HEADER ANTITOXIN/TOXIN 29-MAR-22 7UIE TITLE CRYSTAL STRUCTURE OF HCE-JLE-G6 COMPND MOL_ID: 1; COMPND 2 MOLECULE: JLE-G6; COMPND 3 CHAIN: B, C, E, I, G; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: BOTULINUM NEUROTOXIN E HEAVY CHAIN; COMPND 7 CHAIN: A, D, F, H, J; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 3 ORGANISM_TAXID: 30538; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: CLOSTRIDIUM BOTULINUM; SOURCE 8 ORGANISM_TAXID: 1491; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS SINGLE DOMAIN ANTIBODY, BOTULINUM NEUROTOXIN, VHH, RECEPTOR, KEYWDS 2 ANTITOXIN, ANTITOXIN-TOXIN COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR R.JIN,K.LAM REVDAT 3 08-NOV-23 7UIE 1 JRNL REVDAT 2 25-OCT-23 7UIE 1 REMARK REVDAT 1 05-APR-23 7UIE 0 JRNL AUTH Z.LIU,P.G.LEE,N.KREZ,K.H.LAM,H.LIU,A.PRZYKOPANSKI,P.CHEN, JRNL AUTH 2 G.YAO,S.ZHANG,J.M.TREMBLAY,K.PERRY,C.B.SHOEMAKER,A.RUMMEL, JRNL AUTH 3 M.DONG,R.JIN JRNL TITL STRUCTURAL BASIS FOR BOTULINUM NEUROTOXIN E RECOGNITION OF JRNL TITL 2 SYNAPTIC VESICLE PROTEIN 2. JRNL REF NAT COMMUN V. 14 2338 2023 JRNL REFN ESSN 2041-1723 JRNL PMID 37095076 JRNL DOI 10.1038/S41467-023-37860-8 REMARK 2 REMARK 2 RESOLUTION. 3.23 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 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) : 3.23 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 135.41 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 3 NUMBER OF REFLECTIONS : 53969 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.232 REMARK 3 R VALUE (WORKING SET) : 0.230 REMARK 3 FREE R VALUE : 0.273 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.850 REMARK 3 FREE R VALUE TEST SET COUNT : 4868 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1135.4100 - 10.0400 0.95 3120 157 0.1877 0.2174 REMARK 3 2 10.0400 - 7.9700 0.97 3122 205 0.1983 0.2448 REMARK 3 3 7.9700 - 6.9600 0.97 3166 187 0.2168 0.2672 REMARK 3 4 6.9600 - 6.3200 0.98 3197 141 0.2125 0.2527 REMARK 3 5 6.3200 - 5.8700 0.98 3232 177 0.2137 0.2610 REMARK 3 6 5.8700 - 5.5200 0.98 3168 179 0.1984 0.2665 REMARK 3 7 5.5200 - 5.2500 0.98 3222 137 0.2001 0.2089 REMARK 3 8 5.2500 - 5.0200 0.98 3242 139 0.1842 0.2719 REMARK 3 9 5.0200 - 4.8200 0.98 3201 170 0.1816 0.2411 REMARK 3 10 4.8200 - 4.6600 0.98 3205 161 0.1810 0.2046 REMARK 3 11 4.6600 - 4.5100 0.97 3194 173 0.1791 0.2155 REMARK 3 12 4.5100 - 4.3800 0.98 3247 130 0.1919 0.2352 REMARK 3 13 4.3800 - 4.2700 0.98 3191 170 0.1963 0.2567 REMARK 3 14 4.2700 - 4.1600 0.98 3190 178 0.2077 0.2842 REMARK 3 15 4.1600 - 4.0700 0.97 3159 183 0.2245 0.2568 REMARK 3 16 4.0700 - 3.9800 0.98 3199 157 0.2345 0.2205 REMARK 3 17 3.9800 - 3.9000 0.97 3221 160 0.2379 0.3334 REMARK 3 18 3.9000 - 3.8300 0.98 3196 165 0.2544 0.2928 REMARK 3 19 3.8300 - 3.7600 0.97 3177 163 0.2579 0.2988 REMARK 3 20 3.7600 - 3.7000 0.97 3168 155 0.2734 0.3299 REMARK 3 21 3.7000 - 3.6400 0.97 3198 158 0.2995 0.3570 REMARK 3 22 3.6400 - 3.5800 0.97 3202 173 0.3116 0.3681 REMARK 3 23 3.5800 - 3.5300 0.97 3193 137 0.3260 0.3334 REMARK 3 24 3.5300 - 3.4800 0.97 3202 169 0.3257 0.3620 REMARK 3 25 3.4800 - 3.4300 0.97 3105 172 0.3261 0.3452 REMARK 3 26 3.4300 - 3.3900 0.97 3194 168 0.3419 0.3983 REMARK 3 27 3.3900 - 3.3500 0.96 3201 158 0.3377 0.3644 REMARK 3 28 3.3500 - 3.3100 0.97 3141 156 0.3598 0.3802 REMARK 3 29 3.3100 - 3.2700 0.97 3166 156 0.3792 0.4014 REMARK 3 30 3.2700 - 3.2300 0.95 3173 134 0.3703 0.3643 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.500 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.490 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 : 0.002 21768 REMARK 3 ANGLE : 0.484 29628 REMARK 3 CHIRALITY : 0.046 3248 REMARK 3 PLANARITY : 0.003 3837 REMARK 3 DIHEDRAL : 13.017 7706 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 54 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): 64.4304 9.2263 70.7497 REMARK 3 T TENSOR REMARK 3 T11: 0.8956 T22: 0.9666 REMARK 3 T33: 0.6308 T12: 0.3148 REMARK 3 T13: -0.0579 T23: 0.1531 REMARK 3 L TENSOR REMARK 3 L11: 1.3322 L22: 2.1993 REMARK 3 L33: 0.4127 L12: -0.0882 REMARK 3 L13: -0.4514 L23: -0.4813 REMARK 3 S TENSOR REMARK 3 S11: 0.0801 S12: -0.6471 S13: -0.6108 REMARK 3 S21: 0.0333 S22: -0.1210 S23: -0.4083 REMARK 3 S31: 0.2506 S32: 0.4463 S33: 0.0202 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 40 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): 60.5343 18.6266 77.2598 REMARK 3 T TENSOR REMARK 3 T11: 1.0302 T22: 0.8204 REMARK 3 T33: 0.5680 T12: 0.2798 REMARK 3 T13: -0.0761 T23: 0.0672 REMARK 3 L TENSOR REMARK 3 L11: 2.7078 L22: 2.4175 REMARK 3 L33: 2.8050 L12: 0.4455 REMARK 3 L13: -0.3922 L23: 0.1436 REMARK 3 S TENSOR REMARK 3 S11: -0.0711 S12: -0.5745 S13: 0.0925 REMARK 3 S21: 0.6830 S22: 0.0009 S23: 0.0262 REMARK 3 S31: -0.1818 S32: 0.0346 S33: 0.1467 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 52 THROUGH 122 ) REMARK 3 ORIGIN FOR THE GROUP (A): 63.3393 16.0867 69.6379 REMARK 3 T TENSOR REMARK 3 T11: 0.7855 T22: 0.9666 REMARK 3 T33: 0.6815 T12: 0.2285 REMARK 3 T13: -0.1814 T23: 0.1170 REMARK 3 L TENSOR REMARK 3 L11: 2.0493 L22: 1.1710 REMARK 3 L33: 1.1102 L12: -0.0472 REMARK 3 L13: 0.5671 L23: -0.6302 REMARK 3 S TENSOR REMARK 3 S11: -0.4408 S12: -0.0551 S13: 0.2282 REMARK 3 S21: 0.3717 S22: -0.0042 S23: -0.6011 REMARK 3 S31: -0.2190 S32: 0.6536 S33: 0.3618 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 123 THROUGH 130 ) REMARK 3 ORIGIN FOR THE GROUP (A): 69.7364 9.4039 86.5603 REMARK 3 T TENSOR REMARK 3 T11: 1.2375 T22: 1.6411 REMARK 3 T33: 0.5966 T12: 0.5935 REMARK 3 T13: -0.3305 T23: -0.0284 REMARK 3 L TENSOR REMARK 3 L11: 0.2437 L22: 1.5037 REMARK 3 L33: 1.7717 L12: 0.1248 REMARK 3 L13: 0.3782 L23: -1.1151 REMARK 3 S TENSOR REMARK 3 S11: -0.2155 S12: 0.0840 S13: 0.2024 REMARK 3 S21: 0.1600 S22: 0.1616 S23: -0.1840 REMARK 3 S31: -0.3769 S32: 0.4048 S33: 0.4358 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 847 THROUGH 886 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.7879 33.3699 27.5685 REMARK 3 T TENSOR REMARK 3 T11: 0.4390 T22: 0.4632 REMARK 3 T33: 0.3282 T12: 0.0820 REMARK 3 T13: -0.0240 T23: -0.0514 REMARK 3 L TENSOR REMARK 3 L11: 1.3720 L22: 3.1674 REMARK 3 L33: 5.4248 L12: -0.3445 REMARK 3 L13: -0.2453 L23: -1.0591 REMARK 3 S TENSOR REMARK 3 S11: 0.0261 S12: 0.1245 S13: 0.3331 REMARK 3 S21: 0.1819 S22: -0.1028 S23: -0.0760 REMARK 3 S31: 0.0520 S32: -0.7394 S33: 0.0447 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 887 THROUGH 1050 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.8626 20.3191 22.2561 REMARK 3 T TENSOR REMARK 3 T11: 0.4448 T22: 0.5393 REMARK 3 T33: 0.4283 T12: 0.0200 REMARK 3 T13: -0.0141 T23: -0.0345 REMARK 3 L TENSOR REMARK 3 L11: 1.5713 L22: 1.4092 REMARK 3 L33: 1.9330 L12: 0.2270 REMARK 3 L13: 0.8430 L23: -0.2407 REMARK 3 S TENSOR REMARK 3 S11: 0.2379 S12: 0.3659 S13: -0.1890 REMARK 3 S21: -0.2611 S22: -0.0916 S23: -0.0400 REMARK 3 S31: 0.4308 S32: 0.0719 S33: -0.1216 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1051 THROUGH 1131 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.1364 22.0672 48.3946 REMARK 3 T TENSOR REMARK 3 T11: 0.5453 T22: 0.4962 REMARK 3 T33: 0.3707 T12: 0.0149 REMARK 3 T13: -0.0095 T23: 0.0248 REMARK 3 L TENSOR REMARK 3 L11: 0.8851 L22: 1.0452 REMARK 3 L33: 1.8546 L12: -0.1078 REMARK 3 L13: 0.2179 L23: 0.1623 REMARK 3 S TENSOR REMARK 3 S11: -0.2230 S12: -0.0114 S13: -0.0534 REMARK 3 S21: 0.1945 S22: 0.3524 S23: -0.0581 REMARK 3 S31: 0.2048 S32: -0.3163 S33: -0.1181 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1132 THROUGH 1164 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.4124 31.0542 59.2740 REMARK 3 T TENSOR REMARK 3 T11: 0.6084 T22: 0.4976 REMARK 3 T33: 0.5269 T12: -0.0326 REMARK 3 T13: 0.0048 T23: -0.0923 REMARK 3 L TENSOR REMARK 3 L11: 2.7964 L22: 1.9159 REMARK 3 L33: 5.1210 L12: 0.7421 REMARK 3 L13: -0.9740 L23: -0.0780 REMARK 3 S TENSOR REMARK 3 S11: 0.1887 S12: -0.2773 S13: 0.4344 REMARK 3 S21: 0.2488 S22: -0.1575 S23: 0.4952 REMARK 3 S31: -0.3396 S32: -1.1135 S33: 0.0610 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1165 THROUGH 1226 ) REMARK 3 ORIGIN FOR THE GROUP (A): 41.2055 29.5695 64.1039 REMARK 3 T TENSOR REMARK 3 T11: 0.7566 T22: 0.5590 REMARK 3 T33: 0.3440 T12: 0.0680 REMARK 3 T13: -0.0865 T23: 0.0138 REMARK 3 L TENSOR REMARK 3 L11: 1.4166 L22: 1.0276 REMARK 3 L33: 1.5817 L12: -0.0955 REMARK 3 L13: -0.1743 L23: -0.0135 REMARK 3 S TENSOR REMARK 3 S11: -0.1381 S12: -0.0006 S13: 0.0847 REMARK 3 S21: 0.3492 S22: -0.0081 S23: -0.0383 REMARK 3 S31: 0.3521 S32: 0.2252 S33: 0.1345 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1227 THROUGH 1252 ) REMARK 3 ORIGIN FOR THE GROUP (A): 40.3128 21.2090 50.0294 REMARK 3 T TENSOR REMARK 3 T11: 0.6174 T22: 0.5580 REMARK 3 T33: 0.4171 T12: -0.0505 REMARK 3 T13: -0.0114 T23: 0.0512 REMARK 3 L TENSOR REMARK 3 L11: 2.5101 L22: 1.4459 REMARK 3 L33: 2.4553 L12: 0.1854 REMARK 3 L13: 1.1102 L23: 0.5387 REMARK 3 S TENSOR REMARK 3 S11: -0.3393 S12: -0.1269 S13: 0.1104 REMARK 3 S21: -0.0552 S22: 0.2660 S23: 0.1050 REMARK 3 S31: 0.0152 S32: 0.0874 S33: -0.0106 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 3 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): 47.1443 50.5724 -22.0670 REMARK 3 T TENSOR REMARK 3 T11: 0.7274 T22: 0.7430 REMARK 3 T33: 0.4316 T12: 0.1044 REMARK 3 T13: 0.0222 T23: 0.1207 REMARK 3 L TENSOR REMARK 3 L11: 1.2579 L22: 0.8689 REMARK 3 L33: 1.3651 L12: -0.0607 REMARK 3 L13: -0.7575 L23: -0.0237 REMARK 3 S TENSOR REMARK 3 S11: 0.0543 S12: 0.2502 S13: 0.1742 REMARK 3 S21: -0.4079 S22: 0.0009 S23: -0.1398 REMARK 3 S31: 0.1263 S32: 0.4222 S33: -0.0322 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 40 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): 43.8964 39.1568 -20.5754 REMARK 3 T TENSOR REMARK 3 T11: 0.9234 T22: 0.4600 REMARK 3 T33: 0.4287 T12: -0.0358 REMARK 3 T13: 0.0284 T23: 0.0672 REMARK 3 L TENSOR REMARK 3 L11: 3.1352 L22: 3.4351 REMARK 3 L33: 3.5812 L12: 0.7852 REMARK 3 L13: 1.1358 L23: 1.7633 REMARK 3 S TENSOR REMARK 3 S11: 0.0534 S12: -0.0734 S13: -0.3132 REMARK 3 S21: -0.0702 S22: -0.0968 S23: -0.1498 REMARK 3 S31: 0.1114 S32: -0.1177 S33: -0.0175 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 52 THROUGH 60 ) REMARK 3 ORIGIN FOR THE GROUP (A): 49.3478 49.1313 -7.6495 REMARK 3 T TENSOR REMARK 3 T11: 0.7940 T22: 1.2289 REMARK 3 T33: 0.5014 T12: 0.1014 REMARK 3 T13: 0.0596 T23: 0.0427 REMARK 3 L TENSOR REMARK 3 L11: 0.0045 L22: 3.3357 REMARK 3 L33: 0.1371 L12: 0.1109 REMARK 3 L13: 0.0271 L23: 0.6557 REMARK 3 S TENSOR REMARK 3 S11: -0.2115 S12: -0.5803 S13: 0.2766 REMARK 3 S21: 0.4815 S22: -0.0074 S23: -0.1603 REMARK 3 S31: -0.1627 S32: 0.2242 S33: 0.1675 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 61 THROUGH 84 ) REMARK 3 ORIGIN FOR THE GROUP (A): 53.1723 48.4560 -17.8500 REMARK 3 T TENSOR REMARK 3 T11: 0.7089 T22: 0.8594 REMARK 3 T33: 0.6904 T12: 0.0360 REMARK 3 T13: -0.0057 T23: -0.0225 REMARK 3 L TENSOR REMARK 3 L11: 2.5178 L22: 4.5982 REMARK 3 L33: 2.5086 L12: -0.2107 REMARK 3 L13: -0.2193 L23: -0.1581 REMARK 3 S TENSOR REMARK 3 S11: 0.1967 S12: -0.4206 S13: 0.2109 REMARK 3 S21: -0.1675 S22: -0.3484 S23: 0.0577 REMARK 3 S31: 0.2952 S32: 0.6945 S33: 0.0186 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 85 THROUGH 100 ) REMARK 3 ORIGIN FOR THE GROUP (A): 47.7875 42.2844 -23.2774 REMARK 3 T TENSOR REMARK 3 T11: 0.8588 T22: 0.8234 REMARK 3 T33: 0.4395 T12: 0.1256 REMARK 3 T13: -0.0654 T23: 0.0076 REMARK 3 L TENSOR REMARK 3 L11: 2.2223 L22: 0.2968 REMARK 3 L33: 0.4416 L12: 0.3919 REMARK 3 L13: -0.1224 L23: -0.3388 REMARK 3 S TENSOR REMARK 3 S11: 0.1768 S12: -0.1470 S13: -0.2172 REMARK 3 S21: 0.3116 S22: 0.2009 S23: -0.0317 REMARK 3 S31: 0.4106 S32: 0.7310 S33: -0.3097 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 101 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): 40.1092 44.0918 -18.7983 REMARK 3 T TENSOR REMARK 3 T11: 0.9929 T22: 0.5873 REMARK 3 T33: 0.3957 T12: 0.0774 REMARK 3 T13: 0.1392 T23: -0.1046 REMARK 3 L TENSOR REMARK 3 L11: 0.7166 L22: 0.4026 REMARK 3 L33: 1.6369 L12: 0.4457 REMARK 3 L13: -0.6884 L23: -0.0318 REMARK 3 S TENSOR REMARK 3 S11: -0.0746 S12: -0.0125 S13: -0.4909 REMARK 3 S21: -0.1259 S22: -0.2623 S23: -0.0931 REMARK 3 S31: 0.2624 S32: -0.5767 S33: 0.2655 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 848 THROUGH 886 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.0383 58.5955 27.2427 REMARK 3 T TENSOR REMARK 3 T11: 0.5133 T22: 0.7558 REMARK 3 T33: 1.0162 T12: -0.1693 REMARK 3 T13: 0.1158 T23: -0.1808 REMARK 3 L TENSOR REMARK 3 L11: 0.8691 L22: 1.4259 REMARK 3 L33: 4.0733 L12: 0.2638 REMARK 3 L13: 0.1921 L23: 0.6259 REMARK 3 S TENSOR REMARK 3 S11: 0.3800 S12: -0.2288 S13: 0.0094 REMARK 3 S21: 0.3651 S22: -0.1266 S23: 1.3780 REMARK 3 S31: 0.2956 S32: -0.3217 S33: -0.2188 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 887 THROUGH 1050 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.0684 71.7043 23.4889 REMARK 3 T TENSOR REMARK 3 T11: 0.4541 T22: 0.5077 REMARK 3 T33: 0.7011 T12: -0.0830 REMARK 3 T13: 0.0897 T23: -0.1340 REMARK 3 L TENSOR REMARK 3 L11: 1.1594 L22: 2.1810 REMARK 3 L33: 1.4685 L12: -0.0451 REMARK 3 L13: -0.2319 L23: 0.1932 REMARK 3 S TENSOR REMARK 3 S11: 0.1257 S12: -0.2783 S13: 0.3789 REMARK 3 S21: 0.1198 S22: -0.3400 S23: 0.6518 REMARK 3 S31: -0.5149 S32: -0.0437 S33: 0.1341 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1051 THROUGH 1085 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.5064 53.6978 17.5464 REMARK 3 T TENSOR REMARK 3 T11: 0.5123 T22: 0.7452 REMARK 3 T33: 0.5860 T12: 0.0866 REMARK 3 T13: -0.1402 T23: -0.0630 REMARK 3 L TENSOR REMARK 3 L11: 0.3913 L22: 0.8696 REMARK 3 L33: 2.0975 L12: -0.1030 REMARK 3 L13: 0.1653 L23: 0.6415 REMARK 3 S TENSOR REMARK 3 S11: 0.1715 S12: 0.0980 S13: -0.1729 REMARK 3 S21: 0.1390 S22: -0.1598 S23: 0.2051 REMARK 3 S31: 0.1920 S32: -0.0229 S33: -0.0291 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1086 THROUGH 1131 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.5619 54.6978 -6.7206 REMARK 3 T TENSOR REMARK 3 T11: 0.6237 T22: 0.6290 REMARK 3 T33: 0.5139 T12: 0.0505 REMARK 3 T13: -0.1280 T23: 0.0634 REMARK 3 L TENSOR REMARK 3 L11: 2.3308 L22: 1.4947 REMARK 3 L33: 2.2846 L12: 0.2262 REMARK 3 L13: -0.3654 L23: 0.2631 REMARK 3 S TENSOR REMARK 3 S11: 0.0693 S12: 0.7784 S13: -0.1064 REMARK 3 S21: -0.6658 S22: 0.0900 S23: 0.3670 REMARK 3 S31: -0.2992 S32: -0.5531 S33: -0.1327 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1132 THROUGH 1164 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.1621 40.6096 0.6820 REMARK 3 T TENSOR REMARK 3 T11: 0.5194 T22: 0.7230 REMARK 3 T33: 0.6778 T12: -0.0211 REMARK 3 T13: -0.1278 T23: 0.0563 REMARK 3 L TENSOR REMARK 3 L11: 1.6316 L22: 3.9332 REMARK 3 L33: 3.5243 L12: -0.7462 REMARK 3 L13: 0.5287 L23: 1.5340 REMARK 3 S TENSOR REMARK 3 S11: 0.1128 S12: 0.5170 S13: -0.4951 REMARK 3 S21: -0.1576 S22: -0.2800 S23: 1.1904 REMARK 3 S31: 0.5585 S32: -0.6852 S33: 0.1392 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1165 THROUGH 1226 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.0803 38.5145 -3.7939 REMARK 3 T TENSOR REMARK 3 T11: 0.5949 T22: 0.6054 REMARK 3 T33: 0.3820 T12: 0.0070 REMARK 3 T13: -0.1235 T23: -0.0221 REMARK 3 L TENSOR REMARK 3 L11: 1.3692 L22: 1.7519 REMARK 3 L33: 1.4570 L12: 0.7289 REMARK 3 L13: 0.2600 L23: -0.2082 REMARK 3 S TENSOR REMARK 3 S11: -0.1117 S12: 0.1280 S13: -0.1140 REMARK 3 S21: -0.5073 S22: -0.2166 S23: 0.0472 REMARK 3 S31: 0.2475 S32: -0.1364 S33: 0.3246 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1227 THROUGH 1252 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.5724 53.6847 2.2686 REMARK 3 T TENSOR REMARK 3 T11: 0.5690 T22: 0.6231 REMARK 3 T33: 0.4496 T12: 0.0459 REMARK 3 T13: -0.1379 T23: 0.0274 REMARK 3 L TENSOR REMARK 3 L11: 2.6304 L22: 1.8997 REMARK 3 L33: 0.9155 L12: -0.9995 REMARK 3 L13: -0.5926 L23: 0.5133 REMARK 3 S TENSOR REMARK 3 S11: -0.3143 S12: -0.2186 S13: 0.3180 REMARK 3 S21: 0.0179 S22: 0.2396 S23: -0.1502 REMARK 3 S31: -0.1515 S32: -0.0141 S33: 0.0880 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): 99.7261 0.8941 8.7197 REMARK 3 T TENSOR REMARK 3 T11: 0.6397 T22: 0.6631 REMARK 3 T33: 0.7568 T12: -0.0086 REMARK 3 T13: -0.1059 T23: -0.2342 REMARK 3 L TENSOR REMARK 3 L11: 1.1732 L22: 2.0529 REMARK 3 L33: 1.4833 L12: -0.2789 REMARK 3 L13: -0.5250 L23: 0.7836 REMARK 3 S TENSOR REMARK 3 S11: 0.0077 S12: -0.0447 S13: -0.2693 REMARK 3 S21: -0.7510 S22: 0.4838 S23: 0.1932 REMARK 3 S31: -0.1972 S32: 0.6862 S33: -0.3181 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 40 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): 96.8963 -2.8468 20.3625 REMARK 3 T TENSOR REMARK 3 T11: 0.7733 T22: 0.7453 REMARK 3 T33: 0.7512 T12: 0.0766 REMARK 3 T13: -0.0992 T23: -0.2327 REMARK 3 L TENSOR REMARK 3 L11: 2.7450 L22: 3.0572 REMARK 3 L33: 3.4872 L12: -1.3969 REMARK 3 L13: 0.4970 L23: 1.9261 REMARK 3 S TENSOR REMARK 3 S11: 0.0887 S12: -0.3835 S13: -0.4649 REMARK 3 S21: 0.3065 S22: 0.1729 S23: 0.0420 REMARK 3 S31: 0.5690 S32: 0.3117 S33: 0.0382 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 52 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): 99.9568 2.2629 15.4692 REMARK 3 T TENSOR REMARK 3 T11: 0.6665 T22: 0.7101 REMARK 3 T33: 0.7135 T12: 0.0821 REMARK 3 T13: -0.0787 T23: -0.1379 REMARK 3 L TENSOR REMARK 3 L11: 0.5859 L22: 1.4830 REMARK 3 L33: 0.8301 L12: -0.1121 REMARK 3 L13: 0.1273 L23: 1.0447 REMARK 3 S TENSOR REMARK 3 S11: -0.0460 S12: -0.0728 S13: -0.0901 REMARK 3 S21: 0.6764 S22: 0.2489 S23: -0.2485 REMARK 3 S31: 0.3093 S32: 0.4136 S33: -0.1635 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 848 THROUGH 886 ) REMARK 3 ORIGIN FOR THE GROUP (A): 56.8817 47.6600 20.0206 REMARK 3 T TENSOR REMARK 3 T11: 0.5843 T22: 0.7224 REMARK 3 T33: 1.0495 T12: -0.1674 REMARK 3 T13: -0.0662 T23: 0.0446 REMARK 3 L TENSOR REMARK 3 L11: 0.3637 L22: 2.7964 REMARK 3 L33: 1.4296 L12: -0.5303 REMARK 3 L13: -0.5891 L23: -0.1508 REMARK 3 S TENSOR REMARK 3 S11: 0.1490 S12: 0.3398 S13: -0.5227 REMARK 3 S21: -0.0131 S22: 0.1463 S23: 0.6826 REMARK 3 S31: -0.3009 S32: -0.3273 S33: -0.2213 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 887 THROUGH 976 ) REMARK 3 ORIGIN FOR THE GROUP (A): 65.0534 50.5197 4.8918 REMARK 3 T TENSOR REMARK 3 T11: 0.7275 T22: 0.6592 REMARK 3 T33: 0.6249 T12: 0.0692 REMARK 3 T13: -0.1551 T23: 0.0282 REMARK 3 L TENSOR REMARK 3 L11: 1.7108 L22: 1.4104 REMARK 3 L33: 1.7927 L12: -0.4281 REMARK 3 L13: -0.0900 L23: 0.2578 REMARK 3 S TENSOR REMARK 3 S11: 0.2841 S12: 0.5970 S13: 0.0057 REMARK 3 S21: -1.2231 S22: -0.2353 S23: 0.7166 REMARK 3 S31: -0.3476 S32: -0.0465 S33: -0.1240 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 977 THROUGH 1085 ) REMARK 3 ORIGIN FOR THE GROUP (A): 70.3018 44.3675 12.0243 REMARK 3 T TENSOR REMARK 3 T11: 0.5394 T22: 0.6426 REMARK 3 T33: 0.6691 T12: -0.0426 REMARK 3 T13: -0.0849 T23: -0.0518 REMARK 3 L TENSOR REMARK 3 L11: 0.9630 L22: 2.6690 REMARK 3 L33: 0.7090 L12: -0.8713 REMARK 3 L13: -0.4235 L23: -0.5935 REMARK 3 S TENSOR REMARK 3 S11: 0.3047 S12: 0.1346 S13: -0.0623 REMARK 3 S21: -0.1343 S22: -0.3197 S23: 0.5023 REMARK 3 S31: -0.0011 S32: 0.2549 S33: -0.0149 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1086 THROUGH 1131 ) REMARK 3 ORIGIN FOR THE GROUP (A): 72.3034 15.2286 11.2730 REMARK 3 T TENSOR REMARK 3 T11: 0.5474 T22: 0.7183 REMARK 3 T33: 0.8911 T12: -0.2102 REMARK 3 T13: 0.0427 T23: -0.1858 REMARK 3 L TENSOR REMARK 3 L11: 1.5390 L22: 1.9025 REMARK 3 L33: 1.0135 L12: -0.4078 REMARK 3 L13: -0.2196 L23: 0.2678 REMARK 3 S TENSOR REMARK 3 S11: -0.2386 S12: 0.0466 S13: -0.8298 REMARK 3 S21: -0.4321 S22: -0.2592 S23: 0.8092 REMARK 3 S31: 0.3762 S32: -0.4834 S33: 0.3590 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1132 THROUGH 1164 ) REMARK 3 ORIGIN FOR THE GROUP (A): 62.8672 16.7937 27.0091 REMARK 3 T TENSOR REMARK 3 T11: 0.8068 T22: 0.6699 REMARK 3 T33: 1.2177 T12: -0.2844 REMARK 3 T13: 0.4040 T23: -0.1503 REMARK 3 L TENSOR REMARK 3 L11: 1.1586 L22: 2.6688 REMARK 3 L33: 0.7342 L12: 0.9040 REMARK 3 L13: 0.2261 L23: -0.9759 REMARK 3 S TENSOR REMARK 3 S11: 0.0850 S12: -0.2889 S13: -0.5289 REMARK 3 S21: 0.7298 S22: -0.3870 S23: 1.1918 REMARK 3 S31: 0.0403 S32: -0.3143 S33: -0.0186 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1165 THROUGH 1226 ) REMARK 3 ORIGIN FOR THE GROUP (A): 77.0250 12.3303 27.3531 REMARK 3 T TENSOR REMARK 3 T11: 0.7011 T22: 0.5572 REMARK 3 T33: 0.8133 T12: -0.1240 REMARK 3 T13: 0.2531 T23: -0.0239 REMARK 3 L TENSOR REMARK 3 L11: 1.0087 L22: 1.3879 REMARK 3 L33: 1.1054 L12: 1.1627 REMARK 3 L13: -0.2572 L23: -0.0578 REMARK 3 S TENSOR REMARK 3 S11: -0.2409 S12: -0.3098 S13: -0.1748 REMARK 3 S21: 0.8260 S22: 0.0572 S23: 0.9593 REMARK 3 S31: 0.2854 S32: 0.0654 S33: 0.1290 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1227 THROUGH 1252 ) REMARK 3 ORIGIN FOR THE GROUP (A): 75.9599 23.4532 15.4315 REMARK 3 T TENSOR REMARK 3 T11: 0.4419 T22: 0.5873 REMARK 3 T33: 0.7760 T12: -0.0451 REMARK 3 T13: -0.0203 T23: -0.1395 REMARK 3 L TENSOR REMARK 3 L11: 2.2314 L22: 1.9459 REMARK 3 L33: 1.8412 L12: -0.7049 REMARK 3 L13: 0.5316 L23: -0.5004 REMARK 3 S TENSOR REMARK 3 S11: 0.0151 S12: -0.1805 S13: 0.3486 REMARK 3 S21: -0.0065 S22: -0.0875 S23: 0.5480 REMARK 3 S31: -0.4412 S32: -0.0050 S33: -0.0987 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 3 THROUGH 24 ) REMARK 3 ORIGIN FOR THE GROUP (A): 35.3161 77.6354 81.6675 REMARK 3 T TENSOR REMARK 3 T11: 1.3436 T22: 2.3546 REMARK 3 T33: 1.6690 T12: -0.4369 REMARK 3 T13: 0.2333 T23: -1.0096 REMARK 3 L TENSOR REMARK 3 L11: 0.7993 L22: 0.3434 REMARK 3 L33: 0.9242 L12: -0.5138 REMARK 3 L13: -0.0297 L23: 0.0645 REMARK 3 S TENSOR REMARK 3 S11: 0.4421 S12: 0.1993 S13: 0.3435 REMARK 3 S21: -0.4203 S22: 0.1668 S23: -0.7939 REMARK 3 S31: 0.2999 S32: 0.0318 S33: -0.3651 REMARK 3 TLS GROUP : 35 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 25 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.8657 74.4223 72.0619 REMARK 3 T TENSOR REMARK 3 T11: 1.8707 T22: 1.5863 REMARK 3 T33: 1.2704 T12: -0.6476 REMARK 3 T13: 0.5305 T23: -0.6143 REMARK 3 L TENSOR REMARK 3 L11: 1.1612 L22: 0.0879 REMARK 3 L33: 0.5629 L12: 0.1571 REMARK 3 L13: 0.5501 L23: 0.2183 REMARK 3 S TENSOR REMARK 3 S11: -0.0017 S12: -0.0722 S13: 0.2434 REMARK 3 S21: -0.0050 S22: 0.2079 S23: -0.5838 REMARK 3 S31: -0.2716 S32: 0.1835 S33: -0.0844 REMARK 3 TLS GROUP : 36 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 52 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.1782 73.4656 70.9516 REMARK 3 T TENSOR REMARK 3 T11: 0.9780 T22: 1.4715 REMARK 3 T33: 1.9951 T12: -0.0531 REMARK 3 T13: 0.2492 T23: -0.6370 REMARK 3 L TENSOR REMARK 3 L11: 0.6039 L22: 2.5714 REMARK 3 L33: 0.2719 L12: 0.4333 REMARK 3 L13: 0.1777 L23: 0.8204 REMARK 3 S TENSOR REMARK 3 S11: -0.3199 S12: 0.0217 S13: -0.2050 REMARK 3 S21: -0.3462 S22: 0.1954 S23: 0.0632 REMARK 3 S31: -0.1187 S32: -0.0113 S33: 0.0897 REMARK 3 TLS GROUP : 37 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 92 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.2925 76.8920 72.1713 REMARK 3 T TENSOR REMARK 3 T11: 1.8821 T22: 1.4734 REMARK 3 T33: 1.3019 T12: -0.7125 REMARK 3 T13: 0.6304 T23: -0.7686 REMARK 3 L TENSOR REMARK 3 L11: 0.7045 L22: 0.7766 REMARK 3 L33: 0.5901 L12: 0.6481 REMARK 3 L13: 0.4278 L23: 0.3671 REMARK 3 S TENSOR REMARK 3 S11: -0.0913 S12: -0.4250 S13: 0.2098 REMARK 3 S21: 0.0943 S22: 0.3292 S23: -0.5378 REMARK 3 S31: 0.3950 S32: 0.1323 S33: -0.0666 REMARK 3 TLS GROUP : 38 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 4 THROUGH 31 ) REMARK 3 ORIGIN FOR THE GROUP (A): 81.9419 102.5431 25.5679 REMARK 3 T TENSOR REMARK 3 T11: 0.9731 T22: 0.9901 REMARK 3 T33: 1.5320 T12: -0.3464 REMARK 3 T13: -0.0196 T23: 0.0891 REMARK 3 L TENSOR REMARK 3 L11: 0.2586 L22: 0.5520 REMARK 3 L33: 0.0160 L12: 0.3811 REMARK 3 L13: -0.0822 L23: -0.1183 REMARK 3 S TENSOR REMARK 3 S11: -0.0027 S12: 0.2578 S13: 0.4799 REMARK 3 S21: 0.1336 S22: 0.0213 S23: -0.2577 REMARK 3 S31: -0.2583 S32: 0.5379 S33: -0.0907 REMARK 3 TLS GROUP : 39 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 32 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): 76.7759 96.2557 17.3937 REMARK 3 T TENSOR REMARK 3 T11: 1.0914 T22: 0.9760 REMARK 3 T33: 1.4125 T12: -0.0824 REMARK 3 T13: 0.0021 T23: 0.4575 REMARK 3 L TENSOR REMARK 3 L11: 0.2928 L22: 2.0996 REMARK 3 L33: 1.8512 L12: 0.1745 REMARK 3 L13: -0.2294 L23: -0.6028 REMARK 3 S TENSOR REMARK 3 S11: -0.2815 S12: 0.8112 S13: 0.6181 REMARK 3 S21: -0.7539 S22: -0.3016 S23: -0.4427 REMARK 3 S31: -0.4571 S32: 0.1662 S33: 0.2963 REMARK 3 TLS GROUP : 40 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 52 THROUGH 84 ) REMARK 3 ORIGIN FOR THE GROUP (A): 85.0323 92.9060 24.3716 REMARK 3 T TENSOR REMARK 3 T11: 0.5243 T22: 1.1568 REMARK 3 T33: 1.4183 T12: -0.3304 REMARK 3 T13: -0.0120 T23: 0.5716 REMARK 3 L TENSOR REMARK 3 L11: 1.9282 L22: 1.7433 REMARK 3 L33: 1.7212 L12: 0.8717 REMARK 3 L13: -0.4659 L23: -0.2835 REMARK 3 S TENSOR REMARK 3 S11: -0.0233 S12: -0.2430 S13: 0.1245 REMARK 3 S21: -0.0773 S22: -0.3748 S23: -0.6514 REMARK 3 S31: 0.1781 S32: 0.3143 S33: 0.1044 REMARK 3 TLS GROUP : 41 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 85 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): 75.8942 97.4706 17.9590 REMARK 3 T TENSOR REMARK 3 T11: 0.8842 T22: 0.7596 REMARK 3 T33: 1.4550 T12: -0.3114 REMARK 3 T13: 0.3099 T23: 0.6024 REMARK 3 L TENSOR REMARK 3 L11: 0.4145 L22: 0.8305 REMARK 3 L33: 0.2539 L12: 0.4189 REMARK 3 L13: 0.0263 L23: 0.3421 REMARK 3 S TENSOR REMARK 3 S11: -0.0803 S12: 0.3966 S13: 0.8327 REMARK 3 S21: -0.2958 S22: -0.2825 S23: -0.5716 REMARK 3 S31: -0.5322 S32: 0.5817 S33: -0.2604 REMARK 3 TLS GROUP : 42 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 849 THROUGH 886 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.9947 53.6977 42.9204 REMARK 3 T TENSOR REMARK 3 T11: 0.4490 T22: 0.5002 REMARK 3 T33: 0.6611 T12: 0.0321 REMARK 3 T13: -0.0518 T23: 0.1040 REMARK 3 L TENSOR REMARK 3 L11: 1.0569 L22: 3.5640 REMARK 3 L33: 2.4040 L12: 0.1507 REMARK 3 L13: 0.1449 L23: -1.0920 REMARK 3 S TENSOR REMARK 3 S11: 0.2592 S12: 0.4910 S13: 0.3451 REMARK 3 S21: -0.3151 S22: 0.1934 S23: 0.0429 REMARK 3 S31: 0.1081 S32: -0.3913 S33: -0.4960 REMARK 3 TLS GROUP : 43 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 887 THROUGH 936 ) REMARK 3 ORIGIN FOR THE GROUP (A): 45.0393 59.9424 53.4428 REMARK 3 T TENSOR REMARK 3 T11: 0.5332 T22: 0.4338 REMARK 3 T33: 0.6977 T12: 0.0501 REMARK 3 T13: 0.2026 T23: -0.0411 REMARK 3 L TENSOR REMARK 3 L11: 1.2589 L22: 1.7437 REMARK 3 L33: 1.0406 L12: -0.0040 REMARK 3 L13: -0.0766 L23: 0.2892 REMARK 3 S TENSOR REMARK 3 S11: 0.3580 S12: -0.3403 S13: 0.6421 REMARK 3 S21: 0.4838 S22: -0.0116 S23: 0.5539 REMARK 3 S31: -0.4138 S32: -0.0675 S33: -0.2168 REMARK 3 TLS GROUP : 44 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 937 THROUGH 1050 ) REMARK 3 ORIGIN FOR THE GROUP (A): 51.6156 60.6179 55.8736 REMARK 3 T TENSOR REMARK 3 T11: 0.5094 T22: 0.4637 REMARK 3 T33: 0.5572 T12: -0.0277 REMARK 3 T13: 0.0824 T23: -0.0745 REMARK 3 L TENSOR REMARK 3 L11: 1.4461 L22: 1.7882 REMARK 3 L33: 1.5448 L12: 0.2397 REMARK 3 L13: -0.1553 L23: -0.4028 REMARK 3 S TENSOR REMARK 3 S11: 0.3801 S12: -0.3195 S13: 0.4363 REMARK 3 S21: 0.2830 S22: -0.4141 S23: 0.1130 REMARK 3 S31: -0.0899 S32: 0.2119 S33: 0.0168 REMARK 3 TLS GROUP : 45 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1051 THROUGH 1105 ) REMARK 3 ORIGIN FOR THE GROUP (A): 53.2090 70.9182 33.6195 REMARK 3 T TENSOR REMARK 3 T11: 0.5096 T22: 0.5806 REMARK 3 T33: 0.7466 T12: 0.0059 REMARK 3 T13: 0.0316 T23: 0.1106 REMARK 3 L TENSOR REMARK 3 L11: 1.1206 L22: 1.7418 REMARK 3 L33: 1.1636 L12: 0.6653 REMARK 3 L13: -0.6688 L23: 0.1537 REMARK 3 S TENSOR REMARK 3 S11: 0.0265 S12: 0.0688 S13: 0.5164 REMARK 3 S21: -0.3167 S22: 0.2208 S23: 0.4312 REMARK 3 S31: -0.0143 S32: 0.3620 S33: -0.2002 REMARK 3 TLS GROUP : 46 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1106 THROUGH 1131 ) REMARK 3 ORIGIN FOR THE GROUP (A): 51.1349 85.3744 33.6808 REMARK 3 T TENSOR REMARK 3 T11: 0.7557 T22: 0.3867 REMARK 3 T33: 1.1702 T12: 0.0069 REMARK 3 T13: 0.1534 T23: 0.1211 REMARK 3 L TENSOR REMARK 3 L11: 1.5862 L22: 0.8115 REMARK 3 L33: 3.9278 L12: -0.1652 REMARK 3 L13: 0.6119 L23: 0.9954 REMARK 3 S TENSOR REMARK 3 S11: 0.0369 S12: -0.1588 S13: 0.5366 REMARK 3 S21: 0.4070 S22: 0.5924 S23: 0.2435 REMARK 3 S31: -0.1819 S32: -0.0428 S33: -0.3526 REMARK 3 TLS GROUP : 47 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1132 THROUGH 1165 ) REMARK 3 ORIGIN FOR THE GROUP (A): 44.3371 75.4283 19.1816 REMARK 3 T TENSOR REMARK 3 T11: 0.6439 T22: 0.6903 REMARK 3 T33: 0.9585 T12: 0.0058 REMARK 3 T13: -0.0789 T23: 0.1558 REMARK 3 L TENSOR REMARK 3 L11: 0.6581 L22: 2.9628 REMARK 3 L33: 4.0305 L12: -0.5742 REMARK 3 L13: 0.3310 L23: -1.1056 REMARK 3 S TENSOR REMARK 3 S11: 0.3443 S12: 0.6095 S13: 0.0880 REMARK 3 S21: -0.6359 S22: -0.0436 S23: 0.5223 REMARK 3 S31: 0.6023 S32: -0.6641 S33: -0.3013 REMARK 3 TLS GROUP : 48 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1166 THROUGH 1226 ) REMARK 3 ORIGIN FOR THE GROUP (A): 57.5775 79.3252 16.7616 REMARK 3 T TENSOR REMARK 3 T11: 0.6701 T22: 0.7651 REMARK 3 T33: 0.8259 T12: -0.0350 REMARK 3 T13: 0.0169 T23: 0.1939 REMARK 3 L TENSOR REMARK 3 L11: 1.4806 L22: 1.4234 REMARK 3 L33: 2.4819 L12: -0.3645 REMARK 3 L13: 0.7008 L23: 0.0394 REMARK 3 S TENSOR REMARK 3 S11: 0.0348 S12: 0.5710 S13: 0.0755 REMARK 3 S21: -0.5339 S22: 0.1314 S23: 0.1257 REMARK 3 S31: -0.1758 S32: 0.1802 S33: -0.1061 REMARK 3 TLS GROUP : 49 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1227 THROUGH 1251 ) REMARK 3 ORIGIN FOR THE GROUP (A): 57.3472 76.7081 32.4127 REMARK 3 T TENSOR REMARK 3 T11: 0.5282 T22: 0.5455 REMARK 3 T33: 0.7880 T12: 0.1154 REMARK 3 T13: 0.0581 T23: 0.1818 REMARK 3 L TENSOR REMARK 3 L11: 1.5722 L22: 1.4425 REMARK 3 L33: 2.3621 L12: 0.0040 REMARK 3 L13: -0.7290 L23: 0.1275 REMARK 3 S TENSOR REMARK 3 S11: -0.3920 S12: 0.1656 S13: -0.0846 REMARK 3 S21: 0.2437 S22: -0.1797 S23: 0.5002 REMARK 3 S31: 0.1066 S32: 0.2247 S33: 0.4540 REMARK 3 TLS GROUP : 50 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 848 THROUGH 914 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.4061 35.3948 43.8658 REMARK 3 T TENSOR REMARK 3 T11: 1.0680 T22: 0.8404 REMARK 3 T33: 1.0776 T12: -0.1358 REMARK 3 T13: 0.5596 T23: -0.1052 REMARK 3 L TENSOR REMARK 3 L11: 0.8773 L22: 0.6519 REMARK 3 L33: 3.0348 L12: 0.7596 REMARK 3 L13: 0.7415 L23: 0.7921 REMARK 3 S TENSOR REMARK 3 S11: 0.5866 S12: -0.5035 S13: 0.5980 REMARK 3 S21: 1.2171 S22: -0.2189 S23: 0.9510 REMARK 3 S31: 0.3436 S32: 0.8102 S33: -0.0447 REMARK 3 TLS GROUP : 51 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 915 THROUGH 976 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.5731 29.6815 57.5285 REMARK 3 T TENSOR REMARK 3 T11: 2.3380 T22: 0.9455 REMARK 3 T33: 0.6693 T12: -0.3959 REMARK 3 T13: 0.3095 T23: 0.0679 REMARK 3 L TENSOR REMARK 3 L11: 2.5561 L22: 0.1146 REMARK 3 L33: 0.0814 L12: -0.5650 REMARK 3 L13: -0.4573 L23: 0.1015 REMARK 3 S TENSOR REMARK 3 S11: 0.9397 S12: -0.9814 S13: 0.3006 REMARK 3 S21: 1.0136 S22: -0.3160 S23: -0.0399 REMARK 3 S31: 1.2304 S32: 0.2930 S33: 0.2996 REMARK 3 TLS GROUP : 52 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 977 THROUGH 1131 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.0090 45.7316 55.9678 REMARK 3 T TENSOR REMARK 3 T11: 1.7836 T22: 1.0572 REMARK 3 T33: 0.6909 T12: -0.4589 REMARK 3 T13: 0.5049 T23: -0.2873 REMARK 3 L TENSOR REMARK 3 L11: 1.1922 L22: 0.6091 REMARK 3 L33: 1.6987 L12: 0.4864 REMARK 3 L13: 0.9562 L23: 0.9730 REMARK 3 S TENSOR REMARK 3 S11: 0.9329 S12: -0.8838 S13: 0.1119 REMARK 3 S21: 1.8343 S22: -0.6081 S23: 0.2943 REMARK 3 S31: 0.4334 S32: -0.0373 S33: -0.1086 REMARK 3 TLS GROUP : 53 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 1132 THROUGH 1164 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.5475 69.8561 53.6602 REMARK 3 T TENSOR REMARK 3 T11: 0.9294 T22: 1.1882 REMARK 3 T33: 1.8034 T12: -0.3805 REMARK 3 T13: 0.7655 T23: -0.5771 REMARK 3 L TENSOR REMARK 3 L11: 1.1943 L22: 1.8835 REMARK 3 L33: 1.2320 L12: -1.0389 REMARK 3 L13: -0.8641 L23: -0.0284 REMARK 3 S TENSOR REMARK 3 S11: 0.1180 S12: 0.3147 S13: 0.1371 REMARK 3 S21: -0.0777 S22: 0.0479 S23: 0.8806 REMARK 3 S31: -0.2114 S32: -0.3626 S33: 0.4940 REMARK 3 TLS GROUP : 54 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 1165 THROUGH 1251 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.9352 68.6965 57.1496 REMARK 3 T TENSOR REMARK 3 T11: 1.3735 T22: 1.1024 REMARK 3 T33: 1.2277 T12: -0.4516 REMARK 3 T13: 1.1449 T23: -0.6770 REMARK 3 L TENSOR REMARK 3 L11: 0.5382 L22: 0.8843 REMARK 3 L33: 1.3683 L12: -0.1870 REMARK 3 L13: -0.0421 L23: 0.2393 REMARK 3 S TENSOR REMARK 3 S11: 0.1494 S12: -0.2355 S13: 0.3066 REMARK 3 S21: 0.6629 S22: -0.2731 S23: 0.4375 REMARK 3 S31: 0.2604 S32: 0.0501 S33: -1.3619 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 7UIE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-22. REMARK 100 THE DEPOSITION ID IS D_1000264241. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-AUG-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 24-ID-E REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54051 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.230 REMARK 200 RESOLUTION RANGE LOW (A) : 174.630 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 4.100 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.23 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.32 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 : 1.060 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: 3FFZ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.64 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, PH 7.0, 0.2 M NACL AND 18% REMARK 280 PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 X,-Y,-Z REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 -X,-Y+1/2,Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 87.31300 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 107.21950 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 87.31300 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 107.21950 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 5 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER B 0 REMARK 465 GLN B 1 REMARK 465 LEU B 2 REMARK 465 PRO B 131 REMARK 465 LYS B 132 REMARK 465 THR B 133 REMARK 465 PRO B 134 REMARK 465 LYS B 135 REMARK 465 PRO B 136 REMARK 465 GLN B 137 REMARK 465 HIS A 830 REMARK 465 HIS A 831 REMARK 465 HIS A 832 REMARK 465 HIS A 833 REMARK 465 HIS A 834 REMARK 465 HIS A 835 REMARK 465 GLY A 836 REMARK 465 SER A 837 REMARK 465 LEU A 838 REMARK 465 GLU A 839 REMARK 465 VAL A 840 REMARK 465 LEU A 841 REMARK 465 PHE A 842 REMARK 465 GLN A 843 REMARK 465 GLY A 844 REMARK 465 PRO A 845 REMARK 465 ARG A 846 REMARK 465 SER C 0 REMARK 465 GLN C 1 REMARK 465 LEU C 2 REMARK 465 GLU C 130 REMARK 465 PRO C 131 REMARK 465 LYS C 132 REMARK 465 THR C 133 REMARK 465 PRO C 134 REMARK 465 LYS C 135 REMARK 465 PRO C 136 REMARK 465 GLN C 137 REMARK 465 HIS D 830 REMARK 465 HIS D 831 REMARK 465 HIS D 832 REMARK 465 HIS D 833 REMARK 465 HIS D 834 REMARK 465 HIS D 835 REMARK 465 GLY D 836 REMARK 465 SER D 837 REMARK 465 LEU D 838 REMARK 465 GLU D 839 REMARK 465 VAL D 840 REMARK 465 LEU D 841 REMARK 465 PHE D 842 REMARK 465 GLN D 843 REMARK 465 GLY D 844 REMARK 465 PRO D 845 REMARK 465 ARG D 846 REMARK 465 ILE D 847 REMARK 465 SER E 0 REMARK 465 GLU E 130 REMARK 465 PRO E 131 REMARK 465 LYS E 132 REMARK 465 THR E 133 REMARK 465 PRO E 134 REMARK 465 LYS E 135 REMARK 465 PRO E 136 REMARK 465 GLN E 137 REMARK 465 HIS F 830 REMARK 465 HIS F 831 REMARK 465 HIS F 832 REMARK 465 HIS F 833 REMARK 465 HIS F 834 REMARK 465 HIS F 835 REMARK 465 GLY F 836 REMARK 465 SER F 837 REMARK 465 LEU F 838 REMARK 465 GLU F 839 REMARK 465 VAL F 840 REMARK 465 LEU F 841 REMARK 465 PHE F 842 REMARK 465 GLN F 843 REMARK 465 GLY F 844 REMARK 465 PRO F 845 REMARK 465 ARG F 846 REMARK 465 ILE F 847 REMARK 465 SER I 0 REMARK 465 GLN I 1 REMARK 465 LEU I 2 REMARK 465 GLU I 130 REMARK 465 PRO I 131 REMARK 465 LYS I 132 REMARK 465 THR I 133 REMARK 465 PRO I 134 REMARK 465 LYS I 135 REMARK 465 PRO I 136 REMARK 465 GLN I 137 REMARK 465 SER G 0 REMARK 465 GLN G 1 REMARK 465 LEU G 2 REMARK 465 GLN G 3 REMARK 465 GLU G 130 REMARK 465 PRO G 131 REMARK 465 LYS G 132 REMARK 465 THR G 133 REMARK 465 PRO G 134 REMARK 465 LYS G 135 REMARK 465 PRO G 136 REMARK 465 GLN G 137 REMARK 465 HIS H 830 REMARK 465 HIS H 831 REMARK 465 HIS H 832 REMARK 465 HIS H 833 REMARK 465 HIS H 834 REMARK 465 HIS H 835 REMARK 465 GLY H 836 REMARK 465 SER H 837 REMARK 465 LEU H 838 REMARK 465 GLU H 839 REMARK 465 VAL H 840 REMARK 465 LEU H 841 REMARK 465 PHE H 842 REMARK 465 GLN H 843 REMARK 465 GLY H 844 REMARK 465 PRO H 845 REMARK 465 ARG H 846 REMARK 465 ILE H 847 REMARK 465 LYS H 848 REMARK 465 LYS H 1252 REMARK 465 HIS J 830 REMARK 465 HIS J 831 REMARK 465 HIS J 832 REMARK 465 HIS J 833 REMARK 465 HIS J 834 REMARK 465 HIS J 835 REMARK 465 GLY J 836 REMARK 465 SER J 837 REMARK 465 LEU J 838 REMARK 465 GLU J 839 REMARK 465 VAL J 840 REMARK 465 LEU J 841 REMARK 465 PHE J 842 REMARK 465 GLN J 843 REMARK 465 GLY J 844 REMARK 465 PRO J 845 REMARK 465 ARG J 846 REMARK 465 ILE J 847 REMARK 465 LYS J 1252 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLN B 3 CG CD OE1 NE2 REMARK 470 LYS B 13 CG CD CE NZ REMARK 470 ARG B 19 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 43 CG CD CE NZ REMARK 470 GLU B 61 CG CD OE1 OE2 REMARK 470 LYS B 65 CG CD CE NZ REMARK 470 LYS B 76 CG CD CE NZ REMARK 470 GLN B 121 CG CD OE1 NE2 REMARK 470 GLU B 130 CG CD OE1 OE2 REMARK 470 LYS A 848 CG CD CE NZ REMARK 470 LYS A 858 CG CD CE NZ REMARK 470 LYS A 861 CG CD CE NZ REMARK 470 LYS A1156 CG CD CE NZ REMARK 470 GLN C 3 CG CD OE1 NE2 REMARK 470 ARG C 19 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 43 CG CD CE NZ REMARK 470 LYS C 65 CG CD CE NZ REMARK 470 LYS C 76 CG CD CE NZ REMARK 470 GLN C 121 CG CD OE1 NE2 REMARK 470 LYS D 848 CG CD CE NZ REMARK 470 ASP D 860 CG OD1 OD2 REMARK 470 LYS D1102 CG CD CE NZ REMARK 470 LYS D1156 CG CD CE NZ REMARK 470 LYS D1252 CG CD CE NZ REMARK 470 ARG E 19 CG CD NE CZ NH1 NH2 REMARK 470 LYS E 43 CG CD CE NZ REMARK 470 LYS E 65 CG CD CE NZ REMARK 470 LYS E 76 CG CD CE NZ REMARK 470 GLN E 121 CG CD OE1 NE2 REMARK 470 LYS F 858 CG CD CE NZ REMARK 470 LYS F1102 CG CD CE NZ REMARK 470 LYS F1252 CG CD CE NZ REMARK 470 GLN I 3 CG CD OE1 NE2 REMARK 470 ARG I 19 CG CD NE CZ NH1 NH2 REMARK 470 PHE I 29 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS I 43 CG CD CE NZ REMARK 470 LYS I 65 CG CD CE NZ REMARK 470 LYS I 76 CG CD CE NZ REMARK 470 ASN I 77 CG OD1 ND2 REMARK 470 GLN I 121 CG CD OE1 NE2 REMARK 470 ARG G 19 CG CD NE CZ NH1 NH2 REMARK 470 LYS G 43 CG CD CE NZ REMARK 470 GLU G 61 CG CD OE1 OE2 REMARK 470 LYS G 65 CG CD CE NZ REMARK 470 ARG G 67 CG CD NE CZ NH1 NH2 REMARK 470 ASP G 73 CG OD1 OD2 REMARK 470 ASN G 74 CG OD1 ND2 REMARK 470 LYS G 76 CG CD CE NZ REMARK 470 GLN G 82 CG CD OE1 NE2 REMARK 470 GLN G 121 CG CD OE1 NE2 REMARK 470 LYS H 858 CG CD CE NZ REMARK 470 LYS H 861 CG CD CE NZ REMARK 470 LYS H 929 CG CD CE NZ REMARK 470 LYS H1102 CG CD CE NZ REMARK 470 LYS H1156 CG CD CE NZ REMARK 470 LYS H1171 CG CD CE NZ REMARK 470 LYS J 848 CG CD CE NZ REMARK 470 LYS J 858 CG CD CE NZ REMARK 470 ASP J 860 CG OD1 OD2 REMARK 470 LYS J 861 CG CD CE NZ REMARK 470 ASP J 877 CG OD1 OD2 REMARK 470 LYS J 880 CG CD CE NZ REMARK 470 ASP J 893 CG OD1 OD2 REMARK 470 GLU J 897 CG CD OE1 OE2 REMARK 470 ASP J 945 CG OD1 OD2 REMARK 470 LYS J 951 CG CD CE NZ REMARK 470 ASN J 979 CG OD1 ND2 REMARK 470 ASN J1019 CG OD1 ND2 REMARK 470 LYS J1032 CG CD CE NZ REMARK 470 LYS J1102 CG CD CE NZ REMARK 470 ARG J1120 CG CD NE CZ NH1 NH2 REMARK 470 ASN J1133 CG OD1 ND2 REMARK 470 ASN J1134 CG OD1 ND2 REMARK 470 LYS J1156 CG CD CE NZ REMARK 470 LYS J1171 CG CD CE NZ REMARK 470 LYS J1173 CG CD CE NZ REMARK 470 LYS J1202 CG CD CE NZ REMARK 470 ARG J1230 CG CD NE CZ NH1 NH2 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 OH TYR F 908 O LYS F 913 2.19 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 B 129 -72.02 -87.90 REMARK 500 ASP A 909 49.50 -148.46 REMARK 500 ASN A 928 17.25 58.65 REMARK 500 LYS A 929 -39.94 -132.30 REMARK 500 CYS A 942 63.27 -110.85 REMARK 500 HIS A 956 106.61 -58.75 REMARK 500 ASN A 988 17.46 58.94 REMARK 500 ASP A1051 30.73 -95.42 REMARK 500 LYS A1093 77.94 -119.65 REMARK 500 LEU A1116 -108.52 59.22 REMARK 500 TYR A1122 49.97 -89.75 REMARK 500 ASN A1134 -80.67 -71.89 REMARK 500 ASN A1138 -113.17 56.27 REMARK 500 ALA A1167 56.15 -90.93 REMARK 500 ALA A1216 -97.59 55.30 REMARK 500 ASN C 74 -33.73 62.92 REMARK 500 ASP D 869 65.91 60.35 REMARK 500 ASP D 909 49.67 -147.77 REMARK 500 ASN D 928 17.43 59.00 REMARK 500 LYS D 929 -40.20 -132.71 REMARK 500 CYS D 942 63.92 -110.13 REMARK 500 HIS D 956 106.69 -59.05 REMARK 500 ASN D 988 17.87 58.59 REMARK 500 ASP D1051 30.20 -95.35 REMARK 500 LYS D1093 77.71 -119.28 REMARK 500 LEU D1116 -108.15 58.98 REMARK 500 TYR D1122 49.12 -89.92 REMARK 500 ASN D1134 -80.93 -71.14 REMARK 500 ASN D1138 -113.63 55.98 REMARK 500 ALA D1167 56.83 -90.21 REMARK 500 ALA D1216 -97.59 55.64 REMARK 500 ASN E 74 -33.33 67.79 REMARK 500 ASP F 909 49.07 -148.36 REMARK 500 ASN F 928 16.98 58.26 REMARK 500 LYS F 929 -40.24 -132.80 REMARK 500 CYS F 942 62.82 -110.15 REMARK 500 HIS F 956 106.27 -59.08 REMARK 500 ASN F 988 17.92 58.88 REMARK 500 ASP F1051 30.01 -95.20 REMARK 500 LYS F1093 76.96 -119.61 REMARK 500 LEU F1116 -107.99 58.32 REMARK 500 TYR F1122 48.98 -89.01 REMARK 500 ASN F1134 -79.02 -69.62 REMARK 500 ASN F1138 -113.64 56.00 REMARK 500 ALA F1167 56.40 -90.26 REMARK 500 ALA F1216 -97.98 55.60 REMARK 500 ASN G 74 -34.69 62.05 REMARK 500 ASP H 909 49.16 -148.13 REMARK 500 ASN H 928 17.03 58.80 REMARK 500 LYS H 929 -39.84 -132.79 REMARK 500 REMARK 500 THIS ENTRY HAS 74 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 7UIE B 0 137 PDB 7UIE 7UIE 0 137 DBREF 7UIE A 846 1252 UNP A5H0J8 A5H0J8_CLOBO 27 433 DBREF 7UIE C 0 137 PDB 7UIE 7UIE 0 137 DBREF 7UIE D 846 1252 UNP A5H0J8 A5H0J8_CLOBO 27 433 DBREF 7UIE E 0 137 PDB 7UIE 7UIE 0 137 DBREF 7UIE F 846 1252 UNP A5H0J8 A5H0J8_CLOBO 27 433 DBREF 7UIE I 0 137 PDB 7UIE 7UIE 0 137 DBREF 7UIE G 0 137 PDB 7UIE 7UIE 0 137 DBREF 7UIE H 846 1252 UNP A5H0J8 A5H0J8_CLOBO 27 433 DBREF 7UIE J 846 1252 UNP A5H0J8 A5H0J8_CLOBO 27 433 SEQADV 7UIE HIS A 830 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS A 831 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS A 832 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS A 833 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS A 834 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS A 835 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLY A 836 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE SER A 837 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE LEU A 838 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLU A 839 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE VAL A 840 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE LEU A 841 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE PHE A 842 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLN A 843 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLY A 844 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE PRO A 845 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS D 830 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS D 831 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS D 832 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS D 833 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS D 834 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS D 835 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLY D 836 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE SER D 837 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE LEU D 838 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLU D 839 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE VAL D 840 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE LEU D 841 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE PHE D 842 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLN D 843 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLY D 844 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE PRO D 845 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS F 830 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS F 831 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS F 832 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS F 833 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS F 834 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS F 835 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLY F 836 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE SER F 837 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE LEU F 838 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLU F 839 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE VAL F 840 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE LEU F 841 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE PHE F 842 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLN F 843 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLY F 844 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE PRO F 845 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS H 830 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS H 831 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS H 832 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS H 833 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS H 834 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS H 835 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLY H 836 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE SER H 837 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE LEU H 838 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLU H 839 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE VAL H 840 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE LEU H 841 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE PHE H 842 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLN H 843 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLY H 844 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE PRO H 845 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS J 830 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS J 831 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS J 832 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS J 833 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS J 834 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE HIS J 835 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLY J 836 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE SER J 837 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE LEU J 838 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLU J 839 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE VAL J 840 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE LEU J 841 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE PHE J 842 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLN J 843 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE GLY J 844 UNP A5H0J8 EXPRESSION TAG SEQADV 7UIE PRO J 845 UNP A5H0J8 EXPRESSION TAG SEQRES 1 B 138 SER GLN LEU GLN LEU VAL GLU THR GLY GLY GLY LEU VAL SEQRES 2 B 138 LYS PRO GLY GLY SER LEU ARG LEU SER CYS VAL VAL SER SEQRES 3 B 138 GLY PHE THR PHE ASP ASP TYR ARG MET ALA TRP VAL ARG SEQRES 4 B 138 GLN ALA PRO GLY LYS GLU LEU GLU TRP VAL SER SER ILE SEQRES 5 B 138 ASP SER TRP SER ILE ASN THR TYR TYR GLU ASP SER VAL SEQRES 6 B 138 LYS GLY ARG PHE THR ILE SER THR ASP ASN ALA LYS ASN SEQRES 7 B 138 THR LEU TYR LEU GLN MET SER SER LEU LYS PRO GLU ASP SEQRES 8 B 138 THR ALA VAL TYR TYR CYS ALA ALA GLU ASP ARG LEU GLY SEQRES 9 B 138 VAL PRO THR ILE ASN ALA HIS PRO SER LYS TYR ASP TYR SEQRES 10 B 138 ASN TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 B 138 GLU PRO LYS THR PRO LYS PRO GLN SEQRES 1 A 423 HIS HIS HIS HIS HIS HIS GLY SER LEU GLU VAL LEU PHE SEQRES 2 A 423 GLN GLY PRO ARG ILE LYS SER SER SER VAL LEU ASN MET SEQRES 3 A 423 ARG TYR LYS ASN ASP LYS TYR VAL ASP THR SER GLY TYR SEQRES 4 A 423 ASP SER ASN ILE ASN ILE ASN GLY ASP VAL TYR LYS TYR SEQRES 5 A 423 PRO THR ASN LYS ASN GLN PHE GLY ILE TYR ASN ASP LYS SEQRES 6 A 423 LEU SER GLU VAL ASN ILE SER GLN ASN ASP TYR ILE ILE SEQRES 7 A 423 TYR ASP ASN LYS TYR LYS ASN PHE SER ILE SER PHE TRP SEQRES 8 A 423 VAL ARG ILE PRO ASN TYR ASP ASN LYS ILE VAL ASN VAL SEQRES 9 A 423 ASN ASN GLU TYR THR ILE ILE ASN CYS MET ARG ASP ASN SEQRES 10 A 423 ASN SER GLY TRP LYS VAL SER LEU ASN HIS ASN GLU ILE SEQRES 11 A 423 ILE TRP THR LEU GLN ASP ASN ALA GLY ILE ASN GLN LYS SEQRES 12 A 423 LEU ALA PHE ASN TYR GLY ASN ALA ASN GLY ILE SER ASP SEQRES 13 A 423 TYR ILE ASN LYS TRP ILE PHE VAL THR ILE THR ASN ASP SEQRES 14 A 423 ARG LEU GLY ASP SER LYS LEU TYR ILE ASN GLY ASN LEU SEQRES 15 A 423 ILE ASP GLN LYS SER ILE LEU ASN LEU GLY ASN ILE HIS SEQRES 16 A 423 VAL SER ASP ASN ILE LEU PHE LYS ILE VAL ASN CYS SER SEQRES 17 A 423 TYR THR ARG TYR ILE GLY ILE ARG TYR PHE ASN ILE PHE SEQRES 18 A 423 ASP LYS GLU LEU ASP GLU THR GLU ILE GLN THR LEU TYR SEQRES 19 A 423 SER ASN GLU PRO ASN THR ASN ILE LEU LYS ASP PHE TRP SEQRES 20 A 423 GLY ASN TYR LEU LEU TYR ASP LYS GLU TYR TYR LEU LEU SEQRES 21 A 423 ASN VAL LEU LYS PRO ASN ASN PHE ILE ASP ARG ARG LYS SEQRES 22 A 423 ASP SER THR LEU SER ILE ASN ASN ILE ARG SER THR ILE SEQRES 23 A 423 LEU LEU ALA ASN ARG LEU TYR SER GLY ILE LYS VAL LYS SEQRES 24 A 423 ILE GLN ARG VAL ASN ASN SER SER THR ASN ASP ASN LEU SEQRES 25 A 423 VAL ARG LYS ASN ASP GLN VAL TYR ILE ASN PHE VAL ALA SEQRES 26 A 423 SER LYS THR HIS LEU PHE PRO LEU TYR ALA ASP THR ALA SEQRES 27 A 423 THR THR ASN LYS GLU LYS THR ILE LYS ILE SER SER SER SEQRES 28 A 423 GLY ASN ARG PHE ASN GLN VAL VAL VAL MET ASN SER VAL SEQRES 29 A 423 GLY ASN ASN CYS THR MET ASN PHE LYS ASN ASN ASN GLY SEQRES 30 A 423 ASN ASN ILE GLY LEU LEU GLY PHE LYS ALA ASP THR VAL SEQRES 31 A 423 VAL ALA SER THR TRP TYR TYR THR HIS MET ARG ASP HIS SEQRES 32 A 423 THR ASN SER ASN GLY CYS PHE TRP ASN PHE ILE SER GLU SEQRES 33 A 423 GLU HIS GLY TRP GLN GLU LYS SEQRES 1 C 138 SER GLN LEU GLN LEU VAL GLU THR GLY GLY GLY LEU VAL SEQRES 2 C 138 LYS PRO GLY GLY SER LEU ARG LEU SER CYS VAL VAL SER SEQRES 3 C 138 GLY PHE THR PHE ASP ASP TYR ARG MET ALA TRP VAL ARG SEQRES 4 C 138 GLN ALA PRO GLY LYS GLU LEU GLU TRP VAL SER SER ILE SEQRES 5 C 138 ASP SER TRP SER ILE ASN THR TYR TYR GLU ASP SER VAL SEQRES 6 C 138 LYS GLY ARG PHE THR ILE SER THR ASP ASN ALA LYS ASN SEQRES 7 C 138 THR LEU TYR LEU GLN MET SER SER LEU LYS PRO GLU ASP SEQRES 8 C 138 THR ALA VAL TYR TYR CYS ALA ALA GLU ASP ARG LEU GLY SEQRES 9 C 138 VAL PRO THR ILE ASN ALA HIS PRO SER LYS TYR ASP TYR SEQRES 10 C 138 ASN TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 C 138 GLU PRO LYS THR PRO LYS PRO GLN SEQRES 1 D 423 HIS HIS HIS HIS HIS HIS GLY SER LEU GLU VAL LEU PHE SEQRES 2 D 423 GLN GLY PRO ARG ILE LYS SER SER SER VAL LEU ASN MET SEQRES 3 D 423 ARG TYR LYS ASN ASP LYS TYR VAL ASP THR SER GLY TYR SEQRES 4 D 423 ASP SER ASN ILE ASN ILE ASN GLY ASP VAL TYR LYS TYR SEQRES 5 D 423 PRO THR ASN LYS ASN GLN PHE GLY ILE TYR ASN ASP LYS SEQRES 6 D 423 LEU SER GLU VAL ASN ILE SER GLN ASN ASP TYR ILE ILE SEQRES 7 D 423 TYR ASP ASN LYS TYR LYS ASN PHE SER ILE SER PHE TRP SEQRES 8 D 423 VAL ARG ILE PRO ASN TYR ASP ASN LYS ILE VAL ASN VAL SEQRES 9 D 423 ASN ASN GLU TYR THR ILE ILE ASN CYS MET ARG ASP ASN SEQRES 10 D 423 ASN SER GLY TRP LYS VAL SER LEU ASN HIS ASN GLU ILE SEQRES 11 D 423 ILE TRP THR LEU GLN ASP ASN ALA GLY ILE ASN GLN LYS SEQRES 12 D 423 LEU ALA PHE ASN TYR GLY ASN ALA ASN GLY ILE SER ASP SEQRES 13 D 423 TYR ILE ASN LYS TRP ILE PHE VAL THR ILE THR ASN ASP SEQRES 14 D 423 ARG LEU GLY ASP SER LYS LEU TYR ILE ASN GLY ASN LEU SEQRES 15 D 423 ILE ASP GLN LYS SER ILE LEU ASN LEU GLY ASN ILE HIS SEQRES 16 D 423 VAL SER ASP ASN ILE LEU PHE LYS ILE VAL ASN CYS SER SEQRES 17 D 423 TYR THR ARG TYR ILE GLY ILE ARG TYR PHE ASN ILE PHE SEQRES 18 D 423 ASP LYS GLU LEU ASP GLU THR GLU ILE GLN THR LEU TYR SEQRES 19 D 423 SER ASN GLU PRO ASN THR ASN ILE LEU LYS ASP PHE TRP SEQRES 20 D 423 GLY ASN TYR LEU LEU TYR ASP LYS GLU TYR TYR LEU LEU SEQRES 21 D 423 ASN VAL LEU LYS PRO ASN ASN PHE ILE ASP ARG ARG LYS SEQRES 22 D 423 ASP SER THR LEU SER ILE ASN ASN ILE ARG SER THR ILE SEQRES 23 D 423 LEU LEU ALA ASN ARG LEU TYR SER GLY ILE LYS VAL LYS SEQRES 24 D 423 ILE GLN ARG VAL ASN ASN SER SER THR ASN ASP ASN LEU SEQRES 25 D 423 VAL ARG LYS ASN ASP GLN VAL TYR ILE ASN PHE VAL ALA SEQRES 26 D 423 SER LYS THR HIS LEU PHE PRO LEU TYR ALA ASP THR ALA SEQRES 27 D 423 THR THR ASN LYS GLU LYS THR ILE LYS ILE SER SER SER SEQRES 28 D 423 GLY ASN ARG PHE ASN GLN VAL VAL VAL MET ASN SER VAL SEQRES 29 D 423 GLY ASN ASN CYS THR MET ASN PHE LYS ASN ASN ASN GLY SEQRES 30 D 423 ASN ASN ILE GLY LEU LEU GLY PHE LYS ALA ASP THR VAL SEQRES 31 D 423 VAL ALA SER THR TRP TYR TYR THR HIS MET ARG ASP HIS SEQRES 32 D 423 THR ASN SER ASN GLY CYS PHE TRP ASN PHE ILE SER GLU SEQRES 33 D 423 GLU HIS GLY TRP GLN GLU LYS SEQRES 1 E 138 SER GLN LEU GLN LEU VAL GLU THR GLY GLY GLY LEU VAL SEQRES 2 E 138 LYS PRO GLY GLY SER LEU ARG LEU SER CYS VAL VAL SER SEQRES 3 E 138 GLY PHE THR PHE ASP ASP TYR ARG MET ALA TRP VAL ARG SEQRES 4 E 138 GLN ALA PRO GLY LYS GLU LEU GLU TRP VAL SER SER ILE SEQRES 5 E 138 ASP SER TRP SER ILE ASN THR TYR TYR GLU ASP SER VAL SEQRES 6 E 138 LYS GLY ARG PHE THR ILE SER THR ASP ASN ALA LYS ASN SEQRES 7 E 138 THR LEU TYR LEU GLN MET SER SER LEU LYS PRO GLU ASP SEQRES 8 E 138 THR ALA VAL TYR TYR CYS ALA ALA GLU ASP ARG LEU GLY SEQRES 9 E 138 VAL PRO THR ILE ASN ALA HIS PRO SER LYS TYR ASP TYR SEQRES 10 E 138 ASN TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 E 138 GLU PRO LYS THR PRO LYS PRO GLN SEQRES 1 F 423 HIS HIS HIS HIS HIS HIS GLY SER LEU GLU VAL LEU PHE SEQRES 2 F 423 GLN GLY PRO ARG ILE LYS SER SER SER VAL LEU ASN MET SEQRES 3 F 423 ARG TYR LYS ASN ASP LYS TYR VAL ASP THR SER GLY TYR SEQRES 4 F 423 ASP SER ASN ILE ASN ILE ASN GLY ASP VAL TYR LYS TYR SEQRES 5 F 423 PRO THR ASN LYS ASN GLN PHE GLY ILE TYR ASN ASP LYS SEQRES 6 F 423 LEU SER GLU VAL ASN ILE SER GLN ASN ASP TYR ILE ILE SEQRES 7 F 423 TYR ASP ASN LYS TYR LYS ASN PHE SER ILE SER PHE TRP SEQRES 8 F 423 VAL ARG ILE PRO ASN TYR ASP ASN LYS ILE VAL ASN VAL SEQRES 9 F 423 ASN ASN GLU TYR THR ILE ILE ASN CYS MET ARG ASP ASN SEQRES 10 F 423 ASN SER GLY TRP LYS VAL SER LEU ASN HIS ASN GLU ILE SEQRES 11 F 423 ILE TRP THR LEU GLN ASP ASN ALA GLY ILE ASN GLN LYS SEQRES 12 F 423 LEU ALA PHE ASN TYR GLY ASN ALA ASN GLY ILE SER ASP SEQRES 13 F 423 TYR ILE ASN LYS TRP ILE PHE VAL THR ILE THR ASN ASP SEQRES 14 F 423 ARG LEU GLY ASP SER LYS LEU TYR ILE ASN GLY ASN LEU SEQRES 15 F 423 ILE ASP GLN LYS SER ILE LEU ASN LEU GLY ASN ILE HIS SEQRES 16 F 423 VAL SER ASP ASN ILE LEU PHE LYS ILE VAL ASN CYS SER SEQRES 17 F 423 TYR THR ARG TYR ILE GLY ILE ARG TYR PHE ASN ILE PHE SEQRES 18 F 423 ASP LYS GLU LEU ASP GLU THR GLU ILE GLN THR LEU TYR SEQRES 19 F 423 SER ASN GLU PRO ASN THR ASN ILE LEU LYS ASP PHE TRP SEQRES 20 F 423 GLY ASN TYR LEU LEU TYR ASP LYS GLU TYR TYR LEU LEU SEQRES 21 F 423 ASN VAL LEU LYS PRO ASN ASN PHE ILE ASP ARG ARG LYS SEQRES 22 F 423 ASP SER THR LEU SER ILE ASN ASN ILE ARG SER THR ILE SEQRES 23 F 423 LEU LEU ALA ASN ARG LEU TYR SER GLY ILE LYS VAL LYS SEQRES 24 F 423 ILE GLN ARG VAL ASN ASN SER SER THR ASN ASP ASN LEU SEQRES 25 F 423 VAL ARG LYS ASN ASP GLN VAL TYR ILE ASN PHE VAL ALA SEQRES 26 F 423 SER LYS THR HIS LEU PHE PRO LEU TYR ALA ASP THR ALA SEQRES 27 F 423 THR THR ASN LYS GLU LYS THR ILE LYS ILE SER SER SER SEQRES 28 F 423 GLY ASN ARG PHE ASN GLN VAL VAL VAL MET ASN SER VAL SEQRES 29 F 423 GLY ASN ASN CYS THR MET ASN PHE LYS ASN ASN ASN GLY SEQRES 30 F 423 ASN ASN ILE GLY LEU LEU GLY PHE LYS ALA ASP THR VAL SEQRES 31 F 423 VAL ALA SER THR TRP TYR TYR THR HIS MET ARG ASP HIS SEQRES 32 F 423 THR ASN SER ASN GLY CYS PHE TRP ASN PHE ILE SER GLU SEQRES 33 F 423 GLU HIS GLY TRP GLN GLU LYS SEQRES 1 I 138 SER GLN LEU GLN LEU VAL GLU THR GLY GLY GLY LEU VAL SEQRES 2 I 138 LYS PRO GLY GLY SER LEU ARG LEU SER CYS VAL VAL SER SEQRES 3 I 138 GLY PHE THR PHE ASP ASP TYR ARG MET ALA TRP VAL ARG SEQRES 4 I 138 GLN ALA PRO GLY LYS GLU LEU GLU TRP VAL SER SER ILE SEQRES 5 I 138 ASP SER TRP SER ILE ASN THR TYR TYR GLU ASP SER VAL SEQRES 6 I 138 LYS GLY ARG PHE THR ILE SER THR ASP ASN ALA LYS ASN SEQRES 7 I 138 THR LEU TYR LEU GLN MET SER SER LEU LYS PRO GLU ASP SEQRES 8 I 138 THR ALA VAL TYR TYR CYS ALA ALA GLU ASP ARG LEU GLY SEQRES 9 I 138 VAL PRO THR ILE ASN ALA HIS PRO SER LYS TYR ASP TYR SEQRES 10 I 138 ASN TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 I 138 GLU PRO LYS THR PRO LYS PRO GLN SEQRES 1 G 138 SER GLN LEU GLN LEU VAL GLU THR GLY GLY GLY LEU VAL SEQRES 2 G 138 LYS PRO GLY GLY SER LEU ARG LEU SER CYS VAL VAL SER SEQRES 3 G 138 GLY PHE THR PHE ASP ASP TYR ARG MET ALA TRP VAL ARG SEQRES 4 G 138 GLN ALA PRO GLY LYS GLU LEU GLU TRP VAL SER SER ILE SEQRES 5 G 138 ASP SER TRP SER ILE ASN THR TYR TYR GLU ASP SER VAL SEQRES 6 G 138 LYS GLY ARG PHE THR ILE SER THR ASP ASN ALA LYS ASN SEQRES 7 G 138 THR LEU TYR LEU GLN MET SER SER LEU LYS PRO GLU ASP SEQRES 8 G 138 THR ALA VAL TYR TYR CYS ALA ALA GLU ASP ARG LEU GLY SEQRES 9 G 138 VAL PRO THR ILE ASN ALA HIS PRO SER LYS TYR ASP TYR SEQRES 10 G 138 ASN TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 G 138 GLU PRO LYS THR PRO LYS PRO GLN SEQRES 1 H 423 HIS HIS HIS HIS HIS HIS GLY SER LEU GLU VAL LEU PHE SEQRES 2 H 423 GLN GLY PRO ARG ILE LYS SER SER SER VAL LEU ASN MET SEQRES 3 H 423 ARG TYR LYS ASN ASP LYS TYR VAL ASP THR SER GLY TYR SEQRES 4 H 423 ASP SER ASN ILE ASN ILE ASN GLY ASP VAL TYR LYS TYR SEQRES 5 H 423 PRO THR ASN LYS ASN GLN PHE GLY ILE TYR ASN ASP LYS SEQRES 6 H 423 LEU SER GLU VAL ASN ILE SER GLN ASN ASP TYR ILE ILE SEQRES 7 H 423 TYR ASP ASN LYS TYR LYS ASN PHE SER ILE SER PHE TRP SEQRES 8 H 423 VAL ARG ILE PRO ASN TYR ASP ASN LYS ILE VAL ASN VAL SEQRES 9 H 423 ASN ASN GLU TYR THR ILE ILE ASN CYS MET ARG ASP ASN SEQRES 10 H 423 ASN SER GLY TRP LYS VAL SER LEU ASN HIS ASN GLU ILE SEQRES 11 H 423 ILE TRP THR LEU GLN ASP ASN ALA GLY ILE ASN GLN LYS SEQRES 12 H 423 LEU ALA PHE ASN TYR GLY ASN ALA ASN GLY ILE SER ASP SEQRES 13 H 423 TYR ILE ASN LYS TRP ILE PHE VAL THR ILE THR ASN ASP SEQRES 14 H 423 ARG LEU GLY ASP SER LYS LEU TYR ILE ASN GLY ASN LEU SEQRES 15 H 423 ILE ASP GLN LYS SER ILE LEU ASN LEU GLY ASN ILE HIS SEQRES 16 H 423 VAL SER ASP ASN ILE LEU PHE LYS ILE VAL ASN CYS SER SEQRES 17 H 423 TYR THR ARG TYR ILE GLY ILE ARG TYR PHE ASN ILE PHE SEQRES 18 H 423 ASP LYS GLU LEU ASP GLU THR GLU ILE GLN THR LEU TYR SEQRES 19 H 423 SER ASN GLU PRO ASN THR ASN ILE LEU LYS ASP PHE TRP SEQRES 20 H 423 GLY ASN TYR LEU LEU TYR ASP LYS GLU TYR TYR LEU LEU SEQRES 21 H 423 ASN VAL LEU LYS PRO ASN ASN PHE ILE ASP ARG ARG LYS SEQRES 22 H 423 ASP SER THR LEU SER ILE ASN ASN ILE ARG SER THR ILE SEQRES 23 H 423 LEU LEU ALA ASN ARG LEU TYR SER GLY ILE LYS VAL LYS SEQRES 24 H 423 ILE GLN ARG VAL ASN ASN SER SER THR ASN ASP ASN LEU SEQRES 25 H 423 VAL ARG LYS ASN ASP GLN VAL TYR ILE ASN PHE VAL ALA SEQRES 26 H 423 SER LYS THR HIS LEU PHE PRO LEU TYR ALA ASP THR ALA SEQRES 27 H 423 THR THR ASN LYS GLU LYS THR ILE LYS ILE SER SER SER SEQRES 28 H 423 GLY ASN ARG PHE ASN GLN VAL VAL VAL MET ASN SER VAL SEQRES 29 H 423 GLY ASN ASN CYS THR MET ASN PHE LYS ASN ASN ASN GLY SEQRES 30 H 423 ASN ASN ILE GLY LEU LEU GLY PHE LYS ALA ASP THR VAL SEQRES 31 H 423 VAL ALA SER THR TRP TYR TYR THR HIS MET ARG ASP HIS SEQRES 32 H 423 THR ASN SER ASN GLY CYS PHE TRP ASN PHE ILE SER GLU SEQRES 33 H 423 GLU HIS GLY TRP GLN GLU LYS SEQRES 1 J 423 HIS HIS HIS HIS HIS HIS GLY SER LEU GLU VAL LEU PHE SEQRES 2 J 423 GLN GLY PRO ARG ILE LYS SER SER SER VAL LEU ASN MET SEQRES 3 J 423 ARG TYR LYS ASN ASP LYS TYR VAL ASP THR SER GLY TYR SEQRES 4 J 423 ASP SER ASN ILE ASN ILE ASN GLY ASP VAL TYR LYS TYR SEQRES 5 J 423 PRO THR ASN LYS ASN GLN PHE GLY ILE TYR ASN ASP LYS SEQRES 6 J 423 LEU SER GLU VAL ASN ILE SER GLN ASN ASP TYR ILE ILE SEQRES 7 J 423 TYR ASP ASN LYS TYR LYS ASN PHE SER ILE SER PHE TRP SEQRES 8 J 423 VAL ARG ILE PRO ASN TYR ASP ASN LYS ILE VAL ASN VAL SEQRES 9 J 423 ASN ASN GLU TYR THR ILE ILE ASN CYS MET ARG ASP ASN SEQRES 10 J 423 ASN SER GLY TRP LYS VAL SER LEU ASN HIS ASN GLU ILE SEQRES 11 J 423 ILE TRP THR LEU GLN ASP ASN ALA GLY ILE ASN GLN LYS SEQRES 12 J 423 LEU ALA PHE ASN TYR GLY ASN ALA ASN GLY ILE SER ASP SEQRES 13 J 423 TYR ILE ASN LYS TRP ILE PHE VAL THR ILE THR ASN ASP SEQRES 14 J 423 ARG LEU GLY ASP SER LYS LEU TYR ILE ASN GLY ASN LEU SEQRES 15 J 423 ILE ASP GLN LYS SER ILE LEU ASN LEU GLY ASN ILE HIS SEQRES 16 J 423 VAL SER ASP ASN ILE LEU PHE LYS ILE VAL ASN CYS SER SEQRES 17 J 423 TYR THR ARG TYR ILE GLY ILE ARG TYR PHE ASN ILE PHE SEQRES 18 J 423 ASP LYS GLU LEU ASP GLU THR GLU ILE GLN THR LEU TYR SEQRES 19 J 423 SER ASN GLU PRO ASN THR ASN ILE LEU LYS ASP PHE TRP SEQRES 20 J 423 GLY ASN TYR LEU LEU TYR ASP LYS GLU TYR TYR LEU LEU SEQRES 21 J 423 ASN VAL LEU LYS PRO ASN ASN PHE ILE ASP ARG ARG LYS SEQRES 22 J 423 ASP SER THR LEU SER ILE ASN ASN ILE ARG SER THR ILE SEQRES 23 J 423 LEU LEU ALA ASN ARG LEU TYR SER GLY ILE LYS VAL LYS SEQRES 24 J 423 ILE GLN ARG VAL ASN ASN SER SER THR ASN ASP ASN LEU SEQRES 25 J 423 VAL ARG LYS ASN ASP GLN VAL TYR ILE ASN PHE VAL ALA SEQRES 26 J 423 SER LYS THR HIS LEU PHE PRO LEU TYR ALA ASP THR ALA SEQRES 27 J 423 THR THR ASN LYS GLU LYS THR ILE LYS ILE SER SER SER SEQRES 28 J 423 GLY ASN ARG PHE ASN GLN VAL VAL VAL MET ASN SER VAL SEQRES 29 J 423 GLY ASN ASN CYS THR MET ASN PHE LYS ASN ASN ASN GLY SEQRES 30 J 423 ASN ASN ILE GLY LEU LEU GLY PHE LYS ALA ASP THR VAL SEQRES 31 J 423 VAL ALA SER THR TRP TYR TYR THR HIS MET ARG ASP HIS SEQRES 32 J 423 THR ASN SER ASN GLY CYS PHE TRP ASN PHE ILE SER GLU SEQRES 33 J 423 GLU HIS GLY TRP GLN GLU LYS HELIX 1 AA1 LYS B 87 THR B 91 5 5 HELIX 2 AA2 SER B 112 TYR B 116 5 5 HELIX 3 AA3 ASP A 1055 GLU A 1066 1 12 HELIX 4 AA4 THR A 1223 THR A 1227 5 5 HELIX 5 AA5 ASN A 1234 CYS A 1238 5 5 HELIX 6 AA6 LYS C 87 THR C 91 5 5 HELIX 7 AA7 SER C 112 TYR C 116 5 5 HELIX 8 AA8 ASP D 1055 GLU D 1066 1 12 HELIX 9 AA9 THR D 1223 THR D 1227 5 5 HELIX 10 AB1 ASN D 1234 CYS D 1238 5 5 HELIX 11 AB2 LYS E 87 THR E 91 5 5 HELIX 12 AB3 SER E 112 TYR E 116 5 5 HELIX 13 AB4 ASP F 1055 GLU F 1066 1 12 HELIX 14 AB5 THR F 1223 THR F 1227 5 5 HELIX 15 AB6 ASN F 1234 CYS F 1238 5 5 HELIX 16 AB7 LYS I 87 THR I 91 5 5 HELIX 17 AB8 SER I 112 TYR I 116 5 5 HELIX 18 AB9 LYS G 87 THR G 91 5 5 HELIX 19 AC1 SER G 112 TYR G 116 5 5 HELIX 20 AC2 ASP H 1055 GLU H 1066 1 12 HELIX 21 AC3 THR H 1223 THR H 1227 5 5 HELIX 22 AC4 ASN H 1234 CYS H 1238 5 5 HELIX 23 AC5 ASP J 1055 GLU J 1066 1 12 HELIX 24 AC6 THR J 1223 THR J 1227 5 5 HELIX 25 AC7 ASN J 1234 CYS J 1238 5 5 SHEET 1 AA1 4 VAL B 5 THR B 7 0 SHEET 2 AA1 4 SER B 17 VAL B 23 -1 O SER B 21 N THR B 7 SHEET 3 AA1 4 THR B 78 SER B 84 -1 O MET B 83 N LEU B 18 SHEET 4 AA1 4 PHE B 68 THR B 72 -1 N THR B 69 O GLN B 82 SHEET 1 AA2 6 LEU B 11 VAL B 12 0 SHEET 2 AA2 6 THR B 123 VAL B 127 1 O THR B 126 N VAL B 12 SHEET 3 AA2 6 ALA B 92 ASP B 100 -1 N TYR B 94 O THR B 123 SHEET 4 AA2 6 TYR B 32 GLN B 39 -1 N VAL B 37 O TYR B 95 SHEET 5 AA2 6 LEU B 45 ILE B 51 -1 O GLU B 46 N ARG B 38 SHEET 6 AA2 6 THR B 58 TYR B 60 -1 O TYR B 59 N SER B 50 SHEET 1 AA3 4 LEU B 11 VAL B 12 0 SHEET 2 AA3 4 THR B 123 VAL B 127 1 O THR B 126 N VAL B 12 SHEET 3 AA3 4 ALA B 92 ASP B 100 -1 N TYR B 94 O THR B 123 SHEET 4 AA3 4 TYR B 118 TRP B 119 -1 O TYR B 118 N ALA B 98 SHEET 1 AA4 5 LYS A 861 ASP A 864 0 SHEET 2 AA4 5 SER A 851 LYS A 858 -1 N ARG A 856 O VAL A 863 SHEET 3 AA4 5 TYR A1041 PHE A1050 -1 O ILE A1049 N VAL A 852 SHEET 4 AA4 5 GLN A 887 TYR A 891 -1 N PHE A 888 O ILE A1044 SHEET 5 AA4 5 TYR A 879 LYS A 880 -1 N TYR A 879 O GLY A 889 SHEET 1 AA5 7 LYS A 861 ASP A 864 0 SHEET 2 AA5 7 SER A 851 LYS A 858 -1 N ARG A 856 O VAL A 863 SHEET 3 AA5 7 TYR A1041 PHE A1050 -1 O ILE A1049 N VAL A 852 SHEET 4 AA5 7 PHE A 915 ARG A 922 -1 N SER A 918 O ASN A1048 SHEET 5 AA5 7 TRP A 990 ASN A 997 -1 O VAL A 993 N PHE A 919 SHEET 6 AA5 7 ASP A1002 ILE A1007 -1 O TYR A1006 N THR A 994 SHEET 7 AA5 7 ASN A1010 SER A1016 -1 O LYS A1015 N SER A1003 SHEET 1 AA6 7 ASN A 871 GLY A 876 0 SHEET 2 AA6 7 SER A 896 SER A 901 -1 O SER A 901 N ASN A 871 SHEET 3 AA6 7 ASN A1028 VAL A1034 -1 O PHE A1031 N VAL A 898 SHEET 4 AA6 7 TYR A 937 MET A 943 -1 N ILE A 939 O LYS A1032 SHEET 5 AA6 7 GLY A 949 ASN A 955 -1 O LEU A 954 N TYR A 937 SHEET 6 AA6 7 GLU A 958 GLN A 964 -1 O ILE A 960 N SER A 953 SHEET 7 AA6 7 ASN A 970 ASN A 976 -1 O LEU A 973 N TRP A 961 SHEET 1 AA7 2 ASP A 909 ASN A 910 0 SHEET 2 AA7 2 ILE A1023 HIS A1024 -1 O ILE A1023 N ASN A 910 SHEET 1 AA813 ASP A1146 VAL A1153 0 SHEET 2 AA813 LEU A1159 ALA A1164 -1 O PHE A1160 N PHE A1152 SHEET 3 AA813 LYS A1173 ILE A1177 -1 O LYS A1176 N TYR A1163 SHEET 4 AA813 THR A1218 SER A1222 -1 O ALA A1221 N LYS A1173 SHEET 5 AA813 ASN A1208 LYS A1215 -1 N LYS A1215 O THR A1218 SHEET 6 AA813 ASN A1196 ASN A1203 -1 N PHE A1201 O GLY A1210 SHEET 7 AA813 ASP A1146 VAL A1153 0 SHEET 8 AA813 LYS A1126 ARG A1131 -1 N LYS A1128 O ASN A1151 SHEET 9 AA813 TYR A1086 ASN A1090 -1 N TYR A1086 O VAL A1127 SHEET 10 AA813 TRP A1240 ILE A1243 -1 O ILE A1243 N TYR A1087 SHEET 11 AA813 ASN A1196 ASN A1203 -1 N CYS A1197 O TRP A1240 SHEET 12 AA813 GLN A1186 VAL A1193 -1 N VAL A1187 O LYS A1202 SHEET 13 AA813 ASN A1196 ASN A1203 -1 O LYS A1202 N VAL A1187 SHEET 1 AA9 2 ASN A1096 ARG A1100 0 SHEET 2 AA9 2 LEU A1106 ILE A1111 -1 O ASN A1110 N PHE A1097 SHEET 1 AB1 2 THR A1114 ILE A1115 0 SHEET 2 AB1 2 ALA A1118 ASN A1119 -1 O ALA A1118 N ILE A1115 SHEET 1 AB2 4 VAL C 5 THR C 7 0 SHEET 2 AB2 4 SER C 17 VAL C 23 -1 O SER C 21 N THR C 7 SHEET 3 AB2 4 THR C 78 SER C 84 -1 O LEU C 79 N CYS C 22 SHEET 4 AB2 4 PHE C 68 THR C 72 -1 N THR C 69 O GLN C 82 SHEET 1 AB3 6 LEU C 11 VAL C 12 0 SHEET 2 AB3 6 THR C 123 VAL C 127 1 O THR C 126 N VAL C 12 SHEET 3 AB3 6 ALA C 92 ASP C 100 -1 N TYR C 94 O THR C 123 SHEET 4 AB3 6 TYR C 32 GLN C 39 -1 N VAL C 37 O TYR C 95 SHEET 5 AB3 6 LEU C 45 ILE C 51 -1 O GLU C 46 N ARG C 38 SHEET 6 AB3 6 THR C 58 TYR C 60 -1 O TYR C 59 N SER C 50 SHEET 1 AB4 4 LEU C 11 VAL C 12 0 SHEET 2 AB4 4 THR C 123 VAL C 127 1 O THR C 126 N VAL C 12 SHEET 3 AB4 4 ALA C 92 ASP C 100 -1 N TYR C 94 O THR C 123 SHEET 4 AB4 4 TYR C 118 TRP C 119 -1 O TYR C 118 N ALA C 98 SHEET 1 AB5 5 LYS D 861 ASP D 864 0 SHEET 2 AB5 5 SER D 851 LYS D 858 -1 N ARG D 856 O VAL D 863 SHEET 3 AB5 5 TYR D1041 PHE D1050 -1 O ILE D1049 N VAL D 852 SHEET 4 AB5 5 PHE D 888 TYR D 891 -1 N PHE D 888 O ILE D1044 SHEET 5 AB5 5 TYR D 879 LYS D 880 -1 N TYR D 879 O GLY D 889 SHEET 1 AB6 7 LYS D 861 ASP D 864 0 SHEET 2 AB6 7 SER D 851 LYS D 858 -1 N ARG D 856 O VAL D 863 SHEET 3 AB6 7 TYR D1041 PHE D1050 -1 O ILE D1049 N VAL D 852 SHEET 4 AB6 7 PHE D 915 ARG D 922 -1 N SER D 918 O ASN D1048 SHEET 5 AB6 7 TRP D 990 ASN D 997 -1 O VAL D 993 N PHE D 919 SHEET 6 AB6 7 ASP D1002 ILE D1007 -1 O TYR D1006 N THR D 994 SHEET 7 AB6 7 ASN D1010 SER D1016 -1 O LYS D1015 N SER D1003 SHEET 1 AB7 7 ASN D 871 GLY D 876 0 SHEET 2 AB7 7 SER D 896 SER D 901 -1 O SER D 901 N ASN D 871 SHEET 3 AB7 7 ASN D1028 VAL D1034 -1 O PHE D1031 N VAL D 898 SHEET 4 AB7 7 TYR D 937 MET D 943 -1 N ILE D 939 O LYS D1032 SHEET 5 AB7 7 GLY D 949 ASN D 955 -1 O LEU D 954 N TYR D 937 SHEET 6 AB7 7 GLU D 958 GLN D 964 -1 O ILE D 960 N SER D 953 SHEET 7 AB7 7 ASN D 970 ASN D 976 -1 O LEU D 973 N TRP D 961 SHEET 1 AB8 2 ASP D 909 ASN D 910 0 SHEET 2 AB8 2 ILE D1023 HIS D1024 -1 O ILE D1023 N ASN D 910 SHEET 1 AB913 GLN D1147 VAL D1153 0 SHEET 2 AB913 LEU D1159 ALA D1164 -1 O PHE D1160 N PHE D1152 SHEET 3 AB913 LYS D1173 ILE D1177 -1 O LYS D1176 N TYR D1163 SHEET 4 AB913 THR D1218 SER D1222 -1 O ALA D1221 N LYS D1173 SHEET 5 AB913 ASN D1208 LYS D1215 -1 N LYS D1215 O THR D1218 SHEET 6 AB913 ASN D1196 ASN D1203 -1 N PHE D1201 O GLY D1210 SHEET 7 AB913 GLN D1147 VAL D1153 0 SHEET 8 AB913 LYS D1126 ARG D1131 -1 N LYS D1128 O ASN D1151 SHEET 9 AB913 TYR D1086 ASN D1090 -1 N TYR D1086 O VAL D1127 SHEET 10 AB913 TRP D1240 ILE D1243 -1 O ILE D1243 N TYR D1087 SHEET 11 AB913 ASN D1196 ASN D1203 -1 N CYS D1197 O TRP D1240 SHEET 12 AB913 GLN D1186 VAL D1193 -1 N VAL D1189 O ASN D1200 SHEET 13 AB913 ASN D1196 ASN D1203 -1 O ASN D1200 N VAL D1189 SHEET 1 AC1 2 ASN D1096 ARG D1100 0 SHEET 2 AC1 2 LEU D1106 ILE D1111 -1 O SER D1107 N ASP D1099 SHEET 1 AC2 2 THR D1114 ILE D1115 0 SHEET 2 AC2 2 ALA D1118 ASN D1119 -1 O ALA D1118 N ILE D1115 SHEET 1 AC3 4 GLN E 3 THR E 7 0 SHEET 2 AC3 4 SER E 17 SER E 25 -1 O SER E 21 N THR E 7 SHEET 3 AC3 4 THR E 78 SER E 84 -1 O MET E 83 N LEU E 18 SHEET 4 AC3 4 PHE E 68 THR E 72 -1 N THR E 69 O GLN E 82 SHEET 1 AC4 6 LEU E 11 VAL E 12 0 SHEET 2 AC4 6 THR E 123 VAL E 127 1 O THR E 126 N VAL E 12 SHEET 3 AC4 6 ALA E 92 ASP E 100 -1 N TYR E 94 O THR E 123 SHEET 4 AC4 6 TYR E 32 GLN E 39 -1 N VAL E 37 O TYR E 95 SHEET 5 AC4 6 LEU E 45 ILE E 51 -1 O GLU E 46 N ARG E 38 SHEET 6 AC4 6 THR E 58 TYR E 60 -1 O TYR E 59 N SER E 50 SHEET 1 AC5 4 LEU E 11 VAL E 12 0 SHEET 2 AC5 4 THR E 123 VAL E 127 1 O THR E 126 N VAL E 12 SHEET 3 AC5 4 ALA E 92 ASP E 100 -1 N TYR E 94 O THR E 123 SHEET 4 AC5 4 TYR E 118 TRP E 119 -1 O TYR E 118 N ALA E 98 SHEET 1 AC6 5 LYS F 861 ASP F 864 0 SHEET 2 AC6 5 SER F 851 LYS F 858 -1 N ARG F 856 O VAL F 863 SHEET 3 AC6 5 TYR F1041 PHE F1050 -1 O ILE F1049 N VAL F 852 SHEET 4 AC6 5 GLN F 887 TYR F 891 -1 N PHE F 888 O ILE F1044 SHEET 5 AC6 5 TYR F 879 LYS F 880 -1 N TYR F 879 O GLY F 889 SHEET 1 AC7 7 LYS F 861 ASP F 864 0 SHEET 2 AC7 7 SER F 851 LYS F 858 -1 N ARG F 856 O VAL F 863 SHEET 3 AC7 7 TYR F1041 PHE F1050 -1 O ILE F1049 N VAL F 852 SHEET 4 AC7 7 PHE F 915 ARG F 922 -1 N SER F 918 O ASN F1048 SHEET 5 AC7 7 TRP F 990 ASN F 997 -1 O VAL F 993 N PHE F 919 SHEET 6 AC7 7 ASP F1002 ILE F1007 -1 O TYR F1006 N THR F 994 SHEET 7 AC7 7 ASN F1010 SER F1016 -1 O LYS F1015 N SER F1003 SHEET 1 AC8 7 ASN F 871 GLY F 876 0 SHEET 2 AC8 7 SER F 896 SER F 901 -1 O GLU F 897 N ASN F 875 SHEET 3 AC8 7 ASN F1028 VAL F1034 -1 O PHE F1031 N VAL F 898 SHEET 4 AC8 7 TYR F 937 MET F 943 -1 N ILE F 939 O LYS F1032 SHEET 5 AC8 7 GLY F 949 ASN F 955 -1 O LEU F 954 N TYR F 937 SHEET 6 AC8 7 GLU F 958 GLN F 964 -1 O ILE F 960 N SER F 953 SHEET 7 AC8 7 ASN F 970 ASN F 976 -1 O LEU F 973 N TRP F 961 SHEET 1 AC9 2 ASP F 909 ASN F 910 0 SHEET 2 AC9 2 ILE F1023 HIS F1024 -1 O ILE F1023 N ASN F 910 SHEET 1 AD113 ASP F1146 VAL F1153 0 SHEET 2 AD113 LEU F1159 ALA F1164 -1 O PHE F1160 N PHE F1152 SHEET 3 AD113 LYS F1173 ILE F1177 -1 O LYS F1176 N TYR F1163 SHEET 4 AD113 THR F1218 SER F1222 -1 O ALA F1221 N LYS F1173 SHEET 5 AD113 ASN F1208 LYS F1215 -1 N LYS F1215 O THR F1218 SHEET 6 AD113 ASN F1196 ASN F1203 -1 N PHE F1201 O GLY F1210 SHEET 7 AD113 ASP F1146 VAL F1153 0 SHEET 8 AD113 LYS F1126 ARG F1131 -1 N LYS F1128 O ASN F1151 SHEET 9 AD113 TYR F1086 ASN F1090 -1 N TYR F1086 O VAL F1127 SHEET 10 AD113 TRP F1240 ILE F1243 -1 O ILE F1243 N TYR F1087 SHEET 11 AD113 ASN F1196 ASN F1203 -1 N CYS F1197 O TRP F1240 SHEET 12 AD113 GLN F1186 VAL F1193 -1 N VAL F1187 O LYS F1202 SHEET 13 AD113 ASN F1196 ASN F1203 -1 O LYS F1202 N VAL F1187 SHEET 1 AD2 2 ASN F1096 ARG F1100 0 SHEET 2 AD2 2 LEU F1106 ILE F1111 -1 O SER F1107 N ASP F1099 SHEET 1 AD3 2 THR F1114 ILE F1115 0 SHEET 2 AD3 2 ALA F1118 ASN F1119 -1 O ALA F1118 N ILE F1115 SHEET 1 AD4 4 LEU I 4 THR I 7 0 SHEET 2 AD4 4 SER I 17 VAL I 24 -1 O SER I 21 N THR I 7 SHEET 3 AD4 4 THR I 78 SER I 84 -1 O MET I 83 N LEU I 18 SHEET 4 AD4 4 PHE I 68 THR I 72 -1 N THR I 69 O GLN I 82 SHEET 1 AD5 6 LEU I 11 VAL I 12 0 SHEET 2 AD5 6 THR I 123 VAL I 127 1 O THR I 126 N VAL I 12 SHEET 3 AD5 6 ALA I 92 ASP I 100 -1 N TYR I 94 O THR I 123 SHEET 4 AD5 6 TYR I 32 GLN I 39 -1 N VAL I 37 O TYR I 95 SHEET 5 AD5 6 GLU I 46 ILE I 51 -1 O VAL I 48 N TRP I 36 SHEET 6 AD5 6 THR I 58 TYR I 60 -1 O TYR I 59 N SER I 50 SHEET 1 AD6 4 LEU I 11 VAL I 12 0 SHEET 2 AD6 4 THR I 123 VAL I 127 1 O THR I 126 N VAL I 12 SHEET 3 AD6 4 ALA I 92 ASP I 100 -1 N TYR I 94 O THR I 123 SHEET 4 AD6 4 TYR I 118 TRP I 119 -1 O TYR I 118 N ALA I 98 SHEET 1 AD7 4 VAL G 5 THR G 7 0 SHEET 2 AD7 4 SER G 17 VAL G 23 -1 O SER G 21 N THR G 7 SHEET 3 AD7 4 THR G 78 SER G 84 -1 O MET G 83 N LEU G 18 SHEET 4 AD7 4 PHE G 68 THR G 72 -1 N THR G 69 O GLN G 82 SHEET 1 AD8 6 LEU G 11 VAL G 12 0 SHEET 2 AD8 6 THR G 123 VAL G 127 1 O THR G 126 N VAL G 12 SHEET 3 AD8 6 ALA G 92 ASP G 100 -1 N TYR G 94 O THR G 123 SHEET 4 AD8 6 TYR G 32 GLN G 39 -1 N VAL G 37 O TYR G 95 SHEET 5 AD8 6 LEU G 45 ILE G 51 -1 O GLU G 46 N ARG G 38 SHEET 6 AD8 6 THR G 58 TYR G 60 -1 O TYR G 59 N SER G 50 SHEET 1 AD9 4 LEU G 11 VAL G 12 0 SHEET 2 AD9 4 THR G 123 VAL G 127 1 O THR G 126 N VAL G 12 SHEET 3 AD9 4 ALA G 92 ASP G 100 -1 N TYR G 94 O THR G 123 SHEET 4 AD9 4 TYR G 118 TRP G 119 -1 O TYR G 118 N ALA G 98 SHEET 1 AE1 5 LYS H 861 ASP H 864 0 SHEET 2 AE1 5 SER H 851 LYS H 858 -1 N ARG H 856 O VAL H 863 SHEET 3 AE1 5 TYR H1041 PHE H1050 -1 O ILE H1049 N VAL H 852 SHEET 4 AE1 5 GLN H 887 TYR H 891 -1 N PHE H 888 O ILE H1044 SHEET 5 AE1 5 TYR H 879 LYS H 880 -1 N TYR H 879 O GLY H 889 SHEET 1 AE2 7 LYS H 861 ASP H 864 0 SHEET 2 AE2 7 SER H 851 LYS H 858 -1 N ARG H 856 O VAL H 863 SHEET 3 AE2 7 TYR H1041 PHE H1050 -1 O ILE H1049 N VAL H 852 SHEET 4 AE2 7 PHE H 915 ARG H 922 -1 N SER H 918 O ASN H1048 SHEET 5 AE2 7 TRP H 990 ASN H 997 -1 O ILE H 991 N VAL H 921 SHEET 6 AE2 7 ASP H1002 ILE H1007 -1 O TYR H1006 N THR H 994 SHEET 7 AE2 7 ASN H1010 SER H1016 -1 O LYS H1015 N SER H1003 SHEET 1 AE3 7 ASN H 871 GLY H 876 0 SHEET 2 AE3 7 SER H 896 SER H 901 -1 O SER H 901 N ASN H 871 SHEET 3 AE3 7 ASN H1028 VAL H1034 -1 O PHE H1031 N VAL H 898 SHEET 4 AE3 7 TYR H 937 MET H 943 -1 N ILE H 939 O LYS H1032 SHEET 5 AE3 7 GLY H 949 ASN H 955 -1 O LEU H 954 N TYR H 937 SHEET 6 AE3 7 GLU H 958 GLN H 964 -1 O ILE H 960 N SER H 953 SHEET 7 AE3 7 ASN H 970 ASN H 976 -1 O LEU H 973 N TRP H 961 SHEET 1 AE4 2 ASP H 909 ASN H 910 0 SHEET 2 AE4 2 ILE H1023 HIS H1024 -1 O ILE H1023 N ASN H 910 SHEET 1 AE513 ASP H1146 VAL H1153 0 SHEET 2 AE513 LEU H1159 ALA H1164 -1 O PHE H1160 N PHE H1152 SHEET 3 AE513 LYS H1173 ILE H1177 -1 O LYS H1176 N TYR H1163 SHEET 4 AE513 THR H1218 SER H1222 -1 O ALA H1221 N LYS H1173 SHEET 5 AE513 ASN H1208 LYS H1215 -1 N LYS H1215 O THR H1218 SHEET 6 AE513 ASN H1196 ASN H1203 -1 N PHE H1201 O GLY H1210 SHEET 7 AE513 ASP H1146 VAL H1153 0 SHEET 8 AE513 LYS H1126 ARG H1131 -1 N LYS H1128 O ASN H1151 SHEET 9 AE513 TYR H1086 ASN H1090 -1 N TYR H1086 O VAL H1127 SHEET 10 AE513 TRP H1240 ILE H1243 -1 O ILE H1243 N TYR H1087 SHEET 11 AE513 ASN H1196 ASN H1203 -1 N CYS H1197 O TRP H1240 SHEET 12 AE513 GLN H1186 VAL H1193 -1 N VAL H1189 O ASN H1200 SHEET 13 AE513 ASN H1196 ASN H1203 -1 O ASN H1200 N VAL H1189 SHEET 1 AE6 2 ASN H1096 ARG H1100 0 SHEET 2 AE6 2 LEU H1106 ILE H1111 -1 O SER H1107 N ASP H1099 SHEET 1 AE7 2 THR H1114 ILE H1115 0 SHEET 2 AE7 2 ALA H1118 ASN H1119 -1 O ALA H1118 N ILE H1115 SHEET 1 AE8 5 LYS J 861 ASP J 864 0 SHEET 2 AE8 5 SER J 851 LYS J 858 -1 N ARG J 856 O VAL J 863 SHEET 3 AE8 5 TYR J1041 PHE J1050 -1 O ILE J1049 N VAL J 852 SHEET 4 AE8 5 GLN J 887 TYR J 891 -1 N PHE J 888 O ILE J1044 SHEET 5 AE8 5 TYR J 879 LYS J 880 -1 N TYR J 879 O GLY J 889 SHEET 1 AE9 7 LYS J 861 ASP J 864 0 SHEET 2 AE9 7 SER J 851 LYS J 858 -1 N ARG J 856 O VAL J 863 SHEET 3 AE9 7 TYR J1041 PHE J1050 -1 O ILE J1049 N VAL J 852 SHEET 4 AE9 7 PHE J 915 ARG J 922 -1 N SER J 918 O ASN J1048 SHEET 5 AE9 7 TRP J 990 ASN J 997 -1 O ILE J 991 N VAL J 921 SHEET 6 AE9 7 ASP J1002 ILE J1007 -1 O TYR J1006 N THR J 994 SHEET 7 AE9 7 ASN J1010 SER J1016 -1 O LYS J1015 N SER J1003 SHEET 1 AF1 7 ASN J 871 GLY J 876 0 SHEET 2 AF1 7 SER J 896 SER J 901 -1 O SER J 901 N ASN J 871 SHEET 3 AF1 7 ASN J1028 VAL J1034 -1 O PHE J1031 N VAL J 898 SHEET 4 AF1 7 TYR J 937 MET J 943 -1 N ILE J 939 O LYS J1032 SHEET 5 AF1 7 GLY J 949 ASN J 955 -1 O LEU J 954 N TYR J 937 SHEET 6 AF1 7 GLU J 958 GLN J 964 -1 O ILE J 960 N SER J 953 SHEET 7 AF1 7 ASN J 970 ASN J 976 -1 O LEU J 973 N TRP J 961 SHEET 1 AF2 2 ASP J 909 ASN J 910 0 SHEET 2 AF2 2 ILE J1023 HIS J1024 -1 O ILE J1023 N ASN J 910 SHEET 1 AF313 ASP J1146 VAL J1153 0 SHEET 2 AF313 LEU J1159 ALA J1164 -1 O PHE J1160 N PHE J1152 SHEET 3 AF313 LYS J1173 ILE J1177 -1 O LYS J1176 N TYR J1163 SHEET 4 AF313 THR J1218 SER J1222 -1 O ALA J1221 N LYS J1173 SHEET 5 AF313 ASN J1208 LYS J1215 -1 N LYS J1215 O THR J1218 SHEET 6 AF313 ASN J1196 ASN J1203 -1 N PHE J1201 O GLY J1210 SHEET 7 AF313 ASP J1146 VAL J1153 0 SHEET 8 AF313 LYS J1126 ARG J1131 -1 N LYS J1128 O ASN J1151 SHEET 9 AF313 TYR J1086 ASN J1090 -1 N TYR J1086 O VAL J1127 SHEET 10 AF313 TRP J1240 ILE J1243 -1 O ILE J1243 N TYR J1087 SHEET 11 AF313 ASN J1196 ASN J1203 -1 N CYS J1197 O TRP J1240 SHEET 12 AF313 GLN J1186 VAL J1193 -1 N VAL J1189 O ASN J1200 SHEET 13 AF313 ASN J1196 ASN J1203 -1 O ASN J1200 N VAL J1189 SHEET 1 AF4 2 ASN J1096 ARG J1100 0 SHEET 2 AF4 2 LEU J1106 ILE J1111 -1 O SER J1107 N ASP J1099 SHEET 1 AF5 2 THR J1114 ILE J1115 0 SHEET 2 AF5 2 ALA J1118 ASN J1119 -1 O ALA J1118 N ILE J1115 SSBOND 1 CYS B 22 CYS B 96 1555 1555 2.04 SSBOND 2 CYS C 22 CYS C 96 1555 1555 2.04 SSBOND 3 CYS E 22 CYS E 96 1555 1555 2.04 SSBOND 4 CYS I 22 CYS I 96 1555 1555 2.61 SSBOND 5 CYS G 22 CYS G 96 1555 1555 2.03 CRYST1 88.737 174.626 214.439 90.00 90.00 90.00 P 2 21 21 20 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 0.011269 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005727 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004663 0.00000