HEADER IMMUNE SYSTEM 23-APR-24 9BIF TITLE FAB B11-OSPCA COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: VH-CH1 DOMAIN OF B11 FAB; COMPND 3 CHAIN: H, C, G, J, O, Q, U, W; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: VH-VL DOMAIN OF B11 FAB; COMPND 7 CHAIN: L, D, I, K, P, R, V, X; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: OUTER SURFACE PROTEIN C; COMPND 11 CHAIN: A, B, E, F, M, N, S, T; COMPND 12 SYNONYM: PC; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: BORRELIELLA BURGDORFERI B31; SOURCE 13 ORGANISM_TAXID: 224326; SOURCE 14 GENE: OSPC, BB_B19; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTI-OSPCA MONOCLONAL ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.J.RUDOLPH,N.MANTIS REVDAT 1 20-NOV-24 9BIF 0 JRNL AUTH M.J.RUDOLPH,Y.CHEN,C.VORAUER,D.J.VANCE,C.L.PIAZZA, JRNL AUTH 2 G.G.WILLSEY,K.MCCARTHY,B.MURIUKI,L.A.CAVACINI,M.GUTTMAN, JRNL AUTH 3 N.J.MANTIS JRNL TITL STRUCTURE OF A HUMAN MONOCLONAL ANTIBODY IN COMPLEX WITH JRNL TITL 2 OUTER SURFACE PROTEIN C OF THE LYME DISEASE SPIROCHETE, JRNL TITL 3 BORRELIELLA BURGDORFERI. JRNL REF J IMMUNOL. V. 213 1234 2024 JRNL REFN ESSN 1550-6606 JRNL PMID 39240158 JRNL DOI 10.4049/JIMMUNOL.2400247 REMARK 2 REMARK 2 RESOLUTION. 3.09 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.09 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.62 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.930 REMARK 3 COMPLETENESS FOR RANGE (%) : 90.0 REMARK 3 NUMBER OF REFLECTIONS : 96238 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.243 REMARK 3 R VALUE (WORKING SET) : 0.240 REMARK 3 FREE R VALUE : 0.295 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910 REMARK 3 FREE R VALUE TEST SET COUNT : 4723 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 48.6200 - 9.5800 0.95 3230 148 0.2039 0.2344 REMARK 3 2 9.5800 - 7.6100 0.85 2932 132 0.2002 0.2369 REMARK 3 3 7.6100 - 6.6500 0.93 3174 160 0.2342 0.3045 REMARK 3 4 6.6500 - 6.0500 0.94 3135 198 0.2371 0.2809 REMARK 3 5 6.0500 - 5.6100 0.95 3252 157 0.2329 0.2676 REMARK 3 6 5.6100 - 5.2800 0.95 3239 143 0.2290 0.2870 REMARK 3 7 5.2800 - 5.0200 0.93 3158 152 0.2230 0.2785 REMARK 3 8 5.0200 - 4.8000 0.80 2726 112 0.2129 0.2454 REMARK 3 9 4.8000 - 4.6200 0.82 2734 144 0.2124 0.2609 REMARK 3 10 4.6200 - 4.4600 0.86 2923 166 0.2100 0.2601 REMARK 3 11 4.4600 - 4.3200 0.88 2956 181 0.2058 0.2529 REMARK 3 12 4.3200 - 4.1900 0.90 3050 164 0.2191 0.2605 REMARK 3 13 4.1900 - 4.0800 0.92 3161 159 0.2304 0.2605 REMARK 3 14 4.0800 - 3.9800 0.92 3089 168 0.2398 0.3229 REMARK 3 15 3.9800 - 3.8900 0.93 3100 165 0.2511 0.3218 REMARK 3 16 3.8900 - 3.8100 0.94 3217 154 0.2523 0.3142 REMARK 3 17 3.8100 - 3.7300 0.94 3132 190 0.2491 0.3281 REMARK 3 18 3.7300 - 3.6600 0.95 3249 174 0.2573 0.3079 REMARK 3 19 3.6600 - 3.6000 0.94 3177 151 0.2594 0.2897 REMARK 3 20 3.6000 - 3.5400 0.95 3222 184 0.2660 0.3409 REMARK 3 21 3.5400 - 3.4800 0.95 3190 184 0.2652 0.3241 REMARK 3 22 3.4800 - 3.4300 0.95 3262 156 0.2642 0.3670 REMARK 3 23 3.4300 - 3.3800 0.95 3210 176 0.2876 0.3456 REMARK 3 24 3.3800 - 3.3300 0.92 3107 149 0.2978 0.3882 REMARK 3 25 3.3300 - 3.2800 0.79 2717 141 0.2897 0.3632 REMARK 3 26 3.2800 - 3.2400 0.82 2739 123 0.2894 0.3138 REMARK 3 27 3.2400 - 3.2000 0.88 3042 153 0.2838 0.3338 REMARK 3 28 3.2000 - 3.1600 0.89 3012 153 0.2795 0.3436 REMARK 3 29 3.1600 - 3.1300 0.91 3021 166 0.2929 0.3385 REMARK 3 30 3.1300 - 3.0900 0.68 2359 120 0.3173 0.4310 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) : 0.510 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.700 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 35994 REMARK 3 ANGLE : 0.968 48802 REMARK 3 CHIRALITY : 0.052 5664 REMARK 3 PLANARITY : 0.006 6203 REMARK 3 DIHEDRAL : 7.341 4930 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 95 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 37 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.6915 -53.5926 18.4672 REMARK 3 T TENSOR REMARK 3 T11: 0.5487 T22: 1.5008 REMARK 3 T33: 0.5626 T12: 0.1148 REMARK 3 T13: -0.2295 T23: 0.3323 REMARK 3 L TENSOR REMARK 3 L11: 0.3108 L22: 0.7906 REMARK 3 L33: 0.1949 L12: -0.2900 REMARK 3 L13: 0.2259 L23: -0.0854 REMARK 3 S TENSOR REMARK 3 S11: -0.4727 S12: -0.3368 S13: 0.0672 REMARK 3 S21: -0.1966 S22: -0.1673 S23: 0.1419 REMARK 3 S31: -0.2039 S32: -0.6623 S33: -0.0746 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 38 THROUGH 151 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.2795 -47.7614 26.9461 REMARK 3 T TENSOR REMARK 3 T11: 0.2111 T22: 1.4967 REMARK 3 T33: 0.1720 T12: 0.0261 REMARK 3 T13: -0.2595 T23: 0.2898 REMARK 3 L TENSOR REMARK 3 L11: 0.7517 L22: 0.5442 REMARK 3 L33: 0.5653 L12: -0.1999 REMARK 3 L13: 0.5756 L23: 0.0322 REMARK 3 S TENSOR REMARK 3 S11: -0.1835 S12: -0.3723 S13: -0.1204 REMARK 3 S21: -0.0545 S22: 0.0482 S23: 0.0019 REMARK 3 S31: -0.0116 S32: 0.4010 S33: 0.1239 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 152 THROUGH 221 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.4237 -56.6245 48.8622 REMARK 3 T TENSOR REMARK 3 T11: 0.3727 T22: 1.4697 REMARK 3 T33: 0.5690 T12: 0.0981 REMARK 3 T13: -0.1264 T23: 0.4771 REMARK 3 L TENSOR REMARK 3 L11: 3.5986 L22: 1.1982 REMARK 3 L33: 0.0474 L12: -2.0917 REMARK 3 L13: -0.3886 L23: 0.2179 REMARK 3 S TENSOR REMARK 3 S11: -0.2736 S12: -0.7966 S13: -1.2463 REMARK 3 S21: 0.0828 S22: 0.0715 S23: 0.3653 REMARK 3 S31: 0.3367 S32: 0.2015 S33: -0.2559 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.3301 -27.9537 26.5238 REMARK 3 T TENSOR REMARK 3 T11: 0.4835 T22: 0.6784 REMARK 3 T33: 0.6859 T12: -0.1145 REMARK 3 T13: -0.1104 T23: 0.0257 REMARK 3 L TENSOR REMARK 3 L11: 2.1740 L22: 2.8134 REMARK 3 L33: 3.3341 L12: 1.3474 REMARK 3 L13: -2.5897 L23: -0.9139 REMARK 3 S TENSOR REMARK 3 S11: 0.2230 S12: -0.5742 S13: 1.6644 REMARK 3 S21: -0.0533 S22: -0.0397 S23: -0.0266 REMARK 3 S31: -1.1141 S32: 0.4863 S33: -0.2913 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 26 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.9900 -33.9386 16.9076 REMARK 3 T TENSOR REMARK 3 T11: 0.3577 T22: 0.8198 REMARK 3 T33: 0.4625 T12: -0.2856 REMARK 3 T13: -0.2278 T23: 0.1484 REMARK 3 L TENSOR REMARK 3 L11: 3.5449 L22: 1.9588 REMARK 3 L33: 3.3586 L12: -2.2555 REMARK 3 L13: 1.0255 L23: 0.6168 REMARK 3 S TENSOR REMARK 3 S11: -0.0441 S12: 0.1856 S13: 0.4625 REMARK 3 S21: -0.1951 S22: 0.2539 S23: 0.2170 REMARK 3 S31: -0.8468 S32: 0.6375 S33: -0.0054 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 76 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.4660 -34.9881 25.8833 REMARK 3 T TENSOR REMARK 3 T11: 0.3510 T22: 0.8571 REMARK 3 T33: 0.3370 T12: -0.1929 REMARK 3 T13: -0.0257 T23: 0.1379 REMARK 3 L TENSOR REMARK 3 L11: 4.2450 L22: 1.7930 REMARK 3 L33: 1.1514 L12: -1.0875 REMARK 3 L13: -2.2111 L23: 0.5917 REMARK 3 S TENSOR REMARK 3 S11: -0.0403 S12: 0.0511 S13: 0.1743 REMARK 3 S21: 0.0383 S22: -0.0116 S23: 0.1658 REMARK 3 S31: -0.6808 S32: 1.0284 S33: 0.0808 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 115 THROUGH 164 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.5678 -41.8183 56.1913 REMARK 3 T TENSOR REMARK 3 T11: 0.4496 T22: 1.5327 REMARK 3 T33: 0.4911 T12: 0.1328 REMARK 3 T13: -0.0480 T23: -0.0194 REMARK 3 L TENSOR REMARK 3 L11: 4.3066 L22: 2.8722 REMARK 3 L33: 6.6037 L12: -2.9121 REMARK 3 L13: 4.5539 L23: -2.8907 REMARK 3 S TENSOR REMARK 3 S11: -0.1956 S12: -0.9734 S13: 0.2412 REMARK 3 S21: 0.5027 S22: 0.2373 S23: -0.5950 REMARK 3 S31: -0.5140 S32: 0.6025 S33: 0.1685 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 165 THROUGH 175 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.4749 -42.0902 40.0433 REMARK 3 T TENSOR REMARK 3 T11: 0.4021 T22: 0.7815 REMARK 3 T33: 0.6804 T12: 0.2392 REMARK 3 T13: -0.1840 T23: -0.1279 REMARK 3 L TENSOR REMARK 3 L11: 4.7743 L22: 3.0750 REMARK 3 L33: 4.9915 L12: 2.0159 REMARK 3 L13: 2.6469 L23: -1.6804 REMARK 3 S TENSOR REMARK 3 S11: 0.5550 S12: 0.3736 S13: -1.2172 REMARK 3 S21: -0.3735 S22: 0.0526 S23: 0.0691 REMARK 3 S31: 0.5412 S32: 0.6188 S33: -0.4900 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 176 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.2809 -39.5960 62.1085 REMARK 3 T TENSOR REMARK 3 T11: 0.6496 T22: 2.2016 REMARK 3 T33: 0.4770 T12: -0.0049 REMARK 3 T13: 0.0048 T23: 0.0318 REMARK 3 L TENSOR REMARK 3 L11: 0.6785 L22: 1.9121 REMARK 3 L33: 0.4177 L12: -1.1025 REMARK 3 L13: -0.3601 L23: 0.4111 REMARK 3 S TENSOR REMARK 3 S11: -0.5924 S12: -0.5266 S13: -0.1235 REMARK 3 S21: 0.4986 S22: 0.5434 S23: -0.1565 REMARK 3 S31: -0.6126 S32: 0.9144 S33: 0.0208 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 45 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.3242 -50.5858 -7.0906 REMARK 3 T TENSOR REMARK 3 T11: 0.5277 T22: 0.9289 REMARK 3 T33: 0.3220 T12: -0.0994 REMARK 3 T13: -0.1250 T23: 0.1332 REMARK 3 L TENSOR REMARK 3 L11: 5.3941 L22: 2.2724 REMARK 3 L33: 1.7785 L12: -2.0134 REMARK 3 L13: -1.3794 L23: 1.1517 REMARK 3 S TENSOR REMARK 3 S11: -0.0539 S12: -0.5129 S13: -0.0447 REMARK 3 S21: 0.0347 S22: 0.0294 S23: -0.0913 REMARK 3 S31: -0.5824 S32: 0.7588 S33: -0.0084 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 76 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.7473 -59.6446 -8.1799 REMARK 3 T TENSOR REMARK 3 T11: 0.6213 T22: 0.7740 REMARK 3 T33: 0.3541 T12: -0.0124 REMARK 3 T13: -0.1655 T23: 0.1024 REMARK 3 L TENSOR REMARK 3 L11: 9.5251 L22: 2.2310 REMARK 3 L33: 6.7578 L12: -0.2153 REMARK 3 L13: -2.7199 L23: 0.2015 REMARK 3 S TENSOR REMARK 3 S11: 0.3551 S12: -0.8648 S13: -0.6961 REMARK 3 S21: -0.2148 S22: -0.0910 S23: -0.0515 REMARK 3 S31: 0.4126 S32: 0.6728 S33: -0.2839 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 121 THROUGH 159 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.6736 -69.7797 -9.0922 REMARK 3 T TENSOR REMARK 3 T11: 0.6017 T22: 1.1671 REMARK 3 T33: 0.5797 T12: 0.0766 REMARK 3 T13: -0.1674 T23: 0.3068 REMARK 3 L TENSOR REMARK 3 L11: 7.7903 L22: 3.1094 REMARK 3 L33: 1.6521 L12: -2.2882 REMARK 3 L13: 0.8926 L23: 0.1812 REMARK 3 S TENSOR REMARK 3 S11: 0.6499 S12: -0.0138 S13: -1.3983 REMARK 3 S21: -0.3003 S22: -0.5412 S23: -0.0463 REMARK 3 S31: 0.2065 S32: 0.6532 S33: -0.1293 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 160 THROUGH 199 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.6263 -56.7858 -14.3152 REMARK 3 T TENSOR REMARK 3 T11: 0.4929 T22: 0.9239 REMARK 3 T33: 0.3683 T12: 0.1029 REMARK 3 T13: -0.1756 T23: 0.0165 REMARK 3 L TENSOR REMARK 3 L11: 2.6663 L22: 4.6651 REMARK 3 L33: 2.6785 L12: -0.1780 REMARK 3 L13: -1.2639 L23: 1.1256 REMARK 3 S TENSOR REMARK 3 S11: 0.7888 S12: 0.0039 S13: -0.6825 REMARK 3 S21: -0.7776 S22: -0.7523 S23: 0.7462 REMARK 3 S31: -0.0059 S32: -0.3248 S33: 0.0175 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 45 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.9153 -44.1791 -5.1996 REMARK 3 T TENSOR REMARK 3 T11: 0.5459 T22: 1.1018 REMARK 3 T33: 0.3120 T12: -0.0740 REMARK 3 T13: -0.3048 T23: 0.2103 REMARK 3 L TENSOR REMARK 3 L11: 1.4752 L22: 3.0795 REMARK 3 L33: 0.9448 L12: -0.7006 REMARK 3 L13: -0.9046 L23: 1.3412 REMARK 3 S TENSOR REMARK 3 S11: 0.1875 S12: 0.2507 S13: 0.1937 REMARK 3 S21: -0.5272 S22: 0.0482 S23: 0.4797 REMARK 3 S31: 0.1283 S32: -0.3912 S33: -0.1142 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 76 THROUGH 140 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.7763 -50.1591 -5.8196 REMARK 3 T TENSOR REMARK 3 T11: 0.4452 T22: 1.2718 REMARK 3 T33: 0.3680 T12: -0.0287 REMARK 3 T13: -0.0350 T23: 0.1282 REMARK 3 L TENSOR REMARK 3 L11: 2.6660 L22: 1.4095 REMARK 3 L33: 1.3900 L12: -0.1747 REMARK 3 L13: -0.7132 L23: 1.3472 REMARK 3 S TENSOR REMARK 3 S11: 0.1792 S12: 0.0019 S13: -0.2439 REMARK 3 S21: 0.1860 S22: -0.1241 S23: -0.2838 REMARK 3 S31: -0.2123 S32: 0.7126 S33: -0.0808 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 141 THROUGH 145 ) REMARK 3 ORIGIN FOR THE GROUP (A): 50.1109 -52.7110 -5.9096 REMARK 3 T TENSOR REMARK 3 T11: 1.0117 T22: 1.7593 REMARK 3 T33: 0.5732 T12: -0.5376 REMARK 3 T13: -0.0598 T23: -0.0179 REMARK 3 L TENSOR REMARK 3 L11: 4.6760 L22: 5.1617 REMARK 3 L33: 4.4049 L12: 0.7545 REMARK 3 L13: -3.6600 L23: 1.6281 REMARK 3 S TENSOR REMARK 3 S11: 0.1058 S12: -0.0335 S13: -0.1172 REMARK 3 S21: -0.1453 S22: 0.2531 S23: -0.3245 REMARK 3 S31: 0.3406 S32: 1.2347 S33: -0.3730 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 146 THROUGH 195 ) REMARK 3 ORIGIN FOR THE GROUP (A): 33.8784 -45.8095 1.2344 REMARK 3 T TENSOR REMARK 3 T11: 0.3680 T22: 1.3662 REMARK 3 T33: 0.2831 T12: -0.1300 REMARK 3 T13: -0.1612 T23: 0.1208 REMARK 3 L TENSOR REMARK 3 L11: 0.5776 L22: 0.9793 REMARK 3 L33: 1.6891 L12: -0.1005 REMARK 3 L13: 0.5963 L23: -0.4741 REMARK 3 S TENSOR REMARK 3 S11: -0.3780 S12: -0.1789 S13: 0.1227 REMARK 3 S21: 0.3792 S22: 0.2711 S23: -0.4014 REMARK 3 S31: -0.0269 S32: 0.6800 S33: 0.1170 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 196 THROUGH 201 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.3525 -28.7146 1.6386 REMARK 3 T TENSOR REMARK 3 T11: 0.6720 T22: 1.7767 REMARK 3 T33: 1.6162 T12: 0.1269 REMARK 3 T13: -0.1406 T23: -0.4324 REMARK 3 L TENSOR REMARK 3 L11: 1.6319 L22: 2.6038 REMARK 3 L33: 2.3944 L12: 0.5407 REMARK 3 L13: 1.9164 L23: 0.0443 REMARK 3 S TENSOR REMARK 3 S11: 0.2502 S12: 0.2434 S13: 0.1515 REMARK 3 S21: 0.0205 S22: -0.1963 S23: 2.6883 REMARK 3 S31: -0.1463 S32: -1.8315 S33: -0.0470 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 37 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.4273 -46.1709 -30.5216 REMARK 3 T TENSOR REMARK 3 T11: 0.5052 T22: 1.0806 REMARK 3 T33: 0.5597 T12: -0.1139 REMARK 3 T13: -0.1661 T23: 0.0586 REMARK 3 L TENSOR REMARK 3 L11: 2.0768 L22: 2.5323 REMARK 3 L33: 3.1887 L12: -0.4003 REMARK 3 L13: 0.3553 L23: -0.5904 REMARK 3 S TENSOR REMARK 3 S11: 0.1074 S12: -0.6827 S13: -0.1518 REMARK 3 S21: -0.2079 S22: -0.3859 S23: 0.2048 REMARK 3 S31: -0.8370 S32: 0.3758 S33: 0.3465 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 38 THROUGH 127 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.5535 -49.6931 -34.1433 REMARK 3 T TENSOR REMARK 3 T11: 0.5116 T22: 0.8691 REMARK 3 T33: 0.3319 T12: 0.0926 REMARK 3 T13: -0.1781 T23: 0.1033 REMARK 3 L TENSOR REMARK 3 L11: 1.2407 L22: 2.1874 REMARK 3 L33: 2.6089 L12: 0.4924 REMARK 3 L13: 0.2280 L23: -1.0540 REMARK 3 S TENSOR REMARK 3 S11: 0.2497 S12: 0.3381 S13: -0.3075 REMARK 3 S21: -0.1579 S22: -0.2729 S23: -0.1666 REMARK 3 S31: 0.1127 S32: 0.6057 S33: -0.0074 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 128 THROUGH 221 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.7271 -29.2628 -62.8363 REMARK 3 T TENSOR REMARK 3 T11: 0.5354 T22: 0.6945 REMARK 3 T33: 0.3488 T12: -0.1451 REMARK 3 T13: -0.0985 T23: -0.0982 REMARK 3 L TENSOR REMARK 3 L11: 2.1770 L22: 3.1025 REMARK 3 L33: 3.1917 L12: -0.8832 REMARK 3 L13: 0.3337 L23: -0.5643 REMARK 3 S TENSOR REMARK 3 S11: -0.3336 S12: 0.0132 S13: 0.2895 REMARK 3 S21: 0.1875 S22: 0.1856 S23: -0.4449 REMARK 3 S31: -0.4063 S32: 0.9322 S33: 0.1338 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.1058 -37.4743 -30.3574 REMARK 3 T TENSOR REMARK 3 T11: 0.5030 T22: 0.7928 REMARK 3 T33: 0.2655 T12: -0.0123 REMARK 3 T13: -0.0909 T23: -0.0594 REMARK 3 L TENSOR REMARK 3 L11: 3.3010 L22: 2.8307 REMARK 3 L33: 4.3392 L12: -0.4480 REMARK 3 L13: 1.7258 L23: -1.9636 REMARK 3 S TENSOR REMARK 3 S11: -0.0482 S12: -0.7857 S13: -0.1733 REMARK 3 S21: 0.0660 S22: 0.1511 S23: 0.4526 REMARK 3 S31: -0.2305 S32: -0.0226 S33: -0.0623 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 76 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.3396 -36.5154 -36.5538 REMARK 3 T TENSOR REMARK 3 T11: 0.5376 T22: 0.6660 REMARK 3 T33: 0.3204 T12: -0.1540 REMARK 3 T13: -0.1557 T23: 0.0270 REMARK 3 L TENSOR REMARK 3 L11: 0.9288 L22: 1.7472 REMARK 3 L33: 4.1890 L12: -0.7116 REMARK 3 L13: 1.0525 L23: -2.2381 REMARK 3 S TENSOR REMARK 3 S11: 0.1919 S12: -0.3936 S13: -0.0867 REMARK 3 S21: 0.1646 S22: -0.0629 S23: 0.0441 REMARK 3 S31: -0.0766 S32: 0.4230 S33: -0.0729 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 115 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.1113 -34.9356 -67.8168 REMARK 3 T TENSOR REMARK 3 T11: 0.5963 T22: 0.3797 REMARK 3 T33: 0.2863 T12: -0.1638 REMARK 3 T13: -0.1251 T23: 0.0353 REMARK 3 L TENSOR REMARK 3 L11: 4.1867 L22: 3.5230 REMARK 3 L33: 5.5108 L12: -2.2893 REMARK 3 L13: -1.2402 L23: 0.7945 REMARK 3 S TENSOR REMARK 3 S11: 0.1239 S12: 0.1728 S13: -0.0564 REMARK 3 S21: -0.4526 S22: -0.1152 S23: -0.2227 REMARK 3 S31: 0.2107 S32: 0.2244 S33: -0.0114 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.8763 -63.0837 95.0112 REMARK 3 T TENSOR REMARK 3 T11: 0.6343 T22: 1.2701 REMARK 3 T33: 0.5340 T12: -0.0234 REMARK 3 T13: -0.0120 T23: 0.4339 REMARK 3 L TENSOR REMARK 3 L11: 0.0829 L22: 7.3014 REMARK 3 L33: 5.5293 L12: 0.5584 REMARK 3 L13: -0.4429 L23: -6.3399 REMARK 3 S TENSOR REMARK 3 S11: 0.3284 S12: 0.1629 S13: 0.1579 REMARK 3 S21: 0.5054 S22: 0.2766 S23: 0.5592 REMARK 3 S31: -0.1243 S32: -0.5434 S33: -0.4548 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 18 THROUGH 37 ) REMARK 3 ORIGIN FOR THE GROUP (A): 49.3920 -59.6926 81.7652 REMARK 3 T TENSOR REMARK 3 T11: 0.3101 T22: 1.1270 REMARK 3 T33: 0.6134 T12: 0.0369 REMARK 3 T13: -0.1740 T23: 0.0757 REMARK 3 L TENSOR REMARK 3 L11: 9.4059 L22: 3.2180 REMARK 3 L33: 1.3545 L12: -2.0864 REMARK 3 L13: 1.0092 L23: -0.3085 REMARK 3 S TENSOR REMARK 3 S11: -0.0530 S12: 1.4747 S13: -0.2667 REMARK 3 S21: -0.0472 S22: -0.5768 S23: -0.8120 REMARK 3 S31: -0.5596 S32: -0.0510 S33: 0.5463 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 38 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): 54.0437 -67.3448 88.6307 REMARK 3 T TENSOR REMARK 3 T11: 0.2954 T22: 0.7513 REMARK 3 T33: 0.2699 T12: -0.0361 REMARK 3 T13: -0.0927 T23: 0.0738 REMARK 3 L TENSOR REMARK 3 L11: 3.4302 L22: 3.9119 REMARK 3 L33: 5.5976 L12: 0.0753 REMARK 3 L13: 1.6377 L23: 0.6673 REMARK 3 S TENSOR REMARK 3 S11: 0.2028 S12: -0.4815 S13: -0.4527 REMARK 3 S21: 0.2038 S22: -0.2121 S23: 0.2580 REMARK 3 S31: 0.2323 S32: -0.2655 S33: 0.0378 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 103 THROUGH 222 ) REMARK 3 ORIGIN FOR THE GROUP (A): 53.4984 -54.5247 118.0643 REMARK 3 T TENSOR REMARK 3 T11: 0.4111 T22: 0.9051 REMARK 3 T33: 0.6098 T12: 0.0316 REMARK 3 T13: 0.0456 T23: 0.2281 REMARK 3 L TENSOR REMARK 3 L11: 1.1781 L22: 1.2024 REMARK 3 L33: 3.8269 L12: 0.2500 REMARK 3 L13: -0.1396 L23: -1.1664 REMARK 3 S TENSOR REMARK 3 S11: 0.0521 S12: -0.2553 S13: 0.1710 REMARK 3 S21: 0.2990 S22: 0.0770 S23: 0.4142 REMARK 3 S31: -0.2762 S32: -1.3453 S33: -0.1142 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 2 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): 70.5203 -54.5250 97.0503 REMARK 3 T TENSOR REMARK 3 T11: 0.3731 T22: 0.4199 REMARK 3 T33: 0.3441 T12: 0.0324 REMARK 3 T13: -0.1074 T23: 0.1479 REMARK 3 L TENSOR REMARK 3 L11: 1.5558 L22: 1.5413 REMARK 3 L33: 3.1883 L12: 0.3768 REMARK 3 L13: 0.4599 L23: 0.4597 REMARK 3 S TENSOR REMARK 3 S11: 0.0005 S12: 0.1975 S13: -0.1365 REMARK 3 S21: -0.2264 S22: 0.0156 S23: 0.0783 REMARK 3 S31: -0.3848 S32: 0.2832 S33: -0.0059 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 130 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 69.1170 -61.1409 125.3823 REMARK 3 T TENSOR REMARK 3 T11: 0.3974 T22: 0.4766 REMARK 3 T33: 0.2662 T12: 0.0856 REMARK 3 T13: -0.1056 T23: 0.0580 REMARK 3 L TENSOR REMARK 3 L11: 6.1494 L22: 5.4280 REMARK 3 L33: 4.5479 L12: 3.0823 REMARK 3 L13: -1.3474 L23: 0.1941 REMARK 3 S TENSOR REMARK 3 S11: 0.0327 S12: -0.1830 S13: -0.1507 REMARK 3 S21: 0.5250 S22: 0.0556 S23: 0.1970 REMARK 3 S31: -0.1010 S32: -0.0911 S33: -0.1317 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 44 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): 44.3358 -64.8479 63.6275 REMARK 3 T TENSOR REMARK 3 T11: 0.5848 T22: 1.0170 REMARK 3 T33: 0.2463 T12: -0.0648 REMARK 3 T13: -0.1433 T23: 0.1619 REMARK 3 L TENSOR REMARK 3 L11: 5.2240 L22: 2.0612 REMARK 3 L33: 1.7803 L12: 1.1765 REMARK 3 L13: 0.0453 L23: -0.2185 REMARK 3 S TENSOR REMARK 3 S11: 0.4535 S12: 0.5864 S13: 0.0142 REMARK 3 S21: 0.0716 S22: 0.1454 S23: 0.2001 REMARK 3 S31: 0.3471 S32: -0.7203 S33: -0.5767 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 115 THROUGH 140 ) REMARK 3 ORIGIN FOR THE GROUP (A): 57.1129 -73.9121 58.3579 REMARK 3 T TENSOR REMARK 3 T11: 0.5985 T22: 0.9068 REMARK 3 T33: 0.3363 T12: 0.0189 REMARK 3 T13: 0.0044 T23: -0.1328 REMARK 3 L TENSOR REMARK 3 L11: 3.6896 L22: 7.0172 REMARK 3 L33: 5.2855 L12: 1.7700 REMARK 3 L13: 1.5791 L23: -0.1702 REMARK 3 S TENSOR REMARK 3 S11: -0.6035 S12: 0.8096 S13: -0.6969 REMARK 3 S21: -1.0691 S22: 0.6354 S23: -0.7933 REMARK 3 S31: 0.5008 S32: 0.0533 S33: -0.0997 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 141 THROUGH 169 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.2263 -80.9670 66.3968 REMARK 3 T TENSOR REMARK 3 T11: 0.5570 T22: 1.1857 REMARK 3 T33: 0.6882 T12: -0.2329 REMARK 3 T13: -0.0809 T23: -0.0721 REMARK 3 L TENSOR REMARK 3 L11: 6.1277 L22: 0.6099 REMARK 3 L33: 2.6099 L12: 1.0456 REMARK 3 L13: 3.9618 L23: 0.8204 REMARK 3 S TENSOR REMARK 3 S11: -0.1558 S12: 0.3326 S13: -0.7644 REMARK 3 S21: -0.0317 S22: 0.4878 S23: 0.1257 REMARK 3 S31: 0.7211 S32: -0.8216 S33: -0.2015 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 170 THROUGH 201 ) REMARK 3 ORIGIN FOR THE GROUP (A): 61.5097 -62.5691 68.9290 REMARK 3 T TENSOR REMARK 3 T11: 0.5430 T22: 0.9399 REMARK 3 T33: 0.5622 T12: 0.0010 REMARK 3 T13: -0.2212 T23: 0.0674 REMARK 3 L TENSOR REMARK 3 L11: 4.2706 L22: 7.0934 REMARK 3 L33: 0.3397 L12: -0.2401 REMARK 3 L13: 0.2237 L23: 1.4543 REMARK 3 S TENSOR REMARK 3 S11: 0.5877 S12: 0.2520 S13: -0.4174 REMARK 3 S21: 1.2218 S22: -0.0606 S23: -1.9617 REMARK 3 S31: 0.3085 S32: 0.4553 S33: -0.5318 REMARK 3 TLS GROUP : 35 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 45 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 49.5959 -53.4430 63.9131 REMARK 3 T TENSOR REMARK 3 T11: 0.3920 T22: 0.8719 REMARK 3 T33: 0.4089 T12: 0.1529 REMARK 3 T13: -0.0894 T23: 0.0508 REMARK 3 L TENSOR REMARK 3 L11: 2.4885 L22: 3.2780 REMARK 3 L33: 1.5408 L12: 1.5649 REMARK 3 L13: 0.6110 L23: 0.1311 REMARK 3 S TENSOR REMARK 3 S11: 0.2429 S12: 0.3286 S13: 0.1913 REMARK 3 S21: 0.3937 S22: 0.2724 S23: -0.0911 REMARK 3 S31: 0.0885 S32: -0.0466 S33: -0.0992 REMARK 3 TLS GROUP : 36 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 76 THROUGH 94 ) REMARK 3 ORIGIN FOR THE GROUP (A): 33.7786 -76.1149 51.8565 REMARK 3 T TENSOR REMARK 3 T11: 0.9423 T22: 1.1298 REMARK 3 T33: 0.4608 T12: -0.1434 REMARK 3 T13: -0.0564 T23: -0.0259 REMARK 3 L TENSOR REMARK 3 L11: 2.9032 L22: 2.1581 REMARK 3 L33: 1.5964 L12: 0.1348 REMARK 3 L13: 0.1547 L23: -0.7795 REMARK 3 S TENSOR REMARK 3 S11: 0.0336 S12: 0.7380 S13: -0.4701 REMARK 3 S21: -0.4315 S22: -0.0344 S23: 0.3181 REMARK 3 S31: 0.9186 S32: -0.6696 S33: -0.1997 REMARK 3 TLS GROUP : 37 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 95 THROUGH 140 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.4932 -51.7715 67.8447 REMARK 3 T TENSOR REMARK 3 T11: 0.3418 T22: 1.1967 REMARK 3 T33: 0.2681 T12: 0.1610 REMARK 3 T13: -0.1628 T23: 0.1537 REMARK 3 L TENSOR REMARK 3 L11: 2.0000 L22: 0.8106 REMARK 3 L33: 1.7245 L12: 0.0728 REMARK 3 L13: 1.0145 L23: -0.8711 REMARK 3 S TENSOR REMARK 3 S11: -0.0399 S12: -0.6006 S13: 0.2219 REMARK 3 S21: 0.3346 S22: 0.0203 S23: 0.0297 REMARK 3 S31: -0.0715 S32: -0.2290 S33: 0.3048 REMARK 3 TLS GROUP : 38 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 141 THROUGH 198 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.8686 -52.9941 58.1360 REMARK 3 T TENSOR REMARK 3 T11: 0.4811 T22: 1.4511 REMARK 3 T33: 0.3457 T12: 0.0219 REMARK 3 T13: -0.3875 T23: 0.4101 REMARK 3 L TENSOR REMARK 3 L11: 0.7438 L22: 0.5250 REMARK 3 L33: 1.2544 L12: 0.1651 REMARK 3 L13: 0.6964 L23: 0.3053 REMARK 3 S TENSOR REMARK 3 S11: -0.0526 S12: -0.0251 S13: -0.0021 REMARK 3 S21: 0.1840 S22: 0.4190 S23: 0.1083 REMARK 3 S31: 0.1227 S32: -0.2342 S33: 0.2295 REMARK 3 TLS GROUP : 39 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 50.4504 -55.8480 31.7518 REMARK 3 T TENSOR REMARK 3 T11: 0.3643 T22: 1.2800 REMARK 3 T33: 0.6106 T12: 0.2559 REMARK 3 T13: 0.0825 T23: 0.0008 REMARK 3 L TENSOR REMARK 3 L11: 0.0636 L22: 1.8619 REMARK 3 L33: 1.6962 L12: 0.1911 REMARK 3 L13: -0.1025 L23: 1.0859 REMARK 3 S TENSOR REMARK 3 S11: 0.6014 S12: 0.0439 S13: -0.1339 REMARK 3 S21: 0.2330 S22: 0.2354 S23: 0.6139 REMARK 3 S31: 0.1989 S32: 0.3279 S33: -0.5622 REMARK 3 TLS GROUP : 40 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 18 THROUGH 36 ) REMARK 3 ORIGIN FOR THE GROUP (A): 51.3778 -55.7336 45.9218 REMARK 3 T TENSOR REMARK 3 T11: 0.4792 T22: 1.2260 REMARK 3 T33: 0.4109 T12: -0.1189 REMARK 3 T13: -0.1664 T23: 0.0917 REMARK 3 L TENSOR REMARK 3 L11: 0.5339 L22: 2.3861 REMARK 3 L33: 0.4029 L12: 0.8843 REMARK 3 L13: 0.4640 L23: 0.8153 REMARK 3 S TENSOR REMARK 3 S11: 0.0098 S12: 0.2918 S13: -0.2561 REMARK 3 S21: 0.1267 S22: 0.1409 S23: -0.4450 REMARK 3 S31: 0.0294 S32: -0.3402 S33: -0.3499 REMARK 3 TLS GROUP : 41 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 37 THROUGH 78 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.4334 -47.4490 40.5474 REMARK 3 T TENSOR REMARK 3 T11: 0.3894 T22: 1.2595 REMARK 3 T33: 0.2861 T12: 0.1172 REMARK 3 T13: -0.0653 T23: 0.2235 REMARK 3 L TENSOR REMARK 3 L11: 1.2906 L22: 2.4734 REMARK 3 L33: 2.3388 L12: 0.4575 REMARK 3 L13: 0.9032 L23: 0.3013 REMARK 3 S TENSOR REMARK 3 S11: -0.0420 S12: 0.3094 S13: 0.0982 REMARK 3 S21: -0.0126 S22: 0.3062 S23: 0.0163 REMARK 3 S31: -0.0326 S32: -0.5465 S33: -0.2968 REMARK 3 TLS GROUP : 42 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 79 THROUGH 127 ) REMARK 3 ORIGIN FOR THE GROUP (A): 51.9902 -49.9803 34.0175 REMARK 3 T TENSOR REMARK 3 T11: 0.1533 T22: 1.5760 REMARK 3 T33: 0.2555 T12: 0.0605 REMARK 3 T13: -0.3992 T23: 0.0776 REMARK 3 L TENSOR REMARK 3 L11: 0.1711 L22: 0.0709 REMARK 3 L33: 0.7102 L12: -0.0697 REMARK 3 L13: -0.1655 L23: -0.0896 REMARK 3 S TENSOR REMARK 3 S11: 0.2017 S12: 0.5227 S13: -0.1308 REMARK 3 S21: -0.0459 S22: 0.1424 S23: -0.0844 REMARK 3 S31: 0.2620 S32: -0.1993 S33: -0.0880 REMARK 3 TLS GROUP : 43 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 128 THROUGH 221 ) REMARK 3 ORIGIN FOR THE GROUP (A): 68.4404 -50.5967 7.4430 REMARK 3 T TENSOR REMARK 3 T11: 0.4711 T22: 1.6126 REMARK 3 T33: 0.4521 T12: -0.1353 REMARK 3 T13: -0.1897 T23: -0.0581 REMARK 3 L TENSOR REMARK 3 L11: 2.8484 L22: 2.5627 REMARK 3 L33: 0.6268 L12: 1.2968 REMARK 3 L13: 1.2385 L23: 0.1610 REMARK 3 S TENSOR REMARK 3 S11: -0.0888 S12: 0.9961 S13: -0.5418 REMARK 3 S21: -0.2890 S22: 0.2351 S23: -0.4673 REMARK 3 S31: 0.4441 S32: -0.0415 S33: -0.3549 REMARK 3 TLS GROUP : 44 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 1 THROUGH 38 ) REMARK 3 ORIGIN FOR THE GROUP (A): 63.9129 -31.2957 40.3705 REMARK 3 T TENSOR REMARK 3 T11: 0.5716 T22: 0.8801 REMARK 3 T33: 0.4644 T12: 0.1733 REMARK 3 T13: -0.2449 T23: 0.0103 REMARK 3 L TENSOR REMARK 3 L11: 2.6494 L22: 4.6540 REMARK 3 L33: 6.6749 L12: -0.6733 REMARK 3 L13: -2.3832 L23: -0.4363 REMARK 3 S TENSOR REMARK 3 S11: 0.2938 S12: 0.0290 S13: 0.7531 REMARK 3 S21: 0.0525 S22: -0.2531 S23: 0.4645 REMARK 3 S31: -0.9757 S32: -0.3215 S33: 0.1870 REMARK 3 TLS GROUP : 45 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 39 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 68.0043 -38.4692 45.2638 REMARK 3 T TENSOR REMARK 3 T11: 0.4224 T22: 0.7731 REMARK 3 T33: 0.2701 T12: 0.1010 REMARK 3 T13: -0.1176 T23: 0.0663 REMARK 3 L TENSOR REMARK 3 L11: 4.1951 L22: 5.0243 REMARK 3 L33: 7.3627 L12: 1.9525 REMARK 3 L13: -0.4595 L23: -0.4703 REMARK 3 S TENSOR REMARK 3 S11: 0.1015 S12: -0.0911 S13: 0.3112 REMARK 3 S21: 0.2263 S22: 0.5176 S23: -0.2649 REMARK 3 S31: -0.0616 S32: -0.4686 S33: -0.3887 REMARK 3 TLS GROUP : 46 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 76 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): 66.1825 -36.2690 36.2541 REMARK 3 T TENSOR REMARK 3 T11: 0.3557 T22: 0.7108 REMARK 3 T33: 0.4685 T12: 0.1202 REMARK 3 T13: -0.0799 T23: 0.0480 REMARK 3 L TENSOR REMARK 3 L11: 4.7691 L22: 1.3589 REMARK 3 L33: 4.0557 L12: 1.5208 REMARK 3 L13: -2.8954 L23: -1.2188 REMARK 3 S TENSOR REMARK 3 S11: -0.0118 S12: -0.1309 S13: 0.0109 REMARK 3 S21: 0.2553 S22: 0.0005 S23: -0.0490 REMARK 3 S31: -0.7023 S32: -0.2226 S33: 0.0463 REMARK 3 TLS GROUP : 47 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 115 THROUGH 164 ) REMARK 3 ORIGIN FOR THE GROUP (A): 65.2117 -35.3047 4.9955 REMARK 3 T TENSOR REMARK 3 T11: 0.4340 T22: 1.4026 REMARK 3 T33: 0.4060 T12: 0.0402 REMARK 3 T13: 0.0398 T23: 0.1813 REMARK 3 L TENSOR REMARK 3 L11: 3.5911 L22: 1.2800 REMARK 3 L33: 6.1941 L12: 0.4864 REMARK 3 L13: 4.6578 L23: 1.0417 REMARK 3 S TENSOR REMARK 3 S11: -0.2432 S12: 0.7641 S13: 0.3535 REMARK 3 S21: -0.2298 S22: 0.4195 S23: 0.2329 REMARK 3 S31: -0.4912 S32: -0.7432 S33: 0.0506 REMARK 3 TLS GROUP : 48 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 165 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 68.0607 -33.6868 4.5575 REMARK 3 T TENSOR REMARK 3 T11: 0.5121 T22: 1.4832 REMARK 3 T33: 0.6316 T12: 0.1727 REMARK 3 T13: -0.1190 T23: 0.1969 REMARK 3 L TENSOR REMARK 3 L11: 2.7796 L22: 3.2183 REMARK 3 L33: 4.9583 L12: 1.3462 REMARK 3 L13: 3.6893 L23: 1.4998 REMARK 3 S TENSOR REMARK 3 S11: -0.0497 S12: 1.1306 S13: 0.1988 REMARK 3 S21: -0.4549 S22: -0.1049 S23: -0.0716 REMARK 3 S31: -0.4808 S32: -0.5361 S33: 0.0204 REMARK 3 TLS GROUP : 49 REMARK 3 SELECTION: CHAIN 'O' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.7346 -90.0892 40.6423 REMARK 3 T TENSOR REMARK 3 T11: 1.3549 T22: 0.7168 REMARK 3 T33: 0.6088 T12: -0.3712 REMARK 3 T13: -0.0461 T23: 0.0327 REMARK 3 L TENSOR REMARK 3 L11: 5.0370 L22: 1.2609 REMARK 3 L33: 3.7198 L12: -2.2059 REMARK 3 L13: 2.7192 L23: -1.1405 REMARK 3 S TENSOR REMARK 3 S11: -0.2227 S12: -0.0966 S13: 0.5750 REMARK 3 S21: 0.3657 S22: 0.1780 S23: -0.3364 REMARK 3 S31: -1.2055 S32: -0.0262 S33: 0.0017 REMARK 3 TLS GROUP : 50 REMARK 3 SELECTION: CHAIN 'O' AND (RESID 18 THROUGH 62 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.6093 -90.2694 50.4091 REMARK 3 T TENSOR REMARK 3 T11: 0.7592 T22: 0.9237 REMARK 3 T33: 0.4245 T12: -0.1074 REMARK 3 T13: 0.1120 T23: 0.2181 REMARK 3 L TENSOR REMARK 3 L11: 4.3865 L22: 2.9880 REMARK 3 L33: 3.9124 L12: 0.4909 REMARK 3 L13: -0.0040 L23: -1.4716 REMARK 3 S TENSOR REMARK 3 S11: -0.4181 S12: -0.2009 S13: -0.1866 REMARK 3 S21: -0.3743 S22: 0.1253 S23: -0.5236 REMARK 3 S31: 0.5844 S32: -0.8587 S33: 0.2589 REMARK 3 TLS GROUP : 51 REMARK 3 SELECTION: CHAIN 'O' AND (RESID 63 THROUGH 112 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.9899 -88.9812 48.1465 REMARK 3 T TENSOR REMARK 3 T11: 1.0571 T22: 0.6799 REMARK 3 T33: 0.4021 T12: -0.1153 REMARK 3 T13: 0.1009 T23: 0.1381 REMARK 3 L TENSOR REMARK 3 L11: 4.1836 L22: 0.1098 REMARK 3 L33: 3.2930 L12: 0.0183 REMARK 3 L13: -0.9210 L23: 0.5723 REMARK 3 S TENSOR REMARK 3 S11: -0.3216 S12: 0.2436 S13: 0.0056 REMARK 3 S21: -0.8667 S22: 0.0186 S23: -0.3248 REMARK 3 S31: -0.5906 S32: 0.3852 S33: 0.3263 REMARK 3 TLS GROUP : 52 REMARK 3 SELECTION: CHAIN 'O' AND (RESID 113 THROUGH 127 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.5229 -87.6148 28.0758 REMARK 3 T TENSOR REMARK 3 T11: 1.3659 T22: 1.5628 REMARK 3 T33: 0.4145 T12: -0.0981 REMARK 3 T13: 0.1507 T23: 0.0609 REMARK 3 L TENSOR REMARK 3 L11: 2.3899 L22: 6.6083 REMARK 3 L33: 2.7491 L12: -2.6157 REMARK 3 L13: 0.7554 L23: -1.5150 REMARK 3 S TENSOR REMARK 3 S11: -0.3062 S12: 0.8679 S13: -0.1152 REMARK 3 S21: -0.7737 S22: 0.1867 S23: 0.3430 REMARK 3 S31: -0.6873 S32: -0.4676 S33: -0.0267 REMARK 3 TLS GROUP : 53 REMARK 3 SELECTION: CHAIN 'O' AND (RESID 128 THROUGH 196 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.9213 -98.2023 12.9869 REMARK 3 T TENSOR REMARK 3 T11: 1.3516 T22: 1.2268 REMARK 3 T33: 0.5628 T12: -0.0472 REMARK 3 T13: 0.0727 T23: -0.0732 REMARK 3 L TENSOR REMARK 3 L11: 5.0797 L22: 7.1310 REMARK 3 L33: 0.0110 L12: -2.4843 REMARK 3 L13: -0.0501 L23: -0.2211 REMARK 3 S TENSOR REMARK 3 S11: 0.0532 S12: 1.2985 S13: -0.4337 REMARK 3 S21: -1.1888 S22: -0.8059 S23: 0.0788 REMARK 3 S31: -0.5585 S32: -0.9266 S33: 0.6985 REMARK 3 TLS GROUP : 54 REMARK 3 SELECTION: CHAIN 'O' AND (RESID 197 THROUGH 221 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.0030-101.4254 8.7974 REMARK 3 T TENSOR REMARK 3 T11: 1.3453 T22: 1.7622 REMARK 3 T33: 0.7983 T12: 0.2365 REMARK 3 T13: 0.0898 T23: -0.1145 REMARK 3 L TENSOR REMARK 3 L11: 0.8591 L22: 1.6642 REMARK 3 L33: 2.8606 L12: 0.2200 REMARK 3 L13: 0.9515 L23: -1.4613 REMARK 3 S TENSOR REMARK 3 S11: 0.7065 S12: 1.8436 S13: -0.2101 REMARK 3 S21: -1.9064 S22: -0.0123 S23: -0.0402 REMARK 3 S31: -1.1757 S32: -0.6011 S33: -0.6847 REMARK 3 TLS GROUP : 55 REMARK 3 SELECTION: CHAIN 'P' AND (RESID 2 THROUGH 38 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.6786 -97.8344 42.9614 REMARK 3 T TENSOR REMARK 3 T11: 1.0760 T22: 1.7461 REMARK 3 T33: 0.8557 T12: -0.0908 REMARK 3 T13: 0.4112 T23: 0.0820 REMARK 3 L TENSOR REMARK 3 L11: 2.6064 L22: 2.3610 REMARK 3 L33: 0.6370 L12: 0.9877 REMARK 3 L13: 0.9759 L23: -0.3564 REMARK 3 S TENSOR REMARK 3 S11: 0.3274 S12: 0.5166 S13: -0.1871 REMARK 3 S21: -0.6142 S22: -0.2328 S23: -0.7621 REMARK 3 S31: 0.0031 S32: 1.0958 S33: -0.1489 REMARK 3 TLS GROUP : 56 REMARK 3 SELECTION: CHAIN 'P' AND (RESID 39 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.7502-101.8058 42.9308 REMARK 3 T TENSOR REMARK 3 T11: 1.0624 T22: 1.4774 REMARK 3 T33: 0.6857 T12: -0.0537 REMARK 3 T13: 0.2735 T23: 0.0768 REMARK 3 L TENSOR REMARK 3 L11: 1.6502 L22: 1.7033 REMARK 3 L33: 1.6763 L12: 1.3415 REMARK 3 L13: -1.2960 L23: -1.6878 REMARK 3 S TENSOR REMARK 3 S11: -0.3382 S12: -0.0651 S13: -0.4743 REMARK 3 S21: 0.1413 S22: 0.0619 S23: -0.3043 REMARK 3 S31: 0.4887 S32: 1.2369 S33: 0.3039 REMARK 3 TLS GROUP : 57 REMARK 3 SELECTION: CHAIN 'P' AND (RESID 115 THROUGH 211 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.9151 -91.8454 9.6097 REMARK 3 T TENSOR REMARK 3 T11: 1.9775 T22: 1.6199 REMARK 3 T33: 0.6474 T12: -0.3802 REMARK 3 T13: 0.4134 T23: 0.0207 REMARK 3 L TENSOR REMARK 3 L11: 1.0746 L22: 1.9472 REMARK 3 L33: 1.4869 L12: -0.9388 REMARK 3 L13: -0.4970 L23: 0.1302 REMARK 3 S TENSOR REMARK 3 S11: 0.0119 S12: 0.4357 S13: 0.1670 REMARK 3 S21: -0.7197 S22: 0.0306 S23: -0.0473 REMARK 3 S31: -0.3826 S32: -0.1101 S33: -0.0303 REMARK 3 TLS GROUP : 58 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 45 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.7963 -94.9348 71.5107 REMARK 3 T TENSOR REMARK 3 T11: 0.3648 T22: 0.7364 REMARK 3 T33: 0.3724 T12: -0.2131 REMARK 3 T13: 0.0539 T23: 0.2775 REMARK 3 L TENSOR REMARK 3 L11: 4.6532 L22: 3.3728 REMARK 3 L33: 0.6667 L12: -2.6372 REMARK 3 L13: -0.9284 L23: 0.5091 REMARK 3 S TENSOR REMARK 3 S11: 0.2569 S12: -0.9438 S13: 0.1886 REMARK 3 S21: -0.2423 S22: 0.2611 S23: -0.4202 REMARK 3 S31: -0.1270 S32: 0.2719 S33: -0.4130 REMARK 3 TLS GROUP : 59 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 76 THROUGH 169 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.5483 -80.3445 72.9127 REMARK 3 T TENSOR REMARK 3 T11: 0.7414 T22: 0.4098 REMARK 3 T33: 0.4024 T12: -0.1350 REMARK 3 T13: -0.0059 T23: -0.0063 REMARK 3 L TENSOR REMARK 3 L11: 1.0853 L22: 2.2566 REMARK 3 L33: 1.9899 L12: 0.8071 REMARK 3 L13: -0.0274 L23: -1.0150 REMARK 3 S TENSOR REMARK 3 S11: -0.0121 S12: 0.1255 S13: 0.5155 REMARK 3 S21: -0.0767 S22: 0.1012 S23: 0.2919 REMARK 3 S31: -0.5986 S32: 0.1999 S33: -0.0458 REMARK 3 TLS GROUP : 60 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 170 THROUGH 198 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.2010 -90.4007 67.1398 REMARK 3 T TENSOR REMARK 3 T11: 0.6303 T22: 0.9556 REMARK 3 T33: 0.6332 T12: -0.3549 REMARK 3 T13: 0.0833 T23: 0.2410 REMARK 3 L TENSOR REMARK 3 L11: 3.5920 L22: 6.3891 REMARK 3 L33: 2.0319 L12: -2.8029 REMARK 3 L13: 0.5157 L23: -1.1515 REMARK 3 S TENSOR REMARK 3 S11: 0.1241 S12: -0.1549 S13: 0.7748 REMARK 3 S21: -0.7698 S22: -0.5884 S23: -1.4607 REMARK 3 S31: 0.0746 S32: 0.4603 S33: 0.3501 REMARK 3 TLS GROUP : 61 REMARK 3 SELECTION: CHAIN 'N' AND (RESID 44 THROUGH 85 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.3341 -95.8155 74.5956 REMARK 3 T TENSOR REMARK 3 T11: 0.5561 T22: 0.3874 REMARK 3 T33: 0.2350 T12: -0.2056 REMARK 3 T13: 0.1540 T23: 0.0445 REMARK 3 L TENSOR REMARK 3 L11: 1.3896 L22: 0.8490 REMARK 3 L33: 0.9468 L12: 0.2759 REMARK 3 L13: 0.8448 L23: -0.3428 REMARK 3 S TENSOR REMARK 3 S11: -0.2867 S12: 0.0445 S13: 0.0776 REMARK 3 S21: -0.1932 S22: -0.0974 S23: -0.2539 REMARK 3 S31: -0.3529 S32: 0.5440 S33: -0.0187 REMARK 3 TLS GROUP : 62 REMARK 3 SELECTION: CHAIN 'N' AND (RESID 86 THROUGH 201 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.5967-100.5038 74.2625 REMARK 3 T TENSOR REMARK 3 T11: 0.3073 T22: 0.3266 REMARK 3 T33: 0.1955 T12: -0.1208 REMARK 3 T13: -0.1061 T23: 0.0695 REMARK 3 L TENSOR REMARK 3 L11: 4.1674 L22: 2.9439 REMARK 3 L33: 3.0753 L12: -0.6765 REMARK 3 L13: -0.5317 L23: -0.7884 REMARK 3 S TENSOR REMARK 3 S11: -0.0445 S12: 0.1235 S13: -0.3322 REMARK 3 S21: -0.4417 S22: -0.0548 S23: 0.4674 REMARK 3 S31: 0.0372 S32: -0.0761 S33: 0.0059 REMARK 3 TLS GROUP : 63 REMARK 3 SELECTION: CHAIN 'Q' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.7763 -99.0198 104.0030 REMARK 3 T TENSOR REMARK 3 T11: 0.3150 T22: 0.5095 REMARK 3 T33: 0.3794 T12: -0.2244 REMARK 3 T13: 0.0542 T23: 0.0284 REMARK 3 L TENSOR REMARK 3 L11: 2.0550 L22: 1.3776 REMARK 3 L33: 5.1368 L12: -0.9259 REMARK 3 L13: -2.0693 L23: 0.7274 REMARK 3 S TENSOR REMARK 3 S11: 0.7730 S12: -0.2677 S13: 1.1989 REMARK 3 S21: -0.0364 S22: 0.0743 S23: 0.3834 REMARK 3 S31: -0.8942 S32: 0.4344 S33: -0.7345 REMARK 3 TLS GROUP : 64 REMARK 3 SELECTION: CHAIN 'Q' AND (RESID 18 THROUGH 37 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.2944 -98.6002 90.0316 REMARK 3 T TENSOR REMARK 3 T11: 0.3290 T22: 0.7021 REMARK 3 T33: 0.4595 T12: -0.0516 REMARK 3 T13: 0.1142 T23: 0.0662 REMARK 3 L TENSOR REMARK 3 L11: 3.9075 L22: 7.5955 REMARK 3 L33: 3.4955 L12: 0.7347 REMARK 3 L13: 0.8962 L23: -2.5726 REMARK 3 S TENSOR REMARK 3 S11: 0.0991 S12: 1.5433 S13: 0.5304 REMARK 3 S21: -1.0677 S22: -0.0408 S23: -0.9414 REMARK 3 S31: 0.1263 S32: 0.8043 S33: -0.1140 REMARK 3 TLS GROUP : 65 REMARK 3 SELECTION: CHAIN 'Q' AND (RESID 38 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.3543-106.3137 96.9330 REMARK 3 T TENSOR REMARK 3 T11: 0.1384 T22: 0.2994 REMARK 3 T33: 0.1280 T12: 0.0185 REMARK 3 T13: 0.0004 T23: 0.0430 REMARK 3 L TENSOR REMARK 3 L11: 4.1638 L22: 4.1979 REMARK 3 L33: 5.0231 L12: -0.1317 REMARK 3 L13: 0.5262 L23: -0.3599 REMARK 3 S TENSOR REMARK 3 S11: -0.2013 S12: -0.0221 S13: 0.1873 REMARK 3 S21: 0.2143 S22: 0.1212 S23: 0.3366 REMARK 3 S31: -0.0981 S32: -0.2474 S33: 0.0463 REMARK 3 TLS GROUP : 66 REMARK 3 SELECTION: CHAIN 'Q' AND (RESID 103 THROUGH 221 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.9487-104.1946 122.8048 REMARK 3 T TENSOR REMARK 3 T11: 0.2943 T22: 0.5377 REMARK 3 T33: 0.3491 T12: -0.0520 REMARK 3 T13: -0.0466 T23: -0.1914 REMARK 3 L TENSOR REMARK 3 L11: 2.2920 L22: 1.2822 REMARK 3 L33: 1.8286 L12: -0.0632 REMARK 3 L13: 0.2678 L23: -0.3142 REMARK 3 S TENSOR REMARK 3 S11: 0.0221 S12: -0.6196 S13: 0.0265 REMARK 3 S21: 0.4136 S22: 0.1104 S23: -0.1331 REMARK 3 S31: -0.4472 S32: 0.2851 S33: 0.0033 REMARK 3 TLS GROUP : 67 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 1 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.8160-125.3083 98.0218 REMARK 3 T TENSOR REMARK 3 T11: 0.4033 T22: 0.3367 REMARK 3 T33: 0.2908 T12: -0.0917 REMARK 3 T13: 0.0294 T23: -0.0146 REMARK 3 L TENSOR REMARK 3 L11: 1.2432 L22: 1.4941 REMARK 3 L33: 1.4560 L12: 1.1879 REMARK 3 L13: -0.1411 L23: 0.0122 REMARK 3 S TENSOR REMARK 3 S11: -0.2085 S12: 0.5037 S13: -0.2768 REMARK 3 S21: -0.1038 S22: -0.1680 S23: 0.0671 REMARK 3 S31: 0.5618 S32: 0.2529 S33: 0.0931 REMARK 3 TLS GROUP : 68 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 26 THROUGH 61 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.3576-114.9051 90.8784 REMARK 3 T TENSOR REMARK 3 T11: 0.1632 T22: 0.4066 REMARK 3 T33: 0.3268 T12: 0.0588 REMARK 3 T13: 0.0265 T23: 0.0904 REMARK 3 L TENSOR REMARK 3 L11: 3.5651 L22: 4.7140 REMARK 3 L33: 3.4307 L12: -0.3871 REMARK 3 L13: 0.0418 L23: 0.0601 REMARK 3 S TENSOR REMARK 3 S11: -0.3494 S12: 0.2597 S13: -0.1814 REMARK 3 S21: -0.1729 S22: -0.3999 S23: -0.2994 REMARK 3 S31: -0.0459 S32: 0.0970 S33: 0.7352 REMARK 3 TLS GROUP : 69 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 62 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.8241-119.7464 96.8855 REMARK 3 T TENSOR REMARK 3 T11: 0.1862 T22: 0.3440 REMARK 3 T33: 0.2609 T12: -0.0763 REMARK 3 T13: 0.1571 T23: -0.0838 REMARK 3 L TENSOR REMARK 3 L11: 4.0352 L22: 1.4279 REMARK 3 L33: 2.3022 L12: -1.0706 REMARK 3 L13: 2.0917 L23: -1.0251 REMARK 3 S TENSOR REMARK 3 S11: 0.2299 S12: 0.5650 S13: -0.3385 REMARK 3 S21: -0.1444 S22: -0.1087 S23: -0.0912 REMARK 3 S31: 0.5648 S32: -0.1217 S33: -0.1220 REMARK 3 TLS GROUP : 70 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 115 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.9112-120.2763 130.7227 REMARK 3 T TENSOR REMARK 3 T11: 0.2459 T22: 0.7479 REMARK 3 T33: 0.2714 T12: 0.0601 REMARK 3 T13: -0.0802 T23: 0.0337 REMARK 3 L TENSOR REMARK 3 L11: 2.7964 L22: 2.6913 REMARK 3 L33: 5.1995 L12: -0.6780 REMARK 3 L13: -2.3147 L23: 0.9648 REMARK 3 S TENSOR REMARK 3 S11: -0.0484 S12: -0.5996 S13: -0.1426 REMARK 3 S21: 0.5545 S22: -0.0082 S23: 0.0889 REMARK 3 S31: 0.3335 S32: -0.6903 S33: 0.0497 REMARK 3 TLS GROUP : 71 REMARK 3 SELECTION: CHAIN 'U' AND (RESID 1 THROUGH 37 ) REMARK 3 ORIGIN FOR THE GROUP (A): 71.1832 -85.5368 0.7144 REMARK 3 T TENSOR REMARK 3 T11: 0.9436 T22: 0.8132 REMARK 3 T33: 0.4107 T12: 0.1793 REMARK 3 T13: 0.2336 T23: 0.1223 REMARK 3 L TENSOR REMARK 3 L11: 3.0376 L22: 2.4152 REMARK 3 L33: 7.2023 L12: 0.4580 REMARK 3 L13: -0.8335 L23: -0.2250 REMARK 3 S TENSOR REMARK 3 S11: -0.2775 S12: -0.3361 S13: 0.0627 REMARK 3 S21: 1.2830 S22: -0.0662 S23: 0.5437 REMARK 3 S31: 1.7388 S32: 0.4366 S33: 0.3121 REMARK 3 TLS GROUP : 72 REMARK 3 SELECTION: CHAIN 'U' AND (RESID 38 THROUGH 73 ) REMARK 3 ORIGIN FOR THE GROUP (A): 61.7775 -78.5020 1.5979 REMARK 3 T TENSOR REMARK 3 T11: 0.8746 T22: 0.5632 REMARK 3 T33: 0.2009 T12: 0.0260 REMARK 3 T13: 0.2159 T23: 0.0327 REMARK 3 L TENSOR REMARK 3 L11: 4.2434 L22: 1.1570 REMARK 3 L33: 7.0420 L12: 0.6603 REMARK 3 L13: -2.6430 L23: -1.6427 REMARK 3 S TENSOR REMARK 3 S11: 0.3568 S12: 0.3344 S13: 0.1894 REMARK 3 S21: 0.5577 S22: -0.0826 S23: 0.5091 REMARK 3 S31: 0.3493 S32: -0.4299 S33: -0.2423 REMARK 3 TLS GROUP : 73 REMARK 3 SELECTION: CHAIN 'U' AND (RESID 74 THROUGH 127 ) REMARK 3 ORIGIN FOR THE GROUP (A): 66.9888 -84.8655 4.6791 REMARK 3 T TENSOR REMARK 3 T11: 1.4466 T22: 0.6264 REMARK 3 T33: 0.3670 T12: -0.0295 REMARK 3 T13: 0.1343 T23: -0.0079 REMARK 3 L TENSOR REMARK 3 L11: 1.8719 L22: 0.0160 REMARK 3 L33: 5.3577 L12: 0.1385 REMARK 3 L13: -0.4605 L23: -0.1900 REMARK 3 S TENSOR REMARK 3 S11: 0.0702 S12: -0.5473 S13: -0.1392 REMARK 3 S21: 0.9312 S22: -0.0934 S23: 0.1791 REMARK 3 S31: 0.4696 S32: 0.2561 S33: 0.0547 REMARK 3 TLS GROUP : 74 REMARK 3 SELECTION: CHAIN 'U' AND (RESID 128 THROUGH 221 ) REMARK 3 ORIGIN FOR THE GROUP (A): 67.0897-102.3490 32.5690 REMARK 3 T TENSOR REMARK 3 T11: 2.8060 T22: 1.5215 REMARK 3 T33: 0.7804 T12: -0.2754 REMARK 3 T13: 0.2388 T23: 0.0772 REMARK 3 L TENSOR REMARK 3 L11: 2.4724 L22: 0.0944 REMARK 3 L33: 0.4720 L12: 0.3975 REMARK 3 L13: 1.0211 L23: 0.2051 REMARK 3 S TENSOR REMARK 3 S11: 0.4408 S12: -0.5579 S13: -0.6705 REMARK 3 S21: 0.4535 S22: -0.3026 S23: -0.0041 REMARK 3 S31: 0.7749 S32: 0.1027 S33: -0.0442 REMARK 3 TLS GROUP : 75 REMARK 3 SELECTION: CHAIN 'V' AND (RESID 2 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.1823 -94.7595 0.1315 REMARK 3 T TENSOR REMARK 3 T11: 1.4612 T22: 1.2437 REMARK 3 T33: 0.8712 T12: -0.6105 REMARK 3 T13: 0.7235 T23: -0.5244 REMARK 3 L TENSOR REMARK 3 L11: 1.7702 L22: 0.7700 REMARK 3 L33: 1.7038 L12: -0.9842 REMARK 3 L13: -0.9739 L23: 0.6897 REMARK 3 S TENSOR REMARK 3 S11: -0.0642 S12: 0.0693 S13: -0.1239 REMARK 3 S21: 0.4658 S22: -0.3494 S23: 0.4104 REMARK 3 S31: 0.9675 S32: -0.8949 S33: 0.2524 REMARK 3 TLS GROUP : 76 REMARK 3 SELECTION: CHAIN 'V' AND (RESID 76 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): 52.1603 -95.8012 15.8301 REMARK 3 T TENSOR REMARK 3 T11: 2.2078 T22: 0.8687 REMARK 3 T33: 1.0073 T12: -0.3748 REMARK 3 T13: 0.8877 T23: -0.1244 REMARK 3 L TENSOR REMARK 3 L11: 0.7876 L22: 1.4386 REMARK 3 L33: 0.9219 L12: 0.5804 REMARK 3 L13: -0.6853 L23: 0.0601 REMARK 3 S TENSOR REMARK 3 S11: -0.0283 S12: -0.3725 S13: -0.1307 REMARK 3 S21: 1.3079 S22: 0.1269 S23: 0.3787 REMARK 3 S31: 0.7675 S32: -0.1893 S33: -0.0081 REMARK 3 TLS GROUP : 77 REMARK 3 SELECTION: CHAIN 'V' AND (RESID 130 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): 50.3837 -95.8585 35.9475 REMARK 3 T TENSOR REMARK 3 T11: 2.8661 T22: 1.4459 REMARK 3 T33: 0.9119 T12: -0.2533 REMARK 3 T13: 0.9711 T23: 0.1177 REMARK 3 L TENSOR REMARK 3 L11: 0.6965 L22: 0.2041 REMARK 3 L33: 0.2284 L12: 0.2054 REMARK 3 L13: -0.2596 L23: -0.1386 REMARK 3 S TENSOR REMARK 3 S11: -0.2779 S12: -0.4457 S13: -0.3345 REMARK 3 S21: 0.1600 S22: -0.0058 S23: 0.0061 REMARK 3 S31: 0.2938 S32: 0.0861 S33: 0.0122 REMARK 3 TLS GROUP : 78 REMARK 3 SELECTION: CHAIN 'S' AND (RESID 43 THROUGH 89 ) REMARK 3 ORIGIN FOR THE GROUP (A): 71.8783 -80.3340 -21.7316 REMARK 3 T TENSOR REMARK 3 T11: 0.4205 T22: 0.4362 REMARK 3 T33: 0.2805 T12: 0.1730 REMARK 3 T13: 0.0821 T23: -0.1363 REMARK 3 L TENSOR REMARK 3 L11: 5.1832 L22: 1.8664 REMARK 3 L33: 1.4341 L12: 1.5310 REMARK 3 L13: 1.2143 L23: 0.2165 REMARK 3 S TENSOR REMARK 3 S11: 0.4213 S12: 0.1568 S13: -0.3083 REMARK 3 S21: 0.3885 S22: -0.0719 S23: 0.1026 REMARK 3 S31: 0.2018 S32: 0.3953 S33: -0.1877 REMARK 3 TLS GROUP : 79 REMARK 3 SELECTION: CHAIN 'S' AND (RESID 90 THROUGH 140 ) REMARK 3 ORIGIN FOR THE GROUP (A): 68.6051 -67.2275 -25.3638 REMARK 3 T TENSOR REMARK 3 T11: 0.4438 T22: 0.3217 REMARK 3 T33: 0.2928 T12: 0.1173 REMARK 3 T13: 0.0384 T23: -0.0340 REMARK 3 L TENSOR REMARK 3 L11: 2.3657 L22: 2.5322 REMARK 3 L33: 3.4295 L12: 1.6318 REMARK 3 L13: 0.5144 L23: 0.6979 REMARK 3 S TENSOR REMARK 3 S11: 0.0153 S12: 0.5826 S13: 0.2883 REMARK 3 S21: 0.0781 S22: -0.0754 S23: 0.4533 REMARK 3 S31: -0.2214 S32: -0.3217 S33: 0.1214 REMARK 3 TLS GROUP : 80 REMARK 3 SELECTION: CHAIN 'S' AND (RESID 141 THROUGH 169 ) REMARK 3 ORIGIN FOR THE GROUP (A): 80.0453 -61.1266 -16.0583 REMARK 3 T TENSOR REMARK 3 T11: 0.3971 T22: 0.4832 REMARK 3 T33: 0.3736 T12: 0.0843 REMARK 3 T13: -0.0916 T23: -0.0692 REMARK 3 L TENSOR REMARK 3 L11: 1.5672 L22: 4.5324 REMARK 3 L33: 6.0927 L12: 0.9044 REMARK 3 L13: 0.7315 L23: 0.7638 REMARK 3 S TENSOR REMARK 3 S11: -0.1072 S12: -0.1229 S13: 0.1818 REMARK 3 S21: 0.8604 S22: 0.0161 S23: -0.2163 REMARK 3 S31: -0.1816 S32: 0.3283 S33: -0.1713 REMARK 3 TLS GROUP : 81 REMARK 3 SELECTION: CHAIN 'S' AND (RESID 170 THROUGH 199 ) REMARK 3 ORIGIN FOR THE GROUP (A): 57.3266 -78.3880 -18.1475 REMARK 3 T TENSOR REMARK 3 T11: 0.4689 T22: 0.7001 REMARK 3 T33: 0.3627 T12: 0.1718 REMARK 3 T13: 0.1524 T23: -0.1477 REMARK 3 L TENSOR REMARK 3 L11: 2.2479 L22: 3.6441 REMARK 3 L33: 0.8877 L12: 1.7939 REMARK 3 L13: 0.3256 L23: -0.1071 REMARK 3 S TENSOR REMARK 3 S11: -0.0274 S12: 0.2938 S13: 0.2215 REMARK 3 S21: 0.8881 S22: -0.0661 S23: 0.4251 REMARK 3 S31: 0.1959 S32: -0.5285 S33: -0.1354 REMARK 3 TLS GROUP : 82 REMARK 3 SELECTION: CHAIN 'T' AND (RESID 44 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 68.1797 -88.1258 -25.4772 REMARK 3 T TENSOR REMARK 3 T11: 0.4393 T22: 0.3180 REMARK 3 T33: 0.3115 T12: 0.1020 REMARK 3 T13: 0.1086 T23: 0.0083 REMARK 3 L TENSOR REMARK 3 L11: 4.5840 L22: 7.8441 REMARK 3 L33: 4.4364 L12: 3.3152 REMARK 3 L13: 0.2138 L23: -1.5970 REMARK 3 S TENSOR REMARK 3 S11: 0.5217 S12: -0.1106 S13: -0.1329 REMARK 3 S21: 0.7890 S22: 0.0235 S23: 0.2624 REMARK 3 S31: 0.1688 S32: -0.7202 S33: -0.4861 REMARK 3 TLS GROUP : 83 REMARK 3 SELECTION: CHAIN 'T' AND (RESID 76 THROUGH 89 ) REMARK 3 ORIGIN FOR THE GROUP (A): 81.3343 -60.7370 -31.8316 REMARK 3 T TENSOR REMARK 3 T11: 0.6089 T22: 0.3954 REMARK 3 T33: 0.1577 T12: 0.1045 REMARK 3 T13: -0.0114 T23: 0.0115 REMARK 3 L TENSOR REMARK 3 L11: 3.4538 L22: 8.5383 REMARK 3 L33: 1.3463 L12: -0.1591 REMARK 3 L13: 0.4195 L23: 1.0804 REMARK 3 S TENSOR REMARK 3 S11: -0.7284 S12: 0.1739 S13: 0.3491 REMARK 3 S21: -0.6113 S22: 0.3439 S23: -0.2636 REMARK 3 S31: -1.0086 S32: -0.5771 S33: -0.0549 REMARK 3 TLS GROUP : 84 REMARK 3 SELECTION: CHAIN 'T' AND (RESID 90 THROUGH 140 ) REMARK 3 ORIGIN FOR THE GROUP (A): 83.0884 -86.8424 -23.2732 REMARK 3 T TENSOR REMARK 3 T11: 0.3867 T22: 0.5622 REMARK 3 T33: 0.2394 T12: 0.1566 REMARK 3 T13: -0.0902 T23: -0.1597 REMARK 3 L TENSOR REMARK 3 L11: 2.0024 L22: 2.9276 REMARK 3 L33: 1.6829 L12: 0.2507 REMARK 3 L13: 0.2946 L23: 1.9042 REMARK 3 S TENSOR REMARK 3 S11: -0.1744 S12: -0.2648 S13: -0.1945 REMARK 3 S21: 0.3848 S22: 0.4012 S23: -0.4982 REMARK 3 S31: 0.3440 S32: -0.0077 S33: -0.1815 REMARK 3 TLS GROUP : 85 REMARK 3 SELECTION: CHAIN 'T' AND (RESID 141 THROUGH 151 ) REMARK 3 ORIGIN FOR THE GROUP (A): 96.9766 -74.6757 -25.4762 REMARK 3 T TENSOR REMARK 3 T11: 0.4398 T22: 0.5416 REMARK 3 T33: 0.4468 T12: 0.2489 REMARK 3 T13: -0.1842 T23: -0.2290 REMARK 3 L TENSOR REMARK 3 L11: 3.9268 L22: 7.4785 REMARK 3 L33: 6.7150 L12: 0.8326 REMARK 3 L13: -0.7458 L23: -0.3821 REMARK 3 S TENSOR REMARK 3 S11: -0.1455 S12: -0.4475 S13: 0.2990 REMARK 3 S21: 0.4490 S22: 0.2091 S23: -0.7879 REMARK 3 S31: -0.0273 S32: 0.8289 S33: -0.0894 REMARK 3 TLS GROUP : 86 REMARK 3 SELECTION: CHAIN 'T' AND (RESID 152 THROUGH 169 ) REMARK 3 ORIGIN FOR THE GROUP (A): 90.4319 -78.7826 -35.1436 REMARK 3 T TENSOR REMARK 3 T11: 0.5123 T22: 0.5597 REMARK 3 T33: 0.2117 T12: 0.0147 REMARK 3 T13: 0.0709 T23: -0.1710 REMARK 3 L TENSOR REMARK 3 L11: 2.3250 L22: 2.2416 REMARK 3 L33: 2.9606 L12: 0.1455 REMARK 3 L13: -0.5596 L23: -0.6409 REMARK 3 S TENSOR REMARK 3 S11: 0.3305 S12: -0.1874 S13: 0.0750 REMARK 3 S21: -0.3323 S22: -0.0267 S23: -0.3756 REMARK 3 S31: -0.1374 S32: 0.3767 S33: -0.0639 REMARK 3 TLS GROUP : 87 REMARK 3 SELECTION: CHAIN 'T' AND (RESID 170 THROUGH 199 ) REMARK 3 ORIGIN FOR THE GROUP (A): 69.9368 -94.5502 -31.6026 REMARK 3 T TENSOR REMARK 3 T11: 0.3382 T22: 0.6057 REMARK 3 T33: 0.2547 T12: -0.0161 REMARK 3 T13: 0.0261 T23: -0.0837 REMARK 3 L TENSOR REMARK 3 L11: 5.6761 L22: 3.6428 REMARK 3 L33: 2.7179 L12: 2.2447 REMARK 3 L13: -1.0900 L23: -0.3777 REMARK 3 S TENSOR REMARK 3 S11: -0.2656 S12: 0.3396 S13: -0.2639 REMARK 3 S21: -0.2913 S22: 0.1667 S23: 0.4665 REMARK 3 S31: 0.2806 S32: -0.6693 S33: 0.1111 REMARK 3 TLS GROUP : 88 REMARK 3 SELECTION: CHAIN 'W' AND (RESID 1 THROUGH 37 ) REMARK 3 ORIGIN FOR THE GROUP (A): 67.3577 -78.2101 -48.8881 REMARK 3 T TENSOR REMARK 3 T11: 0.3510 T22: 0.2200 REMARK 3 T33: 0.3480 T12: -0.0936 REMARK 3 T13: -0.0764 T23: 0.0668 REMARK 3 L TENSOR REMARK 3 L11: 2.2088 L22: 2.7485 REMARK 3 L33: 5.0006 L12: -0.6155 REMARK 3 L13: 0.8136 L23: 3.1460 REMARK 3 S TENSOR REMARK 3 S11: 0.0912 S12: -0.1193 S13: 0.0119 REMARK 3 S21: 0.4201 S22: -0.2722 S23: -0.2767 REMARK 3 S31: -0.3577 S32: -0.5421 S33: 0.1497 REMARK 3 TLS GROUP : 89 REMARK 3 SELECTION: CHAIN 'W' AND (RESID 38 THROUGH 151 ) REMARK 3 ORIGIN FOR THE GROUP (A): 66.1856 -83.4662 -57.8587 REMARK 3 T TENSOR REMARK 3 T11: 0.1528 T22: 0.1832 REMARK 3 T33: 0.2657 T12: 0.0517 REMARK 3 T13: -0.0620 T23: 0.0555 REMARK 3 L TENSOR REMARK 3 L11: 2.3880 L22: 0.8387 REMARK 3 L33: 3.7523 L12: -0.0933 REMARK 3 L13: 1.3329 L23: -0.5908 REMARK 3 S TENSOR REMARK 3 S11: -0.1405 S12: 0.1648 S13: 0.1450 REMARK 3 S21: -0.1100 S22: 0.0607 S23: 0.0698 REMARK 3 S31: 0.0341 S32: 0.1821 S33: 0.0723 REMARK 3 TLS GROUP : 90 REMARK 3 SELECTION: CHAIN 'W' AND (RESID 152 THROUGH 221 ) REMARK 3 ORIGIN FOR THE GROUP (A): 50.4051 -74.2959 -79.6638 REMARK 3 T TENSOR REMARK 3 T11: 0.2832 T22: 0.5619 REMARK 3 T33: 0.4809 T12: 0.0286 REMARK 3 T13: -0.0867 T23: 0.2048 REMARK 3 L TENSOR REMARK 3 L11: 5.6378 L22: 1.9813 REMARK 3 L33: 1.5460 L12: -0.7342 REMARK 3 L13: 1.5448 L23: 1.1451 REMARK 3 S TENSOR REMARK 3 S11: 0.0710 S12: 0.3630 S13: 0.7344 REMARK 3 S21: -0.3888 S22: 0.1113 S23: 0.3736 REMARK 3 S31: -0.4823 S32: -0.3305 S33: 0.0329 REMARK 3 TLS GROUP : 91 REMARK 3 SELECTION: CHAIN 'X' AND (RESID 1 THROUGH 13 ) REMARK 3 ORIGIN FOR THE GROUP (A): 57.3213-103.3431 -58.9607 REMARK 3 T TENSOR REMARK 3 T11: 0.5332 T22: 0.4284 REMARK 3 T33: 0.7026 T12: 0.0853 REMARK 3 T13: 0.0794 T23: -0.0670 REMARK 3 L TENSOR REMARK 3 L11: 3.2715 L22: 2.8341 REMARK 3 L33: 4.7869 L12: -0.6613 REMARK 3 L13: 3.4753 L23: -0.6203 REMARK 3 S TENSOR REMARK 3 S11: 0.4981 S12: 0.2131 S13: -2.2255 REMARK 3 S21: -0.8796 S22: 0.0321 S23: 0.2579 REMARK 3 S31: 1.1252 S32: 0.6574 S33: -0.5821 REMARK 3 TLS GROUP : 92 REMARK 3 SELECTION: CHAIN 'X' AND (RESID 14 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.7901-103.7407 -55.9572 REMARK 3 T TENSOR REMARK 3 T11: 0.2929 T22: 0.4720 REMARK 3 T33: 0.3437 T12: 0.0687 REMARK 3 T13: 0.0944 T23: -0.0524 REMARK 3 L TENSOR REMARK 3 L11: 7.2837 L22: 4.0668 REMARK 3 L33: 2.6820 L12: -4.1801 REMARK 3 L13: 2.5964 L23: -1.4327 REMARK 3 S TENSOR REMARK 3 S11: -0.0396 S12: -0.2099 S13: -0.7169 REMARK 3 S21: -0.2941 S22: -0.4570 S23: 0.3484 REMARK 3 S31: 0.7041 S32: -0.1238 S33: 0.2285 REMARK 3 TLS GROUP : 93 REMARK 3 SELECTION: CHAIN 'X' AND (RESID 26 THROUGH 61 ) REMARK 3 ORIGIN FOR THE GROUP (A): 53.4789 -95.2493 -47.8012 REMARK 3 T TENSOR REMARK 3 T11: 0.1181 T22: 0.3707 REMARK 3 T33: 0.2167 T12: 0.0362 REMARK 3 T13: -0.0574 T23: -0.0938 REMARK 3 L TENSOR REMARK 3 L11: 4.3737 L22: 3.2374 REMARK 3 L33: 4.7566 L12: 0.1313 REMARK 3 L13: 0.4360 L23: 0.4429 REMARK 3 S TENSOR REMARK 3 S11: 0.0783 S12: 0.0916 S13: -0.4906 REMARK 3 S21: 0.3672 S22: 0.0264 S23: -0.0166 REMARK 3 S31: -0.4392 S32: -0.6013 S33: -0.0163 REMARK 3 TLS GROUP : 94 REMARK 3 SELECTION: CHAIN 'X' AND (RESID 62 THROUGH 151 ) REMARK 3 ORIGIN FOR THE GROUP (A): 51.9711 -93.9131 -68.2481 REMARK 3 T TENSOR REMARK 3 T11: 0.1313 T22: 0.3215 REMARK 3 T33: 0.3034 T12: 0.0683 REMARK 3 T13: -0.0280 T23: 0.0069 REMARK 3 L TENSOR REMARK 3 L11: 2.4608 L22: 0.9486 REMARK 3 L33: 1.4602 L12: 0.9243 REMARK 3 L13: 0.4202 L23: 0.5924 REMARK 3 S TENSOR REMARK 3 S11: 0.0928 S12: 0.5046 S13: -0.1590 REMARK 3 S21: -0.0694 S22: 0.0766 S23: 0.1216 REMARK 3 S31: 0.3143 S32: 0.1187 S33: -0.1304 REMARK 3 TLS GROUP : 95 REMARK 3 SELECTION: CHAIN 'X' AND (RESID 152 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 52.3258 -91.1425 -88.2769 REMARK 3 T TENSOR REMARK 3 T11: 0.4041 T22: 0.7935 REMARK 3 T33: 0.3865 T12: -0.1125 REMARK 3 T13: -0.0182 T23: -0.0189 REMARK 3 L TENSOR REMARK 3 L11: 1.7945 L22: 4.0861 REMARK 3 L33: 4.9712 L12: 0.7175 REMARK 3 L13: -0.0850 L23: -0.8830 REMARK 3 S TENSOR REMARK 3 S11: -0.5598 S12: 1.1827 S13: -0.0786 REMARK 3 S21: -0.6638 S22: 0.0769 S23: -0.4143 REMARK 3 S31: 0.3074 S32: -0.0554 S33: 0.3483 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 9BIF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1000283445. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-DEC-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) : 0.979 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 : 96279 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.090 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 90.8 REMARK 200 DATA REDUNDANCY : 3.100 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.09 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.15 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.33 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM HEPES [PH 6.5], 18.6% REMARK 280 PEG 6K, AND 6.6 MM PRASSEODYMIUM ACETATE, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 16630 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 48490 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -136.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, A, B, C, D 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 16870 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 48060 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -123.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, I, E, F, J, K 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 16800 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 48180 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -132.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, P, M, N, 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 16780 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 48470 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -169.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: U, V, S, T, W, X 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 TYR H 34 REMARK 465 SER H 136 REMARK 465 LYS H 137 REMARK 465 SER H 138 REMARK 465 THR H 139 REMARK 465 SER H 140 REMARK 465 GLY H 141 REMARK 465 LYS H 222 REMARK 465 SER H 223 REMARK 465 CYS H 224 REMARK 465 ASP H 225 REMARK 465 LYS H 226 REMARK 465 THR H 227 REMARK 465 HIS H 228 REMARK 465 CYS L 215 REMARK 465 LYS A 38 REMARK 465 GLY A 39 REMARK 465 PRO A 40 REMARK 465 ASN A 41 REMARK 465 LEU A 42 REMARK 465 THR A 43 REMARK 465 GLU A 44 REMARK 465 SER A 200 REMARK 465 PRO A 201 REMARK 465 LYS B 38 REMARK 465 GLY B 39 REMARK 465 PRO B 40 REMARK 465 ASN B 41 REMARK 465 LEU B 42 REMARK 465 THR B 43 REMARK 465 GLU B 44 REMARK 465 SER C 136 REMARK 465 LYS C 137 REMARK 465 SER C 138 REMARK 465 THR C 139 REMARK 465 SER C 140 REMARK 465 GLY C 141 REMARK 465 LYS C 222 REMARK 465 SER C 223 REMARK 465 CYS C 224 REMARK 465 ASP C 225 REMARK 465 LYS C 226 REMARK 465 THR C 227 REMARK 465 HIS C 228 REMARK 465 SER G 136 REMARK 465 LYS G 137 REMARK 465 SER G 138 REMARK 465 THR G 139 REMARK 465 SER G 140 REMARK 465 GLY G 141 REMARK 465 SER G 223 REMARK 465 CYS G 224 REMARK 465 ASP G 225 REMARK 465 LYS G 226 REMARK 465 THR G 227 REMARK 465 HIS G 228 REMARK 465 GLU I 1 REMARK 465 GLU I 214 REMARK 465 CYS I 215 REMARK 465 LYS E 38 REMARK 465 GLY E 39 REMARK 465 PRO E 40 REMARK 465 ASN E 41 REMARK 465 LEU E 42 REMARK 465 THR E 43 REMARK 465 LYS F 38 REMARK 465 GLY F 39 REMARK 465 PRO F 40 REMARK 465 ASN F 41 REMARK 465 LEU F 42 REMARK 465 THR F 43 REMARK 465 GLU F 44 REMARK 465 THR F 199 REMARK 465 SER F 200 REMARK 465 PRO F 201 REMARK 465 SER J 136 REMARK 465 LYS J 137 REMARK 465 SER J 138 REMARK 465 THR J 139 REMARK 465 SER J 140 REMARK 465 GLY J 141 REMARK 465 LYS J 222 REMARK 465 SER J 223 REMARK 465 CYS J 224 REMARK 465 ASP J 225 REMARK 465 LYS J 226 REMARK 465 THR J 227 REMARK 465 HIS J 228 REMARK 465 CYS K 215 REMARK 465 SER O 136 REMARK 465 LYS O 137 REMARK 465 SER O 138 REMARK 465 THR O 139 REMARK 465 SER O 140 REMARK 465 GLY O 141 REMARK 465 LYS O 222 REMARK 465 SER O 223 REMARK 465 CYS O 224 REMARK 465 ASP O 225 REMARK 465 LYS O 226 REMARK 465 THR O 227 REMARK 465 HIS O 228 REMARK 465 GLU P 1 REMARK 465 ARG P 212 REMARK 465 GLY P 213 REMARK 465 GLU P 214 REMARK 465 CYS P 215 REMARK 465 LYS M 38 REMARK 465 GLY M 39 REMARK 465 PRO M 40 REMARK 465 ASN M 41 REMARK 465 LEU M 42 REMARK 465 THR M 43 REMARK 465 GLU M 44 REMARK 465 THR M 199 REMARK 465 SER M 200 REMARK 465 PRO M 201 REMARK 465 LYS N 38 REMARK 465 GLY N 39 REMARK 465 PRO N 40 REMARK 465 ASN N 41 REMARK 465 LEU N 42 REMARK 465 THR N 43 REMARK 465 SER Q 136 REMARK 465 LYS Q 137 REMARK 465 SER Q 138 REMARK 465 THR Q 139 REMARK 465 SER Q 140 REMARK 465 GLY Q 141 REMARK 465 LYS Q 222 REMARK 465 SER Q 223 REMARK 465 CYS Q 224 REMARK 465 ASP Q 225 REMARK 465 LYS Q 226 REMARK 465 THR Q 227 REMARK 465 HIS Q 228 REMARK 465 CYS R 215 REMARK 465 SER U 33 REMARK 465 TYR U 34 REMARK 465 SER U 136 REMARK 465 LYS U 137 REMARK 465 SER U 138 REMARK 465 THR U 139 REMARK 465 SER U 140 REMARK 465 GLY U 141 REMARK 465 LYS U 222 REMARK 465 SER U 223 REMARK 465 CYS U 224 REMARK 465 ASP U 225 REMARK 465 LYS U 226 REMARK 465 THR U 227 REMARK 465 HIS U 228 REMARK 465 GLU V 1 REMARK 465 GLY V 213 REMARK 465 GLU V 214 REMARK 465 CYS V 215 REMARK 465 LYS S 38 REMARK 465 GLY S 39 REMARK 465 PRO S 40 REMARK 465 ASN S 41 REMARK 465 LEU S 42 REMARK 465 SER S 200 REMARK 465 PRO S 201 REMARK 465 LYS T 38 REMARK 465 GLY T 39 REMARK 465 PRO T 40 REMARK 465 ASN T 41 REMARK 465 LEU T 42 REMARK 465 THR T 43 REMARK 465 SER T 200 REMARK 465 PRO T 201 REMARK 465 SER W 136 REMARK 465 LYS W 137 REMARK 465 SER W 138 REMARK 465 THR W 139 REMARK 465 SER W 140 REMARK 465 GLY W 141 REMARK 465 LYS W 222 REMARK 465 SER W 223 REMARK 465 CYS W 224 REMARK 465 ASP W 225 REMARK 465 LYS W 226 REMARK 465 THR W 227 REMARK 465 HIS W 228 REMARK 465 CYS X 215 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 SER E 200 OG 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 HIS K 190 O HOH K 401 1.80 REMARK 500 O GLY O 101 O HOH O 401 1.83 REMARK 500 O ASP B 51 O HOH B 301 1.83 REMARK 500 O GLU I 188 O HOH I 401 1.85 REMARK 500 O LEU X 126 O HOH X 401 1.91 REMARK 500 OD1 ASN J 58 O HOH J 301 1.92 REMARK 500 OG SER K 122 O HOH K 402 1.96 REMARK 500 O SER V 26 O HOH V 301 1.97 REMARK 500 OG1 THR T 167 O HOH T 401 1.98 REMARK 500 NE2 GLN L 161 O HOH L 401 1.99 REMARK 500 O HIS L 38 O HOH L 402 1.99 REMARK 500 NZ LYS S 75 O HOH S 401 2.00 REMARK 500 O VAL C 215 O HOH C 301 2.00 REMARK 500 O THR H 143 O HOH H 301 2.00 REMARK 500 O CYS C 204 O HOH C 301 2.02 REMARK 500 O SER J 31 OG SER J 33 2.05 REMARK 500 O LYS B 128 O HOH B 302 2.05 REMARK 500 NZ LYS B 188 O HOH B 303 2.05 REMARK 500 N LYS M 185 O HOH M 301 2.05 REMARK 500 O GLN C 79 O HOH C 302 2.07 REMARK 500 N VAL B 55 O HOH B 301 2.08 REMARK 500 O THR O 116 O HOH O 402 2.08 REMARK 500 O HIS I 190 O HOH I 401 2.10 REMARK 500 O HOH W 418 O HOH X 413 2.10 REMARK 500 O ALA Q 133 O HOH Q 301 2.10 REMARK 500 NH2 ARG Q 83 O HOH Q 302 2.10 REMARK 500 OE2 GLU B 157 OG1 THR B 167 2.11 REMARK 500 O ASN P 32 O HOH P 401 2.11 REMARK 500 O TRP Q 36 O HOH Q 303 2.11 REMARK 500 OG SER Q 31 O HOH Q 304 2.12 REMARK 500 OH TYR Q 184 O HOH Q 305 2.12 REMARK 500 O LYS G 222 O HOH G 301 2.13 REMARK 500 O LEU N 65 OG SER N 68 2.13 REMARK 500 OG SER Q 33 O HOH Q 306 2.14 REMARK 500 O HOH G 310 O HOH G 311 2.14 REMARK 500 O ALA M 54 O HOH Q 304 2.14 REMARK 500 O HOH O 402 O HOH O 403 2.15 REMARK 500 O ILE I 107 OH TYR I 141 2.15 REMARK 500 OG SER U 31 O HOH U 301 2.15 REMARK 500 OE1 GLU V 106 OH TYR V 174 2.15 REMARK 500 OH TYR I 36 OE1 GLN I 89 2.15 REMARK 500 O TYR K 187 OH TYR K 193 2.16 REMARK 500 OG SER M 105 OG1 THR M 135 2.17 REMARK 500 O ALA T 158 O HOH T 402 2.17 REMARK 500 ND2 ASN D 31 O ASP D 50 2.17 REMARK 500 N ALA T 170 O HOH T 402 2.17 REMARK 500 O SER I 204 O HOH I 402 2.18 REMARK 500 O ILE T 45 O HOH T 403 2.18 REMARK 500 OE2 GLU X 106 OH TYR X 174 2.18 REMARK 500 NZ LYS E 111 OG SER J 30 2.18 REMARK 500 REMARK 500 THIS ENTRY HAS 54 CLOSE CONTACTS 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 OG1 THR C 168 NH2 ARG X 18 1565 2.15 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 PRO D 95 CD PRO D 95 N -0.116 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 MET H 108 C - N - CA ANGL. DEV. = 18.0 DEGREES REMARK 500 THR C 32 C - N - CA ANGL. DEV. = 16.7 DEGREES REMARK 500 MET C 108 C - N - CA ANGL. DEV. = 17.0 DEGREES REMARK 500 MET G 108 C - N - CA ANGL. DEV. = 18.0 DEGREES REMARK 500 MET J 108 C - N - CA ANGL. DEV. = 15.8 DEGREES REMARK 500 MET O 108 C - N - CA ANGL. DEV. = 15.6 DEGREES REMARK 500 MET Q 108 C - N - CA ANGL. DEV. = 18.1 DEGREES REMARK 500 MET U 108 C - N - CA ANGL. DEV. = 15.3 DEGREES REMARK 500 MET W 108 C - N - CA ANGL. DEV. = 15.8 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER H 63 -3.42 75.27 REMARK 500 SER H 106 -110.69 63.97 REMARK 500 ALA H 122 -134.65 48.04 REMARK 500 ASP L 50 14.60 58.42 REMARK 500 ALA L 51 -4.36 73.79 REMARK 500 ASP A 70 -66.30 122.30 REMARK 500 LYS B 141 31.30 -99.23 REMARK 500 LYS B 196 0.73 -66.61 REMARK 500 SER B 200 152.99 71.24 REMARK 500 SER C 63 141.54 75.32 REMARK 500 SER C 64 -4.63 74.56 REMARK 500 ALA C 90 -1.30 77.32 REMARK 500 LEU C 100 53.01 -91.39 REMARK 500 ALA C 122 -135.24 48.52 REMARK 500 ASP D 50 15.43 56.12 REMARK 500 ALA D 51 -2.47 69.94 REMARK 500 TYR G 34 -173.06 62.31 REMARK 500 SER G 64 -2.14 78.28 REMARK 500 LEU G 100 53.79 -91.53 REMARK 500 ALA G 122 -132.42 45.68 REMARK 500 ASP I 50 19.31 55.02 REMARK 500 ALA I 51 -2.61 70.17 REMARK 500 LYS E 141 31.09 -98.89 REMARK 500 THR E 199 15.82 55.63 REMARK 500 LYS F 196 1.73 -69.16 REMARK 500 ALA J 89 -4.73 75.32 REMARK 500 LEU J 100 31.00 -96.01 REMARK 500 ALA J 122 -137.92 48.48 REMARK 500 ASP K 50 18.77 54.77 REMARK 500 ALA K 51 -2.26 69.38 REMARK 500 TRP K 94 71.20 44.94 REMARK 500 ALA O 89 -2.88 70.79 REMARK 500 LEU O 100 52.91 -91.82 REMARK 500 ALA O 122 -137.65 46.28 REMARK 500 ASP P 50 14.23 58.60 REMARK 500 ALA P 51 -4.40 73.53 REMARK 500 LYS M 141 31.09 -98.43 REMARK 500 LYS N 141 31.82 -98.84 REMARK 500 SER Q 33 -116.06 57.46 REMARK 500 TYR Q 34 -106.79 64.43 REMARK 500 ALA Q 89 -3.03 71.56 REMARK 500 LEU Q 100 53.94 -92.99 REMARK 500 ALA Q 122 -132.63 37.48 REMARK 500 ALA R 51 -3.75 73.89 REMARK 500 PRO R 95 42.37 -87.36 REMARK 500 SER U 64 -3.38 76.24 REMARK 500 ALA U 89 -4.45 73.40 REMARK 500 LEU U 100 53.23 -91.54 REMARK 500 VAL U 110 66.18 39.39 REMARK 500 ALA U 122 -135.14 46.66 REMARK 500 REMARK 500 THIS ENTRY HAS 59 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLU H 6 SER H 7 -148.56 REMARK 500 SER H 31 THR H 32 -34.36 REMARK 500 SER H 76 ARG H 77 -146.84 REMARK 500 MET H 108 ASP H 109 -144.02 REMARK 500 GLU C 6 SER C 7 -127.27 REMARK 500 GLY C 8 PRO C 9 -149.83 REMARK 500 SER C 63 SER C 64 -146.51 REMARK 500 SER C 76 ARG C 77 -145.20 REMARK 500 MET C 108 ASP C 109 -144.55 REMARK 500 SER G 76 ARG G 77 -149.19 REMARK 500 MET G 108 ASP G 109 -139.36 REMARK 500 GLN I 6 SER I 7 -149.53 REMARK 500 ASN I 31 ASN I 32 -145.42 REMARK 500 SER J 31 THR J 32 -112.50 REMARK 500 SER J 33 TYR J 34 138.34 REMARK 500 TYR J 35 TRP J 36 -142.10 REMARK 500 TRP J 36 GLY J 37 -140.41 REMARK 500 SER J 76 ARG J 77 -148.24 REMARK 500 VAL J 87 THR J 88 -148.80 REMARK 500 ASN K 93 TRP K 94 140.92 REMARK 500 TRP K 94 PRO K 95 30.74 REMARK 500 GLU O 6 SER O 7 -145.50 REMARK 500 SER O 76 ARG O 77 -148.96 REMARK 500 VAL O 87 THR O 88 -145.83 REMARK 500 ASN P 93 TRP P 94 -121.02 REMARK 500 GLU Q 6 SER Q 7 -146.34 REMARK 500 GLY Q 8 PRO Q 9 -149.03 REMARK 500 SER Q 31 THR Q 32 -40.97 REMARK 500 SER Q 33 TYR Q 34 -148.10 REMARK 500 SER Q 76 ARG Q 77 -149.81 REMARK 500 MET Q 108 ASP Q 109 -149.75 REMARK 500 GLU U 6 SER U 7 -143.46 REMARK 500 GLY U 8 PRO U 9 -149.40 REMARK 500 SER U 31 THR U 32 -33.24 REMARK 500 GLU W 6 SER W 7 -145.18 REMARK 500 GLY W 8 PRO W 9 -148.13 REMARK 500 THR W 32 SER W 33 -143.14 REMARK 500 SER W 76 ARG W 77 -145.42 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH G 311 DISTANCE = 6.26 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 PR L 301 PR REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN L 32 OD1 REMARK 620 2 HOH L 404 O 105.6 REMARK 620 3 HOH L 407 O 85.0 140.2 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 PR D 301 PR REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 189 OE2 REMARK 620 2 HOH A 403 O 153.2 REMARK 620 3 ASN D 32 OD1 77.4 127.1 REMARK 620 4 ASN D 32 ND2 76.3 128.7 40.0 REMARK 620 5 ASP D 50 OD1 127.4 54.8 119.4 87.9 REMARK 620 6 HOH D 405 O 56.7 131.7 42.0 75.3 161.4 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 PR I 301 PR REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN I 32 OD1 REMARK 620 2 ASP I 50 OD1 73.8 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 PR K 301 PR REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH J 306 O REMARK 620 2 ASN K 32 ND2 81.9 REMARK 620 3 ASP K 50 OD1 82.0 93.3 REMARK 620 4 HOH K 403 O 174.0 92.2 97.2 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 PR P 301 PR REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN P 32 OD1 REMARK 620 2 ASN P 32 ND2 52.6 REMARK 620 3 ASP P 50 OD1 51.8 102.6 REMARK 620 4 GLU M 189 OE2 119.3 105.3 123.2 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 PR R 301 PR REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN R 32 ND2 REMARK 620 2 ASP R 50 OD1 95.4 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 PR S 301 PR REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP V 50 OD1 REMARK 620 2 GLU S 189 OE2 128.0 REMARK 620 3 HOH S 407 O 169.8 49.8 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 PR X 301 PR REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH T 406 O REMARK 620 2 ASN X 32 OD1 101.1 REMARK 620 3 ASN X 32 ND2 70.6 44.0 REMARK 620 4 ASP X 50 OD1 83.1 123.2 88.1 REMARK 620 N 1 2 3 DBREF 9BIF H 1 228 PDB 9BIF 9BIF 1 228 DBREF 9BIF L 1 215 PDB 9BIF 9BIF 1 215 DBREF 9BIF A 38 201 UNP Q07337 OSPC_BORBU 38 201 DBREF 9BIF B 38 201 UNP Q07337 OSPC_BORBU 38 201 DBREF 9BIF C 1 228 PDB 9BIF 9BIF 1 228 DBREF 9BIF D 1 215 PDB 9BIF 9BIF 1 215 DBREF 9BIF G 1 228 PDB 9BIF 9BIF 1 228 DBREF 9BIF I 1 215 PDB 9BIF 9BIF 1 215 DBREF 9BIF E 38 201 UNP Q07337 OSPC_BORBU 38 201 DBREF 9BIF F 38 201 UNP Q07337 OSPC_BORBU 38 201 DBREF 9BIF J 1 228 PDB 9BIF 9BIF 1 228 DBREF 9BIF K 1 215 PDB 9BIF 9BIF 1 215 DBREF 9BIF O 1 228 PDB 9BIF 9BIF 1 228 DBREF 9BIF P 1 215 PDB 9BIF 9BIF 1 215 DBREF 9BIF M 38 201 UNP Q07337 OSPC_BORBU 38 201 DBREF 9BIF N 38 201 UNP Q07337 OSPC_BORBU 38 201 DBREF 9BIF Q 1 228 PDB 9BIF 9BIF 1 228 DBREF 9BIF R 1 215 PDB 9BIF 9BIF 1 215 DBREF 9BIF U 1 228 PDB 9BIF 9BIF 1 228 DBREF 9BIF V 1 215 PDB 9BIF 9BIF 1 215 DBREF 9BIF S 38 201 UNP Q07337 OSPC_BORBU 38 201 DBREF 9BIF T 38 201 UNP Q07337 OSPC_BORBU 38 201 DBREF 9BIF W 1 228 PDB 9BIF 9BIF 1 228 DBREF 9BIF X 1 215 PDB 9BIF 9BIF 1 215 SEQRES 1 H 228 GLN LEU GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 228 PRO SER GLN THR LEU SER LEU THR CYS THR LEU SER GLY SEQRES 3 H 228 GLY SER ILE SER SER THR SER TYR TYR TRP GLY TRP ILE SEQRES 4 H 228 ARG GLN PRO PRO GLY SER GLY LEU GLU TRP ILE GLY SER SEQRES 5 H 228 MET TYR HIS SER GLY ASN THR TYR TYR LYS SER SER LEU SEQRES 6 H 228 LYS GLY ARG VAL THR ILE SER LEU ASP THR SER ARG THR SEQRES 7 H 228 GLN PHE SER LEU ARG LEU THR SER VAL THR ALA ALA ASP SEQRES 8 H 228 THR ALA VAL TYR TYR CYS ALA ARG LEU GLY ASP VAL PHE SEQRES 9 H 228 ASN SER ALA MET ASP VAL TRP GLY GLN GLY THR THR VAL SEQRES 10 H 228 ILE VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 H 228 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 H 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 H 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 H 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 H 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 H 228 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 H 228 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 H 228 LYS SER CYS ASP LYS THR HIS SEQRES 1 L 215 GLU ILE VAL MET THR GLN SER PRO VAL THR LEU SER VAL SEQRES 2 L 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 215 GLN SER VAL GLY ASN ASN LEU ALA TRP TYR GLN HIS LYS SEQRES 4 L 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 L 215 THR ARG ALA THR GLY ILE PRO GLY ARG PHE SER GLY SER SEQRES 6 L 215 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 215 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLU TYR SEQRES 8 L 215 ASN ASN TRP PRO ARG TYR THR PHE GLY GLN GLY ALA LYS SEQRES 9 L 215 LEU GLU ILE ARG ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 A 164 LYS GLY PRO ASN LEU THR GLU ILE SER LYS LYS ILE THR SEQRES 2 A 164 ASP SER ASN ALA VAL LEU LEU ALA VAL LYS GLU VAL GLU SEQRES 3 A 164 ALA LEU LEU SER SER ILE ASP GLU ILE ALA ALA LYS ALA SEQRES 4 A 164 ILE GLY LYS LYS ILE HIS GLN ASN ASN GLY LEU ASP THR SEQRES 5 A 164 GLU ASN ASN HIS ASN GLY SER LEU LEU ALA GLY ALA TYR SEQRES 6 A 164 ALA ILE SER THR LEU ILE LYS GLN LYS LEU ASP GLY LEU SEQRES 7 A 164 LYS ASN GLU GLY LEU LYS GLU LYS ILE ASP ALA ALA LYS SEQRES 8 A 164 LYS CYS SER GLU THR PHE THR ASN LYS LEU LYS GLU LYS SEQRES 9 A 164 HIS THR ASP LEU GLY LYS GLU GLY VAL THR ASP ALA ASP SEQRES 10 A 164 ALA LYS GLU ALA ILE LEU LYS THR ASN GLY THR LYS THR SEQRES 11 A 164 LYS GLY ALA GLU GLU LEU GLY LYS LEU PHE GLU SER VAL SEQRES 12 A 164 GLU VAL LEU SER LYS ALA ALA LYS GLU MET LEU ALA ASN SEQRES 13 A 164 SER VAL LYS GLU LEU THR SER PRO SEQRES 1 B 164 LYS GLY PRO ASN LEU THR GLU ILE SER LYS LYS ILE THR SEQRES 2 B 164 ASP SER ASN ALA VAL LEU LEU ALA VAL LYS GLU VAL GLU SEQRES 3 B 164 ALA LEU LEU SER SER ILE ASP GLU ILE ALA ALA LYS ALA SEQRES 4 B 164 ILE GLY LYS LYS ILE HIS GLN ASN ASN GLY LEU ASP THR SEQRES 5 B 164 GLU ASN ASN HIS ASN GLY SER LEU LEU ALA GLY ALA TYR SEQRES 6 B 164 ALA ILE SER THR LEU ILE LYS GLN LYS LEU ASP GLY LEU SEQRES 7 B 164 LYS ASN GLU GLY LEU LYS GLU LYS ILE ASP ALA ALA LYS SEQRES 8 B 164 LYS CYS SER GLU THR PHE THR ASN LYS LEU LYS GLU LYS SEQRES 9 B 164 HIS THR ASP LEU GLY LYS GLU GLY VAL THR ASP ALA ASP SEQRES 10 B 164 ALA LYS GLU ALA ILE LEU LYS THR ASN GLY THR LYS THR SEQRES 11 B 164 LYS GLY ALA GLU GLU LEU GLY LYS LEU PHE GLU SER VAL SEQRES 12 B 164 GLU VAL LEU SER LYS ALA ALA LYS GLU MET LEU ALA ASN SEQRES 13 B 164 SER VAL LYS GLU LEU THR SER PRO SEQRES 1 C 228 GLN LEU GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 C 228 PRO SER GLN THR LEU SER LEU THR CYS THR LEU SER GLY SEQRES 3 C 228 GLY SER ILE SER SER THR SER TYR TYR TRP GLY TRP ILE SEQRES 4 C 228 ARG GLN PRO PRO GLY SER GLY LEU GLU TRP ILE GLY SER SEQRES 5 C 228 MET TYR HIS SER GLY ASN THR TYR TYR LYS SER SER LEU SEQRES 6 C 228 LYS GLY ARG VAL THR ILE SER LEU ASP THR SER ARG THR SEQRES 7 C 228 GLN PHE SER LEU ARG LEU THR SER VAL THR ALA ALA ASP SEQRES 8 C 228 THR ALA VAL TYR TYR CYS ALA ARG LEU GLY ASP VAL PHE SEQRES 9 C 228 ASN SER ALA MET ASP VAL TRP GLY GLN GLY THR THR VAL SEQRES 10 C 228 ILE VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 C 228 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 C 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 C 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 C 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 C 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 C 228 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 C 228 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 C 228 LYS SER CYS ASP LYS THR HIS SEQRES 1 D 215 GLU ILE VAL MET THR GLN SER PRO VAL THR LEU SER VAL SEQRES 2 D 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 D 215 GLN SER VAL GLY ASN ASN LEU ALA TRP TYR GLN HIS LYS SEQRES 4 D 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 D 215 THR ARG ALA THR GLY ILE PRO GLY ARG PHE SER GLY SER SEQRES 6 D 215 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 D 215 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLU TYR SEQRES 8 D 215 ASN ASN TRP PRO ARG TYR THR PHE GLY GLN GLY ALA LYS SEQRES 9 D 215 LEU GLU ILE ARG ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 D 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 D 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 D 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 D 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 D 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 D 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 D 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 D 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 G 228 GLN LEU GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 G 228 PRO SER GLN THR LEU SER LEU THR CYS THR LEU SER GLY SEQRES 3 G 228 GLY SER ILE SER SER THR SER TYR TYR TRP GLY TRP ILE SEQRES 4 G 228 ARG GLN PRO PRO GLY SER GLY LEU GLU TRP ILE GLY SER SEQRES 5 G 228 MET TYR HIS SER GLY ASN THR TYR TYR LYS SER SER LEU SEQRES 6 G 228 LYS GLY ARG VAL THR ILE SER LEU ASP THR SER ARG THR SEQRES 7 G 228 GLN PHE SER LEU ARG LEU THR SER VAL THR ALA ALA ASP SEQRES 8 G 228 THR ALA VAL TYR TYR CYS ALA ARG LEU GLY ASP VAL PHE SEQRES 9 G 228 ASN SER ALA MET ASP VAL TRP GLY GLN GLY THR THR VAL SEQRES 10 G 228 ILE VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 G 228 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 G 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 G 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 G 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 G 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 G 228 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 G 228 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 G 228 LYS SER CYS ASP LYS THR HIS SEQRES 1 I 215 GLU ILE VAL MET THR GLN SER PRO VAL THR LEU SER VAL SEQRES 2 I 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 I 215 GLN SER VAL GLY ASN ASN LEU ALA TRP TYR GLN HIS LYS SEQRES 4 I 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 I 215 THR ARG ALA THR GLY ILE PRO GLY ARG PHE SER GLY SER SEQRES 6 I 215 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 I 215 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLU TYR SEQRES 8 I 215 ASN ASN TRP PRO ARG TYR THR PHE GLY GLN GLY ALA LYS SEQRES 9 I 215 LEU GLU ILE ARG ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 I 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 I 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 I 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 I 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 I 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 I 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 I 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 I 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 E 164 LYS GLY PRO ASN LEU THR GLU ILE SER LYS LYS ILE THR SEQRES 2 E 164 ASP SER ASN ALA VAL LEU LEU ALA VAL LYS GLU VAL GLU SEQRES 3 E 164 ALA LEU LEU SER SER ILE ASP GLU ILE ALA ALA LYS ALA SEQRES 4 E 164 ILE GLY LYS LYS ILE HIS GLN ASN ASN GLY LEU ASP THR SEQRES 5 E 164 GLU ASN ASN HIS ASN GLY SER LEU LEU ALA GLY ALA TYR SEQRES 6 E 164 ALA ILE SER THR LEU ILE LYS GLN LYS LEU ASP GLY LEU SEQRES 7 E 164 LYS ASN GLU GLY LEU LYS GLU LYS ILE ASP ALA ALA LYS SEQRES 8 E 164 LYS CYS SER GLU THR PHE THR ASN LYS LEU LYS GLU LYS SEQRES 9 E 164 HIS THR ASP LEU GLY LYS GLU GLY VAL THR ASP ALA ASP SEQRES 10 E 164 ALA LYS GLU ALA ILE LEU LYS THR ASN GLY THR LYS THR SEQRES 11 E 164 LYS GLY ALA GLU GLU LEU GLY LYS LEU PHE GLU SER VAL SEQRES 12 E 164 GLU VAL LEU SER LYS ALA ALA LYS GLU MET LEU ALA ASN SEQRES 13 E 164 SER VAL LYS GLU LEU THR SER PRO SEQRES 1 F 164 LYS GLY PRO ASN LEU THR GLU ILE SER LYS LYS ILE THR SEQRES 2 F 164 ASP SER ASN ALA VAL LEU LEU ALA VAL LYS GLU VAL GLU SEQRES 3 F 164 ALA LEU LEU SER SER ILE ASP GLU ILE ALA ALA LYS ALA SEQRES 4 F 164 ILE GLY LYS LYS ILE HIS GLN ASN ASN GLY LEU ASP THR SEQRES 5 F 164 GLU ASN ASN HIS ASN GLY SER LEU LEU ALA GLY ALA TYR SEQRES 6 F 164 ALA ILE SER THR LEU ILE LYS GLN LYS LEU ASP GLY LEU SEQRES 7 F 164 LYS ASN GLU GLY LEU LYS GLU LYS ILE ASP ALA ALA LYS SEQRES 8 F 164 LYS CYS SER GLU THR PHE THR ASN LYS LEU LYS GLU LYS SEQRES 9 F 164 HIS THR ASP LEU GLY LYS GLU GLY VAL THR ASP ALA ASP SEQRES 10 F 164 ALA LYS GLU ALA ILE LEU LYS THR ASN GLY THR LYS THR SEQRES 11 F 164 LYS GLY ALA GLU GLU LEU GLY LYS LEU PHE GLU SER VAL SEQRES 12 F 164 GLU VAL LEU SER LYS ALA ALA LYS GLU MET LEU ALA ASN SEQRES 13 F 164 SER VAL LYS GLU LEU THR SER PRO SEQRES 1 J 228 GLN LEU GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 J 228 PRO SER GLN THR LEU SER LEU THR CYS THR LEU SER GLY SEQRES 3 J 228 GLY SER ILE SER SER THR SER TYR TYR TRP GLY TRP ILE SEQRES 4 J 228 ARG GLN PRO PRO GLY SER GLY LEU GLU TRP ILE GLY SER SEQRES 5 J 228 MET TYR HIS SER GLY ASN THR TYR TYR LYS SER SER LEU SEQRES 6 J 228 LYS GLY ARG VAL THR ILE SER LEU ASP THR SER ARG THR SEQRES 7 J 228 GLN PHE SER LEU ARG LEU THR SER VAL THR ALA ALA ASP SEQRES 8 J 228 THR ALA VAL TYR TYR CYS ALA ARG LEU GLY ASP VAL PHE SEQRES 9 J 228 ASN SER ALA MET ASP VAL TRP GLY GLN GLY THR THR VAL SEQRES 10 J 228 ILE VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 J 228 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 J 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 J 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 J 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 J 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 J 228 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 J 228 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 J 228 LYS SER CYS ASP LYS THR HIS SEQRES 1 K 215 GLU ILE VAL MET THR GLN SER PRO VAL THR LEU SER VAL SEQRES 2 K 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 K 215 GLN SER VAL GLY ASN ASN LEU ALA TRP TYR GLN HIS LYS SEQRES 4 K 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 K 215 THR ARG ALA THR GLY ILE PRO GLY ARG PHE SER GLY SER SEQRES 6 K 215 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 K 215 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLU TYR SEQRES 8 K 215 ASN ASN TRP PRO ARG TYR THR PHE GLY GLN GLY ALA LYS SEQRES 9 K 215 LEU GLU ILE ARG ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 K 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 K 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 K 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 K 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 K 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 K 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 K 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 K 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 O 228 GLN LEU GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 O 228 PRO SER GLN THR LEU SER LEU THR CYS THR LEU SER GLY SEQRES 3 O 228 GLY SER ILE SER SER THR SER TYR TYR TRP GLY TRP ILE SEQRES 4 O 228 ARG GLN PRO PRO GLY SER GLY LEU GLU TRP ILE GLY SER SEQRES 5 O 228 MET TYR HIS SER GLY ASN THR TYR TYR LYS SER SER LEU SEQRES 6 O 228 LYS GLY ARG VAL THR ILE SER LEU ASP THR SER ARG THR SEQRES 7 O 228 GLN PHE SER LEU ARG LEU THR SER VAL THR ALA ALA ASP SEQRES 8 O 228 THR ALA VAL TYR TYR CYS ALA ARG LEU GLY ASP VAL PHE SEQRES 9 O 228 ASN SER ALA MET ASP VAL TRP GLY GLN GLY THR THR VAL SEQRES 10 O 228 ILE VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 O 228 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 O 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 O 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 O 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 O 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 O 228 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 O 228 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 O 228 LYS SER CYS ASP LYS THR HIS SEQRES 1 P 215 GLU ILE VAL MET THR GLN SER PRO VAL THR LEU SER VAL SEQRES 2 P 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 P 215 GLN SER VAL GLY ASN ASN LEU ALA TRP TYR GLN HIS LYS SEQRES 4 P 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 P 215 THR ARG ALA THR GLY ILE PRO GLY ARG PHE SER GLY SER SEQRES 6 P 215 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 P 215 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLU TYR SEQRES 8 P 215 ASN ASN TRP PRO ARG TYR THR PHE GLY GLN GLY ALA LYS SEQRES 9 P 215 LEU GLU ILE ARG ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 P 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 P 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 P 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 P 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 P 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 P 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 P 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 P 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 M 164 LYS GLY PRO ASN LEU THR GLU ILE SER LYS LYS ILE THR SEQRES 2 M 164 ASP SER ASN ALA VAL LEU LEU ALA VAL LYS GLU VAL GLU SEQRES 3 M 164 ALA LEU LEU SER SER ILE ASP GLU ILE ALA ALA LYS ALA SEQRES 4 M 164 ILE GLY LYS LYS ILE HIS GLN ASN ASN GLY LEU ASP THR SEQRES 5 M 164 GLU ASN ASN HIS ASN GLY SER LEU LEU ALA GLY ALA TYR SEQRES 6 M 164 ALA ILE SER THR LEU ILE LYS GLN LYS LEU ASP GLY LEU SEQRES 7 M 164 LYS ASN GLU GLY LEU LYS GLU LYS ILE ASP ALA ALA LYS SEQRES 8 M 164 LYS CYS SER GLU THR PHE THR ASN LYS LEU LYS GLU LYS SEQRES 9 M 164 HIS THR ASP LEU GLY LYS GLU GLY VAL THR ASP ALA ASP SEQRES 10 M 164 ALA LYS GLU ALA ILE LEU LYS THR ASN GLY THR LYS THR SEQRES 11 M 164 LYS GLY ALA GLU GLU LEU GLY LYS LEU PHE GLU SER VAL SEQRES 12 M 164 GLU VAL LEU SER LYS ALA ALA LYS GLU MET LEU ALA ASN SEQRES 13 M 164 SER VAL LYS GLU LEU THR SER PRO SEQRES 1 N 164 LYS GLY PRO ASN LEU THR GLU ILE SER LYS LYS ILE THR SEQRES 2 N 164 ASP SER ASN ALA VAL LEU LEU ALA VAL LYS GLU VAL GLU SEQRES 3 N 164 ALA LEU LEU SER SER ILE ASP GLU ILE ALA ALA LYS ALA SEQRES 4 N 164 ILE GLY LYS LYS ILE HIS GLN ASN ASN GLY LEU ASP THR SEQRES 5 N 164 GLU ASN ASN HIS ASN GLY SER LEU LEU ALA GLY ALA TYR SEQRES 6 N 164 ALA ILE SER THR LEU ILE LYS GLN LYS LEU ASP GLY LEU SEQRES 7 N 164 LYS ASN GLU GLY LEU LYS GLU LYS ILE ASP ALA ALA LYS SEQRES 8 N 164 LYS CYS SER GLU THR PHE THR ASN LYS LEU LYS GLU LYS SEQRES 9 N 164 HIS THR ASP LEU GLY LYS GLU GLY VAL THR ASP ALA ASP SEQRES 10 N 164 ALA LYS GLU ALA ILE LEU LYS THR ASN GLY THR LYS THR SEQRES 11 N 164 LYS GLY ALA GLU GLU LEU GLY LYS LEU PHE GLU SER VAL SEQRES 12 N 164 GLU VAL LEU SER LYS ALA ALA LYS GLU MET LEU ALA ASN SEQRES 13 N 164 SER VAL LYS GLU LEU THR SER PRO SEQRES 1 Q 228 GLN LEU GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 Q 228 PRO SER GLN THR LEU SER LEU THR CYS THR LEU SER GLY SEQRES 3 Q 228 GLY SER ILE SER SER THR SER TYR TYR TRP GLY TRP ILE SEQRES 4 Q 228 ARG GLN PRO PRO GLY SER GLY LEU GLU TRP ILE GLY SER SEQRES 5 Q 228 MET TYR HIS SER GLY ASN THR TYR TYR LYS SER SER LEU SEQRES 6 Q 228 LYS GLY ARG VAL THR ILE SER LEU ASP THR SER ARG THR SEQRES 7 Q 228 GLN PHE SER LEU ARG LEU THR SER VAL THR ALA ALA ASP SEQRES 8 Q 228 THR ALA VAL TYR TYR CYS ALA ARG LEU GLY ASP VAL PHE SEQRES 9 Q 228 ASN SER ALA MET ASP VAL TRP GLY GLN GLY THR THR VAL SEQRES 10 Q 228 ILE VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 Q 228 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 Q 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 Q 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 Q 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 Q 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 Q 228 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 Q 228 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 Q 228 LYS SER CYS ASP LYS THR HIS SEQRES 1 R 215 GLU ILE VAL MET THR GLN SER PRO VAL THR LEU SER VAL SEQRES 2 R 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 R 215 GLN SER VAL GLY ASN ASN LEU ALA TRP TYR GLN HIS LYS SEQRES 4 R 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 R 215 THR ARG ALA THR GLY ILE PRO GLY ARG PHE SER GLY SER SEQRES 6 R 215 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 R 215 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLU TYR SEQRES 8 R 215 ASN ASN TRP PRO ARG TYR THR PHE GLY GLN GLY ALA LYS SEQRES 9 R 215 LEU GLU ILE ARG ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 R 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 R 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 R 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 R 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 R 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 R 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 R 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 R 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 U 228 GLN LEU GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 U 228 PRO SER GLN THR LEU SER LEU THR CYS THR LEU SER GLY SEQRES 3 U 228 GLY SER ILE SER SER THR SER TYR TYR TRP GLY TRP ILE SEQRES 4 U 228 ARG GLN PRO PRO GLY SER GLY LEU GLU TRP ILE GLY SER SEQRES 5 U 228 MET TYR HIS SER GLY ASN THR TYR TYR LYS SER SER LEU SEQRES 6 U 228 LYS GLY ARG VAL THR ILE SER LEU ASP THR SER ARG THR SEQRES 7 U 228 GLN PHE SER LEU ARG LEU THR SER VAL THR ALA ALA ASP SEQRES 8 U 228 THR ALA VAL TYR TYR CYS ALA ARG LEU GLY ASP VAL PHE SEQRES 9 U 228 ASN SER ALA MET ASP VAL TRP GLY GLN GLY THR THR VAL SEQRES 10 U 228 ILE VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 U 228 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 U 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 U 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 U 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 U 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 U 228 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 U 228 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 U 228 LYS SER CYS ASP LYS THR HIS SEQRES 1 V 215 GLU ILE VAL MET THR GLN SER PRO VAL THR LEU SER VAL SEQRES 2 V 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 V 215 GLN SER VAL GLY ASN ASN LEU ALA TRP TYR GLN HIS LYS SEQRES 4 V 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 V 215 THR ARG ALA THR GLY ILE PRO GLY ARG PHE SER GLY SER SEQRES 6 V 215 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 V 215 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLU TYR SEQRES 8 V 215 ASN ASN TRP PRO ARG TYR THR PHE GLY GLN GLY ALA LYS SEQRES 9 V 215 LEU GLU ILE ARG ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 V 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 V 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 V 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 V 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 V 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 V 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 V 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 V 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 S 164 LYS GLY PRO ASN LEU THR GLU ILE SER LYS LYS ILE THR SEQRES 2 S 164 ASP SER ASN ALA VAL LEU LEU ALA VAL LYS GLU VAL GLU SEQRES 3 S 164 ALA LEU LEU SER SER ILE ASP GLU ILE ALA ALA LYS ALA SEQRES 4 S 164 ILE GLY LYS LYS ILE HIS GLN ASN ASN GLY LEU ASP THR SEQRES 5 S 164 GLU ASN ASN HIS ASN GLY SER LEU LEU ALA GLY ALA TYR SEQRES 6 S 164 ALA ILE SER THR LEU ILE LYS GLN LYS LEU ASP GLY LEU SEQRES 7 S 164 LYS ASN GLU GLY LEU LYS GLU LYS ILE ASP ALA ALA LYS SEQRES 8 S 164 LYS CYS SER GLU THR PHE THR ASN LYS LEU LYS GLU LYS SEQRES 9 S 164 HIS THR ASP LEU GLY LYS GLU GLY VAL THR ASP ALA ASP SEQRES 10 S 164 ALA LYS GLU ALA ILE LEU LYS THR ASN GLY THR LYS THR SEQRES 11 S 164 LYS GLY ALA GLU GLU LEU GLY LYS LEU PHE GLU SER VAL SEQRES 12 S 164 GLU VAL LEU SER LYS ALA ALA LYS GLU MET LEU ALA ASN SEQRES 13 S 164 SER VAL LYS GLU LEU THR SER PRO SEQRES 1 T 164 LYS GLY PRO ASN LEU THR GLU ILE SER LYS LYS ILE THR SEQRES 2 T 164 ASP SER ASN ALA VAL LEU LEU ALA VAL LYS GLU VAL GLU SEQRES 3 T 164 ALA LEU LEU SER SER ILE ASP GLU ILE ALA ALA LYS ALA SEQRES 4 T 164 ILE GLY LYS LYS ILE HIS GLN ASN ASN GLY LEU ASP THR SEQRES 5 T 164 GLU ASN ASN HIS ASN GLY SER LEU LEU ALA GLY ALA TYR SEQRES 6 T 164 ALA ILE SER THR LEU ILE LYS GLN LYS LEU ASP GLY LEU SEQRES 7 T 164 LYS ASN GLU GLY LEU LYS GLU LYS ILE ASP ALA ALA LYS SEQRES 8 T 164 LYS CYS SER GLU THR PHE THR ASN LYS LEU LYS GLU LYS SEQRES 9 T 164 HIS THR ASP LEU GLY LYS GLU GLY VAL THR ASP ALA ASP SEQRES 10 T 164 ALA LYS GLU ALA ILE LEU LYS THR ASN GLY THR LYS THR SEQRES 11 T 164 LYS GLY ALA GLU GLU LEU GLY LYS LEU PHE GLU SER VAL SEQRES 12 T 164 GLU VAL LEU SER LYS ALA ALA LYS GLU MET LEU ALA ASN SEQRES 13 T 164 SER VAL LYS GLU LEU THR SER PRO SEQRES 1 W 228 GLN LEU GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 W 228 PRO SER GLN THR LEU SER LEU THR CYS THR LEU SER GLY SEQRES 3 W 228 GLY SER ILE SER SER THR SER TYR TYR TRP GLY TRP ILE SEQRES 4 W 228 ARG GLN PRO PRO GLY SER GLY LEU GLU TRP ILE GLY SER SEQRES 5 W 228 MET TYR HIS SER GLY ASN THR TYR TYR LYS SER SER LEU SEQRES 6 W 228 LYS GLY ARG VAL THR ILE SER LEU ASP THR SER ARG THR SEQRES 7 W 228 GLN PHE SER LEU ARG LEU THR SER VAL THR ALA ALA ASP SEQRES 8 W 228 THR ALA VAL TYR TYR CYS ALA ARG LEU GLY ASP VAL PHE SEQRES 9 W 228 ASN SER ALA MET ASP VAL TRP GLY GLN GLY THR THR VAL SEQRES 10 W 228 ILE VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 W 228 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 W 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 W 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 W 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 W 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 W 228 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 W 228 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 W 228 LYS SER CYS ASP LYS THR HIS SEQRES 1 X 215 GLU ILE VAL MET THR GLN SER PRO VAL THR LEU SER VAL SEQRES 2 X 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 X 215 GLN SER VAL GLY ASN ASN LEU ALA TRP TYR GLN HIS LYS SEQRES 4 X 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 X 215 THR ARG ALA THR GLY ILE PRO GLY ARG PHE SER GLY SER SEQRES 6 X 215 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 X 215 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLU TYR SEQRES 8 X 215 ASN ASN TRP PRO ARG TYR THR PHE GLY GLN GLY ALA LYS SEQRES 9 X 215 LEU GLU ILE ARG ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 X 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 X 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 X 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 X 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 X 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 X 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 X 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 X 215 SER PHE ASN ARG GLY GLU CYS HET PR L 301 1 HET CL A 301 1 HET PR D 301 1 HET PR I 301 1 HET PR K 301 1 HET CL O 301 1 HET PR P 301 1 HET PR R 301 1 HET PR S 301 1 HET CL S 302 1 HET CL T 301 1 HET CL W 301 1 HET PR X 301 1 HET CL X 302 1 HETNAM PR PRASEODYMIUM ION HETNAM CL CHLORIDE ION FORMUL 25 PR 8(PR 3+) FORMUL 26 CL 6(CL 1-) FORMUL 39 HOH *220(H2 O) HELIX 1 AA1 THR H 88 THR H 92 5 5 HELIX 2 AA2 SER H 164 ALA H 166 5 3 HELIX 3 AA3 SER H 195 LEU H 197 5 3 HELIX 4 AA4 GLN L 79 PHE L 83 5 5 HELIX 5 AA5 SER L 122 LYS L 127 1 6 HELIX 6 AA6 LYS L 184 HIS L 190 1 7 HELIX 7 AA7 SER A 46 ALA A 76 1 31 HELIX 8 AA8 ASN A 94 GLY A 114 1 21 HELIX 9 AA9 LEU A 120 LYS A 141 1 22 HELIX 10 AB1 LYS A 141 GLY A 146 1 6 HELIX 11 AB2 THR A 151 LEU A 160 1 10 HELIX 12 AB3 GLY A 169 LYS A 196 1 28 HELIX 13 AB4 GLU A 197 THR A 199 5 3 HELIX 14 AB5 SER B 46 ALA B 76 1 31 HELIX 15 AB6 ASN B 94 LEU B 115 1 22 HELIX 16 AB7 LEU B 120 LYS B 141 1 22 HELIX 17 AB8 LYS B 141 GLY B 146 1 6 HELIX 18 AB9 THR B 151 LEU B 160 1 10 HELIX 19 AC1 GLY B 169 LYS B 196 1 28 HELIX 20 AC2 SER C 164 ALA C 166 5 3 HELIX 21 AC3 SER C 195 LEU C 197 5 3 HELIX 22 AC4 GLN D 79 PHE D 83 5 5 HELIX 23 AC5 SER D 122 LYS D 127 1 6 HELIX 24 AC6 LYS D 184 HIS D 190 1 7 HELIX 25 AC7 THR G 88 THR G 92 5 5 HELIX 26 AC8 SER G 164 ALA G 166 5 3 HELIX 27 AC9 SER G 195 LEU G 197 5 3 HELIX 28 AD1 GLN I 79 PHE I 83 5 5 HELIX 29 AD2 SER I 122 LYS I 127 1 6 HELIX 30 AD3 LYS I 184 HIS I 190 1 7 HELIX 31 AD4 SER E 46 ALA E 76 1 31 HELIX 32 AD5 ASN E 94 LEU E 115 1 22 HELIX 33 AD6 LEU E 120 LYS E 141 1 22 HELIX 34 AD7 LYS E 141 GLY E 146 1 6 HELIX 35 AD8 THR E 151 LEU E 160 1 10 HELIX 36 AD9 GLY E 169 LYS E 196 1 28 HELIX 37 AE1 SER F 46 ALA F 76 1 31 HELIX 38 AE2 ASN F 94 LEU F 115 1 22 HELIX 39 AE3 LEU F 120 LYS F 141 1 22 HELIX 40 AE4 LYS F 141 GLY F 146 1 6 HELIX 41 AE5 THR F 151 LEU F 160 1 10 HELIX 42 AE6 GLY F 169 LYS F 196 1 28 HELIX 43 AE7 SER J 63 LYS J 66 5 4 HELIX 44 AE8 SER J 164 ALA J 166 5 3 HELIX 45 AE9 SER J 195 LEU J 197 5 3 HELIX 46 AF1 GLN K 79 PHE K 83 5 5 HELIX 47 AF2 SER K 122 LYS K 127 1 6 HELIX 48 AF3 LYS K 184 HIS K 190 1 7 HELIX 49 AF4 SER O 63 LYS O 66 5 4 HELIX 50 AF5 SER O 164 ALA O 166 5 3 HELIX 51 AF6 SER O 195 LEU O 197 5 3 HELIX 52 AF7 GLN P 79 PHE P 83 5 5 HELIX 53 AF8 SER P 122 LYS P 127 1 6 HELIX 54 AF9 LYS P 184 HIS P 190 1 7 HELIX 55 AG1 SER M 46 ALA M 76 1 31 HELIX 56 AG2 ASN M 94 LEU M 115 1 22 HELIX 57 AG3 LEU M 120 LYS M 141 1 22 HELIX 58 AG4 LYS M 141 GLY M 146 1 6 HELIX 59 AG5 THR M 151 LEU M 160 1 10 HELIX 60 AG6 GLY M 169 LYS M 196 1 28 HELIX 61 AG7 SER N 46 ALA N 76 1 31 HELIX 62 AG8 ASN N 94 LEU N 115 1 22 HELIX 63 AG9 LEU N 120 LYS N 141 1 22 HELIX 64 AH1 LYS N 141 GLY N 146 1 6 HELIX 65 AH2 THR N 151 LEU N 160 1 10 HELIX 66 AH3 GLY N 169 LYS N 196 1 28 HELIX 67 AH4 SER Q 164 ALA Q 166 5 3 HELIX 68 AH5 SER Q 195 LEU Q 197 5 3 HELIX 69 AH6 GLN R 79 PHE R 83 5 5 HELIX 70 AH7 SER R 122 LYS R 127 1 6 HELIX 71 AH8 LYS R 184 HIS R 190 1 7 HELIX 72 AH9 SER U 164 ALA U 166 5 3 HELIX 73 AI1 SER U 195 LEU U 197 5 3 HELIX 74 AI2 GLN V 79 PHE V 83 5 5 HELIX 75 AI3 SER V 122 LYS V 127 1 6 HELIX 76 AI4 LYS V 184 HIS V 190 1 7 HELIX 77 AI5 GLU S 44 ALA S 76 1 33 HELIX 78 AI6 ASN S 94 LEU S 115 1 22 HELIX 79 AI7 LEU S 120 LYS S 141 1 22 HELIX 80 AI8 LYS S 141 GLY S 146 1 6 HELIX 81 AI9 THR S 151 LEU S 160 1 10 HELIX 82 AJ1 GLY S 169 LYS S 196 1 28 HELIX 83 AJ2 GLU S 197 THR S 199 5 3 HELIX 84 AJ3 SER T 46 ALA T 76 1 31 HELIX 85 AJ4 ASN T 94 LEU T 115 1 22 HELIX 86 AJ5 LEU T 120 LYS T 141 1 22 HELIX 87 AJ6 LYS T 141 GLY T 146 1 6 HELIX 88 AJ7 THR T 151 LEU T 160 1 10 HELIX 89 AJ8 GLY T 169 LYS T 196 1 28 HELIX 90 AJ9 GLU T 197 THR T 199 5 3 HELIX 91 AK1 SER W 164 ALA W 166 5 3 HELIX 92 AK2 SER W 195 LEU W 197 5 3 HELIX 93 AK3 GLN X 79 PHE X 83 5 5 HELIX 94 AK4 SER X 122 LYS X 127 1 6 HELIX 95 AK5 LYS X 184 HIS X 190 1 7 SHEET 1 AA1 4 GLN H 3 GLN H 5 0 SHEET 2 AA1 4 THR H 17 SER H 25 -1 O THR H 23 N GLN H 5 SHEET 3 AA1 4 GLN H 79 THR H 85 -1 O PHE H 80 N CYS H 22 SHEET 4 AA1 4 VAL H 69 LEU H 73 -1 N SER H 72 O SER H 81 SHEET 1 AA2 5 TYR H 60 TYR H 61 0 SHEET 2 AA2 5 GLU H 48 SER H 52 -1 N SER H 52 O TYR H 60 SHEET 3 AA2 5 TRP H 36 GLN H 41 -1 N ARG H 40 O GLU H 48 SHEET 4 AA2 5 ALA H 93 ARG H 99 -1 O TYR H 96 N ILE H 39 SHEET 5 AA2 5 VAL H 110 TRP H 111 -1 O VAL H 110 N ARG H 99 SHEET 1 AA3 5 TYR H 60 TYR H 61 0 SHEET 2 AA3 5 GLU H 48 SER H 52 -1 N SER H 52 O TYR H 60 SHEET 3 AA3 5 TRP H 36 GLN H 41 -1 N ARG H 40 O GLU H 48 SHEET 4 AA3 5 ALA H 93 ARG H 99 -1 O TYR H 96 N ILE H 39 SHEET 5 AA3 5 THR H 115 VAL H 117 -1 O THR H 115 N TYR H 95 SHEET 1 AA4 4 SER H 128 LEU H 132 0 SHEET 2 AA4 4 THR H 143 TYR H 153 -1 O LEU H 149 N PHE H 130 SHEET 3 AA4 4 TYR H 184 PRO H 193 -1 O VAL H 190 N LEU H 146 SHEET 4 AA4 4 VAL H 171 THR H 173 -1 N HIS H 172 O VAL H 189 SHEET 1 AA5 4 SER H 128 LEU H 132 0 SHEET 2 AA5 4 THR H 143 TYR H 153 -1 O LEU H 149 N PHE H 130 SHEET 3 AA5 4 TYR H 184 PRO H 193 -1 O VAL H 190 N LEU H 146 SHEET 4 AA5 4 VAL H 177 LEU H 178 -1 N VAL H 177 O SER H 185 SHEET 1 AA6 3 VAL H 158 TRP H 162 0 SHEET 2 AA6 3 ILE H 203 HIS H 208 -1 O ASN H 205 N SER H 161 SHEET 3 AA6 3 LYS H 214 ARG H 218 -1 O VAL H 215 N VAL H 206 SHEET 1 AA7 4 MET L 4 GLN L 6 0 SHEET 2 AA7 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 GLU L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AA7 4 PHE L 62 SER L 65 -1 N SER L 63 O THR L 74 SHEET 1 AA8 6 THR L 10 VAL L 13 0 SHEET 2 AA8 6 ALA L 103 ILE L 107 1 O GLU L 106 N LEU L 11 SHEET 3 AA8 6 VAL L 85 ASN L 93 -1 N TYR L 86 O ALA L 103 SHEET 4 AA8 6 LEU L 33 HIS L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA8 6 ARG L 45 TYR L 49 -1 O ARG L 45 N GLN L 37 SHEET 6 AA8 6 THR L 53 ARG L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AA9 4 THR L 10 VAL L 13 0 SHEET 2 AA9 4 ALA L 103 ILE L 107 1 O GLU L 106 N LEU L 11 SHEET 3 AA9 4 VAL L 85 ASN L 93 -1 N TYR L 86 O ALA L 103 SHEET 4 AA9 4 ARG L 96 PHE L 99 -1 O ARG L 96 N ASN L 93 SHEET 1 AB1 4 SER L 115 PHE L 119 0 SHEET 2 AB1 4 THR L 130 PHE L 140 -1 O LEU L 136 N PHE L 117 SHEET 3 AB1 4 TYR L 174 SER L 183 -1 O LEU L 180 N VAL L 133 SHEET 4 AB1 4 SER L 160 VAL L 164 -1 N SER L 163 O SER L 177 SHEET 1 AB2 4 ALA L 154 LEU L 155 0 SHEET 2 AB2 4 LYS L 146 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 AB2 4 VAL L 192 THR L 198 -1 O ALA L 194 N LYS L 150 SHEET 4 AB2 4 VAL L 206 ASN L 211 -1 O VAL L 206 N VAL L 197 SHEET 1 AB3 2 LYS A 79 HIS A 82 0 SHEET 2 AB3 2 GLY A 86 THR A 89 -1 O ASP A 88 N LYS A 80 SHEET 1 AB4 2 LYS B 79 HIS B 82 0 SHEET 2 AB4 2 GLY B 86 THR B 89 -1 O ASP B 88 N LYS B 80 SHEET 1 AB5 4 GLN C 3 GLN C 5 0 SHEET 2 AB5 4 GLN C 16 SER C 25 -1 O THR C 23 N GLN C 5 SHEET 3 AB5 4 GLN C 79 VAL C 87 -1 O LEU C 82 N LEU C 20 SHEET 4 AB5 4 VAL C 69 LEU C 73 -1 N SER C 72 O SER C 81 SHEET 1 AB6 6 LEU C 11 VAL C 12 0 SHEET 2 AB6 6 THR C 115 VAL C 119 1 O ILE C 118 N VAL C 12 SHEET 3 AB6 6 ALA C 93 CYS C 97 -1 N TYR C 95 O THR C 115 SHEET 4 AB6 6 TRP C 38 GLN C 41 -1 N ILE C 39 O TYR C 96 SHEET 5 AB6 6 GLU C 48 SER C 52 -1 O GLY C 51 N TRP C 38 SHEET 6 AB6 6 TYR C 60 TYR C 61 -1 O TYR C 60 N SER C 52 SHEET 1 AB7 4 SER C 128 LEU C 132 0 SHEET 2 AB7 4 THR C 143 TYR C 153 -1 O LYS C 151 N SER C 128 SHEET 3 AB7 4 TYR C 184 PRO C 193 -1 O SER C 188 N CYS C 148 SHEET 4 AB7 4 VAL C 171 THR C 173 -1 N HIS C 172 O VAL C 189 SHEET 1 AB8 4 SER C 128 LEU C 132 0 SHEET 2 AB8 4 THR C 143 TYR C 153 -1 O LYS C 151 N SER C 128 SHEET 3 AB8 4 TYR C 184 PRO C 193 -1 O SER C 188 N CYS C 148 SHEET 4 AB8 4 VAL C 177 LEU C 178 -1 N VAL C 177 O SER C 185 SHEET 1 AB9 3 VAL C 158 TRP C 162 0 SHEET 2 AB9 3 TYR C 202 HIS C 208 -1 O ASN C 205 N SER C 161 SHEET 3 AB9 3 THR C 213 VAL C 219 -1 O LYS C 217 N CYS C 204 SHEET 1 AC1 4 MET D 4 GLN D 6 0 SHEET 2 AC1 4 ALA D 19 ALA D 25 -1 O ARG D 24 N THR D 5 SHEET 3 AC1 4 GLU D 70 ILE D 75 -1 O LEU D 73 N LEU D 21 SHEET 4 AC1 4 PHE D 62 SER D 65 -1 N SER D 65 O THR D 72 SHEET 1 AC2 6 THR D 10 VAL D 13 0 SHEET 2 AC2 6 ALA D 103 ILE D 107 1 O GLU D 106 N LEU D 11 SHEET 3 AC2 6 VAL D 85 ASN D 93 -1 N TYR D 86 O ALA D 103 SHEET 4 AC2 6 LEU D 33 HIS D 38 -1 N TYR D 36 O TYR D 87 SHEET 5 AC2 6 ARG D 45 TYR D 49 -1 O ARG D 45 N GLN D 37 SHEET 6 AC2 6 THR D 53 ARG D 54 -1 O THR D 53 N TYR D 49 SHEET 1 AC3 4 THR D 10 VAL D 13 0 SHEET 2 AC3 4 ALA D 103 ILE D 107 1 O GLU D 106 N LEU D 11 SHEET 3 AC3 4 VAL D 85 ASN D 93 -1 N TYR D 86 O ALA D 103 SHEET 4 AC3 4 ARG D 96 PHE D 99 -1 O THR D 98 N GLU D 90 SHEET 1 AC4 4 SER D 115 PHE D 119 0 SHEET 2 AC4 4 THR D 130 PHE D 140 -1 O VAL D 134 N PHE D 119 SHEET 3 AC4 4 TYR D 174 SER D 183 -1 O LEU D 180 N VAL D 133 SHEET 4 AC4 4 SER D 160 VAL D 164 -1 N GLN D 161 O THR D 179 SHEET 1 AC5 4 ALA D 154 LEU D 155 0 SHEET 2 AC5 4 ALA D 145 VAL D 151 -1 N VAL D 151 O ALA D 154 SHEET 3 AC5 4 TYR D 193 HIS D 199 -1 O ALA D 194 N LYS D 150 SHEET 4 AC5 4 VAL D 206 PHE D 210 -1 O VAL D 206 N VAL D 197 SHEET 1 AC6 4 GLN G 3 GLN G 5 0 SHEET 2 AC6 4 THR G 17 SER G 25 -1 O SER G 25 N GLN G 3 SHEET 3 AC6 4 GLN G 79 THR G 85 -1 O LEU G 82 N LEU G 20 SHEET 4 AC6 4 VAL G 69 LEU G 73 -1 N SER G 72 O SER G 81 SHEET 1 AC7 5 TYR G 60 TYR G 61 0 SHEET 2 AC7 5 GLU G 48 SER G 52 -1 N SER G 52 O TYR G 60 SHEET 3 AC7 5 TRP G 38 GLN G 41 -1 N TRP G 38 O ILE G 50 SHEET 4 AC7 5 ALA G 93 CYS G 97 -1 O TYR G 96 N ILE G 39 SHEET 5 AC7 5 THR G 115 VAL G 117 -1 O THR G 115 N TYR G 95 SHEET 1 AC8 4 SER G 128 LEU G 132 0 SHEET 2 AC8 4 THR G 143 TYR G 153 -1 O LEU G 149 N PHE G 130 SHEET 3 AC8 4 TYR G 184 PRO G 193 -1 O TYR G 184 N TYR G 153 SHEET 4 AC8 4 VAL G 171 THR G 173 -1 N HIS G 172 O VAL G 189 SHEET 1 AC9 4 SER G 128 LEU G 132 0 SHEET 2 AC9 4 THR G 143 TYR G 153 -1 O LEU G 149 N PHE G 130 SHEET 3 AC9 4 TYR G 184 PRO G 193 -1 O TYR G 184 N TYR G 153 SHEET 4 AC9 4 VAL G 177 LEU G 178 -1 N VAL G 177 O SER G 185 SHEET 1 AD1 3 VAL G 158 TRP G 162 0 SHEET 2 AD1 3 ILE G 203 HIS G 208 -1 O ASN G 205 N SER G 161 SHEET 3 AD1 3 THR G 213 ARG G 218 -1 O THR G 213 N HIS G 208 SHEET 1 AD2 4 MET I 4 GLN I 6 0 SHEET 2 AD2 4 ALA I 19 ALA I 25 -1 O ARG I 24 N THR I 5 SHEET 3 AD2 4 GLU I 70 ILE I 75 -1 O LEU I 73 N LEU I 21 SHEET 4 AD2 4 PHE I 62 GLY I 64 -1 N SER I 63 O THR I 74 SHEET 1 AD3 2 THR I 10 VAL I 13 0 SHEET 2 AD3 2 LYS I 104 ILE I 107 1 O GLU I 106 N LEU I 11 SHEET 1 AD4 5 THR I 53 ARG I 54 0 SHEET 2 AD4 5 ARG I 45 TYR I 49 -1 N TYR I 49 O THR I 53 SHEET 3 AD4 5 LEU I 33 HIS I 38 -1 N GLN I 37 O ARG I 45 SHEET 4 AD4 5 VAL I 85 ASN I 93 -1 O TYR I 87 N TYR I 36 SHEET 5 AD4 5 ARG I 96 PHE I 99 -1 O ARG I 96 N ASN I 93 SHEET 1 AD5 4 SER I 115 PHE I 119 0 SHEET 2 AD5 4 THR I 130 PHE I 140 -1 O VAL I 134 N PHE I 119 SHEET 3 AD5 4 TYR I 174 SER I 183 -1 O LEU I 182 N ALA I 131 SHEET 4 AD5 4 SER I 160 VAL I 164 -1 N GLN I 161 O THR I 179 SHEET 1 AD6 4 ALA I 154 GLN I 156 0 SHEET 2 AD6 4 LYS I 146 VAL I 151 -1 N TRP I 149 O GLN I 156 SHEET 3 AD6 4 VAL I 192 THR I 198 -1 O ALA I 194 N LYS I 150 SHEET 4 AD6 4 VAL I 206 ASN I 211 -1 O VAL I 206 N VAL I 197 SHEET 1 AD7 2 LYS E 79 HIS E 82 0 SHEET 2 AD7 2 GLY E 86 THR E 89 -1 O ASP E 88 N LYS E 80 SHEET 1 AD8 2 LYS F 79 ILE F 81 0 SHEET 2 AD8 2 LEU F 87 THR F 89 -1 O ASP F 88 N LYS F 80 SHEET 1 AD9 4 GLN J 3 GLN J 5 0 SHEET 2 AD9 4 LEU J 18 SER J 25 -1 O SER J 25 N GLN J 3 SHEET 3 AD9 4 GLN J 79 LEU J 84 -1 O LEU J 82 N LEU J 20 SHEET 4 AD9 4 VAL J 69 LEU J 73 -1 N SER J 72 O SER J 81 SHEET 1 AE1 5 TYR J 60 TYR J 61 0 SHEET 2 AE1 5 GLU J 48 SER J 52 -1 N SER J 52 O TYR J 60 SHEET 3 AE1 5 TRP J 38 GLN J 41 -1 N TRP J 38 O ILE J 50 SHEET 4 AE1 5 ALA J 93 ARG J 99 -1 O TYR J 96 N ILE J 39 SHEET 5 AE1 5 VAL J 110 TRP J 111 -1 O VAL J 110 N ARG J 99 SHEET 1 AE2 5 TYR J 60 TYR J 61 0 SHEET 2 AE2 5 GLU J 48 SER J 52 -1 N SER J 52 O TYR J 60 SHEET 3 AE2 5 TRP J 38 GLN J 41 -1 N TRP J 38 O ILE J 50 SHEET 4 AE2 5 ALA J 93 ARG J 99 -1 O TYR J 96 N ILE J 39 SHEET 5 AE2 5 THR J 115 VAL J 117 -1 O THR J 115 N TYR J 95 SHEET 1 AE3 4 SER J 128 LEU J 132 0 SHEET 2 AE3 4 THR J 143 TYR J 153 -1 O LYS J 151 N SER J 128 SHEET 3 AE3 4 TYR J 184 PRO J 193 -1 O TYR J 184 N TYR J 153 SHEET 4 AE3 4 VAL J 171 THR J 173 -1 N HIS J 172 O VAL J 189 SHEET 1 AE4 4 SER J 128 LEU J 132 0 SHEET 2 AE4 4 THR J 143 TYR J 153 -1 O LYS J 151 N SER J 128 SHEET 3 AE4 4 TYR J 184 PRO J 193 -1 O TYR J 184 N TYR J 153 SHEET 4 AE4 4 VAL J 177 LEU J 178 -1 N VAL J 177 O SER J 185 SHEET 1 AE5 3 VAL J 158 TRP J 162 0 SHEET 2 AE5 3 TYR J 202 HIS J 208 -1 O ASN J 205 N SER J 161 SHEET 3 AE5 3 THR J 213 VAL J 219 -1 O VAL J 215 N VAL J 206 SHEET 1 AE6 4 MET K 4 GLN K 6 0 SHEET 2 AE6 4 ALA K 19 ALA K 25 -1 O ARG K 24 N THR K 5 SHEET 3 AE6 4 GLU K 70 ILE K 75 -1 O LEU K 73 N LEU K 21 SHEET 4 AE6 4 PHE K 62 SER K 65 -1 N SER K 65 O THR K 72 SHEET 1 AE7 6 THR K 10 VAL K 13 0 SHEET 2 AE7 6 ALA K 103 ILE K 107 1 O GLU K 106 N LEU K 11 SHEET 3 AE7 6 VAL K 85 GLU K 90 -1 N TYR K 86 O ALA K 103 SHEET 4 AE7 6 LEU K 33 HIS K 38 -1 N TYR K 36 O TYR K 87 SHEET 5 AE7 6 ARG K 45 TYR K 49 -1 O ARG K 45 N GLN K 37 SHEET 6 AE7 6 THR K 53 ARG K 54 -1 O THR K 53 N TYR K 49 SHEET 1 AE8 4 THR K 10 VAL K 13 0 SHEET 2 AE8 4 ALA K 103 ILE K 107 1 O GLU K 106 N LEU K 11 SHEET 3 AE8 4 VAL K 85 GLU K 90 -1 N TYR K 86 O ALA K 103 SHEET 4 AE8 4 THR K 98 PHE K 99 -1 O THR K 98 N GLU K 90 SHEET 1 AE9 4 SER K 115 PHE K 119 0 SHEET 2 AE9 4 THR K 130 PHE K 140 -1 O VAL K 134 N PHE K 119 SHEET 3 AE9 4 TYR K 174 SER K 183 -1 O LEU K 182 N ALA K 131 SHEET 4 AE9 4 SER K 160 VAL K 164 -1 N GLN K 161 O THR K 179 SHEET 1 AF1 4 ALA K 154 LEU K 155 0 SHEET 2 AF1 4 ALA K 145 VAL K 151 -1 N VAL K 151 O ALA K 154 SHEET 3 AF1 4 VAL K 192 HIS K 199 -1 O THR K 198 N LYS K 146 SHEET 4 AF1 4 VAL K 206 ASN K 211 -1 O VAL K 206 N VAL K 197 SHEET 1 AF2 4 GLN O 3 GLN O 5 0 SHEET 2 AF2 4 LEU O 18 SER O 25 -1 O THR O 23 N GLN O 5 SHEET 3 AF2 4 GLN O 79 LEU O 84 -1 O LEU O 82 N LEU O 20 SHEET 4 AF2 4 VAL O 69 LEU O 73 -1 N THR O 70 O ARG O 83 SHEET 1 AF3 5 TYR O 60 TYR O 61 0 SHEET 2 AF3 5 GLU O 48 SER O 52 -1 N SER O 52 O TYR O 60 SHEET 3 AF3 5 TRP O 38 GLN O 41 -1 N ARG O 40 O GLU O 48 SHEET 4 AF3 5 ALA O 93 CYS O 97 -1 O TYR O 96 N ILE O 39 SHEET 5 AF3 5 THR O 115 VAL O 117 -1 O THR O 115 N TYR O 95 SHEET 1 AF4 4 SER O 128 LEU O 132 0 SHEET 2 AF4 4 THR O 143 TYR O 153 -1 O LYS O 151 N SER O 128 SHEET 3 AF4 4 TYR O 184 PRO O 193 -1 O SER O 188 N CYS O 148 SHEET 4 AF4 4 VAL O 171 THR O 173 -1 N HIS O 172 O VAL O 189 SHEET 1 AF5 4 SER O 128 LEU O 132 0 SHEET 2 AF5 4 THR O 143 TYR O 153 -1 O LYS O 151 N SER O 128 SHEET 3 AF5 4 TYR O 184 PRO O 193 -1 O SER O 188 N CYS O 148 SHEET 4 AF5 4 VAL O 177 LEU O 178 -1 N VAL O 177 O SER O 185 SHEET 1 AF6 3 VAL O 158 TRP O 162 0 SHEET 2 AF6 3 ILE O 203 HIS O 208 -1 O ASN O 205 N SER O 161 SHEET 3 AF6 3 THR O 213 ARG O 218 -1 O VAL O 215 N VAL O 206 SHEET 1 AF7 4 MET P 4 GLN P 6 0 SHEET 2 AF7 4 ALA P 19 ALA P 25 -1 O ARG P 24 N THR P 5 SHEET 3 AF7 4 GLU P 70 ILE P 75 -1 O LEU P 73 N LEU P 21 SHEET 4 AF7 4 PHE P 62 GLY P 64 -1 N SER P 63 O THR P 74 SHEET 1 AF8 6 THR P 10 SER P 12 0 SHEET 2 AF8 6 ALA P 103 GLU P 106 1 O GLU P 106 N LEU P 11 SHEET 3 AF8 6 VAL P 85 ASN P 93 -1 N TYR P 86 O ALA P 103 SHEET 4 AF8 6 LEU P 33 HIS P 38 -1 N TYR P 36 O TYR P 87 SHEET 5 AF8 6 ARG P 45 TYR P 49 -1 O ARG P 45 N GLN P 37 SHEET 6 AF8 6 THR P 53 ARG P 54 -1 O THR P 53 N TYR P 49 SHEET 1 AF9 4 THR P 10 SER P 12 0 SHEET 2 AF9 4 ALA P 103 GLU P 106 1 O GLU P 106 N LEU P 11 SHEET 3 AF9 4 VAL P 85 ASN P 93 -1 N TYR P 86 O ALA P 103 SHEET 4 AF9 4 ARG P 96 PHE P 99 -1 O THR P 98 N GLU P 90 SHEET 1 AG1 4 SER P 115 PHE P 119 0 SHEET 2 AG1 4 THR P 130 PHE P 140 -1 O LEU P 136 N PHE P 117 SHEET 3 AG1 4 TYR P 174 SER P 183 -1 O LEU P 180 N VAL P 133 SHEET 4 AG1 4 SER P 160 VAL P 164 -1 N SER P 163 O SER P 177 SHEET 1 AG2 4 ALA P 154 GLN P 156 0 SHEET 2 AG2 4 LYS P 146 VAL P 151 -1 N TRP P 149 O GLN P 156 SHEET 3 AG2 4 TYR P 193 THR P 198 -1 O ALA P 194 N LYS P 150 SHEET 4 AG2 4 VAL P 206 PHE P 210 -1 O VAL P 206 N VAL P 197 SHEET 1 AG3 2 LYS M 79 HIS M 82 0 SHEET 2 AG3 2 GLY M 86 THR M 89 -1 O ASP M 88 N LYS M 80 SHEET 1 AG4 2 LYS N 79 LYS N 80 0 SHEET 2 AG4 2 ASP N 88 THR N 89 -1 O ASP N 88 N LYS N 80 SHEET 1 AG5 4 GLN Q 3 GLN Q 5 0 SHEET 2 AG5 4 THR Q 17 SER Q 25 -1 O THR Q 23 N GLN Q 5 SHEET 3 AG5 4 GLN Q 79 THR Q 85 -1 O LEU Q 82 N LEU Q 20 SHEET 4 AG5 4 VAL Q 69 LEU Q 73 -1 N SER Q 72 O SER Q 81 SHEET 1 AG6 6 LEU Q 11 VAL Q 12 0 SHEET 2 AG6 6 THR Q 115 VAL Q 119 1 O ILE Q 118 N VAL Q 12 SHEET 3 AG6 6 ALA Q 93 ARG Q 99 -1 N TYR Q 95 O THR Q 115 SHEET 4 AG6 6 TRP Q 38 GLN Q 41 -1 N ILE Q 39 O TYR Q 96 SHEET 5 AG6 6 GLU Q 48 SER Q 52 -1 O GLU Q 48 N ARG Q 40 SHEET 6 AG6 6 TYR Q 60 TYR Q 61 -1 O TYR Q 60 N SER Q 52 SHEET 1 AG7 4 LEU Q 11 VAL Q 12 0 SHEET 2 AG7 4 THR Q 115 VAL Q 119 1 O ILE Q 118 N VAL Q 12 SHEET 3 AG7 4 ALA Q 93 ARG Q 99 -1 N TYR Q 95 O THR Q 115 SHEET 4 AG7 4 VAL Q 110 TRP Q 111 -1 O VAL Q 110 N ARG Q 99 SHEET 1 AG8 4 SER Q 128 LEU Q 132 0 SHEET 2 AG8 4 THR Q 143 TYR Q 153 -1 O LYS Q 151 N SER Q 128 SHEET 3 AG8 4 TYR Q 184 PRO Q 193 -1 O TYR Q 184 N TYR Q 153 SHEET 4 AG8 4 VAL Q 171 THR Q 173 -1 N HIS Q 172 O VAL Q 189 SHEET 1 AG9 4 SER Q 128 LEU Q 132 0 SHEET 2 AG9 4 THR Q 143 TYR Q 153 -1 O LYS Q 151 N SER Q 128 SHEET 3 AG9 4 TYR Q 184 PRO Q 193 -1 O TYR Q 184 N TYR Q 153 SHEET 4 AG9 4 VAL Q 177 LEU Q 178 -1 N VAL Q 177 O SER Q 185 SHEET 1 AH1 3 VAL Q 158 TRP Q 162 0 SHEET 2 AH1 3 TYR Q 202 HIS Q 208 -1 O ASN Q 205 N SER Q 161 SHEET 3 AH1 3 THR Q 213 VAL Q 219 -1 O VAL Q 215 N VAL Q 206 SHEET 1 AH2 4 MET R 4 GLN R 6 0 SHEET 2 AH2 4 ALA R 19 ALA R 25 -1 O ARG R 24 N THR R 5 SHEET 3 AH2 4 GLU R 70 ILE R 75 -1 O LEU R 73 N LEU R 21 SHEET 4 AH2 4 PHE R 62 SER R 65 -1 N SER R 65 O THR R 72 SHEET 1 AH3 6 THR R 10 VAL R 13 0 SHEET 2 AH3 6 ALA R 103 ILE R 107 1 O GLU R 106 N LEU R 11 SHEET 3 AH3 6 VAL R 85 GLU R 90 -1 N TYR R 86 O ALA R 103 SHEET 4 AH3 6 LEU R 33 HIS R 38 -1 N TYR R 36 O TYR R 87 SHEET 5 AH3 6 ARG R 45 TYR R 49 -1 O LEU R 47 N TRP R 35 SHEET 6 AH3 6 THR R 53 ARG R 54 -1 O THR R 53 N TYR R 49 SHEET 1 AH4 4 THR R 10 VAL R 13 0 SHEET 2 AH4 4 ALA R 103 ILE R 107 1 O GLU R 106 N LEU R 11 SHEET 3 AH4 4 VAL R 85 GLU R 90 -1 N TYR R 86 O ALA R 103 SHEET 4 AH4 4 THR R 98 PHE R 99 -1 O THR R 98 N GLU R 90 SHEET 1 AH5 4 SER R 115 PHE R 119 0 SHEET 2 AH5 4 THR R 130 PHE R 140 -1 O LEU R 136 N PHE R 117 SHEET 3 AH5 4 TYR R 174 SER R 183 -1 O LEU R 180 N VAL R 133 SHEET 4 AH5 4 SER R 160 VAL R 164 -1 N GLN R 161 O THR R 179 SHEET 1 AH6 4 ALA R 154 LEU R 155 0 SHEET 2 AH6 4 ALA R 145 VAL R 151 -1 N VAL R 151 O ALA R 154 SHEET 3 AH6 4 VAL R 192 HIS R 199 -1 O ALA R 194 N LYS R 150 SHEET 4 AH6 4 VAL R 206 ASN R 211 -1 O VAL R 206 N VAL R 197 SHEET 1 AH7 4 GLN U 3 GLN U 5 0 SHEET 2 AH7 4 LEU U 18 SER U 25 -1 O THR U 23 N GLN U 5 SHEET 3 AH7 4 GLN U 79 LEU U 84 -1 O LEU U 82 N LEU U 20 SHEET 4 AH7 4 VAL U 69 LEU U 73 -1 N SER U 72 O SER U 81 SHEET 1 AH8 5 TYR U 60 TYR U 61 0 SHEET 2 AH8 5 GLU U 48 SER U 52 -1 N SER U 52 O TYR U 60 SHEET 3 AH8 5 TRP U 38 GLN U 41 -1 N ARG U 40 O GLU U 48 SHEET 4 AH8 5 ALA U 93 CYS U 97 -1 O TYR U 96 N ILE U 39 SHEET 5 AH8 5 THR U 115 VAL U 117 -1 O THR U 115 N TYR U 95 SHEET 1 AH9 4 SER U 128 LEU U 132 0 SHEET 2 AH9 4 THR U 143 TYR U 153 -1 O LEU U 149 N PHE U 130 SHEET 3 AH9 4 TYR U 184 PRO U 193 -1 O VAL U 192 N ALA U 144 SHEET 4 AH9 4 VAL U 171 THR U 173 -1 N HIS U 172 O VAL U 189 SHEET 1 AI1 4 SER U 128 LEU U 132 0 SHEET 2 AI1 4 THR U 143 TYR U 153 -1 O LEU U 149 N PHE U 130 SHEET 3 AI1 4 TYR U 184 PRO U 193 -1 O VAL U 192 N ALA U 144 SHEET 4 AI1 4 VAL U 177 LEU U 178 -1 N VAL U 177 O SER U 185 SHEET 1 AI2 3 VAL U 158 TRP U 162 0 SHEET 2 AI2 3 TYR U 202 HIS U 208 -1 O ASN U 205 N SER U 161 SHEET 3 AI2 3 THR U 213 VAL U 219 -1 O VAL U 219 N TYR U 202 SHEET 1 AI3 4 MET V 4 GLN V 6 0 SHEET 2 AI3 4 ALA V 19 ALA V 25 -1 O ARG V 24 N THR V 5 SHEET 3 AI3 4 THR V 72 ILE V 75 -1 O LEU V 73 N LEU V 21 SHEET 4 AI3 4 PHE V 62 SER V 65 -1 N SER V 65 O THR V 72 SHEET 1 AI4 6 THR V 10 VAL V 13 0 SHEET 2 AI4 6 ALA V 103 ILE V 107 1 O GLU V 106 N LEU V 11 SHEET 3 AI4 6 VAL V 85 ASN V 93 -1 N TYR V 86 O ALA V 103 SHEET 4 AI4 6 LEU V 33 HIS V 38 -1 N HIS V 38 O VAL V 85 SHEET 5 AI4 6 ARG V 45 TYR V 49 -1 O ARG V 45 N GLN V 37 SHEET 6 AI4 6 THR V 53 ARG V 54 -1 O THR V 53 N TYR V 49 SHEET 1 AI5 4 THR V 10 VAL V 13 0 SHEET 2 AI5 4 ALA V 103 ILE V 107 1 O GLU V 106 N LEU V 11 SHEET 3 AI5 4 VAL V 85 ASN V 93 -1 N TYR V 86 O ALA V 103 SHEET 4 AI5 4 ARG V 96 PHE V 99 -1 O ARG V 96 N ASN V 93 SHEET 1 AI6 4 SER V 115 PHE V 119 0 SHEET 2 AI6 4 THR V 130 PHE V 140 -1 O LEU V 136 N PHE V 117 SHEET 3 AI6 4 TYR V 174 SER V 183 -1 O LEU V 180 N VAL V 133 SHEET 4 AI6 4 SER V 160 VAL V 164 -1 N SER V 163 O SER V 177 SHEET 1 AI7 4 ALA V 154 LEU V 155 0 SHEET 2 AI7 4 ALA V 145 VAL V 151 -1 N VAL V 151 O ALA V 154 SHEET 3 AI7 4 VAL V 192 HIS V 199 -1 O ALA V 194 N LYS V 150 SHEET 4 AI7 4 VAL V 206 ASN V 211 -1 O VAL V 206 N VAL V 197 SHEET 1 AI8 2 LYS S 79 HIS S 82 0 SHEET 2 AI8 2 GLY S 86 THR S 89 -1 O ASP S 88 N LYS S 80 SHEET 1 AI9 2 LYS T 79 HIS T 82 0 SHEET 2 AI9 2 GLY T 86 THR T 89 -1 O ASP T 88 N LYS T 80 SHEET 1 AJ1 4 GLN W 3 GLN W 5 0 SHEET 2 AJ1 4 THR W 17 SER W 25 -1 O THR W 23 N GLN W 5 SHEET 3 AJ1 4 GLN W 79 THR W 85 -1 O LEU W 82 N LEU W 20 SHEET 4 AJ1 4 VAL W 69 LEU W 73 -1 N SER W 72 O SER W 81 SHEET 1 AJ2 5 TYR W 60 TYR W 61 0 SHEET 2 AJ2 5 GLU W 48 SER W 52 -1 N SER W 52 O TYR W 60 SHEET 3 AJ2 5 TRP W 38 GLN W 41 -1 N ARG W 40 O GLU W 48 SHEET 4 AJ2 5 ALA W 93 ARG W 99 -1 O TYR W 96 N ILE W 39 SHEET 5 AJ2 5 VAL W 110 TRP W 111 -1 O VAL W 110 N ARG W 99 SHEET 1 AJ3 5 TYR W 60 TYR W 61 0 SHEET 2 AJ3 5 GLU W 48 SER W 52 -1 N SER W 52 O TYR W 60 SHEET 3 AJ3 5 TRP W 38 GLN W 41 -1 N ARG W 40 O GLU W 48 SHEET 4 AJ3 5 ALA W 93 ARG W 99 -1 O TYR W 96 N ILE W 39 SHEET 5 AJ3 5 THR W 115 VAL W 117 -1 O THR W 115 N TYR W 95 SHEET 1 AJ4 4 SER W 128 LEU W 132 0 SHEET 2 AJ4 4 THR W 143 TYR W 153 -1 O LYS W 151 N SER W 128 SHEET 3 AJ4 4 TYR W 184 PRO W 193 -1 O VAL W 190 N LEU W 146 SHEET 4 AJ4 4 VAL W 171 THR W 173 -1 N HIS W 172 O VAL W 189 SHEET 1 AJ5 4 SER W 128 LEU W 132 0 SHEET 2 AJ5 4 THR W 143 TYR W 153 -1 O LYS W 151 N SER W 128 SHEET 3 AJ5 4 TYR W 184 PRO W 193 -1 O VAL W 190 N LEU W 146 SHEET 4 AJ5 4 VAL W 177 LEU W 178 -1 N VAL W 177 O SER W 185 SHEET 1 AJ6 3 VAL W 158 TRP W 162 0 SHEET 2 AJ6 3 TYR W 202 HIS W 208 -1 O ASN W 205 N SER W 161 SHEET 3 AJ6 3 THR W 213 VAL W 219 -1 O THR W 213 N HIS W 208 SHEET 1 AJ7 4 MET X 4 GLN X 6 0 SHEET 2 AJ7 4 ALA X 19 ALA X 25 -1 O ARG X 24 N THR X 5 SHEET 3 AJ7 4 GLU X 70 ILE X 75 -1 O LEU X 73 N LEU X 21 SHEET 4 AJ7 4 PHE X 62 SER X 65 -1 N SER X 63 O THR X 74 SHEET 1 AJ8 6 THR X 10 VAL X 13 0 SHEET 2 AJ8 6 ALA X 103 ILE X 107 1 O GLU X 106 N LEU X 11 SHEET 3 AJ8 6 VAL X 85 ASN X 93 -1 N TYR X 86 O ALA X 103 SHEET 4 AJ8 6 LEU X 33 HIS X 38 -1 N TYR X 36 O TYR X 87 SHEET 5 AJ8 6 ARG X 45 TYR X 49 -1 O LEU X 47 N TRP X 35 SHEET 6 AJ8 6 THR X 53 ARG X 54 -1 O THR X 53 N TYR X 49 SHEET 1 AJ9 4 THR X 10 VAL X 13 0 SHEET 2 AJ9 4 ALA X 103 ILE X 107 1 O GLU X 106 N LEU X 11 SHEET 3 AJ9 4 VAL X 85 ASN X 93 -1 N TYR X 86 O ALA X 103 SHEET 4 AJ9 4 ARG X 96 PHE X 99 -1 O THR X 98 N GLU X 90 SHEET 1 AK1 4 SER X 115 PHE X 119 0 SHEET 2 AK1 4 THR X 130 PHE X 140 -1 O ASN X 138 N SER X 115 SHEET 3 AK1 4 TYR X 174 SER X 183 -1 O LEU X 176 N LEU X 137 SHEET 4 AK1 4 SER X 160 VAL X 164 -1 N GLN X 161 O THR X 179 SHEET 1 AK2 4 ALA X 154 LEU X 155 0 SHEET 2 AK2 4 ALA X 145 VAL X 151 -1 N VAL X 151 O ALA X 154 SHEET 3 AK2 4 VAL X 192 HIS X 199 -1 O THR X 198 N LYS X 146 SHEET 4 AK2 4 VAL X 206 ASN X 211 -1 O VAL X 206 N VAL X 197 SSBOND 1 CYS H 22 CYS H 97 1555 1555 2.03 SSBOND 2 CYS H 148 CYS H 204 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 4 CYS L 135 CYS L 195 1555 1555 2.04 SSBOND 5 CYS C 22 CYS C 97 1555 1555 2.03 SSBOND 6 CYS C 148 CYS C 204 1555 1555 2.03 SSBOND 7 CYS D 23 CYS D 88 1555 1555 2.04 SSBOND 8 CYS D 135 CYS D 195 1555 1555 2.03 SSBOND 9 CYS G 22 CYS G 97 1555 1555 2.03 SSBOND 10 CYS G 148 CYS G 204 1555 1555 2.03 SSBOND 11 CYS I 23 CYS I 88 1555 1555 2.04 SSBOND 12 CYS I 135 CYS I 195 1555 1555 2.04 SSBOND 13 CYS J 22 CYS J 97 1555 1555 2.02 SSBOND 14 CYS J 148 CYS J 204 1555 1555 2.03 SSBOND 15 CYS K 23 CYS K 88 1555 1555 2.04 SSBOND 16 CYS K 135 CYS K 195 1555 1555 2.04 SSBOND 17 CYS O 22 CYS O 97 1555 1555 2.04 SSBOND 18 CYS O 148 CYS O 204 1555 1555 2.03 SSBOND 19 CYS P 23 CYS P 88 1555 1555 2.04 SSBOND 20 CYS P 135 CYS P 195 1555 1555 2.03 SSBOND 21 CYS Q 22 CYS Q 97 1555 1555 2.03 SSBOND 22 CYS Q 148 CYS Q 204 1555 1555 2.03 SSBOND 23 CYS R 23 CYS R 88 1555 1555 2.04 SSBOND 24 CYS R 135 CYS R 195 1555 1555 2.04 SSBOND 25 CYS U 22 CYS U 97 1555 1555 2.03 SSBOND 26 CYS U 148 CYS U 204 1555 1555 2.03 SSBOND 27 CYS V 23 CYS V 88 1555 1555 2.04 SSBOND 28 CYS V 135 CYS V 195 1555 1555 2.03 SSBOND 29 CYS W 22 CYS W 97 1555 1555 2.03 SSBOND 30 CYS W 148 CYS W 204 1555 1555 2.03 SSBOND 31 CYS X 23 CYS X 88 1555 1555 2.04 SSBOND 32 CYS X 135 CYS X 195 1555 1555 2.03 LINK OD1 ASN L 32 PR PR L 301 1555 1555 2.36 LINK PR PR L 301 O HOH L 404 1555 1555 2.33 LINK PR PR L 301 O HOH L 407 1555 1555 2.44 LINK OE2 GLU A 189 PR PR D 301 1555 1555 3.25 LINK O HOH A 403 PR PR D 301 1555 1555 3.15 LINK OD1 ASN D 32 PR PR D 301 1555 1555 3.49 LINK ND2 ASN D 32 PR PR D 301 1555 1555 2.56 LINK OD1 ASP D 50 PR PR D 301 1555 1555 2.60 LINK PR PR D 301 O HOH D 405 1555 1555 2.46 LINK OD1 ASN I 32 PR PR I 301 1555 1555 3.07 LINK OD1 ASP I 50 PR PR I 301 1555 1555 2.82 LINK O HOH J 306 PR PR K 301 1555 1555 2.45 LINK ND2 ASN K 32 PR PR K 301 1555 1555 2.91 LINK OD1 ASP K 50 PR PR K 301 1555 1555 2.83 LINK PR PR K 301 O HOH K 403 1555 1555 2.45 LINK OD1 ASN P 32 PR PR P 301 1555 1555 2.46 LINK ND2 ASN P 32 PR PR P 301 1555 1555 2.60 LINK OD1 ASP P 50 PR PR P 301 1555 1555 3.49 LINK PR PR P 301 OE2 GLU M 189 1555 1555 3.01 LINK ND2 ASN R 32 PR PR R 301 1555 1555 2.68 LINK OD1 ASP R 50 PR PR R 301 1555 1555 3.42 LINK OD1 ASP V 50 PR PR S 301 1555 1555 3.27 LINK OE2 GLU S 189 PR PR S 301 1555 1555 3.17 LINK PR PR S 301 O HOH S 407 1555 1555 2.87 LINK O HOH T 406 PR PR X 301 1555 1555 2.52 LINK OD1 ASN X 32 PR PR X 301 1555 1555 3.20 LINK ND2 ASN X 32 PR PR X 301 1555 1555 2.62 LINK OD1 ASP X 50 PR PR X 301 1555 1555 2.99 CISPEP 1 THR H 85 SER H 86 0 -1.42 CISPEP 2 ALA H 107 MET H 108 0 -7.32 CISPEP 3 PHE H 154 PRO H 155 0 -1.47 CISPEP 4 GLU H 156 PRO H 157 0 3.77 CISPEP 5 TYR L 141 PRO L 142 0 6.34 CISPEP 6 SER C 31 THR C 32 0 -21.07 CISPEP 7 THR C 85 SER C 86 0 -2.52 CISPEP 8 ALA C 107 MET C 108 0 -10.81 CISPEP 9 PHE C 154 PRO C 155 0 -2.96 CISPEP 10 GLU C 156 PRO C 157 0 3.04 CISPEP 11 TYR D 141 PRO D 142 0 3.51 CISPEP 12 THR G 85 SER G 86 0 -1.44 CISPEP 13 ALA G 107 MET G 108 0 -6.45 CISPEP 14 PHE G 154 PRO G 155 0 -3.83 CISPEP 15 GLU G 156 PRO G 157 0 2.86 CISPEP 16 TYR I 141 PRO I 142 0 9.28 CISPEP 17 THR J 85 SER J 86 0 3.09 CISPEP 18 ALA J 107 MET J 108 0 -7.40 CISPEP 19 PHE J 154 PRO J 155 0 -3.53 CISPEP 20 GLU J 156 PRO J 157 0 2.64 CISPEP 21 TYR K 141 PRO K 142 0 4.55 CISPEP 22 SER O 31 THR O 32 0 -23.54 CISPEP 23 THR O 85 SER O 86 0 1.67 CISPEP 24 ALA O 107 MET O 108 0 -10.26 CISPEP 25 PHE O 154 PRO O 155 0 -2.62 CISPEP 26 GLU O 156 PRO O 157 0 3.75 CISPEP 27 TYR P 141 PRO P 142 0 3.69 CISPEP 28 GLU N 44 ILE N 45 0 14.94 CISPEP 29 THR Q 85 SER Q 86 0 1.07 CISPEP 30 ALA Q 107 MET Q 108 0 -8.99 CISPEP 31 PHE Q 154 PRO Q 155 0 -5.93 CISPEP 32 GLU Q 156 PRO Q 157 0 4.04 CISPEP 33 TRP R 94 PRO R 95 0 18.75 CISPEP 34 TYR R 141 PRO R 142 0 4.42 CISPEP 35 THR U 85 SER U 86 0 0.15 CISPEP 36 ALA U 107 MET U 108 0 -4.48 CISPEP 37 PHE U 154 PRO U 155 0 -2.87 CISPEP 38 GLU U 156 PRO U 157 0 -0.50 CISPEP 39 TRP V 94 PRO V 95 0 -8.56 CISPEP 40 TYR V 141 PRO V 142 0 6.52 CISPEP 41 SER W 31 THR W 32 0 -26.87 CISPEP 42 THR W 85 SER W 86 0 -1.32 CISPEP 43 ALA W 107 MET W 108 0 -8.11 CISPEP 44 PHE W 154 PRO W 155 0 -3.83 CISPEP 45 GLU W 156 PRO W 157 0 1.28 CISPEP 46 TRP X 94 PRO X 95 0 15.58 CISPEP 47 TYR X 141 PRO X 142 0 6.25 CRYST1 96.737 97.294 168.343 97.60 90.27 106.21 P 1 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.010337 0.003005 0.000471 0.00000 SCALE2 0.000000 0.010704 0.001504 0.00000 SCALE3 0.000000 0.000000 0.005999 0.00000