE HEAVY CHAIN OF FAB FRAGMENT OF ANTIBODY 7D6; COMPND 8 CHAIN: H, C; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: THE LIGHT CHAIN OF FAB FRAGMENT OF ANTIBODY 7D6; COMPND 11 CHAIN: L, D 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: TRICHOPLUSIA NI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 11 ORGANISM_TAXID: 10090; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 14 ORGANISM_TAXID: 10090 KEYWDS SARS-COV-2, RECEPTOR BINDING DOMAIN, NEUTRALIZING ANTIBODY, VIRAL KEYWDS 2 PROTEIN, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR T.T.LI,Y.GU,S.W.LI REVDAT 1 17-MAR-21 7EAM 0 JRNL AUTH T.T.LI,Y.GU,S.W.LI JRNL TITL IMMUNE COMPLEX OF SARS-COV-2 RBD AND NAB 7D6 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.15.2_3472 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) : 1.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.32 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960 REMARK 3 COMPLETENESS FOR RANGE (%) : 92.3 REMARK 3 NUMBER OF REFLECTIONS : 244139 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.172 REMARK 3 R VALUE (WORKING SET) : 0.172 REMARK 3 FREE R VALUE : 0.182 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3906 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 22.3150 - 4.2418 0.92 16868 150 0.1301 0.1301 REMARK 3 2 4.2418 - 3.3706 0.94 17169 147 0.1311 0.1336 REMARK 3 3 3.3706 - 2.9456 0.95 17324 134 0.1593 0.1815 REMARK 3 4 2.9456 - 2.6768 0.92 16822 150 0.1660 0.1371 REMARK 3 5 2.6768 - 2.4852 0.94 17342 126 0.1708 0.1881 REMARK 3 6 2.4852 - 2.3388 0.95 17214 146 0.1710 0.1759 REMARK 3 7 2.3388 - 2.2218 0.94 17215 144 0.1660 0.1694 REMARK 3 8 2.2218 - 2.1252 0.93 17231 139 0.1723 0.2197 REMARK 3 9 2.1252 - 2.0434 0.94 17122 135 0.1729 0.2243 REMARK 3 10 2.0434 - 1.9730 0.95 17348 151 0.1794 0.2061 REMARK 3 11 1.9730 - 1.9113 0.93 17030 153 0.1877 0.2199 REMARK 3 12 1.9113 - 1.8567 0.95 17267 114 0.1971 0.2151 REMARK 3 13 1.8567 - 1.8078 0.95 17356 139 0.1946 0.2163 REMARK 3 14 1.8078 - 1.7637 0.95 17308 167 0.2031 0.2087 REMARK 3 15 1.7637 - 1.7237 0.95 17323 156 0.2107 0.2347 REMARK 3 16 1.7237 - 1.6870 0.95 17214 143 0.2222 0.2323 REMARK 3 17 1.6870 - 1.6533 0.95 17275 145 0.2306 0.2604 REMARK 3 18 1.6533 - 1.6221 0.94 17244 138 0.2397 0.2853 REMARK 3 19 1.6221 - 1.5931 0.93 17181 139 0.2591 0.3256 REMARK 3 20 1.5931 - 1.5661 0.95 17130 162 0.2665 0.2722 REMARK 3 21 1.5661 - 1.5409 0.92 16851 126 0.2777 0.3181 REMARK 3 22 1.5409 - 1.5172 0.91 16798 145 0.2946 0.3190 REMARK 3 23 1.5172 - 1.4948 0.91 16430 117 0.3139 0.3537 REMARK 3 24 1.4948 - 1.4738 0.88 16242 143 0.3369 0.3529 REMARK 3 25 1.4738 - 1.4539 0.87 15938 124 0.3486 0.4349 REMARK 3 26 1.4539 - 1.4350 0.87 15810 136 0.3637 0.3447 REMARK 3 27 1.4350 - 1.4171 0.83 15208 102 0.3730 0.4012 REMARK 3 28 1.4171 - 1.4000 0.82 14938 135 0.3870 0.3499 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 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) : 0.200 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.510 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 22.73 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.24 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 : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 52 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 324 THROUGH 393 ) REMARK 3 ORIGIN FOR THE GROUP (A): -29.9016 -3.5720 4.0128 REMARK 3 T TENSOR REMARK 3 T11: 0.2567 T22: 0.2050 REMARK 3 T33: 0.2101 T12: 0.0126 REMARK 3 T13: 0.0216 T23: 0.0020 REMARK 3 L TENSOR REMARK 3 L11: 0.2071 L22: 0.5206 REMARK 3 L33: 0.1365 L12: 0.1118 REMARK 3 L13: 0.2012 L23: -0.3527 REMARK 3 S TENSOR REMARK 3 S11: -0.0215 S12: -0.0134 S13: 0.0511 REMARK 3 S21: -0.0841 S22: 0.0859 S23: 0.0785 REMARK 3 S31: 0.0187 S32: -0.0080 S33: -0.0000 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 394 THROUGH 527 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.3496 8.0818 4.9551 REMARK 3 T TENSOR REMARK 3 T11: 0.2313 T22: 0.1824 REMARK 3 T33: 0.2122 T12: 0.0296 REMARK 3 T13: 0.0313 T23: -0.0052 REMARK 3 L TENSOR REMARK 3 L11: 0.3148 L22: 0.9654 REMARK 3 L33: 0.7351 L12: 0.5359 REMARK 3 L13: 0.1596 L23: 0.0077 REMARK 3 S TENSOR REMARK 3 S11: -0.0116 S12: 0.0351 S13: -0.0145 REMARK 3 S21: -0.0645 S22: 0.0001 S23: -0.0883 REMARK 3 S31: 0.0211 S32: 0.0541 S33: 0.0000 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.3232 17.3848 38.5592 REMARK 3 T TENSOR REMARK 3 T11: 0.2257 T22: 0.2398 REMARK 3 T33: 0.2432 T12: -0.0161 REMARK 3 T13: 0.0117 T23: -0.0075 REMARK 3 L TENSOR REMARK 3 L11: 0.1126 L22: 0.0270 REMARK 3 L33: 0.1095 L12: -0.2032 REMARK 3 L13: 0.1220 L23: -0.2054 REMARK 3 S TENSOR REMARK 3 S11: 0.0396 S12: 0.0560 S13: 0.1604 REMARK 3 S21: -0.0099 S22: 0.0019 S23: -0.0438 REMARK 3 S31: -0.1391 S32: -0.1366 S33: -0.0000 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 18 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.3041 16.5310 25.3188 REMARK 3 T TENSOR REMARK 3 T11: 0.2417 T22: 0.2339 REMARK 3 T33: 0.2438 T12: 0.0010 REMARK 3 T13: 0.0245 T23: 0.0010 REMARK 3 L TENSOR REMARK 3 L11: 0.0482 L22: 0.0295 REMARK 3 L33: 0.0772 L12: 0.0630 REMARK 3 L13: 0.0030 L23: 0.0618 REMARK 3 S TENSOR REMARK 3 S11: 0.0437 S12: 0.0042 S13: -0.0044 REMARK 3 S21: -0.0973 S22: -0.0349 S23: 0.0700 REMARK 3 S31: -0.2072 S32: 0.0359 S33: 0.0000 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 33 THROUGH 44 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.5931 5.6149 36.5058 REMARK 3 T TENSOR REMARK 3 T11: 0.2222 T22: 0.2288 REMARK 3 T33: 0.1851 T12: -0.0255 REMARK 3 T13: -0.0079 T23: 0.0038 REMARK 3 L TENSOR REMARK 3 L11: 0.0635 L22: 0.3271 REMARK 3 L33: 0.0505 L12: -0.0862 REMARK 3 L13: -0.0757 L23: 0.0189 REMARK 3 S TENSOR REMARK 3 S11: 0.0901 S12: -0.1356 S13: 0.0108 REMARK 3 S21: -0.0719 S22: 0.0507 S23: 0.0682 REMARK 3 S31: 0.5806 S32: 0.0698 S33: 0.0001 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 45 THROUGH 60 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.0617 7.8384 25.7029 REMARK 3 T TENSOR REMARK 3 T11: 0.2550 T22: 0.2869 REMARK 3 T33: 0.2214 T12: -0.0373 REMARK 3 T13: -0.0203 T23: 0.0265 REMARK 3 L TENSOR REMARK 3 L11: 0.0728 L22: 0.2018 REMARK 3 L33: 0.0793 L12: -0.1290 REMARK 3 L13: -0.0396 L23: 0.1691 REMARK 3 S TENSOR REMARK 3 S11: 0.0351 S12: 0.1548 S13: 0.0501 REMARK 3 S21: -0.1754 S22: 0.0330 S23: 0.0876 REMARK 3 S31: 0.2672 S32: -0.2700 S33: -0.0000 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 61 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.6861 14.1424 29.9213 REMARK 3 T TENSOR REMARK 3 T11: 0.2353 T22: 0.2707 REMARK 3 T33: 0.2445 T12: -0.0258 REMARK 3 T13: 0.0201 T23: -0.0007 REMARK 3 L TENSOR REMARK 3 L11: 0.2349 L22: 0.0740 REMARK 3 L33: 0.3177 L12: -0.0835 REMARK 3 L13: 0.1574 L23: 0.0588 REMARK 3 S TENSOR REMARK 3 S11: -0.0457 S12: 0.1480 S13: 0.0956 REMARK 3 S21: -0.0958 S22: 0.1247 S23: 0.0306 REMARK 3 S31: 0.0063 S32: -0.3487 S33: 0.0003 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 84 THROUGH 98 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.6857 9.9935 39.2548 REMARK 3 T TENSOR REMARK 3 T11: 0.2019 T22: 0.2485 REMARK 3 T33: 0.1962 T12: -0.0241 REMARK 3 T13: 0.0175 T23: -0.0206 REMARK 3 L TENSOR REMARK 3 L11: 0.2195 L22: 0.1785 REMARK 3 L33: 0.0570 L12: -0.2179 REMARK 3 L13: 0.1474 L23: -0.0927 REMARK 3 S TENSOR REMARK 3 S11: 0.0190 S12: -0.0836 S13: -0.0389 REMARK 3 S21: 0.0032 S22: -0.0257 S23: -0.0086 REMARK 3 S31: 0.1090 S32: -0.1212 S33: 0.0000 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 99 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.5716 4.2919 24.6037 REMARK 3 T TENSOR REMARK 3 T11: 0.2913 T22: 0.2008 REMARK 3 T33: 0.2127 T12: 0.0039 REMARK 3 T13: 0.0141 T23: -0.0099 REMARK 3 L TENSOR REMARK 3 L11: 0.0740 L22: 0.0127 REMARK 3 L33: 0.0553 L12: -0.0019 REMARK 3 L13: 0.0082 L23: -0.0439 REMARK 3 S TENSOR REMARK 3 S11: 0.1364 S12: -0.0131 S13: 0.0573 REMARK 3 S21: -0.1178 S22: -0.1063 S23: -0.1826 REMARK 3 S31: 0.0185 S32: -0.0992 S33: -0.0001 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 114 THROUGH 126 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.6225 18.0894 53.0577 REMARK 3 T TENSOR REMARK 3 T11: 0.2432 T22: 0.2846 REMARK 3 T33: 0.2387 T12: 0.0268 REMARK 3 T13: 0.0070 T23: -0.0249 REMARK 3 L TENSOR REMARK 3 L11: -0.0190 L22: 0.0707 REMARK 3 L33: 0.0005 L12: 0.0258 REMARK 3 L13: -0.0192 L23: 0.0064 REMARK 3 S TENSOR REMARK 3 S11: -0.0778 S12: 0.0345 S13: -0.0168 REMARK 3 S21: -0.0192 S22: 0.0214 S23: -0.0349 REMARK 3 S31: -0.0538 S32: -0.1928 S33: 0.0001 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 127 THROUGH 152 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.6840 11.8127 69.9645 REMARK 3 T TENSOR REMARK 3 T11: 0.1452 T22: 0.2818 REMARK 3 T33: 0.2234 T12: 0.0526 REMARK 3 T13: -0.0089 T23: -0.0297 REMARK 3 L TENSOR REMARK 3 L11: 0.0836 L22: 0.1494 REMARK 3 L33: 0.1558 L12: 0.1301 REMARK 3 L13: -0.1094 L23: -0.2074 REMARK 3 S TENSOR REMARK 3 S11: -0.0979 S12: -0.2008 S13: -0.1849 REMARK 3 S21: 0.0462 S22: 0.1459 S23: 0.0897 REMARK 3 S31: -0.0576 S32: -0.0322 S33: 0.0004 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 153 THROUGH 191 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.6503 12.2261 60.9355 REMARK 3 T TENSOR REMARK 3 T11: 0.1504 T22: 0.2826 REMARK 3 T33: 0.2354 T12: 0.0459 REMARK 3 T13: -0.0096 T23: -0.0319 REMARK 3 L TENSOR REMARK 3 L11: 0.1861 L22: 0.6962 REMARK 3 L33: 0.1796 L12: 0.0028 REMARK 3 L13: -0.1975 L23: -0.0303 REMARK 3 S TENSOR REMARK 3 S11: 0.0975 S12: 0.1145 S13: -0.1078 REMARK 3 S21: -0.0744 S22: -0.0586 S23: 0.0306 REMARK 3 S31: 0.0795 S32: 0.0894 S33: -0.0000 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 192 THROUGH 209 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.8084 17.8637 66.6713 REMARK 3 T TENSOR REMARK 3 T11: 0.1730 T22: 0.2796 REMARK 3 T33: 0.2619 T12: 0.0577 REMARK 3 T13: -0.0258 T23: -0.0284 REMARK 3 L TENSOR REMARK 3 L11: 0.2412 L22: 0.2023 REMARK 3 L33: 0.2001 L12: 0.0371 REMARK 3 L13: -0.2933 L23: -0.0056 REMARK 3 S TENSOR REMARK 3 S11: -0.1242 S12: -0.0937 S13: 0.2674 REMARK 3 S21: 0.0503 S22: 0.0318 S23: -0.1518 REMARK 3 S31: -0.1104 S32: 0.0949 S33: -0.0002 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 210 THROUGH 220 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.4844 20.9053 69.5086 REMARK 3 T TENSOR REMARK 3 T11: 0.1920 T22: 0.3079 REMARK 3 T33: 0.2806 T12: 0.0603 REMARK 3 T13: -0.0319 T23: -0.0251 REMARK 3 L TENSOR REMARK 3 L11: 0.0581 L22: 0.3298 REMARK 3 L33: 0.1712 L12: 0.1585 REMARK 3 L13: 0.0702 L23: 0.2107 REMARK 3 S TENSOR REMARK 3 S11: 0.0456 S12: -0.2277 S13: 0.1194 REMARK 3 S21: -0.1557 S22: 0.0833 S23: -0.0000 REMARK 3 S31: -0.0155 S32: 0.0442 S33: 0.0068 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.7238 -11.2544 40.3863 REMARK 3 T TENSOR REMARK 3 T11: 0.3242 T22: 0.2318 REMARK 3 T33: 0.2717 T12: 0.0008 REMARK 3 T13: -0.0007 T23: 0.0207 REMARK 3 L TENSOR REMARK 3 L11: 0.0125 L22: 0.4226 REMARK 3 L33: 0.1367 L12: -0.1223 REMARK 3 L13: 0.0329 L23: 0.4524 REMARK 3 S TENSOR REMARK 3 S11: 0.0192 S12: -0.1982 S13: -0.1874 REMARK 3 S21: 0.2546 S22: 0.0498 S23: 0.1788 REMARK 3 S31: 0.3996 S32: -0.1791 S33: 0.0000 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 19 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.7921 -7.1268 31.9572 REMARK 3 T TENSOR REMARK 3 T11: 0.2101 T22: 0.2179 REMARK 3 T33: 0.2265 T12: -0.0523 REMARK 3 T13: -0.0043 T23: -0.0095 REMARK 3 L TENSOR REMARK 3 L11: 0.6523 L22: 1.0583 REMARK 3 L33: 0.4444 L12: -0.2540 REMARK 3 L13: 0.1765 L23: 0.1703 REMARK 3 S TENSOR REMARK 3 S11: -0.1117 S12: 0.1059 S13: 0.0024 REMARK 3 S21: 0.0561 S22: 0.0673 S23: 0.0585 REMARK 3 S31: -0.0216 S32: 0.0988 S33: -0.0001 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 103 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.6205 -8.4121 53.4525 REMARK 3 T TENSOR REMARK 3 T11: 0.3974 T22: 0.2988 REMARK 3 T33: 0.2502 T12: 0.1038 REMARK 3 T13: -0.0280 T23: -0.0178 REMARK 3 L TENSOR REMARK 3 L11: 0.1644 L22: 0.1683 REMARK 3 L33: 0.0489 L12: 0.2356 REMARK 3 L13: -0.1019 L23: -0.0779 REMARK 3 S TENSOR REMARK 3 S11: -0.2051 S12: -0.0466 S13: 0.0053 REMARK 3 S21: -0.0416 S22: 0.1779 S23: -0.0237 REMARK 3 S31: 0.2340 S32: 0.0666 S33: -0.0001 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 115 THROUGH 145 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.7311 4.7024 70.1632 REMARK 3 T TENSOR REMARK 3 T11: 0.2261 T22: 0.2270 REMARK 3 T33: 0.2385 T12: 0.0615 REMARK 3 T13: -0.0261 T23: -0.0358 REMARK 3 L TENSOR REMARK 3 L11: -0.2517 L22: 0.1914 REMARK 3 L33: 0.3818 L12: -0.1746 REMARK 3 L13: 0.0658 L23: -0.2453 REMARK 3 S TENSOR REMARK 3 S11: -0.0022 S12: -0.0485 S13: 0.0489 REMARK 3 S21: 0.0253 S22: 0.1079 S23: 0.0511 REMARK 3 S31: 0.0960 S32: 0.0806 S33: -0.0000 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 146 THROUGH 156 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.4239 -4.0342 76.3947 REMARK 3 T TENSOR REMARK 3 T11: 0.3289 T22: 0.2685 REMARK 3 T33: 0.2783 T12: -0.0633 REMARK 3 T13: -0.0017 T23: -0.0346 REMARK 3 L TENSOR REMARK 3 L11: -0.0000 L22: 0.0506 REMARK 3 L33: -0.0083 L12: 0.0235 REMARK 3 L13: -0.0127 L23: -0.0001 REMARK 3 S TENSOR REMARK 3 S11: 0.1985 S12: -0.0233 S13: -0.1488 REMARK 3 S21: 0.1884 S22: -0.2683 S23: 0.1763 REMARK 3 S31: 0.3248 S32: -0.0269 S33: -0.0000 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 157 THROUGH 175 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.2284 -0.2907 59.9275 REMARK 3 T TENSOR REMARK 3 T11: 0.2573 T22: 0.2849 REMARK 3 T33: 0.2451 T12: 0.0602 REMARK 3 T13: -0.0070 T23: -0.0314 REMARK 3 L TENSOR REMARK 3 L11: 0.1131 L22: 0.0743 REMARK 3 L33: 0.2524 L12: -0.1144 REMARK 3 L13: -0.0229 L23: -0.0979 REMARK 3 S TENSOR REMARK 3 S11: 0.2088 S12: 0.1097 S13: 0.0249 REMARK 3 S21: -0.1720 S22: -0.0812 S23: 0.0333 REMARK 3 S31: 0.2313 S32: -0.1734 S33: 0.0090 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 176 THROUGH 198 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.9303 3.9415 77.6839 REMARK 3 T TENSOR REMARK 3 T11: 0.2755 T22: 0.3051 REMARK 3 T33: 0.2395 T12: 0.0670 REMARK 3 T13: 0.0045 T23: -0.0081 REMARK 3 L TENSOR REMARK 3 L11: -0.0163 L22: 0.1592 REMARK 3 L33: 0.3906 L12: -0.0714 REMARK 3 L13: -0.0718 L23: 0.0439 REMARK 3 S TENSOR REMARK 3 S11: 0.0538 S12: 0.1476 S13: -0.1004 REMARK 3 S21: 0.1953 S22: -0.0425 S23: 0.0129 REMARK 3 S31: 0.3921 S32: -0.4766 S33: 0.0005 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 199 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.7177 -4.3755 76.5562 REMARK 3 T TENSOR REMARK 3 T11: 0.3647 T22: 0.2367 REMARK 3 T33: 0.2102 T12: 0.0971 REMARK 3 T13: -0.0251 T23: -0.0134 REMARK 3 L TENSOR REMARK 3 L11: 0.1245 L22: 0.1687 REMARK 3 L33: 0.1239 L12: 0.2563 REMARK 3 L13: -0.2876 L23: -0.1615 REMARK 3 S TENSOR REMARK 3 S11: -0.0950 S12: -0.1748 S13: -0.0038 REMARK 3 S21: 0.2561 S22: 0.0373 S23: 0.0940 REMARK 3 S31: 0.5212 S32: 0.1704 S33: -0.0001 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 324 THROUGH 353 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.6151 -43.3970 93.5490 REMARK 3 T TENSOR REMARK 3 T11: 0.2183 T22: 0.2445 REMARK 3 T33: 0.2360 T12: -0.0555 REMARK 3 T13: 0.0217 T23: -0.0466 REMARK 3 L TENSOR REMARK 3 L11: 0.0114 L22: -0.1197 REMARK 3 L33: 0.0970 L12: -0.1083 REMARK 3 L13: 0.0430 L23: 0.0159 REMARK 3 S TENSOR REMARK 3 S11: 0.0331 S12: 0.0663 S13: 0.0065 REMARK 3 S21: -0.0792 S22: 0.0515 S23: 0.0242 REMARK 3 S31: -0.0385 S32: 0.0372 S33: 0.0023 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 354 THROUGH 380 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.9072 -47.4594 101.8743 REMARK 3 T TENSOR REMARK 3 T11: 0.3002 T22: 0.2288 REMARK 3 T33: 0.2247 T12: 0.0052 REMARK 3 T13: 0.0398 T23: 0.0244 REMARK 3 L TENSOR REMARK 3 L11: 0.1842 L22: 0.3367 REMARK 3 L33: 0.1892 L12: -0.2760 REMARK 3 L13: 0.0893 L23: 0.2413 REMARK 3 S TENSOR REMARK 3 S11: -0.0873 S12: -0.0598 S13: -0.0446 REMARK 3 S21: 0.1092 S22: -0.0340 S23: -0.1302 REMARK 3 S31: 0.0234 S32: 0.1037 S33: -0.0001 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 381 THROUGH 393 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.3972 -57.8770 101.6480 REMARK 3 T TENSOR REMARK 3 T11: 0.4452 T22: 0.2740 REMARK 3 T33: 0.3706 T12: -0.0661 REMARK 3 T13: -0.1004 T23: -0.0001 REMARK 3 L TENSOR REMARK 3 L11: 0.0588 L22: 0.0508 REMARK 3 L33: 0.0090 L12: -0.0854 REMARK 3 L13: -0.0473 L23: 0.0220 REMARK 3 S TENSOR REMARK 3 S11: 0.3178 S12: -0.0784 S13: 0.2724 REMARK 3 S21: 0.0723 S22: -0.0812 S23: -0.5020 REMARK 3 S31: 0.0066 S32: -0.0229 S33: 0.0057 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 394 THROUGH 409 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.4926 -39.8604 100.5495 REMARK 3 T TENSOR REMARK 3 T11: 0.2734 T22: 0.2206 REMARK 3 T33: 0.2046 T12: -0.0335 REMARK 3 T13: 0.0287 T23: -0.0074 REMARK 3 L TENSOR REMARK 3 L11: 0.0274 L22: 0.1350 REMARK 3 L33: 0.0944 L12: 0.0752 REMARK 3 L13: -0.1679 L23: -0.1596 REMARK 3 S TENSOR REMARK 3 S11: -0.1008 S12: -0.0472 S13: 0.0091 REMARK 3 S21: 0.1197 S22: 0.0706 S23: -0.0298 REMARK 3 S31: 0.3179 S32: -0.0506 S33: -0.0000 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 410 THROUGH 442 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.9946 -41.2619 101.2408 REMARK 3 T TENSOR REMARK 3 T11: 0.2800 T22: 0.1946 REMARK 3 T33: 0.2284 T12: -0.0425 REMARK 3 T13: 0.0340 T23: 0.0156 REMARK 3 L TENSOR REMARK 3 L11: 0.2524 L22: 0.2030 REMARK 3 L33: 0.2880 L12: -0.3538 REMARK 3 L13: -0.0877 L23: 0.1687 REMARK 3 S TENSOR REMARK 3 S11: -0.0348 S12: 0.0178 S13: -0.0285 REMARK 3 S21: 0.2674 S22: 0.0469 S23: 0.0698 REMARK 3 S31: 0.1410 S32: 0.0190 S33: 0.0000 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 443 THROUGH 459 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.3503 -26.9966 97.4343 REMARK 3 T TENSOR REMARK 3 T11: 0.2581 T22: 0.2440 REMARK 3 T33: 0.2527 T12: -0.0215 REMARK 3 T13: 0.0032 T23: -0.0082 REMARK 3 L TENSOR REMARK 3 L11: 0.0754 L22: 0.0144 REMARK 3 L33: 0.0681 L12: -0.0821 REMARK 3 L13: 0.0771 L23: -0.0144 REMARK 3 S TENSOR REMARK 3 S11: -0.1145 S12: 0.0824 S13: -0.0068 REMARK 3 S21: 0.0280 S22: 0.0953 S23: 0.0971 REMARK 3 S31: -0.2850 S32: -0.0889 S33: -0.0000 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 460 THROUGH 494 ) REMARK 3 ORIGIN FOR THE GROUP (A): -31.1829 -28.5065 88.8024 REMARK 3 T TENSOR REMARK 3 T11: 0.2581 T22: 0.2147 REMARK 3 T33: 0.2467 T12: 0.0037 REMARK 3 T13: -0.0187 T23: 0.0026 REMARK 3 L TENSOR REMARK 3 L11: 0.2303 L22: 0.2734 REMARK 3 L33: -0.0251 L12: -0.0550 REMARK 3 L13: 0.1081 L23: -0.2255 REMARK 3 S TENSOR REMARK 3 S11: 0.0924 S12: 0.0277 S13: 0.0423 REMARK 3 S21: -0.2403 S22: -0.0276 S23: 0.0002 REMARK 3 S31: -0.0114 S32: -0.0296 S33: 0.0000 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 495 THROUGH 527 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.0176 -41.4561 100.7763 REMARK 3 T TENSOR REMARK 3 T11: 0.2912 T22: 0.1721 REMARK 3 T33: 0.1997 T12: -0.0307 REMARK 3 T13: 0.0235 T23: -0.0117 REMARK 3 L TENSOR REMARK 3 L11: 0.2651 L22: 0.2789 REMARK 3 L33: 0.3428 L12: -0.2665 REMARK 3 L13: 0.3309 L23: -0.3294 REMARK 3 S TENSOR REMARK 3 S11: 0.0025 S12: -0.0128 S13: 0.0312 REMARK 3 S21: 0.2145 S22: -0.0237 S23: 0.0069 REMARK 3 S31: 0.1267 S32: -0.0171 S33: -0.0001 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.2980 -26.5820 63.6509 REMARK 3 T TENSOR REMARK 3 T11: 0.2415 T22: 0.2524 REMARK 3 T33: 0.2496 T12: 0.0171 REMARK 3 T13: 0.0245 T23: 0.0066 REMARK 3 L TENSOR REMARK 3 L11: 0.0772 L22: 0.0245 REMARK 3 L33: 0.0546 L12: 0.1681 REMARK 3 L13: 0.0619 L23: 0.1296 REMARK 3 S TENSOR REMARK 3 S11: 0.0506 S12: -0.2021 S13: 0.1145 REMARK 3 S21: 0.0072 S22: -0.0466 S23: 0.0460 REMARK 3 S31: -0.1501 S32: 0.2341 S33: -0.0002 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 18 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.3246 -27.4166 76.9077 REMARK 3 T TENSOR REMARK 3 T11: 0.2490 T22: 0.2351 REMARK 3 T33: 0.2329 T12: 0.0072 REMARK 3 T13: 0.0297 T23: -0.0006 REMARK 3 L TENSOR REMARK 3 L11: 0.0405 L22: 0.0232 REMARK 3 L33: 0.0531 L12: -0.0373 REMARK 3 L13: 0.0025 L23: -0.0087 REMARK 3 S TENSOR REMARK 3 S11: 0.0340 S12: -0.0237 S13: -0.0140 REMARK 3 S21: 0.1003 S22: -0.0203 S23: -0.0891 REMARK 3 S31: -0.1441 S32: -0.0565 S33: -0.0000 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 33 THROUGH 44 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.0134 -38.3458 65.7010 REMARK 3 T TENSOR REMARK 3 T11: 0.2173 T22: 0.2169 REMARK 3 T33: 0.1809 T12: 0.0153 REMARK 3 T13: -0.0048 T23: -0.0094 REMARK 3 L TENSOR REMARK 3 L11: 0.0908 L22: 0.2260 REMARK 3 L33: 0.0506 L12: 0.1478 REMARK 3 L13: -0.0813 L23: -0.0397 REMARK 3 S TENSOR REMARK 3 S11: 0.0588 S12: 0.1001 S13: 0.0496 REMARK 3 S21: 0.0965 S22: 0.1645 S23: -0.0971 REMARK 3 S31: 0.5239 S32: -0.0189 S33: 0.0000 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 45 THROUGH 60 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.5533 -36.1041 76.5194 REMARK 3 T TENSOR REMARK 3 T11: 0.2491 T22: 0.2644 REMARK 3 T33: 0.2114 T12: 0.0416 REMARK 3 T13: -0.0262 T23: -0.0284 REMARK 3 L TENSOR REMARK 3 L11: 0.1015 L22: 0.1815 REMARK 3 L33: 0.0934 L12: 0.1381 REMARK 3 L13: -0.0517 L23: -0.1605 REMARK 3 S TENSOR REMARK 3 S11: 0.0336 S12: -0.0822 S13: 0.0035 REMARK 3 S21: 0.1679 S22: 0.0253 S23: -0.1124 REMARK 3 S31: 0.3369 S32: 0.3225 S33: -0.0001 REMARK 3 TLS GROUP : 35 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 61 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.9416 -29.7994 72.3000 REMARK 3 T TENSOR REMARK 3 T11: 0.2298 T22: 0.2765 REMARK 3 T33: 0.2466 T12: 0.0251 REMARK 3 T13: 0.0186 T23: 0.0027 REMARK 3 L TENSOR REMARK 3 L11: 0.1236 L22: 0.0577 REMARK 3 L33: 0.3213 L12: 0.0271 REMARK 3 L13: 0.0226 L23: -0.1491 REMARK 3 S TENSOR REMARK 3 S11: 0.0057 S12: -0.0838 S13: 0.0440 REMARK 3 S21: 0.0637 S22: 0.0281 S23: 0.0418 REMARK 3 S31: -0.0605 S32: 0.3096 S33: 0.0002 REMARK 3 TLS GROUP : 36 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 84 THROUGH 98 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.9419 -33.9665 62.9678 REMARK 3 T TENSOR REMARK 3 T11: 0.1895 T22: 0.2611 REMARK 3 T33: 0.2015 T12: 0.0196 REMARK 3 T13: 0.0154 T23: 0.0197 REMARK 3 L TENSOR REMARK 3 L11: 0.2229 L22: 0.1539 REMARK 3 L33: 0.0995 L12: 0.1861 REMARK 3 L13: 0.1588 L23: 0.0706 REMARK 3 S TENSOR REMARK 3 S11: -0.0053 S12: 0.1070 S13: -0.0497 REMARK 3 S21: -0.0366 S22: -0.0549 S23: 0.0153 REMARK 3 S31: 0.1055 S32: 0.1679 S33: 0.0000 REMARK 3 TLS GROUP : 37 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 99 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.0489 -39.6645 77.6238 REMARK 3 T TENSOR REMARK 3 T11: 0.3006 T22: 0.2000 REMARK 3 T33: 0.2038 T12: -0.0222 REMARK 3 T13: 0.0152 T23: 0.0059 REMARK 3 L TENSOR REMARK 3 L11: 0.2006 L22: 0.0273 REMARK 3 L33: 0.0378 L12: -0.0383 REMARK 3 L13: -0.0439 L23: 0.0570 REMARK 3 S TENSOR REMARK 3 S11: 0.1252 S12: 0.0011 S13: 0.0697 REMARK 3 S21: 0.1522 S22: -0.0810 S23: 0.2271 REMARK 3 S31: 0.0290 S32: -0.0377 S33: -0.0001 REMARK 3 TLS GROUP : 38 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 114 THROUGH 126 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.0028 -25.8911 49.1644 REMARK 3 T TENSOR REMARK 3 T11: 0.2467 T22: 0.2973 REMARK 3 T33: 0.2516 T12: -0.0270 REMARK 3 T13: -0.0018 T23: 0.0412 REMARK 3 L TENSOR REMARK 3 L11: -0.0176 L22: 0.0303 REMARK 3 L33: 0.0024 L12: -0.0650 REMARK 3 L13: -0.0362 L23: -0.0092 REMARK 3 S TENSOR REMARK 3 S11: -0.1255 S12: -0.0383 S13: 0.0265 REMARK 3 S21: 0.0077 S22: -0.0231 S23: 0.0105 REMARK 3 S31: 0.0064 S32: 0.2355 S33: 0.0002 REMARK 3 TLS GROUP : 39 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 127 THROUGH 152 ) REMARK 3 ORIGIN FOR THE GROUP (A): -26.9322 -32.2146 32.2612 REMARK 3 T TENSOR REMARK 3 T11: 0.1608 T22: 0.2917 REMARK 3 T33: 0.2265 T12: -0.0584 REMARK 3 T13: -0.0123 T23: 0.0303 REMARK 3 L TENSOR REMARK 3 L11: 0.0207 L22: 0.0658 REMARK 3 L33: 0.1110 L12: -0.0557 REMARK 3 L13: 0.0144 L23: 0.1031 REMARK 3 S TENSOR REMARK 3 S11: -0.1575 S12: 0.0781 S13: -0.1195 REMARK 3 S21: -0.0889 S22: 0.1534 S23: -0.0875 REMARK 3 S31: -0.1118 S32: -0.0428 S33: 0.0015 REMARK 3 TLS GROUP : 40 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 153 THROUGH 191 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.9707 -31.7802 41.2843 REMARK 3 T TENSOR REMARK 3 T11: 0.1642 T22: 0.2808 REMARK 3 T33: 0.2421 T12: -0.0424 REMARK 3 T13: -0.0130 T23: 0.0328 REMARK 3 L TENSOR REMARK 3 L11: 0.2103 L22: 0.5825 REMARK 3 L33: 0.2156 L12: -0.0201 REMARK 3 L13: -0.2602 L23: -0.2069 REMARK 3 S TENSOR REMARK 3 S11: 0.0870 S12: -0.0898 S13: -0.0708 REMARK 3 S21: 0.0716 S22: -0.0623 S23: -0.0288 REMARK 3 S31: 0.0298 S32: -0.0929 S33: 0.0000 REMARK 3 TLS GROUP : 41 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 192 THROUGH 209 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.8154 -26.1598 35.5455 REMARK 3 T TENSOR REMARK 3 T11: 0.1884 T22: 0.2896 REMARK 3 T33: 0.2616 T12: -0.0545 REMARK 3 T13: -0.0213 T23: 0.0351 REMARK 3 L TENSOR REMARK 3 L11: 0.1779 L22: 0.2060 REMARK 3 L33: 0.1242 L12: -0.0251 REMARK 3 L13: -0.1933 L23: 0.0008 REMARK 3 S TENSOR REMARK 3 S11: -0.1156 S12: 0.1885 S13: 0.1808 REMARK 3 S21: -0.0640 S22: 0.0982 S23: 0.0834 REMARK 3 S31: -0.1279 S32: 0.0159 S33: -0.0001 REMARK 3 TLS GROUP : 42 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 210 THROUGH 220 ) REMARK 3 ORIGIN FOR THE GROUP (A): -28.1416 -23.0828 32.7045 REMARK 3 T TENSOR REMARK 3 T11: 0.2240 T22: 0.3052 REMARK 3 T33: 0.2949 T12: -0.0614 REMARK 3 T13: -0.0320 T23: 0.0463 REMARK 3 L TENSOR REMARK 3 L11: 0.0293 L22: 0.1155 REMARK 3 L33: 0.0941 L12: -0.0605 REMARK 3 L13: -0.0028 L23: -0.0920 REMARK 3 S TENSOR REMARK 3 S11: 0.0443 S12: 0.2455 S13: 0.1485 REMARK 3 S21: 0.2278 S22: 0.0543 S23: 0.0572 REMARK 3 S31: -0.0218 S32: 0.1631 S33: -0.0021 REMARK 3 TLS GROUP : 43 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.9160 -55.2254 61.8434 REMARK 3 T TENSOR REMARK 3 T11: 0.3212 T22: 0.2321 REMARK 3 T33: 0.2765 T12: -0.0200 REMARK 3 T13: -0.0031 T23: 0.0073 REMARK 3 L TENSOR REMARK 3 L11: 0.0245 L22: 0.3945 REMARK 3 L33: 0.1560 L12: 0.2188 REMARK 3 L13: 0.0382 L23: -0.5475 REMARK 3 S TENSOR REMARK 3 S11: 0.1257 S12: 0.0223 S13: -0.1965 REMARK 3 S21: -0.3444 S22: 0.0046 S23: -0.2388 REMARK 3 S31: 0.4557 S32: 0.0908 S33: -0.0020 REMARK 3 TLS GROUP : 44 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 19 THROUGH 38 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.9844 -54.3137 70.9786 REMARK 3 T TENSOR REMARK 3 T11: 0.2277 T22: 0.1892 REMARK 3 T33: 0.2477 T12: 0.0479 REMARK 3 T13: -0.0072 T23: 0.0009 REMARK 3 L TENSOR REMARK 3 L11: 0.2863 L22: 0.1766 REMARK 3 L33: 0.0630 L12: 0.1155 REMARK 3 L13: -0.1314 L23: -0.1154 REMARK 3 S TENSOR REMARK 3 S11: -0.0928 S12: -0.0795 S13: -0.0521 REMARK 3 S21: -0.0683 S22: 0.0590 S23: -0.1155 REMARK 3 S31: 0.0770 S32: -0.0026 S33: -0.0001 REMARK 3 TLS GROUP : 45 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 39 THROUGH 61 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.1574 -46.4440 71.4618 REMARK 3 T TENSOR REMARK 3 T11: 0.2032 T22: 0.2799 REMARK 3 T33: 0.2495 T12: 0.0823 REMARK 3 T13: -0.0099 T23: 0.0100 REMARK 3 L TENSOR REMARK 3 L11: 0.2780 L22: 0.1382 REMARK 3 L33: 0.1828 L12: 0.1556 REMARK 3 L13: 0.0650 L23: 0.1255 REMARK 3 S TENSOR REMARK 3 S11: -0.1625 S12: -0.1979 S13: 0.1153 REMARK 3 S21: 0.0310 S22: 0.1225 S23: 0.1163 REMARK 3 S31: -0.2405 S32: -0.2150 S33: 0.0002 REMARK 3 TLS GROUP : 46 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 62 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.9487 -51.8996 69.2647 REMARK 3 T TENSOR REMARK 3 T11: 0.2039 T22: 0.2198 REMARK 3 T33: 0.2504 T12: 0.0443 REMARK 3 T13: -0.0094 T23: -0.0040 REMARK 3 L TENSOR REMARK 3 L11: 0.4008 L22: 0.5484 REMARK 3 L33: 0.2432 L12: 0.1536 REMARK 3 L13: 0.2375 L23: -0.4636 REMARK 3 S TENSOR REMARK 3 S11: -0.1395 S12: -0.1278 S13: 0.0052 REMARK 3 S21: -0.1348 S22: 0.0669 S23: -0.1018 REMARK 3 S31: -0.0048 S32: -0.1264 S33: -0.0009 REMARK 3 TLS GROUP : 47 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 103 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.0168 -52.4059 48.7680 REMARK 3 T TENSOR REMARK 3 T11: 0.4065 T22: 0.2935 REMARK 3 T33: 0.2368 T12: -0.1176 REMARK 3 T13: -0.0330 T23: 0.0217 REMARK 3 L TENSOR REMARK 3 L11: 0.0631 L22: 0.0035 REMARK 3 L33: 0.0629 L12: -0.1447 REMARK 3 L13: -0.0918 L23: 0.0465 REMARK 3 S TENSOR REMARK 3 S11: -0.1139 S12: 0.0452 S13: 0.0992 REMARK 3 S21: 0.0947 S22: 0.0816 S23: 0.0507 REMARK 3 S31: 0.5469 S32: -0.1097 S33: 0.0002 REMARK 3 TLS GROUP : 48 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 115 THROUGH 145 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.8951 -39.3246 32.0588 REMARK 3 T TENSOR REMARK 3 T11: 0.2432 T22: 0.2341 REMARK 3 T33: 0.2522 T12: -0.0633 REMARK 3 T13: -0.0252 T23: 0.0368 REMARK 3 L TENSOR REMARK 3 L11: -0.2208 L22: 0.1237 REMARK 3 L33: 0.3472 L12: 0.1386 REMARK 3 L13: 0.1130 L23: 0.1258 REMARK 3 S TENSOR REMARK 3 S11: -0.0043 S12: 0.0421 S13: 0.0264 REMARK 3 S21: -0.0553 S22: 0.0581 S23: -0.0799 REMARK 3 S31: 0.1244 S32: -0.0554 S33: 0.0000 REMARK 3 TLS GROUP : 49 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 146 THROUGH 156 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.2044 -48.0632 25.8156 REMARK 3 T TENSOR REMARK 3 T11: 0.3465 T22: 0.2878 REMARK 3 T33: 0.3228 T12: 0.0581 REMARK 3 T13: -0.0055 T23: 0.0379 REMARK 3 L TENSOR REMARK 3 L11: 0.0036 L22: 0.0788 REMARK 3 L33: 0.0017 L12: -0.0150 REMARK 3 L13: -0.0025 L23: 0.0293 REMARK 3 S TENSOR REMARK 3 S11: 0.2176 S12: 0.0910 S13: -0.0651 REMARK 3 S21: -0.1445 S22: -0.1646 S23: -0.1172 REMARK 3 S31: 0.2915 S32: -0.0038 S33: 0.0004 REMARK 3 TLS GROUP : 50 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 157 THROUGH 175 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.3983 -44.3082 42.2960 REMARK 3 T TENSOR REMARK 3 T11: 0.2629 T22: 0.2680 REMARK 3 T33: 0.2267 T12: -0.0493 REMARK 3 T13: -0.0181 T23: 0.0260 REMARK 3 L TENSOR REMARK 3 L11: 0.2090 L22: 0.1325 REMARK 3 L33: 0.1451 L12: 0.0941 REMARK 3 L13: -0.1637 L23: -0.0422 REMARK 3 S TENSOR REMARK 3 S11: 0.3290 S12: -0.1271 S13: 0.0104 REMARK 3 S21: 0.2150 S22: -0.1496 S23: 0.0066 REMARK 3 S31: 0.1877 S32: 0.1495 S33: 0.0187 REMARK 3 TLS GROUP : 51 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 176 THROUGH 198 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.6865 -40.0986 24.5252 REMARK 3 T TENSOR REMARK 3 T11: 0.2590 T22: 0.2951 REMARK 3 T33: 0.2310 T12: -0.0590 REMARK 3 T13: 0.0137 T23: 0.0023 REMARK 3 L TENSOR REMARK 3 L11: 0.0228 L22: 0.1587 REMARK 3 L33: 0.4367 L12: 0.0321 REMARK 3 L13: -0.0534 L23: -0.0533 REMARK 3 S TENSOR REMARK 3 S11: 0.0551 S12: -0.1058 S13: -0.1184 REMARK 3 S21: -0.2080 S22: -0.0559 S23: -0.0261 REMARK 3 S31: 0.3984 S32: 0.4644 S33: 0.0018 REMARK 3 TLS GROUP : 52 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 199 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -25.9181 -48.4080 25.6614 REMARK 3 T TENSOR REMARK 3 T11: 0.3854 T22: 0.2553 REMARK 3 T33: 0.2309 T12: -0.0953 REMARK 3 T13: -0.0205 T23: 0.0181 REMARK 3 L TENSOR REMARK 3 L11: 0.0904 L22: 0.1242 REMARK 3 L33: 0.1396 L12: -0.1197 REMARK 3 L13: -0.1618 L23: 0.1657 REMARK 3 S TENSOR REMARK 3 S11: -0.1147 S12: 0.1552 S13: -0.0426 REMARK 3 S21: -0.1952 S22: -0.0630 S23: -0.2419 REMARK 3 S31: 0.4323 S32: -0.1272 S33: -0.0003 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 7EAM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-MAR-21. REMARK 100 THE DEPOSITION ID IS D_1300021041. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-JAN-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 : SSRF REMARK 200 BEAMLINE : BL17U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AIMLESS REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 244264 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400 REMARK 200 RESOLUTION RANGE LOW (A) : 29.320 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : 0.06100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.44 REMARK 200 COMPLETENESS FOR SHELL (%) : 89.5 REMARK 200 DATA REDUNDANCY IN SHELL : 2.70 REMARK 200 R MERGE FOR SHELL (I) : 1.24700 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: 6M0J, 6RCO REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.55 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG D5, 0.2M POTASSIUM DIHYDROGEN REMARK 280 PHOSPHATE, 20% PEG3350, EVAPORATION, TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 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: 4960 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 30710 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E 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 APPLY THE FOLLOWING TO CHAINS: H, L REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -37.44000 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 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: 4950 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 30770 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F 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 APPLY THE FOLLOWING TO CHAINS: C, D REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 37.44000 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 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 ARG A 319 REMARK 465 VAL A 320 REMARK 465 GLN A 321 REMARK 465 PRO A 322 REMARK 465 THR A 323 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 LEU A 533 REMARK 465 VAL A 534 REMARK 465 LYS A 535 REMARK 465 ASN A 536 REMARK 465 LYS A 537 REMARK 465 CYS A 538 REMARK 465 VAL A 539 REMARK 465 ASN A 540 REMARK 465 PHE A 541 REMARK 465 HIS A 542 REMARK 465 HIS A 543 REMARK 465 HIS A 544 REMARK 465 HIS A 545 REMARK 465 HIS A 546 REMARK 465 HIS A 547 REMARK 465 HIS A 548 REMARK 465 HIS A 549 REMARK 465 HIS A 550 REMARK 465 HIS A 551 REMARK 465 SER H 135 REMARK 465 ALA H 136 REMARK 465 ALA H 137 REMARK 465 GLN H 138 REMARK 465 THR H 139 REMARK 465 ARG B 319 REMARK 465 VAL B 320 REMARK 465 GLN B 321 REMARK 465 PRO B 322 REMARK 465 THR B 323 REMARK 465 LYS B 528 REMARK 465 LYS B 529 REMARK 465 SER B 530 REMARK 465 THR B 531 REMARK 465 ASN B 532 REMARK 465 LEU B 533 REMARK 465 VAL B 534 REMARK 465 LYS B 535 REMARK 465 ASN B 536 REMARK 465 LYS B 537 REMARK 465 CYS B 538 REMARK 465 VAL B 539 REMARK 465 ASN B 540 REMARK 465 PHE B 541 REMARK 465 HIS B 542 REMARK 465 HIS B 543 REMARK 465 HIS B 544 REMARK 465 HIS B 545 REMARK 465 HIS B 546 REMARK 465 HIS B 547 REMARK 465 HIS B 548 REMARK 465 HIS B 549 REMARK 465 HIS B 550 REMARK 465 HIS B 551 REMARK 465 SER C 135 REMARK 465 ALA C 136 REMARK 465 ALA C 137 REMARK 465 GLN C 138 REMARK 465 THR C 139 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 HOH A 825 O HOH A 830 1.83 REMARK 500 O HOH A 706 O HOH A 833 1.84 REMARK 500 NZ LYS A 417 O HOH A 701 1.85 REMARK 500 O HOH B 828 O HOH B 834 1.86 REMARK 500 O HOH H 479 O HOH H 487 1.86 REMARK 500 OH TYR C 105 O HOH C 301 1.86 REMARK 500 O HOH H 498 O HOH L 509 1.89 REMARK 500 OE1 GLN D 79 O HOH D 301 1.90 REMARK 500 N LEU A 387 O HOH A 702 1.90 REMARK 500 O HOH H 415 O HOH H 488 1.96 REMARK 500 OD2 ASP B 420 O HOH B 701 1.96 REMARK 500 O HOH H 418 O HOH H 504 1.97 REMARK 500 O ALA A 372 O HOH A 703 1.97 REMARK 500 OE2 GLU D 106 O HOH D 302 1.98 REMARK 500 OD2 ASP A 420 O HOH A 704 1.98 REMARK 500 O HOH L 422 O HOH C 303 1.99 REMARK 500 NZ LYS B 417 O HOH B 702 1.99 REMARK 500 NE2 GLN L 79 O HOH L 301 2.00 REMARK 500 O HOH D 474 O HOH D 489 2.00 REMARK 500 OE1 GLN A 474 O HOH A 705 2.02 REMARK 500 O HOH D 410 O HOH D 508 2.02 REMARK 500 O ALA B 372 O HOH B 703 2.04 REMARK 500 O SER L 169 O HOH L 302 2.05 REMARK 500 O HOH H 306 O HOH H 488 2.05 REMARK 500 O HOH C 396 O HOH C 480 2.06 REMARK 500 O HOH H 360 O HOH H 395 2.06 REMARK 500 OD1 ASN B 334 O HOH B 704 2.07 REMARK 500 OH TYR B 473 O HOH B 705 2.07 REMARK 500 OD2 ASP C 101 O HOH C 302 2.08 REMARK 500 N THR B 385 O HOH B 706 2.09 REMARK 500 O GLU H 1 O HOH H 301 2.09 REMARK 500 O4 NAG A 601 O HOH A 706 2.09 REMARK 500 O HOH L 466 O HOH L 488 2.10 REMARK 500 OD1 ASN A 334 O HOH A 707 2.10 REMARK 500 O HOH H 391 O HOH H 439 2.16 REMARK 500 NH1 ARG B 403 O HOH B 707 2.17 REMARK 500 OG SER L 65 O HOH L 303 2.18 REMARK 500 O HOH C 467 O HOH C 494 2.18 REMARK 500 NZ LYS B 386 O HOH B 708 2.19 REMARK 500 OG1 THR A 430 O HOH A 708 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 824 O HOH B 722 1564 1.71 REMARK 500 O HOH L 477 O HOH D 489 1565 1.87 REMARK 500 O HOH H 501 O HOH D 315 1565 1.99 REMARK 500 O HOH H 455 O HOH D 479 1565 1.99 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 L 195 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 CYS D 195 CA - CB - SG ANGL. DEV. = 6.7 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 ASN A 334 -169.07 -124.90 REMARK 500 TYR A 369 -73.76 -42.48 REMARK 500 ALA A 372 -5.79 68.75 REMARK 500 PHE A 377 85.91 -150.07 REMARK 500 THR A 385 -22.86 89.62 REMARK 500 LEU A 390 161.54 70.67 REMARK 500 ASN A 422 -56.25 -127.89 REMARK 500 PHE H 99 116.47 -166.61 REMARK 500 VAL H 103 -51.75 -126.19 REMARK 500 SER H 141 -174.86 154.04 REMARK 500 ALA L 51 -34.39 72.20 REMARK 500 SER L 93 -89.74 72.55 REMARK 500 ASN B 334 -168.74 -125.62 REMARK 500 ALA B 352 50.10 -110.93 REMARK 500 TYR B 369 -70.66 -42.98 REMARK 500 ALA B 372 -4.64 69.97 REMARK 500 THR B 385 -21.68 87.82 REMARK 500 LEU B 390 163.55 67.77 REMARK 500 ASN B 422 -56.32 -130.30 REMARK 500 PHE C 99 115.66 -165.66 REMARK 500 VAL C 103 -54.69 -124.97 REMARK 500 SER C 141 -175.03 153.97 REMARK 500 ALA D 51 -34.58 72.04 REMARK 500 SER D 93 -91.29 72.90 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH B 847 DISTANCE = 7.55 ANGSTROMS REMARK 999 REMARK 999 SEQUENCE REMARK 999 SOME DISORDERED RESIDUES LOCATED AT AA 135-139 OF CHAINS H AND C. DBREF 7EAM A 319 541 UNP P0DTC2 SPIKE_SARS2 319 541 DBREF 7EAM H 1 220 PDB 7EAM 7EAM 1 220 DBREF 7EAM L 1 214 PDB 7EAM 7EAM 1 214 DBREF 7EAM B 319 541 UNP P0DTC2 SPIKE_SARS2 319 541 DBREF 7EAM C 1 220 PDB 7EAM 7EAM 1 220 DBREF 7EAM D 1 214 PDB 7EAM 7EAM 1 214 SEQADV 7EAM HIS A 542 UNP P0DTC2 EXPRESSION TAG SEQADV 7EAM HIS A 543 UNP P0DTC2 EXPRESSION TAG SEQADV 7EAM HIS A 544 UNP P0DTC2 EXPRESSION TAG SEQADV 7EAM HIS A 545 UNP P0DTC2 EXPRESSION TAG SEQADV 7EAM HIS A 546 UNP P0DTC2 EXPRESSION TAG SEQADV 7EAM HIS A 547 UNP P0DTC2 EXPRESSION TAG SEQADV 7EAM HIS A 548 UNP P0DTC2 EXPRESSION TAG SEQADV 7EAM HIS A 549 UNP P0DTC2 EXPRESSION TAG SEQADV 7EAM HIS A 550 UNP P0DTC2 EXPRESSION TAG SEQADV 7EAM HIS A 551 UNP P0DTC2 EXPRESSION TAG SEQADV 7EAM HIS B 542 UNP P0DTC2 EXPRESSION TAG SEQADV 7EAM HIS B 543 UNP P0DTC2 EXPRESSION TAG SEQADV 7EAM HIS B 544 UNP P0DTC2 EXPRESSION TAG SEQADV 7EAM HIS B 545 UNP P0DTC2 EXPRESSION TAG SEQADV 7EAM HIS B 546 UNP P0DTC2 EXPRESSION TAG SEQADV 7EAM HIS B 547 UNP P0DTC2 EXPRESSION TAG SEQADV 7EAM HIS B 548 UNP P0DTC2 EXPRESSION TAG SEQADV 7EAM HIS B 549 UNP P0DTC2 EXPRESSION TAG SEQADV 7EAM HIS B 550 UNP P0DTC2 EXPRESSION TAG SEQADV 7EAM HIS B 551 UNP P0DTC2 EXPRESSION TAG SEQRES 1 A 233 ARG VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN SEQRES 2 A 233 ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA SEQRES 3 A 233 THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG SEQRES 4 A 233 ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SEQRES 5 A 233 SER ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER SEQRES 6 A 233 PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR SEQRES 7 A 233 ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN SEQRES 8 A 233 ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN SEQRES 9 A 233 TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA SEQRES 10 A 233 TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN SEQRES 11 A 233 TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU SEQRES 12 A 233 LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN SEQRES 13 A 233 ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN SEQRES 14 A 233 CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR SEQRES 15 A 233 ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SEQRES 16 A 233 SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY SEQRES 17 A 233 PRO LYS LYS SER THR ASN LEU VAL LYS ASN LYS CYS VAL SEQRES 18 A 233 ASN PHE HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1 H 220 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL ARG SEQRES 2 H 220 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY SEQRES 3 H 220 PHE ASN ILE LYS ASP THR TYR ILE HIS TRP VAL LYS GLN SEQRES 4 H 220 ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP SEQRES 5 H 220 PRO GLY ASP GLY ASP THR GLU TYR ASP PRO SER PHE GLN SEQRES 6 H 220 GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR SEQRES 7 H 220 ALA TYR LEU GLU LEU SER SER LEU THR SER GLU ASP THR SEQRES 8 H 220 ALA VAL TYR TYR CYS THR ARG PHE TYR ASP TYR VAL ASN SEQRES 9 H 220 TYR GLY MET ASP TYR TRP GLY GLN GLY THR SER VAL THR SEQRES 10 H 220 VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR PRO SEQRES 11 H 220 LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER MET VAL SEQRES 12 H 220 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO SEQRES 13 H 220 VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER GLY SEQRES 14 H 220 VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR SEQRES 15 H 220 THR LEU SER SER SER VAL THR VAL PRO SER SER THR TRP SEQRES 16 H 220 PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SEQRES 17 H 220 SER SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO ALA SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY GLU THR VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 214 GLY ASN ILE HIS ASN TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 GLN GLY LYS SER PRO GLN LEU LEU VAL TYR ASN ALA LYS SEQRES 5 L 214 THR LEU ALA ASP GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR GLN TYR SER LEU LYS ILE ASN SER LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE GLY SER TYR TYR CYS GLN HIS PHE SEQRES 8 L 214 TRP SER THR PRO PRO TRP THR PHE GLY GLY GLY THR LYS SEQRES 9 L 214 LEU GLU VAL LYS ARG ALA ASP ALA ALA PRO THR VAL SER SEQRES 10 L 214 ILE PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY SEQRES 11 L 214 ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS SEQRES 12 L 214 ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG SEQRES 13 L 214 GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER SEQRES 14 L 214 LYS ASP SER THR TYR SER MET SER SER THR LEU THR LEU SEQRES 15 L 214 THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS SEQRES 16 L 214 GLU ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SEQRES 17 L 214 SER PHE ASN ARG ASN ASN SEQRES 1 B 233 ARG VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN SEQRES 2 B 233 ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA SEQRES 3 B 233 THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG SEQRES 4 B 233 ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SEQRES 5 B 233 SER ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER SEQRES 6 B 233 PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR SEQRES 7 B 233 ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN SEQRES 8 B 233 ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN SEQRES 9 B 233 TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA SEQRES 10 B 233 TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN SEQRES 11 B 233 TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU SEQRES 12 B 233 LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN SEQRES 13 B 233 ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN SEQRES 14 B 233 CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR SEQRES 15 B 233 ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SEQRES 16 B 233 SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY SEQRES 17 B 233 PRO LYS LYS SER THR ASN LEU VAL LYS ASN LYS CYS VAL SEQRES 18 B 233 ASN PHE HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1 C 220 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL ARG SEQRES 2 C 220 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY SEQRES 3 C 220 PHE ASN ILE LYS ASP THR TYR ILE HIS TRP VAL LYS GLN SEQRES 4 C 220 ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP SEQRES 5 C 220 PRO GLY ASP GLY ASP THR GLU TYR ASP PRO SER PHE GLN SEQRES 6 C 220 GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR SEQRES 7 C 220 ALA TYR LEU GLU LEU SER SER LEU THR SER GLU ASP THR SEQRES 8 C 220 ALA VAL TYR TYR CYS THR ARG PHE TYR ASP TYR VAL ASN SEQRES 9 C 220 TYR GLY MET ASP TYR TRP GLY GLN GLY THR SER VAL THR SEQRES 10 C 220 VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR PRO SEQRES 11 C 220 LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER MET VAL SEQRES 12 C 220 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO SEQRES 13 C 220 VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER GLY SEQRES 14 C 220 VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR SEQRES 15 C 220 THR LEU SER SER SER VAL THR VAL PRO SER SER THR TRP SEQRES 16 C 220 PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SEQRES 17 C 220 SER SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG SEQRES 1 D 214 ASP ILE GLN MET THR GLN SER PRO ALA SER LEU SER ALA SEQRES 2 D 214 SER VAL GLY GLU THR VAL THR ILE THR CYS ARG ALA SER SEQRES 3 D 214 GLY ASN ILE HIS ASN TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 D 214 GLN GLY LYS SER PRO GLN LEU LEU VAL TYR ASN ALA LYS SEQRES 5 D 214 THR LEU ALA ASP GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 D 214 GLY SER GLY THR GLN TYR SER LEU LYS ILE ASN SER LEU SEQRES 7 D 214 GLN PRO GLU ASP PHE GLY SER TYR TYR CYS GLN HIS PHE SEQRES 8 D 214 TRP SER THR PRO PRO TRP THR PHE GLY GLY GLY THR LYS SEQRES 9 D 214 LEU GLU VAL LYS ARG ALA ASP ALA ALA PRO THR VAL SER SEQRES 10 D 214 ILE PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY SEQRES 11 D 214 ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS SEQRES 12 D 214 ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG SEQRES 13 D 214 GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER SEQRES 14 D 214 LYS ASP SER THR TYR SER MET SER SER THR LEU THR LEU SEQRES 15 D 214 THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS SEQRES 16 D 214 GLU ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SEQRES 17 D 214 SER PHE ASN ARG ASN ASN HET NAG E 1 14 HET NAG E 2 14 HET NAG F 1 14 HET NAG F 2 14 HET NAG A 601 14 HET NAG B 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 7 NAG 6(C8 H15 N O6) FORMUL 11 HOH *1164(H2 O) HELIX 1 AA1 PRO A 337 ASN A 343 1 7 HELIX 2 AA2 SER A 349 TRP A 353 5 5 HELIX 3 AA3 TYR A 365 ASN A 370 1 6 HELIX 4 AA4 ASP A 405 ILE A 410 5 6 HELIX 5 AA5 GLY A 416 ASN A 422 1 7 HELIX 6 AA6 SER A 438 SER A 443 1 6 HELIX 7 AA7 GLY A 502 TYR A 505 5 4 HELIX 8 AA8 ASN H 28 THR H 32 5 5 HELIX 9 AA9 PRO H 62 GLN H 65 5 4 HELIX 10 AB1 THR H 87 THR H 91 5 5 HELIX 11 AB2 SER H 163 SER H 165 5 3 HELIX 12 AB3 PRO H 207 SER H 210 5 4 HELIX 13 AB4 GLN L 79 PHE L 83 5 5 HELIX 14 AB5 SER L 122 SER L 128 1 7 HELIX 15 AB6 LYS L 184 GLU L 188 1 5 HELIX 16 AB7 PRO B 337 ASN B 343 1 7 HELIX 17 AB8 SER B 349 TRP B 353 5 5 HELIX 18 AB9 TYR B 365 ASN B 370 1 6 HELIX 19 AC1 ASP B 405 ILE B 410 5 6 HELIX 20 AC2 GLY B 416 ASN B 422 1 7 HELIX 21 AC3 SER B 438 SER B 443 1 6 HELIX 22 AC4 GLY B 502 TYR B 505 5 4 HELIX 23 AC5 ASN C 28 THR C 32 5 5 HELIX 24 AC6 PRO C 62 GLN C 65 5 4 HELIX 25 AC7 THR C 74 SER C 76 5 3 HELIX 26 AC8 THR C 87 THR C 91 5 5 HELIX 27 AC9 SER C 163 SER C 165 5 3 HELIX 28 AD1 PRO C 207 SER C 210 5 4 HELIX 29 AD2 GLN D 79 PHE D 83 5 5 HELIX 30 AD3 SER D 122 SER D 128 1 7 HELIX 31 AD4 LYS D 184 GLU D 188 1 5 SHEET 1 AA1 5 ASN A 354 ILE A 358 0 SHEET 2 AA1 5 ASN A 394 ARG A 403 -1 O VAL A 395 N ILE A 358 SHEET 3 AA1 5 PRO A 507 GLU A 516 -1 O VAL A 512 N ASP A 398 SHEET 4 AA1 5 GLY A 431 ASN A 437 -1 N ILE A 434 O VAL A 511 SHEET 5 AA1 5 THR A 376 TYR A 380 -1 N LYS A 378 O VAL A 433 SHEET 1 AA2 3 CYS A 361 VAL A 362 0 SHEET 2 AA2 3 VAL A 524 CYS A 525 1 O CYS A 525 N CYS A 361 SHEET 3 AA2 3 CYS A 391 PHE A 392 -1 N PHE A 392 O VAL A 524 SHEET 1 AA3 2 LEU A 452 ARG A 454 0 SHEET 2 AA3 2 LEU A 492 SER A 494 -1 O GLN A 493 N TYR A 453 SHEET 1 AA4 2 TYR A 473 GLN A 474 0 SHEET 2 AA4 2 CYS A 488 TYR A 489 -1 O TYR A 489 N TYR A 473 SHEET 1 AA5 4 GLN H 3 GLN H 6 0 SHEET 2 AA5 4 VAL H 18 SER H 25 -1 O THR H 23 N GLN H 5 SHEET 3 AA5 4 THR H 78 LEU H 83 -1 O LEU H 81 N LEU H 20 SHEET 4 AA5 4 ALA H 68 ASP H 73 -1 N ASP H 73 O THR H 78 SHEET 1 AA6 6 GLU H 10 VAL H 12 0 SHEET 2 AA6 6 THR H 114 VAL H 118 1 O SER H 115 N GLU H 10 SHEET 3 AA6 6 ALA H 92 ARG H 98 -1 N ALA H 92 O VAL H 116 SHEET 4 AA6 6 ILE H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA6 6 LEU H 45 ILE H 51 -1 O GLU H 46 N LYS H 38 SHEET 6 AA6 6 THR H 58 TYR H 60 -1 O GLU H 59 N ARG H 50 SHEET 1 AA7 4 SER H 127 LEU H 131 0 SHEET 2 AA7 4 MET H 142 TYR H 152 -1 O LEU H 148 N TYR H 129 SHEET 3 AA7 4 LEU H 181 PRO H 191 -1 O LEU H 184 N VAL H 149 SHEET 4 AA7 4 VAL H 170 THR H 172 -1 N HIS H 171 O SER H 187 SHEET 1 AA8 4 SER H 127 LEU H 131 0 SHEET 2 AA8 4 MET H 142 TYR H 152 -1 O LEU H 148 N TYR H 129 SHEET 3 AA8 4 LEU H 181 PRO H 191 -1 O LEU H 184 N VAL H 149 SHEET 4 AA8 4 VAL H 176 GLN H 178 -1 N GLN H 178 O LEU H 181 SHEET 1 AA9 3 THR H 158 TRP H 161 0 SHEET 2 AA9 3 THR H 201 HIS H 206 -1 O ASN H 203 N THR H 160 SHEET 3 AA9 3 THR H 211 LYS H 216 -1 O VAL H 213 N VAL H 204 SHEET 1 AB1 4 MET L 4 SER L 7 0 SHEET 2 AB1 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AB1 4 GLN L 70 ILE L 75 -1 O TYR L 71 N CYS L 23 SHEET 4 AB1 4 PHE L 62 SER L 67 -1 N SER L 63 O LYS L 74 SHEET 1 AB2 6 SER L 10 ALA L 13 0 SHEET 2 AB2 6 THR L 103 VAL L 107 1 O GLU L 106 N LEU L 11 SHEET 3 AB2 6 GLY L 84 HIS L 90 -1 N GLY L 84 O LEU L 105 SHEET 4 AB2 6 LEU L 33 GLN L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 AB2 6 GLN L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AB2 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AB3 4 THR L 115 PHE L 119 0 SHEET 2 AB3 4 GLY L 130 PHE L 140 -1 O ASN L 138 N THR L 115 SHEET 3 AB3 4 TYR L 174 THR L 183 -1 O MET L 176 N LEU L 137 SHEET 4 AB3 4 VAL L 160 TRP L 164 -1 N LEU L 161 O THR L 179 SHEET 1 AB4 4 SER L 154 ARG L 156 0 SHEET 2 AB4 4 ASN L 146 ILE L 151 -1 N ILE L 151 O SER L 154 SHEET 3 AB4 4 SER L 192 THR L 198 -1 O GLU L 196 N LYS L 148 SHEET 4 AB4 4 ILE L 206 ASN L 211 -1 O ILE L 206 N ALA L 197 SHEET 1 AB5 5 ASN B 354 ILE B 358 0 SHEET 2 AB5 5 ASN B 394 ARG B 403 -1 O VAL B 395 N ILE B 358 SHEET 3 AB5 5 PRO B 507 GLU B 516 -1 O VAL B 512 N ASP B 398 SHEET 4 AB5 5 GLY B 431 ASN B 437 -1 N ILE B 434 O VAL B 511 SHEET 5 AB5 5 THR B 376 TYR B 380 -1 N LYS B 378 O VAL B 433 SHEET 1 AB6 3 CYS B 361 VAL B 362 0 SHEET 2 AB6 3 VAL B 524 CYS B 525 1 O CYS B 525 N CYS B 361 SHEET 3 AB6 3 CYS B 391 PHE B 392 -1 N PHE B 392 O VAL B 524 SHEET 1 AB7 2 LEU B 452 ARG B 454 0 SHEET 2 AB7 2 LEU B 492 SER B 494 -1 O GLN B 493 N TYR B 453 SHEET 1 AB8 2 TYR B 473 GLN B 474 0 SHEET 2 AB8 2 CYS B 488 TYR B 489 -1 O TYR B 489 N TYR B 473 SHEET 1 AB9 4 GLN C 3 GLN C 6 0 SHEET 2 AB9 4 VAL C 18 SER C 25 -1 O THR C 23 N GLN C 5 SHEET 3 AB9 4 THR C 78 LEU C 83 -1 O LEU C 81 N LEU C 20 SHEET 4 AB9 4 ALA C 68 ASP C 73 -1 N ASP C 73 O THR C 78 SHEET 1 AC1 6 GLU C 10 VAL C 12 0 SHEET 2 AC1 6 THR C 114 VAL C 118 1 O SER C 115 N GLU C 10 SHEET 3 AC1 6 ALA C 92 ARG C 98 -1 N ALA C 92 O VAL C 116 SHEET 4 AC1 6 ILE C 34 GLN C 39 -1 N VAL C 37 O TYR C 95 SHEET 5 AC1 6 LEU C 45 ILE C 51 -1 O GLU C 46 N LYS C 38 SHEET 6 AC1 6 THR C 58 TYR C 60 -1 O GLU C 59 N ARG C 50 SHEET 1 AC2 4 SER C 127 LEU C 131 0 SHEET 2 AC2 4 MET C 142 TYR C 152 -1 O LEU C 148 N TYR C 129 SHEET 3 AC2 4 LEU C 181 PRO C 191 -1 O LEU C 184 N VAL C 149 SHEET 4 AC2 4 VAL C 170 THR C 172 -1 N HIS C 171 O SER C 187 SHEET 1 AC3 4 SER C 127 LEU C 131 0 SHEET 2 AC3 4 MET C 142 TYR C 152 -1 O LEU C 148 N TYR C 129 SHEET 3 AC3 4 LEU C 181 PRO C 191 -1 O LEU C 184 N VAL C 149 SHEET 4 AC3 4 VAL C 176 GLN C 178 -1 N GLN C 178 O LEU C 181 SHEET 1 AC4 3 THR C 158 TRP C 161 0 SHEET 2 AC4 3 THR C 201 HIS C 206 -1 O ASN C 203 N THR C 160 SHEET 3 AC4 3 THR C 211 LYS C 216 -1 O VAL C 213 N VAL C 204 SHEET 1 AC5 4 MET D 4 SER D 7 0 SHEET 2 AC5 4 VAL D 19 ALA D 25 -1 O ARG D 24 N THR D 5 SHEET 3 AC5 4 GLN D 70 ILE D 75 -1 O TYR D 71 N CYS D 23 SHEET 4 AC5 4 PHE D 62 SER D 67 -1 N SER D 63 O LYS D 74 SHEET 1 AC6 6 SER D 10 ALA D 13 0 SHEET 2 AC6 6 THR D 103 VAL D 107 1 O GLU D 106 N LEU D 11 SHEET 3 AC6 6 GLY D 84 HIS D 90 -1 N GLY D 84 O LEU D 105 SHEET 4 AC6 6 LEU D 33 GLN D 38 -1 N ALA D 34 O GLN D 89 SHEET 5 AC6 6 GLN D 45 TYR D 49 -1 O LEU D 47 N TRP D 35 SHEET 6 AC6 6 THR D 53 LEU D 54 -1 O THR D 53 N TYR D 49 SHEET 1 AC7 4 THR D 115 PHE D 119 0 SHEET 2 AC7 4 GLY D 130 PHE D 140 -1 O ASN D 138 N THR D 115 SHEET 3 AC7 4 TYR D 174 THR D 183 -1 O MET D 176 N LEU D 137 SHEET 4 AC7 4 VAL D 160 TRP D 164 -1 N LEU D 161 O THR D 179 SHEET 1 AC8 4 SER D 154 ARG D 156 0 SHEET 2 AC8 4 ASN D 146 ILE D 151 -1 N ILE D 151 O SER D 154 SHEET 3 AC8 4 SER D 192 THR D 198 -1 O GLU D 196 N LYS D 148 SHEET 4 AC8 4 ILE D 206 ASN D 211 -1 O ILE D 206 N ALA D 197 SSBOND 1 CYS A 336 CYS A 361 1555 1555 2.04 SSBOND 2 CYS A 379 CYS A 432 1555 1555 2.11 SSBOND 3 CYS A 391 CYS A 525 1555 1555 2.05 SSBOND 4 CYS A 480 CYS A 488 1555 1555 2.07 SSBOND 5 CYS H 22 CYS H 96 1555 1555 2.07 SSBOND 6 CYS H 147 CYS H 202 1555 1555 2.03 SSBOND 7 CYS L 23 CYS L 88 1555 1555 2.10 SSBOND 8 CYS L 135 CYS L 195 1555 1555 2.09 SSBOND 9 CYS B 336 CYS B 361 1555 1555 2.04 SSBOND 10 CYS B 379 CYS B 432 1555 1555 2.11 SSBOND 11 CYS B 391 CYS B 525 1555 1555 2.05 SSBOND 12 CYS B 480 CYS B 488 1555 1555 2.06 SSBOND 13 CYS C 22 CYS C 96 1555 1555 2.08 SSBOND 14 CYS C 147 CYS C 202 1555 1555 2.03 SSBOND 15 CYS D 23 CYS D 88 1555 1555 2.12 SSBOND 16 CYS D 135 CYS D 195 1555 1555 2.09 LINK ND2 ASN A 331 C1 NAG E 1 1555 1555 1.50 LINK ND2 ASN A 343 C1 NAG A 601 1555 1555 1.51 LINK ND2 ASN B 331 C1 NAG F 1 1555 1555 1.50 LINK ND2 ASN B 343 C1 NAG B 601 1555 1555 1.50 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.39 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.39 CISPEP 1 ASN H 140 SER H 141 0 -7.68 CISPEP 2 PHE H 153 PRO H 154 0 -6.40 CISPEP 3 GLU H 155 PRO H 156 0 -0.68 CISPEP 4 TRP H 195 PRO H 196 0 5.32 CISPEP 5 SER L 7 PRO L 8 0 -6.20 CISPEP 6 PRO L 95 PRO L 96 0 6.26 CISPEP 7 TYR L 141 PRO L 142 0 0.22 CISPEP 8 ASN C 140 SER C 141 0 -6.56 CISPEP 9 PHE C 153 PRO C 154 0 -4.97 CISPEP 10 GLU C 155 PRO C 156 0 1.24 CISPEP 11 TRP C 195 PRO C 196 0 5.35 CISPEP 12 SER D 7 PRO D 8 0 -5.16 CISPEP 13 PRO D 95 PRO D 96 0 6.52 CISPEP 14 TYR D 141 PRO D 142 0 -0.04 CRYST1 37.440 87.970 102.720 89.96 87.05 89.98 P 1 2 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 0.026709 -0.000009 -0.001376 0.00000 SCALE2 0.000000 0.011368 -0.000008 0.00000 SCALE3 0.000000 0.000000 0.009748 0.00000