HEADER VIRAL PROTEIN/IMMUNE SYSTEM 11-MAR-24 9AZR TITLE LINEAGE 860 UCA FAB BOUND TO A/MASSACHUSETTS/1/1990 HEMAGGLUTININ HEAD COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMAGGLUTININ HA1 CHAIN; COMPND 3 CHAIN: E; COMPND 4 FRAGMENT: HEAD DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: LINEAGE 860 UCA FAB HEAVY CHAIN; COMPND 8 CHAIN: H; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: LINEAGE 860 UCA FAB LIGHT CHAIN; COMPND 12 CHAIN: L; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_TAXID: 387165; SOURCE 4 STRAIN: A/MASSACHUSETTS/1/1990(H1N1); SOURCE 5 GENE: HA; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTIBODY, INFLUENZA, HEMAGGLUTININ, UCA, ANTIVIRAL PROTEIN, VIRAL KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR D.P.MAURER,A.G.SCHMIDT REVDAT 1 12-MAR-25 9AZR 0 JRNL AUTH D.P.MAURER,M.VU,A.G.SCHMIDT JRNL TITL ANTIGENIC DRIFT EXPANDS INFLUENZA VIRAL ESCAPE PATHWAYS FROM JRNL TITL 2 RECALLED HUMORAL IMMUNITY. JRNL REF IMMUNITY 2025 JRNL REFN ISSN 1074-7613 JRNL PMID 40023162 JRNL DOI 10.1016/J.IMMUNI.2025.02.006 REMARK 2 REMARK 2 RESOLUTION. 2.30 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) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.94 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 3 NUMBER OF REFLECTIONS : 39812 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.231 REMARK 3 R VALUE (WORKING SET) : 0.229 REMARK 3 FREE R VALUE : 0.270 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040 REMARK 3 FREE R VALUE TEST SET COUNT : 2006 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 48.9400 - 5.5400 0.99 2833 152 0.1767 0.1991 REMARK 3 2 5.5400 - 4.4000 0.99 2772 140 0.1607 0.2012 REMARK 3 3 4.4000 - 3.8400 0.99 2749 149 0.1888 0.2252 REMARK 3 4 3.8400 - 3.4900 1.00 2760 146 0.2205 0.2684 REMARK 3 5 3.4900 - 3.2400 1.00 2745 146 0.2475 0.2896 REMARK 3 6 3.2400 - 3.0500 0.98 2750 139 0.2645 0.3480 REMARK 3 7 3.0500 - 2.9000 0.99 2682 148 0.2802 0.3256 REMARK 3 8 2.9000 - 2.7700 1.00 2727 140 0.2832 0.3207 REMARK 3 9 2.7700 - 2.6600 1.00 2760 148 0.3115 0.3917 REMARK 3 10 2.6600 - 2.5700 1.00 2715 146 0.3377 0.3817 REMARK 3 11 2.5700 - 2.4900 0.99 2703 147 0.3089 0.3415 REMARK 3 12 2.4900 - 2.4200 0.99 2727 129 0.3023 0.3654 REMARK 3 13 2.4200 - 2.3600 0.99 2719 157 0.3078 0.3715 REMARK 3 14 2.3600 - 2.3000 0.79 2164 119 0.3255 0.3440 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) : 0.322 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.496 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 43.62 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.46 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 : 0.003 5172 REMARK 3 ANGLE : 0.546 7055 REMARK 3 CHIRALITY : 0.044 770 REMARK 3 PLANARITY : 0.004 907 REMARK 3 DIHEDRAL : 4.628 712 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 22 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 52 THROUGH 86 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.9814 -29.7962 23.9436 REMARK 3 T TENSOR REMARK 3 T11: 0.6624 T22: 0.4819 REMARK 3 T33: 1.3583 T12: 0.0071 REMARK 3 T13: -0.2645 T23: 0.3074 REMARK 3 L TENSOR REMARK 3 L11: 1.9966 L22: 0.7252 REMARK 3 L33: 0.6532 L12: -1.1458 REMARK 3 L13: -0.2669 L23: 0.0344 REMARK 3 S TENSOR REMARK 3 S11: 0.3668 S12: -0.2403 S13: -2.0891 REMARK 3 S21: 0.9727 S22: -0.0775 S23: -0.5281 REMARK 3 S31: 0.4666 S32: -0.0509 S33: -0.2005 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 87 THROUGH 108 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.0711 -23.5187 12.5361 REMARK 3 T TENSOR REMARK 3 T11: 0.5150 T22: 0.5312 REMARK 3 T33: 0.6380 T12: 0.0004 REMARK 3 T13: -0.0119 T23: -0.0929 REMARK 3 L TENSOR REMARK 3 L11: 0.0780 L22: 0.4580 REMARK 3 L33: 0.1638 L12: -0.1161 REMARK 3 L13: 0.0482 L23: 0.1974 REMARK 3 S TENSOR REMARK 3 S11: -0.3573 S12: 0.7152 S13: -1.0826 REMARK 3 S21: -0.1853 S22: 0.1666 S23: -0.3792 REMARK 3 S31: 0.4861 S32: 0.3956 S33: -0.0001 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 109 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.0356 -10.1632 21.1201 REMARK 3 T TENSOR REMARK 3 T11: 0.3878 T22: 0.4562 REMARK 3 T33: 0.3348 T12: -0.0309 REMARK 3 T13: -0.0119 T23: 0.0417 REMARK 3 L TENSOR REMARK 3 L11: 1.9221 L22: 0.4789 REMARK 3 L33: 0.5397 L12: -0.0444 REMARK 3 L13: 0.4429 L23: 0.2290 REMARK 3 S TENSOR REMARK 3 S11: 0.0577 S12: -0.3256 S13: -0.0773 REMARK 3 S21: 0.1079 S22: -0.0206 S23: -0.0199 REMARK 3 S31: -0.0478 S32: -0.0332 S33: 0.0000 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 214 THROUGH 263 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.4305 -13.0853 16.2386 REMARK 3 T TENSOR REMARK 3 T11: 0.3351 T22: 0.3857 REMARK 3 T33: 0.3497 T12: 0.0010 REMARK 3 T13: -0.0025 T23: 0.0988 REMARK 3 L TENSOR REMARK 3 L11: 0.4121 L22: 0.9934 REMARK 3 L33: 0.4496 L12: -0.0948 REMARK 3 L13: -0.2079 L23: 0.0518 REMARK 3 S TENSOR REMARK 3 S11: 0.1187 S12: -0.0282 S13: 0.0638 REMARK 3 S21: 0.0563 S22: -0.1336 S23: 0.0203 REMARK 3 S31: 0.0737 S32: 0.0236 S33: 0.0000 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 28 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.2772 8.9374 16.4474 REMARK 3 T TENSOR REMARK 3 T11: 0.5315 T22: 0.5051 REMARK 3 T33: 0.4675 T12: 0.0168 REMARK 3 T13: 0.0734 T23: 0.0834 REMARK 3 L TENSOR REMARK 3 L11: 0.2208 L22: 0.0966 REMARK 3 L33: 0.3128 L12: -0.2115 REMARK 3 L13: -0.2337 L23: 0.2941 REMARK 3 S TENSOR REMARK 3 S11: 0.0026 S12: -0.1057 S13: 0.4901 REMARK 3 S21: 0.1655 S22: 0.0199 S23: 0.0014 REMARK 3 S31: -0.5251 S32: -0.0997 S33: 0.0010 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 29 THROUGH 40 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.2264 1.0631 15.5932 REMARK 3 T TENSOR REMARK 3 T11: 0.4820 T22: 0.4815 REMARK 3 T33: 0.3543 T12: -0.0105 REMARK 3 T13: 0.0524 T23: 0.0993 REMARK 3 L TENSOR REMARK 3 L11: 0.5759 L22: 0.2594 REMARK 3 L33: 0.2728 L12: 0.0744 REMARK 3 L13: -0.1321 L23: 0.2840 REMARK 3 S TENSOR REMARK 3 S11: 0.3145 S12: -0.0075 S13: -0.7458 REMARK 3 S21: 0.0804 S22: 0.3530 S23: -0.1689 REMARK 3 S31: -0.1094 S32: -0.0829 S33: 0.0132 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 41 THROUGH 60 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.8403 0.4077 10.2467 REMARK 3 T TENSOR REMARK 3 T11: 0.3823 T22: 0.4712 REMARK 3 T33: 0.3747 T12: 0.0085 REMARK 3 T13: 0.0130 T23: -0.0139 REMARK 3 L TENSOR REMARK 3 L11: 0.1417 L22: 0.9068 REMARK 3 L33: 0.3058 L12: -0.2479 REMARK 3 L13: 0.0408 L23: -0.4858 REMARK 3 S TENSOR REMARK 3 S11: 0.0663 S12: -0.0007 S13: 0.3534 REMARK 3 S21: -0.1308 S22: -0.2193 S23: 0.3405 REMARK 3 S31: -0.0529 S32: -0.1789 S33: 0.0003 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 61 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.3269 8.1762 9.9694 REMARK 3 T TENSOR REMARK 3 T11: 0.6118 T22: 0.4877 REMARK 3 T33: 0.4537 T12: 0.0476 REMARK 3 T13: 0.0611 T23: -0.0031 REMARK 3 L TENSOR REMARK 3 L11: 1.0243 L22: 0.3710 REMARK 3 L33: 0.1881 L12: -0.0848 REMARK 3 L13: -0.2584 L23: -0.2176 REMARK 3 S TENSOR REMARK 3 S11: 0.3132 S12: 0.2957 S13: 0.0708 REMARK 3 S21: -0.2262 S22: 0.1717 S23: -0.4880 REMARK 3 S31: -0.3601 S32: 0.4770 S33: 0.0011 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 84 THROUGH 98 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.7488 4.1931 6.4517 REMARK 3 T TENSOR REMARK 3 T11: 0.5467 T22: 0.5466 REMARK 3 T33: 0.3977 T12: 0.0091 REMARK 3 T13: -0.0025 T23: 0.1318 REMARK 3 L TENSOR REMARK 3 L11: 0.3326 L22: 0.2407 REMARK 3 L33: 0.1715 L12: -0.1272 REMARK 3 L13: -0.0464 L23: -0.2172 REMARK 3 S TENSOR REMARK 3 S11: 0.0087 S12: 0.2371 S13: -0.3579 REMARK 3 S21: -0.2328 S22: 0.0127 S23: -0.0380 REMARK 3 S31: 0.3871 S32: -0.3130 S33: -0.0006 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 99 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.7471 -7.8385 19.4825 REMARK 3 T TENSOR REMARK 3 T11: 0.4151 T22: 0.4781 REMARK 3 T33: 0.3908 T12: 0.0408 REMARK 3 T13: 0.0028 T23: 0.0486 REMARK 3 L TENSOR REMARK 3 L11: 0.1300 L22: 0.1456 REMARK 3 L33: 0.3687 L12: -0.0744 REMARK 3 L13: -0.0922 L23: -0.3241 REMARK 3 S TENSOR REMARK 3 S11: -0.2209 S12: -0.4292 S13: -0.1334 REMARK 3 S21: 0.1671 S22: 0.1719 S23: 0.0829 REMARK 3 S31: 0.0538 S32: 0.1718 S33: 0.0001 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 120 THROUGH 132 ) REMARK 3 ORIGIN FOR THE GROUP (A): -33.1879 11.1253 3.4299 REMARK 3 T TENSOR REMARK 3 T11: 0.5182 T22: 0.4893 REMARK 3 T33: 0.4983 T12: 0.1080 REMARK 3 T13: 0.0219 T23: 0.1303 REMARK 3 L TENSOR REMARK 3 L11: 0.0814 L22: 0.1510 REMARK 3 L33: 0.4043 L12: 0.0967 REMARK 3 L13: 0.1690 L23: 0.3266 REMARK 3 S TENSOR REMARK 3 S11: -0.1956 S12: 0.4479 S13: 0.3297 REMARK 3 S21: 0.0616 S22: 0.1341 S23: 0.3699 REMARK 3 S31: -0.5871 S32: 0.3263 S33: -0.0034 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 133 THROUGH 147 ) REMARK 3 ORIGIN FOR THE GROUP (A): -57.2831 -5.2760 -1.9877 REMARK 3 T TENSOR REMARK 3 T11: 0.4499 T22: 0.4880 REMARK 3 T33: 0.7881 T12: -0.0951 REMARK 3 T13: 0.0640 T23: -0.1634 REMARK 3 L TENSOR REMARK 3 L11: 0.2443 L22: 0.2027 REMARK 3 L33: 0.4479 L12: -0.1236 REMARK 3 L13: 0.2059 L23: -0.0315 REMARK 3 S TENSOR REMARK 3 S11: 0.0024 S12: -0.1061 S13: -0.3720 REMARK 3 S21: 0.9034 S22: 0.3425 S23: 0.3476 REMARK 3 S31: 0.1134 S32: -0.4255 S33: 0.0055 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 148 THROUGH 188 ) REMARK 3 ORIGIN FOR THE GROUP (A): -47.7655 2.0081 5.8390 REMARK 3 T TENSOR REMARK 3 T11: 0.4729 T22: 0.3822 REMARK 3 T33: 0.4818 T12: 0.0095 REMARK 3 T13: 0.0636 T23: 0.0172 REMARK 3 L TENSOR REMARK 3 L11: 0.4441 L22: 0.0439 REMARK 3 L33: 0.4924 L12: 0.0277 REMARK 3 L13: 0.5011 L23: 0.1587 REMARK 3 S TENSOR REMARK 3 S11: -0.2269 S12: 0.0890 S13: -0.2826 REMARK 3 S21: 0.1121 S22: 0.0511 S23: -0.2113 REMARK 3 S31: 0.1140 S32: 0.1226 S33: 0.0000 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 189 THROUGH 227 ) REMARK 3 ORIGIN FOR THE GROUP (A): -56.2029 3.3136 5.1612 REMARK 3 T TENSOR REMARK 3 T11: 0.4343 T22: 0.3644 REMARK 3 T33: 0.5236 T12: 0.0033 REMARK 3 T13: 0.0521 T23: -0.1169 REMARK 3 L TENSOR REMARK 3 L11: 0.6546 L22: 1.0059 REMARK 3 L33: 0.4874 L12: -0.5092 REMARK 3 L13: 0.6802 L23: -0.0501 REMARK 3 S TENSOR REMARK 3 S11: -0.1639 S12: 0.1792 S13: -0.1593 REMARK 3 S21: 0.1474 S22: -0.0331 S23: 0.2638 REMARK 3 S31: -0.0309 S32: -0.3177 S33: 0.0001 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 29 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.8236 -21.4807 11.6967 REMARK 3 T TENSOR REMARK 3 T11: 0.4285 T22: 0.4998 REMARK 3 T33: 0.5955 T12: -0.0094 REMARK 3 T13: -0.0102 T23: 0.0974 REMARK 3 L TENSOR REMARK 3 L11: 0.2250 L22: 0.0875 REMARK 3 L33: 0.5042 L12: 0.2423 REMARK 3 L13: 0.4117 L23: 0.2369 REMARK 3 S TENSOR REMARK 3 S11: -0.2493 S12: 0.3174 S13: -0.4887 REMARK 3 S21: -0.3250 S22: 0.3341 S23: 0.1097 REMARK 3 S31: 0.7446 S32: -0.1892 S33: -0.0008 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 30 THROUGH 47 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.9098 -11.2852 18.6175 REMARK 3 T TENSOR REMARK 3 T11: 0.3565 T22: 0.4420 REMARK 3 T33: 0.3191 T12: 0.0092 REMARK 3 T13: 0.0107 T23: 0.1047 REMARK 3 L TENSOR REMARK 3 L11: 0.2651 L22: 0.6922 REMARK 3 L33: 0.3096 L12: 0.4765 REMARK 3 L13: 0.3882 L23: 0.6632 REMARK 3 S TENSOR REMARK 3 S11: -0.2058 S12: 0.1499 S13: -0.4724 REMARK 3 S21: 0.3689 S22: -0.1428 S23: 0.5367 REMARK 3 S31: -0.0924 S32: -0.4872 S33: -0.0030 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 48 THROUGH 60 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.5461 -17.1640 27.1261 REMARK 3 T TENSOR REMARK 3 T11: 0.5734 T22: 0.7052 REMARK 3 T33: 0.5781 T12: 0.0527 REMARK 3 T13: -0.0076 T23: 0.1783 REMARK 3 L TENSOR REMARK 3 L11: 0.2421 L22: 0.3288 REMARK 3 L33: 0.1624 L12: 0.1163 REMARK 3 L13: 0.1032 L23: 0.0121 REMARK 3 S TENSOR REMARK 3 S11: -0.0980 S12: -1.0861 S13: -0.4578 REMARK 3 S21: 0.3041 S22: -0.1583 S23: 0.4551 REMARK 3 S31: 0.5050 S32: 0.1201 S33: -0.0090 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 61 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.8448 -18.8738 17.4547 REMARK 3 T TENSOR REMARK 3 T11: 0.4035 T22: 0.5521 REMARK 3 T33: 0.4430 T12: 0.0205 REMARK 3 T13: 0.0242 T23: 0.1304 REMARK 3 L TENSOR REMARK 3 L11: 0.6424 L22: 0.5985 REMARK 3 L33: 0.2349 L12: 0.7628 REMARK 3 L13: 0.2625 L23: 0.4624 REMARK 3 S TENSOR REMARK 3 S11: 0.2160 S12: -0.2728 S13: -0.3843 REMARK 3 S21: -0.0662 S22: -0.1285 S23: 0.1877 REMARK 3 S31: -0.0155 S32: 0.0567 S33: 0.0001 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 92 THROUGH 115 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.7522 -15.7106 10.4832 REMARK 3 T TENSOR REMARK 3 T11: 0.4622 T22: 0.4491 REMARK 3 T33: 0.4008 T12: -0.0210 REMARK 3 T13: 0.0025 T23: 0.0533 REMARK 3 L TENSOR REMARK 3 L11: 0.3047 L22: 0.3343 REMARK 3 L33: -0.0594 L12: -0.0577 REMARK 3 L13: 0.2708 L23: -0.0574 REMARK 3 S TENSOR REMARK 3 S11: 0.2191 S12: -0.5824 S13: -0.0255 REMARK 3 S21: 0.0162 S22: -0.2247 S23: -0.0964 REMARK 3 S31: -0.0120 S32: 0.0439 S33: 0.0001 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 116 THROUGH 152 ) REMARK 3 ORIGIN FOR THE GROUP (A): -47.1166 -7.1103 -3.4680 REMARK 3 T TENSOR REMARK 3 T11: 0.3545 T22: 0.3635 REMARK 3 T33: 0.4573 T12: 0.0169 REMARK 3 T13: -0.0035 T23: -0.0202 REMARK 3 L TENSOR REMARK 3 L11: 1.0118 L22: 0.3715 REMARK 3 L33: 0.9768 L12: -0.1800 REMARK 3 L13: 0.1806 L23: 0.4439 REMARK 3 S TENSOR REMARK 3 S11: 0.0495 S12: 0.0014 S13: -0.0303 REMARK 3 S21: 0.0847 S22: -0.2027 S23: 0.0678 REMARK 3 S31: -0.0922 S32: 0.0313 S33: 0.0000 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 153 THROUGH 189 ) REMARK 3 ORIGIN FOR THE GROUP (A): -43.0806 -7.3038 -3.5883 REMARK 3 T TENSOR REMARK 3 T11: 0.3402 T22: 0.4078 REMARK 3 T33: 0.4815 T12: 0.0100 REMARK 3 T13: -0.0182 T23: -0.0072 REMARK 3 L TENSOR REMARK 3 L11: 1.3071 L22: 1.2876 REMARK 3 L33: 0.1905 L12: 0.3419 REMARK 3 L13: -0.2613 L23: 0.1234 REMARK 3 S TENSOR REMARK 3 S11: 0.1207 S12: -0.0018 S13: -0.0453 REMARK 3 S21: -0.0381 S22: -0.1246 S23: 0.2093 REMARK 3 S31: -0.3267 S32: 0.1352 S33: -0.0005 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 190 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): -47.0607 -14.9530 -8.5880 REMARK 3 T TENSOR REMARK 3 T11: 0.3963 T22: 0.4184 REMARK 3 T33: 0.5145 T12: 0.0083 REMARK 3 T13: -0.0462 T23: -0.1591 REMARK 3 L TENSOR REMARK 3 L11: 0.2775 L22: 0.2982 REMARK 3 L33: 0.6800 L12: 0.1773 REMARK 3 L13: -0.2323 L23: 0.2253 REMARK 3 S TENSOR REMARK 3 S11: 0.0539 S12: -0.1737 S13: -0.4218 REMARK 3 S21: -0.2455 S22: -0.0313 S23: -0.0031 REMARK 3 S31: 0.4283 S32: 0.0242 S33: -0.0090 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 9AZR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1000281594. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-APR-22 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 : APS REMARK 200 BEAMLINE : 24-ID-E REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39860 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 48.940 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 200 DATA REDUNDANCY : 6.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.3500 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.47 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4K, 200 MM IMIDAZOLE, PH 7.4, REMARK 280 HCL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 101.27150 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.93150 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 101.27150 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.93150 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5590 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 28550 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH H 333 LIES ON A SPECIAL POSITION. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY E 264 REMARK 465 ALA E 265 REMARK 465 GLY E 266 REMARK 465 SER E 267 REMARK 465 SER E 268 REMARK 465 LEU E 269 REMARK 465 GLU E 270 REMARK 465 VAL E 271 REMARK 465 LEU E 272 REMARK 465 PHE E 273 REMARK 465 GLN E 274 REMARK 465 SER H 228 REMARK 465 CYS H 229 REMARK 465 ASP H 230 REMARK 465 LYS H 231 REMARK 465 GLY H 232 REMARK 465 SER H 233 REMARK 465 SER H 234 REMARK 465 LEU H 235 REMARK 465 GLU H 236 REMARK 465 VAL H 237 REMARK 465 LEU H 238 REMARK 465 PHE H 239 REMARK 465 GLN H 240 REMARK 465 CYS L 213 REMARK 465 SER L 214 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 SER E 126 O HOH E 401 1.86 REMARK 500 O VAL L 161 O HOH L 301 1.91 REMARK 500 O HOH E 405 O HOH E 415 2.01 REMARK 500 OG1 THR H 28 O HOH H 301 2.04 REMARK 500 OG SER H 145 O HOH H 302 2.05 REMARK 500 OE1 GLN L 37 O HOH L 302 2.07 REMARK 500 O GLY E 240 O HOH E 402 2.09 REMARK 500 O HOH H 302 O HOH H 308 2.12 REMARK 500 NE ARG H 85 O HOH H 303 2.14 REMARK 500 OE1 GLU E 175 O HOH E 403 2.17 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 GLN H 1 O HOH H 301 2556 2.13 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 PRO E 53 -167.43 -77.82 REMARK 500 GLN E 55 77.60 56.00 REMARK 500 GLU E 72 -9.63 -55.55 REMARK 500 SER E 76 81.07 -171.87 REMARK 500 GLU E 78 -46.16 -136.56 REMARK 500 ILE E 83 -16.08 -143.75 REMARK 500 GLU E 85 -51.02 -125.08 REMARK 500 SER E 125 -14.77 -142.62 REMARK 500 CYS E 139 52.46 -110.66 REMARK 500 HIS E 196 -58.99 65.73 REMARK 500 ASN E 199 54.19 -107.42 REMARK 500 SER E 210 108.54 -160.71 REMARK 500 TYR H 108 72.01 -150.48 REMARK 500 ASP H 157 61.12 66.97 REMARK 500 ASP L 50 -57.19 71.77 REMARK 500 GLN L 110 139.21 -171.07 REMARK 500 REMARK 500 REMARK: NULL DBREF 9AZR E 52 263 UNP Q07775 Q07775_9INFA 65 277 DBREF 9AZR H 1 240 PDB 9AZR 9AZR 1 240 DBREF 9AZR L 1 214 PDB 9AZR 9AZR 1 214 SEQADV 9AZR GLY E 264 UNP Q07775 EXPRESSION TAG SEQADV 9AZR ALA E 265 UNP Q07775 EXPRESSION TAG SEQADV 9AZR GLY E 266 UNP Q07775 EXPRESSION TAG SEQADV 9AZR SER E 267 UNP Q07775 EXPRESSION TAG SEQADV 9AZR SER E 268 UNP Q07775 EXPRESSION TAG SEQADV 9AZR LEU E 269 UNP Q07775 EXPRESSION TAG SEQADV 9AZR GLU E 270 UNP Q07775 EXPRESSION TAG SEQADV 9AZR VAL E 271 UNP Q07775 EXPRESSION TAG SEQADV 9AZR LEU E 272 UNP Q07775 EXPRESSION TAG SEQADV 9AZR PHE E 273 UNP Q07775 EXPRESSION TAG SEQADV 9AZR GLN E 274 UNP Q07775 EXPRESSION TAG SEQRES 1 E 224 ALA PRO LEU GLN LEU GLY ASN CYS SER ILE ALA GLY TRP SEQRES 2 E 224 ILE LEU GLY ASN PRO GLU CYS GLU SER LEU PHE SER LYS SEQRES 3 E 224 GLU SER TRP SER TYR ILE ALA GLU THR PRO ASN SER GLU SEQRES 4 E 224 ASN GLY THR CYS TYR PRO GLY TYR PHE ALA ASP TYR GLU SEQRES 5 E 224 GLU LEU ARG GLU GLN LEU SER SER VAL SER SER PHE GLU SEQRES 6 E 224 ARG PHE GLU ILE PHE PRO LYS GLU SER SER TRP PRO ASN SEQRES 7 E 224 HIS THR VAL THR LYS GLY VAL THR ALA SER CYS SER HIS SEQRES 8 E 224 ASN GLY LYS SER SER PHE TYR ARG ASN LEU LEU TRP LEU SEQRES 9 E 224 THR GLU LYS ASN GLY LEU TYR PRO ASN LEU SER LYS SER SEQRES 10 E 224 TYR VAL ASN ASN LYS GLU LYS GLU VAL LEU VAL LEU TRP SEQRES 11 E 224 GLY VAL HIS HIS PRO SER ASN ILE GLY ASP GLN ARG ALA SEQRES 12 E 224 ILE TYR HIS THR GLU ASN ALA TYR VAL SER VAL VAL SER SEQRES 13 E 224 SER HIS TYR SER ARG ARG PHE THR PRO GLU ILE ALA LYS SEQRES 14 E 224 ARG PRO LYS VAL ARG ASP GLN GLU GLY ARG ILE ASN TYR SEQRES 15 E 224 TYR TRP THR LEU LEU GLU PRO GLY ASP THR ILE ILE PHE SEQRES 16 E 224 GLU ALA ASN GLY ASN LEU ILE ALA PRO TRP TYR ALA PHE SEQRES 17 E 224 ALA LEU SER ARG GLY GLY ALA GLY SER SER LEU GLU VAL SEQRES 18 E 224 LEU PHE GLN SEQRES 1 H 240 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 240 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 240 TYR THR PHE THR GLY TYR TYR MET HIS TRP VAL ARG GLN SEQRES 4 H 240 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 H 240 PRO ASN SER GLY GLY THR ASN TYR ALA GLN LYS PHE GLN SEQRES 6 H 240 GLY TRP VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 H 240 ALA TYR MET GLU LEU SER ARG LEU ARG SER ASP ASP THR SEQRES 8 H 240 ALA VAL TYR TYR CYS ALA ARG GLY GLY LEU GLU PRO ARG SEQRES 9 H 240 SER VAL ASP TYR TYR TYR TYR GLY MET ASP VAL TRP GLY SEQRES 10 H 240 GLN GLY THR THR VAL THR VAL SER SER ALA SER THR LYS SEQRES 11 H 240 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 H 240 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 H 240 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 H 240 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 H 240 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 H 240 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 H 240 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 H 240 LYS ARG VAL GLU PRO LYS SER CYS ASP LYS GLY SER SER SEQRES 19 H 240 LEU GLU VAL LEU PHE GLN SEQRES 1 L 214 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER VAL ALA SEQRES 2 L 214 PRO GLY GLN THR ALA ARG ILE THR CYS GLY GLY ASN ASN SEQRES 3 L 214 ILE GLY SER LYS SER VAL HIS TRP TYR GLN GLN LYS PRO SEQRES 4 L 214 GLY GLN ALA PRO VAL LEU VAL VAL TYR ASP ASP SER ASP SEQRES 5 L 214 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER ASN SEQRES 6 L 214 SER GLY ASN THR ALA THR LEU THR ILE SER ARG VAL GLU SEQRES 7 L 214 ALA GLY ASP GLU ALA ASP TYR TYR CYS GLN VAL TRP ASP SEQRES 8 L 214 SER SER SER ASP HIS VAL VAL PHE GLY GLY GLY THR LYS SEQRES 9 L 214 LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL SEQRES 10 L 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN SEQRES 11 L 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO SEQRES 12 L 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO SEQRES 13 L 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SEQRES 14 L 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU SEQRES 15 L 214 THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS SEQRES 16 L 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL SEQRES 17 L 214 ALA PRO THR GLU CYS SER HET NAG E 301 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 4 NAG C8 H15 N O6 FORMUL 5 HOH *217(H2 O) HELIX 1 AA1 SER E 60 GLY E 67 1 8 HELIX 2 AA2 ASP E 101 LEU E 109 1 9 HELIX 3 AA3 ASN E 187 HIS E 196 1 10 HELIX 4 AA4 THR H 28 TYR H 32 5 5 HELIX 5 AA5 ARG H 87 THR H 91 5 5 HELIX 6 AA6 SER H 105 TYR H 109 5 5 HELIX 7 AA7 SER H 169 ALA H 171 5 3 HELIX 8 AA8 LYS H 214 ASN H 217 5 4 HELIX 9 AA9 ASN L 26 LYS L 30 5 5 HELIX 10 AB1 GLU L 78 GLU L 82 5 5 HELIX 11 AB2 SER L 123 ALA L 129 1 7 HELIX 12 AB3 THR L 183 HIS L 190 1 8 SHEET 1 AA1 5 SER E 114 GLU E 119 0 SHEET 2 AA1 5 TYR E 256 SER E 261 -1 O ALA E 257 N PHE E 118 SHEET 3 AA1 5 GLU E 175 HIS E 184 -1 N LEU E 177 O PHE E 258 SHEET 4 AA1 5 LEU E 251 PRO E 254 -1 O ILE E 252 N GLY E 181 SHEET 5 AA1 5 LEU E 151 TRP E 153 -1 N LEU E 152 O ALA E 253 SHEET 1 AA2 4 SER E 114 GLU E 119 0 SHEET 2 AA2 4 TYR E 256 SER E 261 -1 O ALA E 257 N PHE E 118 SHEET 3 AA2 4 GLU E 175 HIS E 184 -1 N LEU E 177 O PHE E 258 SHEET 4 AA2 4 ARG E 229 LEU E 237 -1 O ARG E 229 N HIS E 184 SHEET 1 AA3 2 THR E 136 HIS E 141 0 SHEET 2 AA3 2 LYS E 144 SER E 146 -1 O LYS E 144 N HIS E 141 SHEET 1 AA4 4 LEU E 164 VAL E 169 0 SHEET 2 AA4 4 THR E 242 ALA E 247 -1 O PHE E 245 N LYS E 166 SHEET 3 AA4 4 VAL E 202 VAL E 205 -1 N SER E 203 O GLU E 246 SHEET 4 AA4 4 SER E 210 PHE E 213 -1 O PHE E 213 N VAL E 202 SHEET 1 AA5 2 GLN H 3 GLN H 6 0 SHEET 2 AA5 2 CYS H 22 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 1 AA6 6 GLU H 10 LYS H 12 0 SHEET 2 AA6 6 THR H 120 VAL H 124 1 O THR H 123 N LYS H 12 SHEET 3 AA6 6 ALA H 92 ARG H 98 -1 N ALA H 92 O VAL H 122 SHEET 4 AA6 6 MET H 34 GLN H 39 -1 N HIS H 35 O ALA H 97 SHEET 5 AA6 6 LEU H 45 ILE H 51 -1 O MET H 48 N TRP H 36 SHEET 6 AA6 6 THR H 58 TYR H 60 -1 O ASN H 59 N TRP H 50 SHEET 1 AA7 3 VAL H 18 VAL H 20 0 SHEET 2 AA7 3 THR H 78 LEU H 83 -1 O MET H 81 N VAL H 20 SHEET 3 AA7 3 VAL H 68 ASP H 73 -1 N ASP H 73 O THR H 78 SHEET 1 AA8 4 SER H 133 LEU H 137 0 SHEET 2 AA8 4 THR H 148 TYR H 158 -1 O LEU H 154 N PHE H 135 SHEET 3 AA8 4 TYR H 189 PRO H 198 -1 O TYR H 189 N TYR H 158 SHEET 4 AA8 4 VAL H 176 THR H 178 -1 N HIS H 177 O VAL H 194 SHEET 1 AA9 4 THR H 144 SER H 145 0 SHEET 2 AA9 4 THR H 148 TYR H 158 -1 O THR H 148 N SER H 145 SHEET 3 AA9 4 TYR H 189 PRO H 198 -1 O TYR H 189 N TYR H 158 SHEET 4 AA9 4 VAL H 182 LEU H 183 -1 N VAL H 182 O SER H 190 SHEET 1 AB1 3 THR H 164 TRP H 167 0 SHEET 2 AB1 3 ILE H 208 HIS H 213 -1 O ASN H 210 N SER H 166 SHEET 3 AB1 3 THR H 218 ARG H 223 -1 O VAL H 220 N VAL H 211 SHEET 1 AB2 5 SER L 9 VAL L 12 0 SHEET 2 AB2 5 THR L 103 VAL L 107 1 O LYS L 104 N VAL L 10 SHEET 3 AB2 5 ALA L 83 TRP L 90 -1 N ALA L 83 O LEU L 105 SHEET 4 AB2 5 HIS L 33 GLN L 37 -1 N GLN L 37 O ASP L 84 SHEET 5 AB2 5 VAL L 44 VAL L 47 -1 O VAL L 44 N GLN L 36 SHEET 1 AB3 4 SER L 9 VAL L 12 0 SHEET 2 AB3 4 THR L 103 VAL L 107 1 O LYS L 104 N VAL L 10 SHEET 3 AB3 4 ALA L 83 TRP L 90 -1 N ALA L 83 O LEU L 105 SHEET 4 AB3 4 VAL L 97 PHE L 99 -1 O VAL L 98 N VAL L 89 SHEET 1 AB4 3 ALA L 18 GLY L 23 0 SHEET 2 AB4 3 THR L 69 ILE L 74 -1 O ILE L 74 N ALA L 18 SHEET 3 AB4 3 PHE L 61 SER L 66 -1 N SER L 62 O THR L 73 SHEET 1 AB5 4 SER L 116 PHE L 120 0 SHEET 2 AB5 4 ALA L 132 PHE L 141 -1 O LEU L 137 N THR L 118 SHEET 3 AB5 4 TYR L 174 LEU L 182 -1 O SER L 178 N CYS L 136 SHEET 4 AB5 4 VAL L 161 THR L 163 -1 N GLU L 162 O TYR L 179 SHEET 1 AB6 4 SER L 116 PHE L 120 0 SHEET 2 AB6 4 ALA L 132 PHE L 141 -1 O LEU L 137 N THR L 118 SHEET 3 AB6 4 TYR L 174 LEU L 182 -1 O SER L 178 N CYS L 136 SHEET 4 AB6 4 SER L 167 LYS L 168 -1 N SER L 167 O ALA L 175 SHEET 1 AB7 4 PRO L 156 VAL L 157 0 SHEET 2 AB7 4 THR L 147 ALA L 152 -1 N TRP L 150 O VAL L 157 SHEET 3 AB7 4 TYR L 193 HIS L 199 -1 O THR L 198 N THR L 147 SHEET 4 AB7 4 SER L 202 VAL L 208 -1 O VAL L 208 N TYR L 193 SSBOND 1 CYS E 59 CYS E 71 1555 1555 2.03 SSBOND 2 CYS E 94 CYS E 139 1555 1555 2.04 SSBOND 3 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 4 CYS H 153 CYS H 209 1555 1555 2.03 SSBOND 5 CYS L 22 CYS L 87 1555 1555 2.04 SSBOND 6 CYS L 136 CYS L 195 1555 1555 2.04 LINK ND2 ASN E 129 C1 NAG E 301 1555 1555 1.44 CISPEP 1 PHE H 159 PRO H 160 0 -8.09 CISPEP 2 GLU H 161 PRO H 162 0 -3.57 CISPEP 3 TYR L 142 PRO L 143 0 -1.67 CRYST1 202.543 71.863 65.402 90.00 104.87 90.00 C 1 2 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.004937 0.000000 0.001311 0.00000 SCALE2 0.000000 0.013915 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015820 0.00000