HEADER IMMUNE SYSTEM 09-DEC-24 9MFG TITLE COMPLEX OF IL23 RECEPTOR AND VHH COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTERLEUKIN-23 RECEPTOR; COMPND 3 CHAIN: A, B, C, D; COMPND 4 SYNONYM: IL-23 RECEPTOR,IL-23R; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: VHH; COMPND 8 CHAIN: E, F, G, H; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: IL23R; SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 12 ORGANISM_TAXID: 9844; SOURCE 13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS IMMUNOLOGY, IBD, INFLAMMATORY BOWEL DISEASE, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.R.KIEFER,H.A.WALLWEBER,J.T.KOERBER,N.OTA,C.DAVIES REVDAT 1 21-MAY-25 9MFG 0 JRNL AUTH N.OTA,C.DAVIES,H.A.WALLWEBER,J.R.KIEFER,J.T.KOERBER JRNL TITL ORAL SINGLE DOMAIN ANTIBODY INHIBITION OF IL-23 SIGNALING JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.85 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2_5419 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.97 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 87.2 REMARK 3 NUMBER OF REFLECTIONS : 74222 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.206 REMARK 3 R VALUE (WORKING SET) : 0.204 REMARK 3 FREE R VALUE : 0.246 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.840 REMARK 3 FREE R VALUE TEST SET COUNT : 3590 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 34.9700 - 8.4000 0.97 3259 179 0.2264 0.2308 REMARK 3 2 8.4000 - 6.6800 0.94 3077 133 0.2179 0.2220 REMARK 3 3 6.6800 - 5.8400 0.98 3089 174 0.1919 0.2387 REMARK 3 4 5.8400 - 5.3100 0.99 3121 172 0.1673 0.1885 REMARK 3 5 5.3100 - 4.9300 0.99 3138 148 0.1516 0.1843 REMARK 3 6 4.9300 - 4.6400 0.99 3079 158 0.1419 0.1882 REMARK 3 7 4.6400 - 4.4100 0.99 3115 142 0.1446 0.1751 REMARK 3 8 4.4100 - 4.2200 0.98 3025 150 0.1483 0.1949 REMARK 3 9 4.2200 - 4.0600 0.94 2920 171 0.1552 0.2080 REMARK 3 10 4.0600 - 3.9200 0.96 3021 148 0.1811 0.2522 REMARK 3 11 3.9200 - 3.7900 0.97 3014 158 0.2022 0.2635 REMARK 3 12 3.7900 - 3.6900 0.97 3026 142 0.2120 0.2742 REMARK 3 13 3.6900 - 3.5900 0.97 3044 142 0.2184 0.2751 REMARK 3 14 3.5900 - 3.5000 0.97 2971 153 0.2290 0.3115 REMARK 3 15 3.5000 - 3.4200 0.96 2980 156 0.2294 0.2877 REMARK 3 16 3.4200 - 3.3500 0.94 2883 140 0.2593 0.2930 REMARK 3 17 3.3500 - 3.2800 0.91 2770 166 0.2557 0.3201 REMARK 3 18 3.2800 - 3.2200 0.87 2663 147 0.2739 0.3529 REMARK 3 19 3.2200 - 3.1600 0.83 2576 121 0.2923 0.3248 REMARK 3 20 3.1600 - 3.1100 0.79 2414 116 0.2933 0.3370 REMARK 3 21 3.1100 - 3.0600 0.76 2337 123 0.3053 0.3676 REMARK 3 22 3.0600 - 3.0100 0.70 2102 128 0.2920 0.3443 REMARK 3 23 3.0100 - 2.9700 0.66 2103 79 0.3052 0.3344 REMARK 3 24 2.9700 - 2.9300 0.62 1862 102 0.3112 0.3474 REMARK 3 25 2.9300 - 2.8900 0.54 1678 73 0.3212 0.3800 REMARK 3 26 2.8900 - 2.8500 0.44 1365 69 0.3515 0.3913 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) : 0.350 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.240 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.005 13748 REMARK 3 ANGLE : 0.751 18758 REMARK 3 CHIRALITY : 0.048 2204 REMARK 3 PLANARITY : 0.005 2319 REMARK 3 DIHEDRAL : 18.287 5304 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 41 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 25 THROUGH 122 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.8028 39.2598 9.5360 REMARK 3 T TENSOR REMARK 3 T11: 0.5778 T22: 0.4604 REMARK 3 T33: 0.4778 T12: 0.0128 REMARK 3 T13: 0.0431 T23: 0.0696 REMARK 3 L TENSOR REMARK 3 L11: 3.7330 L22: 2.3454 REMARK 3 L33: 1.5670 L12: 0.5318 REMARK 3 L13: 0.9303 L23: 0.7065 REMARK 3 S TENSOR REMARK 3 S11: -0.1149 S12: -0.1016 S13: 0.2035 REMARK 3 S21: 0.1459 S22: 0.0816 S23: 0.0893 REMARK 3 S31: -0.0316 S32: 0.1532 S33: 0.0000 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 123 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.0550 9.6437 5.0266 REMARK 3 T TENSOR REMARK 3 T11: 0.4944 T22: 0.5496 REMARK 3 T33: 0.6738 T12: 0.0014 REMARK 3 T13: -0.0316 T23: 0.1306 REMARK 3 L TENSOR REMARK 3 L11: 0.8438 L22: 4.4079 REMARK 3 L33: 1.0193 L12: 0.0644 REMARK 3 L13: -0.0027 L23: 0.8095 REMARK 3 S TENSOR REMARK 3 S11: -0.1252 S12: -0.1751 S13: -0.1948 REMARK 3 S21: -0.0561 S22: 0.0928 S23: 0.3735 REMARK 3 S31: 0.1725 S32: -0.2745 S33: -0.0002 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 217 THROUGH 317 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.4674 -7.3560 -20.9157 REMARK 3 T TENSOR REMARK 3 T11: 1.2126 T22: 0.7789 REMARK 3 T33: 0.8230 T12: -0.0380 REMARK 3 T13: -0.1486 T23: 0.0636 REMARK 3 L TENSOR REMARK 3 L11: 0.5839 L22: 0.2408 REMARK 3 L33: 2.3298 L12: -0.2894 REMARK 3 L13: -0.6532 L23: -0.8558 REMARK 3 S TENSOR REMARK 3 S11: 0.1087 S12: 0.5010 S13: -0.0989 REMARK 3 S21: -0.8507 S22: -0.0355 S23: 0.2537 REMARK 3 S31: 1.0522 S32: 0.0866 S33: -0.0001 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 25 THROUGH 110 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.2795 60.2505 3.7864 REMARK 3 T TENSOR REMARK 3 T11: 0.5288 T22: 0.4759 REMARK 3 T33: 0.5869 T12: -0.0092 REMARK 3 T13: -0.0869 T23: -0.0118 REMARK 3 L TENSOR REMARK 3 L11: 3.8114 L22: 2.1735 REMARK 3 L33: 2.2794 L12: 0.3819 REMARK 3 L13: -0.4536 L23: -0.4732 REMARK 3 S TENSOR REMARK 3 S11: -0.0562 S12: -0.1120 S13: -0.1782 REMARK 3 S21: 0.1841 S22: 0.1383 S23: 0.0848 REMARK 3 S31: -0.0573 S32: -0.0952 S33: -0.0001 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 111 THROUGH 156 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.3097 77.7068 -12.1268 REMARK 3 T TENSOR REMARK 3 T11: 0.5924 T22: 0.6460 REMARK 3 T33: 0.4827 T12: 0.0204 REMARK 3 T13: -0.0101 T23: -0.0264 REMARK 3 L TENSOR REMARK 3 L11: 1.3086 L22: 0.0809 REMARK 3 L33: 0.4522 L12: 0.1825 REMARK 3 L13: -0.1208 L23: -0.0386 REMARK 3 S TENSOR REMARK 3 S11: 0.0367 S12: 0.0749 S13: -0.0088 REMARK 3 S21: -0.0113 S22: -0.0791 S23: 0.2220 REMARK 3 S31: -0.1866 S32: 0.3884 S33: 0.0000 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 157 THROUGH 200 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.5898 90.1027 -9.0634 REMARK 3 T TENSOR REMARK 3 T11: 0.7078 T22: 0.7200 REMARK 3 T33: 0.3909 T12: -0.1038 REMARK 3 T13: -0.0539 T23: 0.0811 REMARK 3 L TENSOR REMARK 3 L11: 0.8324 L22: 1.5502 REMARK 3 L33: 1.7260 L12: -0.9091 REMARK 3 L13: -0.7752 L23: 0.0862 REMARK 3 S TENSOR REMARK 3 S11: 0.0872 S12: -0.0495 S13: 0.8972 REMARK 3 S21: -0.1407 S22: -0.0799 S23: 0.3596 REMARK 3 S31: -0.5849 S32: 0.4432 S33: 0.0001 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 201 THROUGH 298 ) REMARK 3 ORIGIN FOR THE GROUP (A): 31.5461 88.9426 -40.1172 REMARK 3 T TENSOR REMARK 3 T11: 0.9255 T22: 1.1973 REMARK 3 T33: 0.5495 T12: 0.0977 REMARK 3 T13: 0.0726 T23: 0.0101 REMARK 3 L TENSOR REMARK 3 L11: 1.0719 L22: 1.0667 REMARK 3 L33: 1.6932 L12: 0.7116 REMARK 3 L13: -0.3547 L23: -0.8701 REMARK 3 S TENSOR REMARK 3 S11: -0.0059 S12: 0.6332 S13: -0.0990 REMARK 3 S21: -0.5771 S22: -0.0340 S23: -0.2360 REMARK 3 S31: 0.0287 S32: 0.7855 S33: 0.0000 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 299 THROUGH 322 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.8985 86.2971 -44.7141 REMARK 3 T TENSOR REMARK 3 T11: 1.0095 T22: 1.0825 REMARK 3 T33: 0.7636 T12: 0.0809 REMARK 3 T13: 0.0722 T23: 0.1555 REMARK 3 L TENSOR REMARK 3 L11: 0.1244 L22: -0.0491 REMARK 3 L33: 0.5250 L12: 0.3021 REMARK 3 L13: -0.0067 L23: -0.3163 REMARK 3 S TENSOR REMARK 3 S11: -0.0893 S12: 0.5980 S13: 0.1584 REMARK 3 S21: -0.3259 S22: 0.1192 S23: -0.1627 REMARK 3 S31: 0.4342 S32: 1.3570 S33: 0.0018 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 25 THROUGH 110 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.8099 36.4725 8.7183 REMARK 3 T TENSOR REMARK 3 T11: 0.6013 T22: 0.4567 REMARK 3 T33: 0.6427 T12: 0.0353 REMARK 3 T13: -0.1045 T23: -0.0974 REMARK 3 L TENSOR REMARK 3 L11: 4.0844 L22: 1.0479 REMARK 3 L33: 1.4986 L12: 0.7251 REMARK 3 L13: 0.7540 L23: -0.8250 REMARK 3 S TENSOR REMARK 3 S11: -0.0775 S12: 0.0338 S13: 0.2594 REMARK 3 S21: -0.0094 S22: 0.0003 S23: 0.1072 REMARK 3 S31: 0.1396 S32: -0.1182 S33: -0.0000 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 111 THROUGH 222 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.6141 15.9330 22.1548 REMARK 3 T TENSOR REMARK 3 T11: 0.6143 T22: 0.7231 REMARK 3 T33: 0.4317 T12: 0.1091 REMARK 3 T13: 0.0262 T23: 0.0504 REMARK 3 L TENSOR REMARK 3 L11: 1.9245 L22: 0.4473 REMARK 3 L33: 1.8824 L12: 0.1931 REMARK 3 L13: 0.8603 L23: 0.1136 REMARK 3 S TENSOR REMARK 3 S11: -0.1181 S12: -0.2053 S13: -0.0275 REMARK 3 S21: 0.0113 S22: 0.0604 S23: -0.0496 REMARK 3 S31: 0.4172 S32: 0.5979 S33: 0.0000 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 223 THROUGH 319 ) REMARK 3 ORIGIN FOR THE GROUP (A): 37.3355 12.2327 55.8229 REMARK 3 T TENSOR REMARK 3 T11: 1.1103 T22: 1.4338 REMARK 3 T33: 0.6228 T12: 0.1966 REMARK 3 T13: -0.0667 T23: 0.0381 REMARK 3 L TENSOR REMARK 3 L11: -0.3091 L22: -0.7319 REMARK 3 L33: 0.5716 L12: 0.1590 REMARK 3 L13: -0.1397 L23: 0.1363 REMARK 3 S TENSOR REMARK 3 S11: -0.1169 S12: -0.3999 S13: 0.3242 REMARK 3 S21: 0.5887 S22: 0.0957 S23: -0.2203 REMARK 3 S31: 0.0887 S32: 0.7943 S33: 0.0003 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 25 THROUGH 110 ) REMARK 3 ORIGIN FOR THE GROUP (A): 45.2877 62.8671 1.9117 REMARK 3 T TENSOR REMARK 3 T11: 0.5481 T22: 0.4420 REMARK 3 T33: 0.3752 T12: 0.0120 REMARK 3 T13: -0.0322 T23: 0.0617 REMARK 3 L TENSOR REMARK 3 L11: 3.3626 L22: 3.1303 REMARK 3 L33: 1.6565 L12: -0.3194 REMARK 3 L13: -0.7441 L23: 0.3181 REMARK 3 S TENSOR REMARK 3 S11: -0.2641 S12: -0.3034 S13: -0.2975 REMARK 3 S21: -0.1355 S22: 0.1735 S23: -0.0097 REMARK 3 S31: 0.1223 S32: 0.1118 S33: 0.0001 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 111 THROUGH 230 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.2838 88.3402 6.9898 REMARK 3 T TENSOR REMARK 3 T11: 0.4838 T22: 0.5700 REMARK 3 T33: 0.4947 T12: -0.0022 REMARK 3 T13: -0.0363 T23: 0.0893 REMARK 3 L TENSOR REMARK 3 L11: 1.2143 L22: 2.3135 REMARK 3 L33: 0.9079 L12: -1.5836 REMARK 3 L13: -1.1376 L23: 0.8174 REMARK 3 S TENSOR REMARK 3 S11: 0.0358 S12: 0.1918 S13: -0.1603 REMARK 3 S21: 0.0383 S22: -0.0797 S23: 0.3686 REMARK 3 S31: -0.0513 S32: -0.2607 S33: 0.0001 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 231 THROUGH 317 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.7778 106.9609 32.4142 REMARK 3 T TENSOR REMARK 3 T11: 0.8492 T22: 0.8271 REMARK 3 T33: 0.5767 T12: 0.0740 REMARK 3 T13: 0.0933 T23: 0.0688 REMARK 3 L TENSOR REMARK 3 L11: 1.5616 L22: 0.3318 REMARK 3 L33: 1.4521 L12: -0.4944 REMARK 3 L13: 1.7562 L23: -0.2689 REMARK 3 S TENSOR REMARK 3 S11: -0.1788 S12: -0.6335 S13: 0.2581 REMARK 3 S21: 0.5898 S22: -0.0102 S23: 0.1096 REMARK 3 S31: -0.4721 S32: -0.1067 S33: -0.0002 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): 62.6921 83.0980 1.2486 REMARK 3 T TENSOR REMARK 3 T11: 0.5411 T22: 0.4159 REMARK 3 T33: 0.6758 T12: -0.0702 REMARK 3 T13: 0.0153 T23: -0.1258 REMARK 3 L TENSOR REMARK 3 L11: 2.1691 L22: 2.0003 REMARK 3 L33: 1.6752 L12: 0.7149 REMARK 3 L13: 1.4974 L23: -0.4925 REMARK 3 S TENSOR REMARK 3 S11: -0.1011 S12: -0.2180 S13: 1.3790 REMARK 3 S21: 0.0527 S22: -0.0687 S23: -0.0060 REMARK 3 S31: -0.3556 S32: 0.0196 S33: -0.0009 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 40 THROUGH 52 ) REMARK 3 ORIGIN FOR THE GROUP (A): 55.6720 78.6019 -6.0876 REMARK 3 T TENSOR REMARK 3 T11: 0.5657 T22: 0.5031 REMARK 3 T33: 0.4346 T12: 0.0338 REMARK 3 T13: -0.0015 T23: 0.0113 REMARK 3 L TENSOR REMARK 3 L11: 1.3335 L22: 0.5236 REMARK 3 L33: 0.3769 L12: 0.4839 REMARK 3 L13: -0.1900 L23: 0.3268 REMARK 3 S TENSOR REMARK 3 S11: 0.0135 S12: 0.1537 S13: 0.6495 REMARK 3 S21: -0.2550 S22: -0.0132 S23: 0.0173 REMARK 3 S31: -0.1977 S32: -0.8025 S33: -0.0001 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 53 THROUGH 82 ) REMARK 3 ORIGIN FOR THE GROUP (A): 62.9279 74.3469 3.1677 REMARK 3 T TENSOR REMARK 3 T11: 0.5728 T22: 0.4847 REMARK 3 T33: 0.4515 T12: 0.0001 REMARK 3 T13: -0.0645 T23: -0.0704 REMARK 3 L TENSOR REMARK 3 L11: 1.0888 L22: 0.6817 REMARK 3 L33: 0.3733 L12: 0.7153 REMARK 3 L13: -0.2086 L23: -0.4530 REMARK 3 S TENSOR REMARK 3 S11: 0.3356 S12: -0.4469 S13: -0.1451 REMARK 3 S21: 0.2928 S22: -0.1892 S23: -0.3450 REMARK 3 S31: -0.2742 S32: 0.3580 S33: -0.0000 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 83 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): 68.4454 74.4536 -12.2239 REMARK 3 T TENSOR REMARK 3 T11: 0.5903 T22: 0.4983 REMARK 3 T33: 0.4100 T12: -0.0024 REMARK 3 T13: 0.0174 T23: 0.1103 REMARK 3 L TENSOR REMARK 3 L11: 3.2405 L22: 0.5171 REMARK 3 L33: 1.3654 L12: -0.6532 REMARK 3 L13: 2.0549 L23: -0.4982 REMARK 3 S TENSOR REMARK 3 S11: 0.8188 S12: 0.3693 S13: -1.4866 REMARK 3 S21: -0.8543 S22: -0.1002 S23: 0.3936 REMARK 3 S31: 1.0195 S32: -0.3039 S33: 0.0770 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 91 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 56.0165 82.7973 -2.2942 REMARK 3 T TENSOR REMARK 3 T11: 0.5561 T22: 0.3761 REMARK 3 T33: 0.6252 T12: 0.0636 REMARK 3 T13: -0.0180 T23: -0.0321 REMARK 3 L TENSOR REMARK 3 L11: 1.2641 L22: 2.9095 REMARK 3 L33: 1.8683 L12: 0.2556 REMARK 3 L13: 1.1860 L23: -0.7102 REMARK 3 S TENSOR REMARK 3 S11: 0.0413 S12: -0.2160 S13: 0.2853 REMARK 3 S21: 0.5009 S22: -0.1628 S23: -0.0203 REMARK 3 S31: -0.8987 S32: -0.1153 S33: -0.0000 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.4001 18.5286 18.4904 REMARK 3 T TENSOR REMARK 3 T11: 0.6088 T22: 0.6229 REMARK 3 T33: 0.7957 T12: 0.0434 REMARK 3 T13: -0.0780 T23: 0.1002 REMARK 3 L TENSOR REMARK 3 L11: 0.8397 L22: 1.2923 REMARK 3 L33: 0.5081 L12: 0.6050 REMARK 3 L13: -0.0585 L23: -0.8924 REMARK 3 S TENSOR REMARK 3 S11: 0.1780 S12: -0.7605 S13: -1.0614 REMARK 3 S21: 0.3904 S22: 0.1699 S23: 0.2846 REMARK 3 S31: 0.2058 S32: -0.0795 S33: 0.0000 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 40 THROUGH 52 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.4453 19.1214 9.6892 REMARK 3 T TENSOR REMARK 3 T11: 0.5440 T22: 0.5347 REMARK 3 T33: 0.7390 T12: 0.0443 REMARK 3 T13: -0.0616 T23: 0.0073 REMARK 3 L TENSOR REMARK 3 L11: 0.4070 L22: 0.3804 REMARK 3 L33: 0.2165 L12: 0.4722 REMARK 3 L13: -0.3251 L23: -0.2259 REMARK 3 S TENSOR REMARK 3 S11: 0.0616 S12: 0.0936 S13: -0.5267 REMARK 3 S21: 0.8413 S22: -0.1434 S23: -1.0318 REMARK 3 S31: 0.7858 S32: 0.1638 S33: -0.0001 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 53 THROUGH 82 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.7041 27.1017 16.0091 REMARK 3 T TENSOR REMARK 3 T11: 0.6128 T22: 0.5149 REMARK 3 T33: 0.5109 T12: 0.0345 REMARK 3 T13: -0.1269 T23: -0.0401 REMARK 3 L TENSOR REMARK 3 L11: 1.5424 L22: 1.2197 REMARK 3 L33: 0.3309 L12: 0.7340 REMARK 3 L13: -0.5296 L23: 0.0852 REMARK 3 S TENSOR REMARK 3 S11: 0.1564 S12: -0.2204 S13: 0.1461 REMARK 3 S21: 0.3755 S22: -0.1728 S23: 0.5007 REMARK 3 S31: -0.1226 S32: 0.0233 S33: -0.0001 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 83 THROUGH 98 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.3899 18.0689 8.6476 REMARK 3 T TENSOR REMARK 3 T11: 0.5377 T22: 0.5246 REMARK 3 T33: 0.7892 T12: 0.0095 REMARK 3 T13: -0.0892 T23: 0.0544 REMARK 3 L TENSOR REMARK 3 L11: 1.0920 L22: 0.1454 REMARK 3 L33: 0.4006 L12: 0.1450 REMARK 3 L13: -0.3253 L23: 0.3064 REMARK 3 S TENSOR REMARK 3 S11: 0.0484 S12: 0.2710 S13: -0.6845 REMARK 3 S21: 0.3890 S22: -0.3233 S23: 0.4655 REMARK 3 S31: 0.1939 S32: 0.0435 S33: 0.0000 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 99 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.7596 19.5790 18.8607 REMARK 3 T TENSOR REMARK 3 T11: 0.6139 T22: 0.5695 REMARK 3 T33: 0.7408 T12: 0.0335 REMARK 3 T13: -0.3103 T23: 0.0811 REMARK 3 L TENSOR REMARK 3 L11: 0.3636 L22: 0.5912 REMARK 3 L33: 0.2405 L12: 0.2452 REMARK 3 L13: -0.3027 L23: 0.0133 REMARK 3 S TENSOR REMARK 3 S11: 0.5656 S12: -0.5392 S13: -0.6718 REMARK 3 S21: 0.7573 S22: -0.4831 S23: -0.8064 REMARK 3 S31: 0.4272 S32: 0.4533 S33: 0.0020 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 114 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.3465 11.9368 6.5489 REMARK 3 T TENSOR REMARK 3 T11: 0.6467 T22: 0.6124 REMARK 3 T33: 0.6808 T12: -0.0963 REMARK 3 T13: -0.1655 T23: -0.0350 REMARK 3 L TENSOR REMARK 3 L11: 0.6624 L22: 0.0205 REMARK 3 L33: 0.3772 L12: 0.1000 REMARK 3 L13: -0.4897 L23: -0.0765 REMARK 3 S TENSOR REMARK 3 S11: -1.2346 S12: -0.1446 S13: -0.8325 REMARK 3 S21: -0.2457 S22: -0.7203 S23: 0.9054 REMARK 3 S31: -0.0336 S32: -0.3240 S33: -0.5445 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 72.0798 21.1146 15.3046 REMARK 3 T TENSOR REMARK 3 T11: 0.6678 T22: 0.4918 REMARK 3 T33: 1.3916 T12: -0.0549 REMARK 3 T13: -0.1163 T23: 0.0963 REMARK 3 L TENSOR REMARK 3 L11: 1.5277 L22: 0.1603 REMARK 3 L33: 2.1225 L12: 0.2645 REMARK 3 L13: -1.7289 L23: -0.3953 REMARK 3 S TENSOR REMARK 3 S11: 0.1017 S12: -0.5731 S13: -1.2126 REMARK 3 S21: 0.5479 S22: -0.9217 S23: -0.0299 REMARK 3 S31: 0.8211 S32: 0.7807 S33: -0.6777 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 18 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): 63.5328 22.6143 7.7530 REMARK 3 T TENSOR REMARK 3 T11: 0.5119 T22: 0.6245 REMARK 3 T33: 0.8377 T12: 0.0622 REMARK 3 T13: -0.0388 T23: -0.0289 REMARK 3 L TENSOR REMARK 3 L11: 1.2034 L22: 1.2772 REMARK 3 L33: 0.5893 L12: 0.1137 REMARK 3 L13: 0.4610 L23: -0.0293 REMARK 3 S TENSOR REMARK 3 S11: 0.2655 S12: 0.5725 S13: -1.6313 REMARK 3 S21: -0.1430 S22: 0.1920 S23: 0.4207 REMARK 3 S31: 0.0365 S32: -0.1405 S33: 0.0089 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 40 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): 59.3223 25.0059 19.5230 REMARK 3 T TENSOR REMARK 3 T11: 0.6840 T22: 0.7536 REMARK 3 T33: 0.6687 T12: 0.0193 REMARK 3 T13: -0.1158 T23: 0.2228 REMARK 3 L TENSOR REMARK 3 L11: 0.3573 L22: 0.3497 REMARK 3 L33: 0.1026 L12: 0.1609 REMARK 3 L13: 0.1418 L23: 0.1963 REMARK 3 S TENSOR REMARK 3 S11: -0.0011 S12: -1.1319 S13: -1.0525 REMARK 3 S21: 0.3862 S22: 0.1592 S23: 0.0933 REMARK 3 S31: 0.3826 S32: -0.4290 S33: -0.0004 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 52 THROUGH 72 ) REMARK 3 ORIGIN FOR THE GROUP (A): 63.4032 33.0159 9.9491 REMARK 3 T TENSOR REMARK 3 T11: 0.4951 T22: 0.4792 REMARK 3 T33: 0.7261 T12: -0.0450 REMARK 3 T13: -0.0242 T23: 0.0606 REMARK 3 L TENSOR REMARK 3 L11: 1.3526 L22: 0.8218 REMARK 3 L33: 0.4761 L12: -0.2930 REMARK 3 L13: -0.2326 L23: -0.5373 REMARK 3 S TENSOR REMARK 3 S11: -0.0530 S12: -0.2314 S13: -0.4063 REMARK 3 S21: 0.1897 S22: 0.2483 S23: -0.4076 REMARK 3 S31: -0.0618 S32: 0.2539 S33: -0.0003 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 73 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): 70.1421 28.3324 13.8745 REMARK 3 T TENSOR REMARK 3 T11: 0.5718 T22: 0.7304 REMARK 3 T33: 0.7543 T12: -0.0273 REMARK 3 T13: -0.0243 T23: -0.0668 REMARK 3 L TENSOR REMARK 3 L11: 1.3466 L22: 1.2789 REMARK 3 L33: 0.2265 L12: -0.7633 REMARK 3 L13: -0.0321 L23: -0.2819 REMARK 3 S TENSOR REMARK 3 S11: 0.0644 S12: -0.5774 S13: -0.2613 REMARK 3 S21: 0.1759 S22: -0.0754 S23: -0.4039 REMARK 3 S31: 0.3745 S32: -0.1533 S33: 0.0022 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 91 THROUGH 98 ) REMARK 3 ORIGIN FOR THE GROUP (A): 62.4422 21.4392 14.7284 REMARK 3 T TENSOR REMARK 3 T11: 0.5826 T22: 0.5134 REMARK 3 T33: 0.6731 T12: -0.0259 REMARK 3 T13: -0.0167 T23: 0.1291 REMARK 3 L TENSOR REMARK 3 L11: 0.1330 L22: 0.1232 REMARK 3 L33: 0.0723 L12: -0.0919 REMARK 3 L13: -0.0026 L23: 0.0883 REMARK 3 S TENSOR REMARK 3 S11: -0.0725 S12: -0.5529 S13: -1.1403 REMARK 3 S21: -0.1496 S22: -0.2653 S23: -0.3955 REMARK 3 S31: 0.6477 S32: -0.0503 S33: -0.0022 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 99 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): 53.0570 21.0034 9.1266 REMARK 3 T TENSOR REMARK 3 T11: 0.6091 T22: 0.6066 REMARK 3 T33: 0.9466 T12: -0.0910 REMARK 3 T13: -0.1343 T23: 0.0130 REMARK 3 L TENSOR REMARK 3 L11: 0.2097 L22: 0.1602 REMARK 3 L33: 0.3483 L12: 0.0725 REMARK 3 L13: -0.2973 L23: -0.0666 REMARK 3 S TENSOR REMARK 3 S11: -0.3229 S12: 0.0406 S13: -0.9710 REMARK 3 S21: 0.1796 S22: 0.2137 S23: 1.0136 REMARK 3 S31: 0.0577 S32: -0.2277 S33: -0.0001 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 114 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 73.9220 22.9335 24.7723 REMARK 3 T TENSOR REMARK 3 T11: 0.6586 T22: 0.8970 REMARK 3 T33: 0.9157 T12: 0.2071 REMARK 3 T13: -0.1017 T23: 0.3592 REMARK 3 L TENSOR REMARK 3 L11: 0.0636 L22: 0.3947 REMARK 3 L33: 0.2197 L12: 0.1151 REMARK 3 L13: -0.0207 L23: 0.1551 REMARK 3 S TENSOR REMARK 3 S11: -0.9880 S12: -1.0353 S13: -0.1270 REMARK 3 S21: -0.3059 S22: 0.9785 S23: -0.4461 REMARK 3 S31: 0.0046 S32: 0.5180 S33: 0.0033 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 16 ) REMARK 3 ORIGIN FOR THE GROUP (A): -25.5373 79.5809 -1.2957 REMARK 3 T TENSOR REMARK 3 T11: 0.6278 T22: 0.5898 REMARK 3 T33: 1.2277 T12: -0.1054 REMARK 3 T13: -0.0821 T23: 0.1854 REMARK 3 L TENSOR REMARK 3 L11: 0.6841 L22: 0.8797 REMARK 3 L33: 0.3069 L12: -0.0801 REMARK 3 L13: 0.4717 L23: -0.1553 REMARK 3 S TENSOR REMARK 3 S11: -0.3086 S12: -0.3677 S13: 1.8692 REMARK 3 S21: 0.1709 S22: -0.3684 S23: -0.0826 REMARK 3 S31: -0.3713 S32: 1.1079 S33: -0.1534 REMARK 3 TLS GROUP : 35 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 17 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.1316 75.4678 -2.2137 REMARK 3 T TENSOR REMARK 3 T11: 0.5018 T22: 0.6186 REMARK 3 T33: 0.8751 T12: -0.0436 REMARK 3 T13: -0.0968 T23: 0.0274 REMARK 3 L TENSOR REMARK 3 L11: 1.8609 L22: 2.5655 REMARK 3 L33: 1.6592 L12: -0.6396 REMARK 3 L13: 0.3727 L23: -0.7858 REMARK 3 S TENSOR REMARK 3 S11: -0.1693 S12: 0.2445 S13: 1.0293 REMARK 3 S21: 0.0305 S22: -0.0963 S23: -0.4300 REMARK 3 S31: 0.1504 S32: 0.1993 S33: -0.0001 REMARK 3 TLS GROUP : 36 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 52 THROUGH 66 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.3599 65.6692 2.2612 REMARK 3 T TENSOR REMARK 3 T11: 0.5710 T22: 0.5726 REMARK 3 T33: 0.6148 T12: -0.0427 REMARK 3 T13: -0.1349 T23: 0.0540 REMARK 3 L TENSOR REMARK 3 L11: 0.3109 L22: 0.6438 REMARK 3 L33: 0.0242 L12: -0.0398 REMARK 3 L13: -0.1110 L23: -0.0997 REMARK 3 S TENSOR REMARK 3 S11: 0.2422 S12: 0.1446 S13: 0.0852 REMARK 3 S21: -0.0119 S22: -0.3670 S23: 0.3425 REMARK 3 S31: 0.1486 S32: -0.3852 S33: 0.0001 REMARK 3 TLS GROUP : 37 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 67 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.6691 68.9638 -4.4240 REMARK 3 T TENSOR REMARK 3 T11: 0.6077 T22: 0.6132 REMARK 3 T33: 0.8158 T12: 0.0044 REMARK 3 T13: -0.0949 T23: 0.0976 REMARK 3 L TENSOR REMARK 3 L11: 0.8542 L22: 0.5695 REMARK 3 L33: 0.1128 L12: 0.3101 REMARK 3 L13: -0.2877 L23: -0.0391 REMARK 3 S TENSOR REMARK 3 S11: -0.0057 S12: 0.2954 S13: 0.3180 REMARK 3 S21: -0.2296 S22: 0.0592 S23: 0.4203 REMARK 3 S31: 0.6708 S32: -0.4051 S33: 0.0001 REMARK 3 TLS GROUP : 38 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 84 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.4524 76.0906 12.7593 REMARK 3 T TENSOR REMARK 3 T11: 0.6427 T22: 0.9806 REMARK 3 T33: 0.9025 T12: -0.1256 REMARK 3 T13: -0.0247 T23: -0.1064 REMARK 3 L TENSOR REMARK 3 L11: 0.0665 L22: 0.0639 REMARK 3 L33: 0.1064 L12: -0.0653 REMARK 3 L13: -0.0394 L23: 0.0633 REMARK 3 S TENSOR REMARK 3 S11: 0.4012 S12: 0.0130 S13: 0.5806 REMARK 3 S21: 1.5935 S22: 0.4647 S23: -0.5649 REMARK 3 S31: -0.2772 S32: -0.1121 S33: 0.0036 REMARK 3 TLS GROUP : 39 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 91 THROUGH 98 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.2307 78.6465 -1.1479 REMARK 3 T TENSOR REMARK 3 T11: 0.6822 T22: 0.4127 REMARK 3 T33: 0.9795 T12: -0.0246 REMARK 3 T13: -0.0743 T23: 0.0667 REMARK 3 L TENSOR REMARK 3 L11: 0.0550 L22: 0.0055 REMARK 3 L33: 0.1080 L12: 0.0350 REMARK 3 L13: -0.1076 L23: -0.0486 REMARK 3 S TENSOR REMARK 3 S11: 0.0259 S12: -0.0617 S13: 0.9840 REMARK 3 S21: -0.7716 S22: -0.4318 S23: 0.5300 REMARK 3 S31: -0.3301 S32: -0.0792 S33: 0.0001 REMARK 3 TLS GROUP : 40 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 99 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.7796 76.1777 -5.9759 REMARK 3 T TENSOR REMARK 3 T11: 0.5119 T22: 0.8625 REMARK 3 T33: 0.8861 T12: -0.1182 REMARK 3 T13: 0.1223 T23: 0.2122 REMARK 3 L TENSOR REMARK 3 L11: 0.4798 L22: 0.6051 REMARK 3 L33: 0.6489 L12: 0.4265 REMARK 3 L13: 0.3178 L23: -0.1430 REMARK 3 S TENSOR REMARK 3 S11: 0.0345 S12: 1.0303 S13: 0.6964 REMARK 3 S21: 0.2154 S22: -0.6389 S23: -0.4334 REMARK 3 S31: 0.0527 S32: 0.0823 S33: -0.0001 REMARK 3 TLS GROUP : 41 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 114 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.8726 82.3917 8.1886 REMARK 3 T TENSOR REMARK 3 T11: 0.8860 T22: 0.5620 REMARK 3 T33: 1.0858 T12: 0.0677 REMARK 3 T13: -0.2394 T23: -0.0871 REMARK 3 L TENSOR REMARK 3 L11: 5.8424 L22: 0.0870 REMARK 3 L33: 3.5226 L12: -0.4462 REMARK 3 L13: 1.0249 L23: -0.4837 REMARK 3 S TENSOR REMARK 3 S11: -0.6411 S12: -1.0285 S13: 0.5858 REMARK 3 S21: -0.0730 S22: 0.2061 S23: -0.3307 REMARK 3 S31: -0.5197 S32: -0.9800 S33: -0.1249 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 9MFG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1000290874. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-JUL-22 REMARK 200 TEMPERATURE (KELVIN) : 103 REMARK 200 PH : 8.5 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-C 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 : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74785 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850 REMARK 200 RESOLUTION RANGE LOW (A) : 35.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 87.8 REMARK 200 DATA REDUNDANCY : 3.000 REMARK 200 R MERGE (I) : 0.12300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 47.1 REMARK 200 DATA REDUNDANCY IN SHELL : 1.70 REMARK 200 R MERGE FOR SHELL (I) : 0.50700 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 73.38 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.62 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS (PH 8.5), 16% 606 PEG4000, REMARK 280 200 MM LI2SO4, 200 MM NASCN AND WAS CRYOPROTECTED WITH 25% REMARK 280 GLYCEROL, VAPOR DIFFUSION, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 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 52.65650 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 201.73600 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.65650 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 201.73600 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3780 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20440 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 15.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G, I, J REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6100 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21720 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 33.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H, K, L, M, N REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6000 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21160 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 21.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F, O, P, Q, R REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5020 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21020 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 20.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, S, T, U REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 23 REMARK 465 SER A 24 REMARK 465 GLU A 229 REMARK 465 THR A 230 REMARK 465 ILE A 231 REMARK 465 ASN A 232 REMARK 465 ALA A 233 REMARK 465 THR A 234 REMARK 465 VAL A 235 REMARK 465 PRO A 236 REMARK 465 LYS A 237 REMARK 465 GLY A 318 REMARK 465 ASN A 319 REMARK 465 SER A 320 REMARK 465 HIS A 321 REMARK 465 HIS A 322 REMARK 465 HIS A 323 REMARK 465 HIS A 324 REMARK 465 HIS A 325 REMARK 465 HIS A 326 REMARK 465 GLY B 23 REMARK 465 SER B 24 REMARK 465 HIS B 323 REMARK 465 HIS B 324 REMARK 465 HIS B 325 REMARK 465 HIS B 326 REMARK 465 GLY C 23 REMARK 465 SER C 24 REMARK 465 SER C 320 REMARK 465 HIS C 321 REMARK 465 HIS C 322 REMARK 465 HIS C 323 REMARK 465 HIS C 324 REMARK 465 HIS C 325 REMARK 465 HIS C 326 REMARK 465 GLY D 23 REMARK 465 SER D 24 REMARK 465 ASN D 232 REMARK 465 ALA D 233 REMARK 465 GLY D 318 REMARK 465 ASN D 319 REMARK 465 SER D 320 REMARK 465 HIS D 321 REMARK 465 HIS D 322 REMARK 465 HIS D 323 REMARK 465 HIS D 324 REMARK 465 HIS D 325 REMARK 465 HIS D 326 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ILE A 25 CG1 CG2 CD1 REMARK 470 LYS A 43 CG CD CE NZ REMARK 470 LYS A 57 CG CD CE NZ REMARK 470 GLN A 60 CG CD OE1 NE2 REMARK 470 ARG A 62 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 82 CG CD CE NZ REMARK 470 ASN A 91 CG OD1 ND2 REMARK 470 LYS A 107 CG CD CE NZ REMARK 470 PHE A 109 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 191 CG CD CE NZ REMARK 470 LYS A 208 CG CD CE NZ REMARK 470 ARG A 227 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 249 CG CD OE1 OE2 REMARK 470 LYS A 268 CG CD CE NZ REMARK 470 TYR A 276 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU A 281 CG CD OE1 OE2 REMARK 470 GLU A 285 CG CD OE1 OE2 REMARK 470 LYS A 301 CG CD CE NZ REMARK 470 LYS A 314 CG CD CE NZ REMARK 470 GLU A 317 CG CD OE1 OE2 REMARK 470 LYS B 57 CG CD CE NZ REMARK 470 GLN B 60 CG CD OE1 NE2 REMARK 470 ARG B 62 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 63 CG CD CE NZ REMARK 470 LYS B 82 CG CD CE NZ REMARK 470 LYS B 107 CG CD CE NZ REMARK 470 PHE B 109 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS B 163 CG CD CE NZ REMARK 470 GLU B 166 CG CD OE1 OE2 REMARK 470 LYS B 208 CG CD CE NZ REMARK 470 ARG B 227 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 237 CG CD CE NZ REMARK 470 LYS B 258 CG CD CE NZ REMARK 470 GLN B 263 CG CD OE1 NE2 REMARK 470 LYS B 314 CG CD CE NZ REMARK 470 GLU B 317 CG CD OE1 OE2 REMARK 470 HIS B 321 CG ND1 CD2 CE1 NE2 REMARK 470 LYS C 43 CG CD CE NZ REMARK 470 LYS C 57 CG CD CE NZ REMARK 470 GLN C 60 CG CD OE1 NE2 REMARK 470 LYS C 63 CG CD CE NZ REMARK 470 LYS C 90 CG CD CE NZ REMARK 470 LYS C 107 CG CD CE NZ REMARK 470 PHE C 109 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU C 166 CG CD OE1 OE2 REMARK 470 ASP C 184 CG OD1 OD2 REMARK 470 LYS C 191 CG CD CE NZ REMARK 470 ARG C 227 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 229 CG CD OE1 OE2 REMARK 470 GLU C 249 CG CD OE1 OE2 REMARK 470 LYS C 250 CG CD CE NZ REMARK 470 TYR C 257 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS C 258 CG CD CE NZ REMARK 470 THR C 261 OG1 CG2 REMARK 470 ASN C 262 CG OD1 ND2 REMARK 470 GLN C 263 CG CD OE1 NE2 REMARK 470 THR C 264 OG1 CG2 REMARK 470 LYS C 268 CG CD CE NZ REMARK 470 GLU C 269 CG CD OE1 OE2 REMARK 470 TYR C 276 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU C 281 CG CD OE1 OE2 REMARK 470 PHE C 282 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU C 284 CG CD1 CD2 REMARK 470 GLU C 285 CG CD OE1 OE2 REMARK 470 ILE C 288 CG1 CG2 CD1 REMARK 470 LYS C 289 CG CD CE NZ REMARK 470 TYR C 290 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL C 291 CG1 CG2 REMARK 470 ARG C 302 CG CD NE CZ NH1 NH2 REMARK 470 PHE C 312 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS C 314 CG CD CE NZ REMARK 470 ASN C 319 CG OD1 ND2 REMARK 470 LYS D 57 CG CD CE NZ REMARK 470 GLN D 60 CG CD OE1 NE2 REMARK 470 LYS D 63 CG CD CE NZ REMARK 470 LYS D 82 CG CD CE NZ REMARK 470 LYS D 90 CG CD CE NZ REMARK 470 LYS D 107 CG CD CE NZ REMARK 470 PHE D 109 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS D 157 CG CD CE NZ REMARK 470 GLU D 166 CG CD OE1 OE2 REMARK 470 ASP D 184 CG OD1 OD2 REMARK 470 GLN D 187 CG CD OE1 NE2 REMARK 470 LYS D 191 CG CD CE NZ REMARK 470 ARG D 227 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 237 CG CD CE NZ REMARK 470 GLU D 249 CG CD OE1 OE2 REMARK 470 LYS D 250 CG CD CE NZ REMARK 470 GLN D 263 CG CD OE1 NE2 REMARK 470 GLU D 281 CG CD OE1 OE2 REMARK 470 GLU D 285 CG CD OE1 OE2 REMARK 470 ARG D 302 CG CD NE CZ NH1 NH2 REMARK 470 GLU D 317 CG CD OE1 OE2 REMARK 470 GLU E 1 CG CD OE1 OE2 REMARK 470 LYS E 43 CG CD CE NZ REMARK 470 LYS E 75 CG CD CE NZ REMARK 470 GLN E 112 CG CD OE1 NE2 REMARK 470 GLU F 1 CG CD OE1 OE2 REMARK 470 LYS F 43 CG CD CE NZ REMARK 470 LYS F 75 CG CD CE NZ REMARK 470 GLN F 112 CG CD OE1 NE2 REMARK 470 GLU G 1 CG CD OE1 OE2 REMARK 470 LYS G 43 CG CD CE NZ REMARK 470 LYS G 75 CG CD CE NZ REMARK 470 GLN G 112 CG CD OE1 NE2 REMARK 470 GLU H 1 CG CD OE1 OE2 REMARK 470 LYS H 43 CG CD CE NZ REMARK 470 LYS H 75 CG CD CE NZ REMARK 470 GLN H 112 CG CD OE1 NE2 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 OG1 THR A 167 OE2 GLU A 169 1.98 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 31 37.06 -91.36 REMARK 500 ALA A 55 61.78 -151.78 REMARK 500 CYS A 59 101.64 -170.05 REMARK 500 ILE A 80 -93.88 -108.10 REMARK 500 ASN A 81 177.17 -56.66 REMARK 500 LYS A 107 -4.71 90.40 REMARK 500 TYR A 153 -50.91 68.25 REMARK 500 SER A 177 -103.26 -126.04 REMARK 500 TYR A 178 -168.68 -116.17 REMARK 500 SER A 226 -66.78 -129.18 REMARK 500 LYS A 258 132.70 178.40 REMARK 500 PHE A 274 30.58 -79.41 REMARK 500 PRO A 286 -93.67 -70.03 REMARK 500 THR A 299 109.08 -35.63 REMARK 500 TRP A 304 -163.85 -108.93 REMARK 500 HIS A 313 111.76 -167.01 REMARK 500 ALA B 55 58.12 -160.90 REMARK 500 ASN B 91 77.14 52.40 REMARK 500 ALA B 97 147.53 -173.33 REMARK 500 TYR B 138 -4.90 78.37 REMARK 500 TYR B 153 -56.67 67.89 REMARK 500 GLU B 168 -6.78 68.95 REMARK 500 SER B 177 -139.23 -133.17 REMARK 500 TYR B 178 -161.76 -68.41 REMARK 500 ALA B 228 83.48 -167.63 REMARK 500 THR B 261 69.54 -103.32 REMARK 500 GLN B 263 34.23 -95.45 REMARK 500 PHE B 274 42.60 -82.61 REMARK 500 GLN B 297 148.22 178.86 REMARK 500 HIS B 321 -50.24 -135.01 REMARK 500 SER C 31 47.42 -101.70 REMARK 500 ILE C 34 119.25 -163.83 REMARK 500 ALA C 55 58.01 -152.76 REMARK 500 ASN C 91 73.26 50.04 REMARK 500 ASP C 129 -168.62 -128.76 REMARK 500 TYR C 153 -44.16 70.12 REMARK 500 GLU C 168 8.97 57.51 REMARK 500 SER C 177 -159.63 -149.42 REMARK 500 SER C 226 -77.91 -95.49 REMARK 500 GLU C 249 -86.18 -60.16 REMARK 500 ASN C 262 -30.36 -147.89 REMARK 500 GLN C 263 177.61 59.30 REMARK 500 THR C 264 93.78 56.00 REMARK 500 ASP C 271 79.61 -155.20 REMARK 500 TYR C 276 -169.75 -110.95 REMARK 500 GLU C 281 49.37 -84.04 REMARK 500 TYR C 283 -161.64 -105.62 REMARK 500 LEU C 284 135.13 174.72 REMARK 500 ASN C 287 81.64 64.45 REMARK 500 ILE C 288 101.41 178.23 REMARK 500 REMARK 500 THIS ENTRY HAS 74 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9MDZ RELATED DB: PDB DBREF 9MFG A 25 317 UNP Q5VWK5 IL23R_HUMAN 25 317 DBREF 9MFG B 25 317 UNP Q5VWK5 IL23R_HUMAN 25 317 DBREF 9MFG C 25 317 UNP Q5VWK5 IL23R_HUMAN 25 317 DBREF 9MFG D 25 317 UNP Q5VWK5 IL23R_HUMAN 25 317 DBREF 9MFG E 1 120 PDB 9MFG 9MFG 1 120 DBREF 9MFG F 1 120 PDB 9MFG 9MFG 1 120 DBREF 9MFG G 1 120 PDB 9MFG 9MFG 1 120 DBREF 9MFG H 1 120 PDB 9MFG 9MFG 1 120 SEQADV 9MFG GLY A 23 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG SER A 24 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG GLY A 318 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG ASN A 319 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG SER A 320 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS A 321 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS A 322 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS A 323 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS A 324 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS A 325 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS A 326 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG GLY B 23 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG SER B 24 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG GLY B 318 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG ASN B 319 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG SER B 320 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS B 321 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS B 322 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS B 323 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS B 324 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS B 325 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS B 326 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG GLY C 23 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG SER C 24 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG GLY C 318 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG ASN C 319 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG SER C 320 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS C 321 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS C 322 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS C 323 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS C 324 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS C 325 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS C 326 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG GLY D 23 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG SER D 24 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG GLY D 318 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG ASN D 319 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG SER D 320 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS D 321 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS D 322 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS D 323 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS D 324 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS D 325 UNP Q5VWK5 EXPRESSION TAG SEQADV 9MFG HIS D 326 UNP Q5VWK5 EXPRESSION TAG SEQRES 1 A 304 GLY SER ILE THR ASN ILE ASN CYS SER GLY HIS ILE TRP SEQRES 2 A 304 VAL GLU PRO ALA THR ILE PHE LYS MET GLY MET ASN ILE SEQRES 3 A 304 SER ILE TYR CYS GLN ALA ALA ILE LYS ASN CYS GLN PRO SEQRES 4 A 304 ARG LYS LEU HIS PHE TYR LYS ASN GLY ILE LYS GLU ARG SEQRES 5 A 304 PHE GLN ILE THR ARG ILE ASN LYS THR THR ALA ARG LEU SEQRES 6 A 304 TRP TYR LYS ASN PHE LEU GLU PRO HIS ALA SER MET TYR SEQRES 7 A 304 CYS THR ALA GLU CYS PRO LYS HIS PHE GLN GLU THR LEU SEQRES 8 A 304 ILE CYS GLY LYS ASP ILE SER SER GLY TYR PRO PRO ASP SEQRES 9 A 304 ILE PRO ASP GLU VAL THR CYS VAL ILE TYR GLU TYR SER SEQRES 10 A 304 GLY ASN MET THR CYS THR TRP ASN ALA GLY LYS LEU THR SEQRES 11 A 304 TYR ILE ASP THR LYS TYR VAL VAL HIS VAL LYS SER LEU SEQRES 12 A 304 GLU THR GLU GLU GLU GLN GLN TYR LEU THR SER SER TYR SEQRES 13 A 304 ILE ASN ILE SER THR ASP SER LEU GLN GLY GLY LYS LYS SEQRES 14 A 304 TYR LEU VAL TRP VAL GLN ALA ALA ASN ALA LEU GLY MET SEQRES 15 A 304 GLU GLU SER LYS GLN LEU GLN ILE HIS LEU ASP ASP ILE SEQRES 16 A 304 VAL ILE PRO SER ALA ALA VAL ILE SER ARG ALA GLU THR SEQRES 17 A 304 ILE ASN ALA THR VAL PRO LYS THR ILE ILE TYR TRP ASP SEQRES 18 A 304 SER GLN THR THR ILE GLU LYS VAL SER CYS GLU MET ARG SEQRES 19 A 304 TYR LYS ALA THR THR ASN GLN THR TRP ASN VAL LYS GLU SEQRES 20 A 304 PHE ASP THR ASN PHE THR TYR VAL GLN GLN SER GLU PHE SEQRES 21 A 304 TYR LEU GLU PRO ASN ILE LYS TYR VAL PHE GLN VAL ARG SEQRES 22 A 304 CYS GLN GLU THR GLY LYS ARG TYR TRP GLN PRO TRP SER SEQRES 23 A 304 SER LEU PHE PHE HIS LYS THR PRO GLU GLY ASN SER HIS SEQRES 24 A 304 HIS HIS HIS HIS HIS SEQRES 1 B 304 GLY SER ILE THR ASN ILE ASN CYS SER GLY HIS ILE TRP SEQRES 2 B 304 VAL GLU PRO ALA THR ILE PHE LYS MET GLY MET ASN ILE SEQRES 3 B 304 SER ILE TYR CYS GLN ALA ALA ILE LYS ASN CYS GLN PRO SEQRES 4 B 304 ARG LYS LEU HIS PHE TYR LYS ASN GLY ILE LYS GLU ARG SEQRES 5 B 304 PHE GLN ILE THR ARG ILE ASN LYS THR THR ALA ARG LEU SEQRES 6 B 304 TRP TYR LYS ASN PHE LEU GLU PRO HIS ALA SER MET TYR SEQRES 7 B 304 CYS THR ALA GLU CYS PRO LYS HIS PHE GLN GLU THR LEU SEQRES 8 B 304 ILE CYS GLY LYS ASP ILE SER SER GLY TYR PRO PRO ASP SEQRES 9 B 304 ILE PRO ASP GLU VAL THR CYS VAL ILE TYR GLU TYR SER SEQRES 10 B 304 GLY ASN MET THR CYS THR TRP ASN ALA GLY LYS LEU THR SEQRES 11 B 304 TYR ILE ASP THR LYS TYR VAL VAL HIS VAL LYS SER LEU SEQRES 12 B 304 GLU THR GLU GLU GLU GLN GLN TYR LEU THR SER SER TYR SEQRES 13 B 304 ILE ASN ILE SER THR ASP SER LEU GLN GLY GLY LYS LYS SEQRES 14 B 304 TYR LEU VAL TRP VAL GLN ALA ALA ASN ALA LEU GLY MET SEQRES 15 B 304 GLU GLU SER LYS GLN LEU GLN ILE HIS LEU ASP ASP ILE SEQRES 16 B 304 VAL ILE PRO SER ALA ALA VAL ILE SER ARG ALA GLU THR SEQRES 17 B 304 ILE ASN ALA THR VAL PRO LYS THR ILE ILE TYR TRP ASP SEQRES 18 B 304 SER GLN THR THR ILE GLU LYS VAL SER CYS GLU MET ARG SEQRES 19 B 304 TYR LYS ALA THR THR ASN GLN THR TRP ASN VAL LYS GLU SEQRES 20 B 304 PHE ASP THR ASN PHE THR TYR VAL GLN GLN SER GLU PHE SEQRES 21 B 304 TYR LEU GLU PRO ASN ILE LYS TYR VAL PHE GLN VAL ARG SEQRES 22 B 304 CYS GLN GLU THR GLY LYS ARG TYR TRP GLN PRO TRP SER SEQRES 23 B 304 SER LEU PHE PHE HIS LYS THR PRO GLU GLY ASN SER HIS SEQRES 24 B 304 HIS HIS HIS HIS HIS SEQRES 1 C 304 GLY SER ILE THR ASN ILE ASN CYS SER GLY HIS ILE TRP SEQRES 2 C 304 VAL GLU PRO ALA THR ILE PHE LYS MET GLY MET ASN ILE SEQRES 3 C 304 SER ILE TYR CYS GLN ALA ALA ILE LYS ASN CYS GLN PRO SEQRES 4 C 304 ARG LYS LEU HIS PHE TYR LYS ASN GLY ILE LYS GLU ARG SEQRES 5 C 304 PHE GLN ILE THR ARG ILE ASN LYS THR THR ALA ARG LEU SEQRES 6 C 304 TRP TYR LYS ASN PHE LEU GLU PRO HIS ALA SER MET TYR SEQRES 7 C 304 CYS THR ALA GLU CYS PRO LYS HIS PHE GLN GLU THR LEU SEQRES 8 C 304 ILE CYS GLY LYS ASP ILE SER SER GLY TYR PRO PRO ASP SEQRES 9 C 304 ILE PRO ASP GLU VAL THR CYS VAL ILE TYR GLU TYR SER SEQRES 10 C 304 GLY ASN MET THR CYS THR TRP ASN ALA GLY LYS LEU THR SEQRES 11 C 304 TYR ILE ASP THR LYS TYR VAL VAL HIS VAL LYS SER LEU SEQRES 12 C 304 GLU THR GLU GLU GLU GLN GLN TYR LEU THR SER SER TYR SEQRES 13 C 304 ILE ASN ILE SER THR ASP SER LEU GLN GLY GLY LYS LYS SEQRES 14 C 304 TYR LEU VAL TRP VAL GLN ALA ALA ASN ALA LEU GLY MET SEQRES 15 C 304 GLU GLU SER LYS GLN LEU GLN ILE HIS LEU ASP ASP ILE SEQRES 16 C 304 VAL ILE PRO SER ALA ALA VAL ILE SER ARG ALA GLU THR SEQRES 17 C 304 ILE ASN ALA THR VAL PRO LYS THR ILE ILE TYR TRP ASP SEQRES 18 C 304 SER GLN THR THR ILE GLU LYS VAL SER CYS GLU MET ARG SEQRES 19 C 304 TYR LYS ALA THR THR ASN GLN THR TRP ASN VAL LYS GLU SEQRES 20 C 304 PHE ASP THR ASN PHE THR TYR VAL GLN GLN SER GLU PHE SEQRES 21 C 304 TYR LEU GLU PRO ASN ILE LYS TYR VAL PHE GLN VAL ARG SEQRES 22 C 304 CYS GLN GLU THR GLY LYS ARG TYR TRP GLN PRO TRP SER SEQRES 23 C 304 SER LEU PHE PHE HIS LYS THR PRO GLU GLY ASN SER HIS SEQRES 24 C 304 HIS HIS HIS HIS HIS SEQRES 1 D 304 GLY SER ILE THR ASN ILE ASN CYS SER GLY HIS ILE TRP SEQRES 2 D 304 VAL GLU PRO ALA THR ILE PHE LYS MET GLY MET ASN ILE SEQRES 3 D 304 SER ILE TYR CYS GLN ALA ALA ILE LYS ASN CYS GLN PRO SEQRES 4 D 304 ARG LYS LEU HIS PHE TYR LYS ASN GLY ILE LYS GLU ARG SEQRES 5 D 304 PHE GLN ILE THR ARG ILE ASN LYS THR THR ALA ARG LEU SEQRES 6 D 304 TRP TYR LYS ASN PHE LEU GLU PRO HIS ALA SER MET TYR SEQRES 7 D 304 CYS THR ALA GLU CYS PRO LYS HIS PHE GLN GLU THR LEU SEQRES 8 D 304 ILE CYS GLY LYS ASP ILE SER SER GLY TYR PRO PRO ASP SEQRES 9 D 304 ILE PRO ASP GLU VAL THR CYS VAL ILE TYR GLU TYR SER SEQRES 10 D 304 GLY ASN MET THR CYS THR TRP ASN ALA GLY LYS LEU THR SEQRES 11 D 304 TYR ILE ASP THR LYS TYR VAL VAL HIS VAL LYS SER LEU SEQRES 12 D 304 GLU THR GLU GLU GLU GLN GLN TYR LEU THR SER SER TYR SEQRES 13 D 304 ILE ASN ILE SER THR ASP SER LEU GLN GLY GLY LYS LYS SEQRES 14 D 304 TYR LEU VAL TRP VAL GLN ALA ALA ASN ALA LEU GLY MET SEQRES 15 D 304 GLU GLU SER LYS GLN LEU GLN ILE HIS LEU ASP ASP ILE SEQRES 16 D 304 VAL ILE PRO SER ALA ALA VAL ILE SER ARG ALA GLU THR SEQRES 17 D 304 ILE ASN ALA THR VAL PRO LYS THR ILE ILE TYR TRP ASP SEQRES 18 D 304 SER GLN THR THR ILE GLU LYS VAL SER CYS GLU MET ARG SEQRES 19 D 304 TYR LYS ALA THR THR ASN GLN THR TRP ASN VAL LYS GLU SEQRES 20 D 304 PHE ASP THR ASN PHE THR TYR VAL GLN GLN SER GLU PHE SEQRES 21 D 304 TYR LEU GLU PRO ASN ILE LYS TYR VAL PHE GLN VAL ARG SEQRES 22 D 304 CYS GLN GLU THR GLY LYS ARG TYR TRP GLN PRO TRP SER SEQRES 23 D 304 SER LEU PHE PHE HIS LYS THR PRO GLU GLY ASN SER HIS SEQRES 24 D 304 HIS HIS HIS HIS HIS SEQRES 1 E 120 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 120 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 120 PHE THR PHE SER THR TYR ALA MET ALA TRP PHE ARG GLN SEQRES 4 E 120 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA GLU SER TRP SEQRES 5 E 120 SER SER GLY THR THR TYR TYR GLY ALA SER VAL VAL GLY SEQRES 6 E 120 ARG PHE THR MET SER ARG ASP ASP SER LYS ASN THR VAL SEQRES 7 E 120 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 E 120 VAL TYR TYR CYS ALA ALA LYS ARG PRO ASP ALA GLY TRP SEQRES 9 E 120 GLN THR TYR ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 E 120 VAL SER SER SEQRES 1 F 120 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 F 120 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 F 120 PHE THR PHE SER THR TYR ALA MET ALA TRP PHE ARG GLN SEQRES 4 F 120 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA GLU SER TRP SEQRES 5 F 120 SER SER GLY THR THR TYR TYR GLY ALA SER VAL VAL GLY SEQRES 6 F 120 ARG PHE THR MET SER ARG ASP ASP SER LYS ASN THR VAL SEQRES 7 F 120 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 F 120 VAL TYR TYR CYS ALA ALA LYS ARG PRO ASP ALA GLY TRP SEQRES 9 F 120 GLN THR TYR ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 F 120 VAL SER SER SEQRES 1 G 120 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 120 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 G 120 PHE THR PHE SER THR TYR ALA MET ALA TRP PHE ARG GLN SEQRES 4 G 120 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA GLU SER TRP SEQRES 5 G 120 SER SER GLY THR THR TYR TYR GLY ALA SER VAL VAL GLY SEQRES 6 G 120 ARG PHE THR MET SER ARG ASP ASP SER LYS ASN THR VAL SEQRES 7 G 120 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 G 120 VAL TYR TYR CYS ALA ALA LYS ARG PRO ASP ALA GLY TRP SEQRES 9 G 120 GLN THR TYR ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 G 120 VAL SER SER SEQRES 1 H 120 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 120 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 120 PHE THR PHE SER THR TYR ALA MET ALA TRP PHE ARG GLN SEQRES 4 H 120 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA GLU SER TRP SEQRES 5 H 120 SER SER GLY THR THR TYR TYR GLY ALA SER VAL VAL GLY SEQRES 6 H 120 ARG PHE THR MET SER ARG ASP ASP SER LYS ASN THR VAL SEQRES 7 H 120 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 H 120 VAL TYR TYR CYS ALA ALA LYS ARG PRO ASP ALA GLY TRP SEQRES 9 H 120 GLN THR TYR ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 H 120 VAL SER SER HET NAG I 1 25 HET NAG I 2 27 HET FUC I 3 20 HET NAG J 1 26 HET NAG J 2 27 HET NAG K 1 25 HET MAN K 2 20 HET NAG K 3 27 HET FUC K 4 20 HET NAG L 1 24 HET MAN L 2 21 HET NAG L 3 27 HET FUC L 4 20 HET NAG M 1 25 HET MAN M 2 21 HET FUC M 3 20 HET NAG N 1 26 HET NAG N 2 27 HET NAG O 1 25 HET MAN O 2 20 HET NAG O 3 27 HET FUC O 4 20 HET NAG P 1 24 HET MAN P 2 21 HET NAG P 3 27 HET FUC P 4 20 HET NAG Q 1 26 HET NAG Q 2 27 HET NAG R 1 26 HET NAG R 2 27 HET NAG S 1 24 HET MAN S 2 21 HET NAG S 3 27 HET FUC S 4 20 HET NAG T 1 25 HET NAG T 2 27 HET FUC T 3 20 HET NAG U 1 26 HET NAG U 2 27 HET NAG A 401 27 HET NAG A 402 27 HET SCN A 403 3 HET NAG B 401 27 HET NAG C 401 27 HET NAG D 401 27 HET SCN D 402 3 HET SCN D 403 3 HET SCN D 404 3 HET GOL E 201 14 HET SO4 E 202 5 HET SO4 F 201 5 HET SCN G 201 3 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM SCN THIOCYANATE ION HETNAM GOL GLYCEROL HETNAM SO4 SULFATE ION HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 9 NAG 30(C8 H15 N O6) FORMUL 9 FUC 8(C6 H12 O5) FORMUL 11 MAN 6(C6 H12 O6) FORMUL 24 SCN 5(C N S 1-) FORMUL 31 GOL C3 H8 O3 FORMUL 32 SO4 2(O4 S 2-) FORMUL 35 HOH *90(H2 O) HELIX 1 AA1 ASP A 184 LEU A 186 5 3 HELIX 2 AA2 ASP B 184 LEU B 186 5 3 HELIX 3 AA3 ASP C 184 LEU C 186 5 3 HELIX 4 AA4 ASP D 184 LEU D 186 5 3 HELIX 5 AA5 ASP E 73 LYS E 75 5 3 HELIX 6 AA6 ARG E 86 THR E 90 5 5 HELIX 7 AA7 THR F 28 TYR F 32 5 5 HELIX 8 AA8 ASP F 73 LYS F 75 5 3 HELIX 9 AA9 ARG F 86 THR F 90 5 5 HELIX 10 AB1 THR G 28 TYR G 32 5 5 HELIX 11 AB2 ARG G 86 THR G 90 5 5 HELIX 12 AB3 ARG H 86 THR H 90 5 5 SHEET 1 AA1 4 GLY A 32 GLU A 37 0 SHEET 2 AA1 4 ILE A 48 ALA A 54 -1 O SER A 49 N GLU A 37 SHEET 3 AA1 4 THR A 84 TYR A 89 -1 O LEU A 87 N ILE A 50 SHEET 4 AA1 4 ILE A 77 ARG A 79 -1 N THR A 78 O ARG A 86 SHEET 1 AA2 8 ILE A 41 LYS A 43 0 SHEET 2 AA2 8 GLU A 111 GLY A 122 1 O GLY A 122 N PHE A 42 SHEET 3 AA2 8 THR G 57 TYR G 59 1 O TYR G 59 N LEU A 113 SHEET 4 AA2 8 GLU G 46 SER G 51 -1 N GLU G 50 O TYR G 58 SHEET 5 AA2 8 ALA G 33 GLN G 39 -1 N ARG G 38 O GLU G 46 SHEET 6 AA2 8 ALA G 91 LYS G 98 -1 O LYS G 98 N ALA G 33 SHEET 7 AA2 8 THR G 114 VAL G 118 -1 O THR G 114 N TYR G 93 SHEET 8 AA2 8 GLY G 10 VAL G 12 1 N GLY G 10 O THR G 117 SHEET 1 AA3 9 ILE A 71 GLU A 73 0 SHEET 2 AA3 9 LYS A 63 LYS A 68 -1 N PHE A 66 O GLU A 73 SHEET 3 AA3 9 HIS A 96 GLU A 104 -1 O TYR A 100 N TYR A 67 SHEET 4 AA3 9 GLU A 111 GLY A 122 -1 O LYS A 117 N MET A 99 SHEET 5 AA3 9 THR G 57 TYR G 59 1 O TYR G 59 N LEU A 113 SHEET 6 AA3 9 GLU G 46 SER G 51 -1 N GLU G 50 O TYR G 58 SHEET 7 AA3 9 ALA G 33 GLN G 39 -1 N ARG G 38 O GLU G 46 SHEET 8 AA3 9 ALA G 91 LYS G 98 -1 O LYS G 98 N ALA G 33 SHEET 9 AA3 9 TYR G 107 TRP G 110 -1 O TYR G 109 N ALA G 97 SHEET 1 AA4 4 ILE A 179 SER A 182 0 SHEET 2 AA4 4 ASN A 141 ASN A 147 -1 N MET A 142 O ILE A 181 SHEET 3 AA4 4 ASP A 129 TYR A 136 -1 N VAL A 134 O THR A 143 SHEET 4 AA4 4 VAL A 218 ILE A 219 1 O ILE A 219 N ILE A 135 SHEET 1 AA5 4 GLU A 170 THR A 175 0 SHEET 2 AA5 4 THR A 156 SER A 164 -1 N VAL A 160 O TYR A 173 SHEET 3 AA5 4 LYS A 191 ASN A 200 -1 O ALA A 199 N LYS A 157 SHEET 4 AA5 4 GLY A 203 GLU A 206 -1 O GLY A 203 N ASN A 200 SHEET 1 AA6 4 GLU A 170 THR A 175 0 SHEET 2 AA6 4 THR A 156 SER A 164 -1 N VAL A 160 O TYR A 173 SHEET 3 AA6 4 LYS A 191 ASN A 200 -1 O ALA A 199 N LYS A 157 SHEET 4 AA6 4 LEU A 210 HIS A 213 -1 O LEU A 210 N VAL A 194 SHEET 1 AA7 3 ALA A 223 ARG A 227 0 SHEET 2 AA7 3 ILE A 239 SER A 244 -1 O TYR A 241 N SER A 226 SHEET 3 AA7 3 GLN A 278 GLU A 281 -1 O GLN A 278 N TRP A 242 SHEET 1 AA8 4 ASN A 266 GLU A 269 0 SHEET 2 AA8 4 VAL A 251 ALA A 259 -1 N MET A 255 O LYS A 268 SHEET 3 AA8 4 LYS A 289 GLU A 298 -1 O GLN A 297 N SER A 252 SHEET 4 AA8 4 PHE A 311 LYS A 314 -1 O HIS A 313 N TYR A 290 SHEET 1 AA9 4 GLY B 32 GLU B 37 0 SHEET 2 AA9 4 MET B 46 ALA B 54 -1 O GLN B 53 N HIS B 33 SHEET 3 AA9 4 THR B 84 PHE B 92 -1 O LEU B 87 N ILE B 50 SHEET 4 AA9 4 ILE B 77 ASN B 81 -1 N THR B 78 O ARG B 86 SHEET 1 AB1 5 ILE B 41 LYS B 43 0 SHEET 2 AB1 5 GLU B 111 GLY B 122 1 O GLY B 122 N PHE B 42 SHEET 3 AB1 5 HIS B 96 GLU B 104 -1 N ALA B 97 O ILE B 119 SHEET 4 AB1 5 LYS B 63 LYS B 68 -1 N TYR B 67 O TYR B 100 SHEET 5 AB1 5 ILE B 71 GLU B 73 -1 O ILE B 71 N LYS B 68 SHEET 1 AB2 4 ILE B 179 SER B 182 0 SHEET 2 AB2 4 ASN B 141 ASN B 147 -1 N MET B 142 O ILE B 181 SHEET 3 AB2 4 ASP B 129 TYR B 136 -1 N THR B 132 O THR B 145 SHEET 4 AB2 4 VAL B 218 ILE B 219 1 O ILE B 219 N ILE B 135 SHEET 1 AB3 4 GLN B 172 THR B 175 0 SHEET 2 AB3 4 LYS B 157 SER B 164 -1 N TYR B 158 O THR B 175 SHEET 3 AB3 4 LYS B 191 ASN B 200 -1 O LEU B 193 N LYS B 163 SHEET 4 AB3 4 GLY B 203 GLU B 206 -1 O GLU B 205 N ALA B 198 SHEET 1 AB4 4 GLN B 172 THR B 175 0 SHEET 2 AB4 4 LYS B 157 SER B 164 -1 N TYR B 158 O THR B 175 SHEET 3 AB4 4 LYS B 191 ASN B 200 -1 O LEU B 193 N LYS B 163 SHEET 4 AB4 4 LEU B 210 HIS B 213 -1 O LEU B 210 N VAL B 194 SHEET 1 AB5 3 ALA B 223 ILE B 231 0 SHEET 2 AB5 3 LYS B 237 SER B 244 -1 O TYR B 241 N SER B 226 SHEET 3 AB5 3 GLN B 278 PHE B 282 -1 O GLN B 278 N TRP B 242 SHEET 1 AB6 4 ASN B 266 GLU B 269 0 SHEET 2 AB6 4 GLU B 254 ALA B 259 -1 N TYR B 257 O ASN B 266 SHEET 3 AB6 4 ILE B 288 ARG B 295 -1 O VAL B 291 N LYS B 258 SHEET 4 AB6 4 PHE B 311 THR B 315 -1 O PHE B 311 N PHE B 292 SHEET 1 AB7 4 GLY C 32 GLU C 37 0 SHEET 2 AB7 4 MET C 46 ALA C 54 -1 O TYR C 51 N TRP C 35 SHEET 3 AB7 4 THR C 84 PHE C 92 -1 O LEU C 87 N ILE C 50 SHEET 4 AB7 4 ILE C 77 THR C 78 -1 N THR C 78 O ARG C 86 SHEET 1 AB8 8 ILE C 41 LYS C 43 0 SHEET 2 AB8 8 GLU C 111 GLY C 122 1 O SER C 120 N PHE C 42 SHEET 3 AB8 8 THR F 57 TYR F 59 1 O TYR F 59 N LEU C 113 SHEET 4 AB8 8 GLU F 46 SER F 51 -1 N GLU F 50 O TYR F 58 SHEET 5 AB8 8 ALA F 33 GLN F 39 -1 N ARG F 38 O GLU F 46 SHEET 6 AB8 8 ALA F 91 LYS F 98 -1 O TYR F 94 N PHE F 37 SHEET 7 AB8 8 THR F 114 VAL F 118 -1 O THR F 114 N TYR F 93 SHEET 8 AB8 8 GLY F 10 VAL F 12 1 N VAL F 12 O THR F 117 SHEET 1 AB9 9 LYS C 72 GLU C 73 0 SHEET 2 AB9 9 LYS C 63 LYS C 68 -1 N PHE C 66 O GLU C 73 SHEET 3 AB9 9 HIS C 96 GLU C 104 -1 O GLU C 104 N LYS C 63 SHEET 4 AB9 9 GLU C 111 GLY C 122 -1 O LYS C 117 N MET C 99 SHEET 5 AB9 9 THR F 57 TYR F 59 1 O TYR F 59 N LEU C 113 SHEET 6 AB9 9 GLU F 46 SER F 51 -1 N GLU F 50 O TYR F 58 SHEET 7 AB9 9 ALA F 33 GLN F 39 -1 N ARG F 38 O GLU F 46 SHEET 8 AB9 9 ALA F 91 LYS F 98 -1 O TYR F 94 N PHE F 37 SHEET 9 AB9 9 TYR F 109 TRP F 110 -1 O TYR F 109 N ALA F 97 SHEET 1 AC1 4 ILE C 179 SER C 182 0 SHEET 2 AC1 4 ASN C 141 ASN C 147 -1 N MET C 142 O ILE C 181 SHEET 3 AC1 4 ASP C 129 TYR C 136 -1 N ASP C 129 O ASN C 147 SHEET 4 AC1 4 VAL C 218 ILE C 219 1 O ILE C 219 N ILE C 135 SHEET 1 AC2 4 GLU C 170 THR C 175 0 SHEET 2 AC2 4 THR C 156 SER C 164 -1 N TYR C 158 O THR C 175 SHEET 3 AC2 4 LYS C 191 ASN C 200 -1 O TRP C 195 N HIS C 161 SHEET 4 AC2 4 GLY C 203 GLU C 206 -1 O GLU C 205 N ALA C 198 SHEET 1 AC3 4 GLU C 170 THR C 175 0 SHEET 2 AC3 4 THR C 156 SER C 164 -1 N TYR C 158 O THR C 175 SHEET 3 AC3 4 LYS C 191 ASN C 200 -1 O TRP C 195 N HIS C 161 SHEET 4 AC3 4 LEU C 210 HIS C 213 -1 O LEU C 210 N VAL C 194 SHEET 1 AC4 3 ALA C 223 ILE C 231 0 SHEET 2 AC4 3 LYS C 237 SER C 244 -1 O TYR C 241 N SER C 226 SHEET 3 AC4 3 GLN C 278 PHE C 282 -1 O PHE C 282 N THR C 238 SHEET 1 AC5 4 LYS C 268 GLU C 269 0 SHEET 2 AC5 4 VAL C 251 ALA C 259 -1 N MET C 255 O LYS C 268 SHEET 3 AC5 4 LYS C 289 GLU C 298 -1 O ARG C 295 N GLU C 254 SHEET 4 AC5 4 PHE C 311 LYS C 314 -1 O PHE C 311 N PHE C 292 SHEET 1 AC6 4 GLY D 32 GLU D 37 0 SHEET 2 AC6 4 ILE D 48 ALA D 54 -1 O TYR D 51 N TRP D 35 SHEET 3 AC6 4 THR D 84 TYR D 89 -1 O LEU D 87 N ILE D 50 SHEET 4 AC6 4 ILE D 77 ARG D 79 -1 N THR D 78 O ARG D 86 SHEET 1 AC7 5 ILE D 41 LYS D 43 0 SHEET 2 AC7 5 GLU D 111 GLY D 122 1 O SER D 120 N PHE D 42 SHEET 3 AC7 5 HIS D 96 GLU D 104 -1 N MET D 99 O LYS D 117 SHEET 4 AC7 5 LYS D 63 LYS D 68 -1 N TYR D 67 O TYR D 100 SHEET 5 AC7 5 ILE D 71 GLU D 73 -1 O GLU D 73 N PHE D 66 SHEET 1 AC8 4 ILE D 179 SER D 182 0 SHEET 2 AC8 4 ASN D 141 ASN D 147 -1 N MET D 142 O ILE D 181 SHEET 3 AC8 4 ASP D 129 TYR D 136 -1 N VAL D 134 O THR D 143 SHEET 4 AC8 4 VAL D 218 ILE D 219 1 O ILE D 219 N ILE D 135 SHEET 1 AC9 4 GLU D 170 THR D 175 0 SHEET 2 AC9 4 THR D 156 SER D 164 -1 N VAL D 160 O TYR D 173 SHEET 3 AC9 4 LYS D 191 ASN D 200 -1 O TRP D 195 N HIS D 161 SHEET 4 AC9 4 GLY D 203 GLU D 206 -1 O GLU D 205 N ALA D 198 SHEET 1 AD1 4 GLU D 170 THR D 175 0 SHEET 2 AD1 4 THR D 156 SER D 164 -1 N VAL D 160 O TYR D 173 SHEET 3 AD1 4 LYS D 191 ASN D 200 -1 O TRP D 195 N HIS D 161 SHEET 4 AD1 4 LEU D 210 HIS D 213 -1 O LEU D 210 N VAL D 194 SHEET 1 AD2 3 ALA D 223 THR D 230 0 SHEET 2 AD2 3 THR D 238 SER D 244 -1 O ILE D 239 N GLU D 229 SHEET 3 AD2 3 GLN D 278 PHE D 282 -1 O GLN D 278 N TRP D 242 SHEET 1 AD3 4 ASN D 266 THR D 272 0 SHEET 2 AD3 4 VAL D 251 ALA D 259 -1 N CYS D 253 O PHE D 270 SHEET 3 AD3 4 LYS D 289 GLU D 298 -1 O GLN D 297 N SER D 252 SHEET 4 AD3 4 PHE D 311 LYS D 314 -1 O PHE D 311 N PHE D 292 SHEET 1 AD4 4 GLN E 3 SER E 7 0 SHEET 2 AD4 4 LEU E 18 SER E 25 -1 O ALA E 23 N VAL E 5 SHEET 3 AD4 4 THR E 77 MET E 82 -1 O MET E 82 N LEU E 18 SHEET 4 AD4 4 PHE E 67 ASP E 72 -1 N ASP E 72 O THR E 77 SHEET 1 AD5 6 GLY E 10 VAL E 12 0 SHEET 2 AD5 6 THR E 114 VAL E 118 1 O LEU E 115 N GLY E 10 SHEET 3 AD5 6 ALA E 91 LYS E 98 -1 N TYR E 93 O THR E 114 SHEET 4 AD5 6 ALA E 33 GLN E 39 -1 N ALA E 33 O LYS E 98 SHEET 5 AD5 6 GLU E 46 SER E 51 -1 O GLU E 46 N ARG E 38 SHEET 6 AD5 6 THR E 57 TYR E 59 -1 O TYR E 58 N GLU E 50 SHEET 1 AD6 4 GLY E 10 VAL E 12 0 SHEET 2 AD6 4 THR E 114 VAL E 118 1 O LEU E 115 N GLY E 10 SHEET 3 AD6 4 ALA E 91 LYS E 98 -1 N TYR E 93 O THR E 114 SHEET 4 AD6 4 TYR E 109 TRP E 110 -1 O TYR E 109 N ALA E 97 SHEET 1 AD7 4 GLN F 3 SER F 7 0 SHEET 2 AD7 4 LEU F 18 SER F 25 -1 O SER F 25 N GLN F 3 SHEET 3 AD7 4 THR F 77 MET F 82 -1 O LEU F 80 N LEU F 20 SHEET 4 AD7 4 PHE F 67 ASP F 72 -1 N ASP F 72 O THR F 77 SHEET 1 AD8 4 GLN G 3 SER G 7 0 SHEET 2 AD8 4 LEU G 18 SER G 25 -1 O ALA G 23 N VAL G 5 SHEET 3 AD8 4 THR G 77 MET G 82 -1 O MET G 82 N LEU G 18 SHEET 4 AD8 4 PHE G 67 ASP G 72 -1 N ASP G 72 O THR G 77 SHEET 1 AD9 4 GLN H 3 SER H 7 0 SHEET 2 AD9 4 SER H 17 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AD9 4 THR H 77 ASN H 83 -1 O MET H 82 N LEU H 18 SHEET 4 AD9 4 PHE H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AE1 6 LEU H 11 VAL H 12 0 SHEET 2 AE1 6 THR H 114 VAL H 118 1 O THR H 117 N VAL H 12 SHEET 3 AE1 6 ALA H 91 LYS H 98 -1 N TYR H 93 O THR H 114 SHEET 4 AE1 6 ALA H 33 GLN H 39 -1 N ALA H 33 O LYS H 98 SHEET 5 AE1 6 ARG H 45 SER H 51 -1 O ALA H 49 N TRP H 36 SHEET 6 AE1 6 THR H 57 TYR H 59 -1 O TYR H 58 N GLU H 50 SHEET 1 AE2 4 LEU H 11 VAL H 12 0 SHEET 2 AE2 4 THR H 114 VAL H 118 1 O THR H 117 N VAL H 12 SHEET 3 AE2 4 ALA H 91 LYS H 98 -1 N TYR H 93 O THR H 114 SHEET 4 AE2 4 TYR H 109 TRP H 110 -1 O TYR H 109 N ALA H 97 SSBOND 1 CYS A 30 CYS A 115 1555 1555 2.05 SSBOND 2 CYS A 52 CYS A 101 1555 1555 2.03 SSBOND 3 CYS A 59 CYS A 105 1555 1555 2.04 SSBOND 4 CYS A 133 CYS A 144 1555 1555 2.05 SSBOND 5 CYS A 253 CYS A 296 1555 1555 2.04 SSBOND 6 CYS B 30 CYS B 115 1555 1555 2.05 SSBOND 7 CYS B 52 CYS B 101 1555 1555 2.04 SSBOND 8 CYS B 59 CYS B 105 1555 1555 2.04 SSBOND 9 CYS B 133 CYS B 144 1555 1555 2.04 SSBOND 10 CYS B 253 CYS B 296 1555 1555 2.04 SSBOND 11 CYS C 30 CYS C 115 1555 1555 2.05 SSBOND 12 CYS C 52 CYS C 101 1555 1555 2.04 SSBOND 13 CYS C 59 CYS C 105 1555 1555 2.04 SSBOND 14 CYS C 133 CYS C 144 1555 1555 2.04 SSBOND 15 CYS C 253 CYS C 296 1555 1555 2.04 SSBOND 16 CYS D 30 CYS D 115 1555 1555 2.05 SSBOND 17 CYS D 52 CYS D 101 1555 1555 2.02 SSBOND 18 CYS D 59 CYS D 105 1555 1555 2.04 SSBOND 19 CYS D 133 CYS D 144 1555 1555 2.05 SSBOND 20 CYS D 253 CYS D 296 1555 1555 2.04 SSBOND 21 CYS E 22 CYS E 95 1555 1555 2.04 SSBOND 22 CYS F 22 CYS F 95 1555 1555 2.04 SSBOND 23 CYS G 22 CYS G 95 1555 1555 2.05 SSBOND 24 CYS H 22 CYS H 95 1555 1555 2.04 LINK ND2 ASN A 47 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN A 81 C1 NAG A 402 1555 1555 1.44 LINK ND2 ASN A 141 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN A 180 C1 NAG A 401 1555 1555 1.44 LINK ND2 ASN B 47 C1 NAG K 1 1555 1555 1.43 LINK ND2 ASN B 81 C1 NAG M 1 1555 1555 1.46 LINK ND2 ASN B 141 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN B 180 C1 NAG B 401 1555 1555 1.46 LINK ND2 ASN B 232 C1 NAG L 1 1555 1555 1.45 LINK ND2 ASN C 47 C1 NAG P 1 1555 1555 1.43 LINK ND2 ASN C 81 C1 NAG Q 1 1555 1555 1.45 LINK ND2 ASN C 141 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN C 180 C1 NAG C 401 1555 1555 1.44 LINK ND2 ASN C 232 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN D 47 C1 NAG S 1 1555 1555 1.45 LINK ND2 ASN D 81 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN D 141 C1 NAG U 1 1555 1555 1.43 LINK ND2 ASN D 180 C1 NAG D 401 1555 1555 1.47 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.45 LINK O6 NAG I 1 C1 FUC I 3 1555 1555 1.45 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45 LINK O3 NAG K 1 C1 MAN K 2 1555 1555 1.45 LINK O6 NAG K 1 C1 FUC K 4 1555 1555 1.45 LINK O3 MAN K 2 C1 NAG K 3 1555 1555 1.46 LINK O3 NAG L 1 C1 MAN L 2 1555 1555 1.44 LINK O4 NAG L 1 C1 NAG L 3 1555 1555 1.46 LINK O6 NAG L 1 C1 FUC L 4 1555 1555 1.45 LINK O3 NAG M 1 C1 MAN M 2 1555 1555 1.47 LINK O6 NAG M 1 C1 FUC M 3 1555 1555 1.46 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.45 LINK O3 NAG O 1 C1 MAN O 2 1555 1555 1.44 LINK O6 NAG O 1 C1 FUC O 4 1555 1555 1.45 LINK O3 MAN O 2 C1 NAG O 3 1555 1555 1.46 LINK O3 NAG P 1 C1 MAN P 2 1555 1555 1.45 LINK O4 NAG P 1 C1 NAG P 3 1555 1555 1.45 LINK O6 NAG P 1 C1 FUC P 4 1555 1555 1.45 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.45 LINK O3 NAG S 1 C1 MAN S 2 1555 1555 1.44 LINK O4 NAG S 1 C1 NAG S 3 1555 1555 1.47 LINK O6 NAG S 1 C1 FUC S 4 1555 1555 1.45 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.45 LINK O6 NAG T 1 C1 FUC T 3 1555 1555 1.44 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44 CISPEP 1 GLU A 37 PRO A 38 0 7.60 CISPEP 2 GLU B 37 PRO B 38 0 5.03 CISPEP 3 GLU C 37 PRO C 38 0 1.33 CISPEP 4 GLU D 37 PRO D 38 0 9.11 CRYST1 105.313 403.472 84.247 90.00 90.00 90.00 P 21 21 2 16 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 0.009496 0.000000 0.000000 0.00000 SCALE2 0.000000 0.002478 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011870 0.00000