HEADER IMMUNE SYSTEM 16-MAY-18 6DG2 TITLE ANTIGEN BINDING FRAGMENT OF THE PAN-EBOLAVIRUS MONOCLONAL ANTIBODY 6D6 CAVEAT 6DG2 RESIDUE C ALA 119 AND RESIDUE C SER 120 THAT ARE NEXT TO CAVEAT 2 6DG2 EACH OTHER IN THE SAMPLE SEQUENCE ARE NOT PROPERLY LINKED: CAVEAT 3 6DG2 DISTANCE BETWEEN C AND N IS 0.93. RESIDUE B SER 77 AND CAVEAT 4 6DG2 RESIDUE B VAL 78 THAT ARE NEXT TO EACH OTHER IN THE SAMPLE CAVEAT 5 6DG2 SEQUENCE ARE NOT PROPERLY LINKED: DISTANCE BETWEEN C AND N CAVEAT 6 6DG2 IS 1.05. COMPND MOL_ID: 1; COMPND 2 MOLECULE: 6D6 FAB HEAVY CHAIN; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 6D6 FAB LIGHT CHAIN; COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 9 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 10 ORGANISM_TAXID: 10090; SOURCE 11 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7227 KEYWDS ANTIBODY, MONOCLONAL, ANTIGEN BINDING FRAGMENT, FAB, EBOLA, IMMUNE KEYWDS 2 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.C.MILLIGAN,E.O.SAPHIRE REVDAT 1 26-SEP-18 6DG2 0 JRNL AUTH J.C.MILLIGAN,D.V.PAREKH,K.M.FULLER,M.IGARASHI,A.TAKADA, JRNL AUTH 2 E.O.SAPHIRE JRNL TITL STRUCTURAL CHARACTERIZATION OF PAN-EBOLAVIRUS ANTIBODY 6D6 JRNL TITL 2 TARGETING THE FUSION PEPTIDE OF THE SURFACE GLYCOPROTEIN. JRNL REF J. INFECT. DIS. 2018 JRNL REFN ESSN 1537-6613 JRNL PMID 30203042 JRNL DOI 10.1093/INFDIS/JIY532 REMARK 2 REMARK 2 RESOLUTION. 1.96 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.12_2829 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 68.08 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.5 REMARK 3 NUMBER OF REFLECTIONS : 69694 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.192 REMARK 3 R VALUE (WORKING SET) : 0.191 REMARK 3 FREE R VALUE : 0.235 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.810 REMARK 3 FREE R VALUE TEST SET COUNT : 1959 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 68.1207 - 4.7234 0.99 5245 151 0.1498 0.1900 REMARK 3 2 4.7234 - 3.7492 0.95 4976 137 0.1407 0.1832 REMARK 3 3 3.7492 - 3.2753 0.86 4467 130 0.1790 0.2144 REMARK 3 4 3.2753 - 2.9758 0.99 5126 150 0.2038 0.2480 REMARK 3 5 2.9758 - 2.7625 1.00 5167 157 0.2136 0.2599 REMARK 3 6 2.7625 - 2.5996 0.93 4805 132 0.2244 0.2885 REMARK 3 7 2.5996 - 2.4694 1.00 5161 146 0.2331 0.2650 REMARK 3 8 2.4694 - 2.3619 1.00 5134 147 0.2341 0.2881 REMARK 3 9 2.3619 - 2.2710 0.98 5037 145 0.2574 0.3429 REMARK 3 10 2.2710 - 2.1926 0.78 4004 108 0.3491 0.4504 REMARK 3 11 2.1926 - 2.1241 0.99 5135 165 0.2514 0.2655 REMARK 3 12 2.1241 - 2.0633 0.63 3247 100 0.2624 0.3040 REMARK 3 13 2.0633 - 2.0090 1.00 5131 136 0.2847 0.3293 REMARK 3 14 2.0090 - 1.9600 0.99 5100 155 0.3004 0.2959 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL 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) : 0.250 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.820 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 : 0.007 6675 REMARK 3 ANGLE : 0.930 9092 REMARK 3 CHIRALITY : 0.059 1025 REMARK 3 PLANARITY : 0.006 1147 REMARK 3 DIHEDRAL : 4.582 3938 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 22 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.5640 -12.5430 -20.5085 REMARK 3 T TENSOR REMARK 3 T11: 0.3439 T22: 0.3414 REMARK 3 T33: 0.4134 T12: 0.0369 REMARK 3 T13: 0.0701 T23: -0.0019 REMARK 3 L TENSOR REMARK 3 L11: 3.3683 L22: 3.6791 REMARK 3 L33: 5.7820 L12: 3.2506 REMARK 3 L13: -3.9948 L23: -3.4715 REMARK 3 S TENSOR REMARK 3 S11: -0.1831 S12: -0.4377 S13: -0.3480 REMARK 3 S21: -0.0287 S22: -0.2411 S23: -0.4163 REMARK 3 S31: 0.3643 S32: 0.3592 S33: 0.5328 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 26 THROUGH 67 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.4645 -9.0417 -21.2241 REMARK 3 T TENSOR REMARK 3 T11: 0.2289 T22: 0.2579 REMARK 3 T33: 0.2057 T12: -0.0190 REMARK 3 T13: -0.0022 T23: 0.0244 REMARK 3 L TENSOR REMARK 3 L11: 4.4526 L22: 3.4838 REMARK 3 L33: 3.9193 L12: 0.4208 REMARK 3 L13: 0.3828 L23: 2.4098 REMARK 3 S TENSOR REMARK 3 S11: -0.1078 S12: 0.2758 S13: 0.3477 REMARK 3 S21: -0.4865 S22: 0.0887 S23: 0.1998 REMARK 3 S31: -0.2927 S32: -0.1152 S33: -0.0116 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 68 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.4428 -11.1998 -26.5191 REMARK 3 T TENSOR REMARK 3 T11: 0.2727 T22: 0.3086 REMARK 3 T33: 0.3189 T12: 0.0254 REMARK 3 T13: -0.0146 T23: 0.0090 REMARK 3 L TENSOR REMARK 3 L11: 6.0244 L22: 1.6855 REMARK 3 L33: 3.1127 L12: 2.9536 REMARK 3 L13: -1.7051 L23: -1.0657 REMARK 3 S TENSOR REMARK 3 S11: -0.2526 S12: 0.1466 S13: 0.1321 REMARK 3 S21: -0.1766 S22: 0.1606 S23: 0.1307 REMARK 3 S31: 0.2002 S32: -0.0209 S33: -0.0588 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 92 THROUGH 139 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.4396 -0.9006 -12.8704 REMARK 3 T TENSOR REMARK 3 T11: 0.2623 T22: 0.2799 REMARK 3 T33: 0.2658 T12: -0.0065 REMARK 3 T13: 0.0425 T23: -0.0776 REMARK 3 L TENSOR REMARK 3 L11: 3.9319 L22: 2.0048 REMARK 3 L33: 0.3943 L12: 1.7404 REMARK 3 L13: 0.5662 L23: -0.0350 REMARK 3 S TENSOR REMARK 3 S11: 0.1519 S12: -0.2057 S13: 0.2117 REMARK 3 S21: 0.1849 S22: -0.0774 S23: -0.0851 REMARK 3 S31: -0.0905 S32: 0.0629 S33: -0.0260 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 140 THROUGH 162 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.8228 4.9085 -8.9687 REMARK 3 T TENSOR REMARK 3 T11: 0.3127 T22: 0.3034 REMARK 3 T33: 0.3622 T12: 0.0104 REMARK 3 T13: 0.0373 T23: -0.0896 REMARK 3 L TENSOR REMARK 3 L11: 2.5496 L22: 1.8095 REMARK 3 L33: 5.7301 L12: 1.7061 REMARK 3 L13: 1.6324 L23: 0.6939 REMARK 3 S TENSOR REMARK 3 S11: -0.3136 S12: 0.1520 S13: -0.0487 REMARK 3 S21: -0.0077 S22: -0.1523 S23: 0.1748 REMARK 3 S31: 0.2405 S32: -0.0304 S33: 0.5919 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 163 THROUGH 193 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.1058 8.8151 -6.4049 REMARK 3 T TENSOR REMARK 3 T11: 0.2751 T22: 0.2598 REMARK 3 T33: 0.3365 T12: 0.0019 REMARK 3 T13: 0.0205 T23: -0.0382 REMARK 3 L TENSOR REMARK 3 L11: 3.1195 L22: 2.7942 REMARK 3 L33: 4.4812 L12: -0.9702 REMARK 3 L13: -0.0915 L23: 0.7265 REMARK 3 S TENSOR REMARK 3 S11: -0.1619 S12: -0.1122 S13: -0.0599 REMARK 3 S21: 0.1346 S22: 0.0892 S23: -0.0524 REMARK 3 S31: -0.3338 S32: -0.3171 S33: 0.1568 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 194 THROUGH 219 ) REMARK 3 ORIGIN FOR THE GROUP (A): 42.2698 3.8940 -6.3051 REMARK 3 T TENSOR REMARK 3 T11: 0.3561 T22: 0.3721 REMARK 3 T33: 0.4476 T12: 0.0540 REMARK 3 T13: -0.0111 T23: -0.0543 REMARK 3 L TENSOR REMARK 3 L11: 4.2319 L22: 2.7728 REMARK 3 L33: 8.2624 L12: 0.5985 REMARK 3 L13: 2.2009 L23: 1.7573 REMARK 3 S TENSOR REMARK 3 S11: -0.0632 S12: 0.1621 S13: 0.0044 REMARK 3 S21: 0.3855 S22: 0.1065 S23: -0.3506 REMARK 3 S31: 0.2522 S32: 0.5829 S33: -0.1132 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.8162 7.1013 -4.4985 REMARK 3 T TENSOR REMARK 3 T11: 0.3582 T22: 0.5300 REMARK 3 T33: 0.6478 T12: -0.0863 REMARK 3 T13: 0.0983 T23: -0.1515 REMARK 3 L TENSOR REMARK 3 L11: 4.4318 L22: 3.4259 REMARK 3 L33: 3.2744 L12: 0.7218 REMARK 3 L13: 2.6084 L23: 2.0906 REMARK 3 S TENSOR REMARK 3 S11: 0.1231 S12: -0.5450 S13: 0.8409 REMARK 3 S21: 0.0828 S22: -0.4254 S23: 0.5969 REMARK 3 S31: -0.2083 S32: -0.3442 S33: 0.2354 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 33 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.6609 0.4899 -2.5094 REMARK 3 T TENSOR REMARK 3 T11: 0.3086 T22: 0.4328 REMARK 3 T33: 0.3710 T12: -0.0493 REMARK 3 T13: 0.0864 T23: -0.1092 REMARK 3 L TENSOR REMARK 3 L11: 1.9857 L22: 3.2293 REMARK 3 L33: 1.5763 L12: 2.0170 REMARK 3 L13: 1.4774 L23: 1.8553 REMARK 3 S TENSOR REMARK 3 S11: 0.2204 S12: -0.4483 S13: 0.2377 REMARK 3 S21: 0.4357 S22: -0.2952 S23: 0.3247 REMARK 3 S31: 0.1474 S32: -0.2839 S33: 0.0456 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 115 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.3785 21.6257 -9.2206 REMARK 3 T TENSOR REMARK 3 T11: 0.2828 T22: 0.2597 REMARK 3 T33: 0.3181 T12: -0.0362 REMARK 3 T13: 0.0049 T23: -0.0023 REMARK 3 L TENSOR REMARK 3 L11: 4.2281 L22: 4.5787 REMARK 3 L33: 4.3298 L12: 0.3443 REMARK 3 L13: -2.5102 L23: 0.5026 REMARK 3 S TENSOR REMARK 3 S11: 0.0327 S12: 0.3187 S13: 0.3886 REMARK 3 S21: -0.5434 S22: 0.1287 S23: -0.2318 REMARK 3 S31: -0.2085 S32: -0.0505 S33: -0.1632 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.2847 -12.3713 -28.3580 REMARK 3 T TENSOR REMARK 3 T11: 0.2766 T22: 0.3147 REMARK 3 T33: 0.2744 T12: -0.0613 REMARK 3 T13: -0.0217 T23: -0.0088 REMARK 3 L TENSOR REMARK 3 L11: 1.7634 L22: 3.0390 REMARK 3 L33: 1.9050 L12: -1.4697 REMARK 3 L13: 0.5784 L23: -0.6687 REMARK 3 S TENSOR REMARK 3 S11: 0.1110 S12: -0.0289 S13: 0.0085 REMARK 3 S21: -0.0922 S22: 0.0075 S23: -0.0459 REMARK 3 S31: 0.2465 S32: -0.2627 S33: -0.1877 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 26 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.3024 -12.0419 -27.7270 REMARK 3 T TENSOR REMARK 3 T11: 0.2727 T22: 0.2412 REMARK 3 T33: 0.2830 T12: -0.0303 REMARK 3 T13: 0.0213 T23: -0.0182 REMARK 3 L TENSOR REMARK 3 L11: 5.2881 L22: 3.4114 REMARK 3 L33: 3.6080 L12: -0.6808 REMARK 3 L13: 1.2922 L23: 0.9668 REMARK 3 S TENSOR REMARK 3 S11: 0.1001 S12: 0.0865 S13: 0.3591 REMARK 3 S21: 0.1216 S22: 0.0059 S23: -0.0995 REMARK 3 S31: -0.2037 S32: 0.2366 S33: -0.0977 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 84 THROUGH 142 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.9752 -13.2668 -38.7841 REMARK 3 T TENSOR REMARK 3 T11: 0.2612 T22: 0.2223 REMARK 3 T33: 0.1970 T12: -0.0034 REMARK 3 T13: 0.0056 T23: -0.0284 REMARK 3 L TENSOR REMARK 3 L11: 2.5709 L22: 1.5986 REMARK 3 L33: 2.1056 L12: -0.5001 REMARK 3 L13: 1.5214 L23: -0.4057 REMARK 3 S TENSOR REMARK 3 S11: -0.0350 S12: 0.2005 S13: -0.1099 REMARK 3 S21: 0.1033 S22: 0.0191 S23: 0.1930 REMARK 3 S31: -0.0496 S32: 0.0836 S33: 0.0603 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 143 THROUGH 219 ) REMARK 3 ORIGIN FOR THE GROUP (A): -51.4219 -17.8105 -50.5273 REMARK 3 T TENSOR REMARK 3 T11: 0.4749 T22: 0.3890 REMARK 3 T33: 0.6554 T12: -0.0880 REMARK 3 T13: 0.0691 T23: -0.0573 REMARK 3 L TENSOR REMARK 3 L11: 2.8395 L22: 6.6022 REMARK 3 L33: 4.4095 L12: 0.1548 REMARK 3 L13: -0.3353 L23: 2.2116 REMARK 3 S TENSOR REMARK 3 S11: -0.1980 S12: 0.1069 S13: -0.6461 REMARK 3 S21: 0.4236 S22: -0.1483 S23: 0.9502 REMARK 3 S31: 0.7355 S32: -0.5249 S33: 0.2431 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 2 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.1122 -25.4108 -53.0514 REMARK 3 T TENSOR REMARK 3 T11: 0.5936 T22: 0.7377 REMARK 3 T33: 0.4477 T12: 0.1163 REMARK 3 T13: 0.0930 T23: -0.0236 REMARK 3 L TENSOR REMARK 3 L11: 3.2644 L22: 3.4746 REMARK 3 L33: 2.0885 L12: -0.6919 REMARK 3 L13: -0.6483 L23: 0.4480 REMARK 3 S TENSOR REMARK 3 S11: 0.3511 S12: 0.7155 S13: -0.0878 REMARK 3 S21: -0.9173 S22: -0.2517 S23: -0.3563 REMARK 3 S31: -0.1686 S32: 0.3278 S33: -0.0470 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 19 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.8564 -23.1794 -45.1074 REMARK 3 T TENSOR REMARK 3 T11: 0.4383 T22: 0.6718 REMARK 3 T33: 0.4570 T12: -0.0325 REMARK 3 T13: 0.0651 T23: -0.0838 REMARK 3 L TENSOR REMARK 3 L11: 1.9402 L22: 5.3906 REMARK 3 L33: 4.5796 L12: -1.5109 REMARK 3 L13: -2.4848 L23: 0.0528 REMARK 3 S TENSOR REMARK 3 S11: 0.1020 S12: 0.5980 S13: 0.2060 REMARK 3 S21: -0.0662 S22: 0.3145 S23: -0.5723 REMARK 3 S31: -0.2259 S32: 1.4532 S33: -0.3502 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 33 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.4620 -27.6136 -41.6613 REMARK 3 T TENSOR REMARK 3 T11: 0.3693 T22: 0.3998 REMARK 3 T33: 0.2735 T12: 0.0500 REMARK 3 T13: -0.0251 T23: -0.0808 REMARK 3 L TENSOR REMARK 3 L11: 4.0651 L22: 3.8204 REMARK 3 L33: 5.9164 L12: -0.8818 REMARK 3 L13: -0.4468 L23: 1.9812 REMARK 3 S TENSOR REMARK 3 S11: 0.0639 S12: 0.4120 S13: -0.3736 REMARK 3 S21: -0.1684 S22: -0.0275 S23: -0.0213 REMARK 3 S31: 0.4391 S32: 0.3475 S33: -0.0863 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 103 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): -29.1683 -27.9275 -60.7740 REMARK 3 T TENSOR REMARK 3 T11: 0.5900 T22: 0.4300 REMARK 3 T33: 0.3649 T12: 0.1293 REMARK 3 T13: 0.0161 T23: -0.0546 REMARK 3 L TENSOR REMARK 3 L11: 1.5497 L22: 0.1373 REMARK 3 L33: 2.1119 L12: 0.4526 REMARK 3 L13: 1.7595 L23: 0.5022 REMARK 3 S TENSOR REMARK 3 S11: 0.1946 S12: 0.0702 S13: -0.1434 REMARK 3 S21: -0.3161 S22: 0.0703 S23: -0.1387 REMARK 3 S31: -0.0132 S32: 0.3724 S33: -0.2221 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 115 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): -54.3530 -10.1169 -61.2824 REMARK 3 T TENSOR REMARK 3 T11: 0.5895 T22: 0.4672 REMARK 3 T33: 0.8782 T12: 0.1539 REMARK 3 T13: -0.1669 T23: -0.2166 REMARK 3 L TENSOR REMARK 3 L11: 3.6670 L22: 8.0971 REMARK 3 L33: 5.3660 L12: -2.3575 REMARK 3 L13: -1.1614 L23: 2.7427 REMARK 3 S TENSOR REMARK 3 S11: -0.0351 S12: 0.4165 S13: 0.0555 REMARK 3 S21: -0.4457 S22: -0.3493 S23: 1.8150 REMARK 3 S31: -0.4006 S32: -1.2152 S33: 0.5084 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 130 THROUGH 151 ) REMARK 3 ORIGIN FOR THE GROUP (A): -40.2535 -14.9353 -64.8523 REMARK 3 T TENSOR REMARK 3 T11: 0.4893 T22: 0.3836 REMARK 3 T33: 0.3174 T12: -0.0218 REMARK 3 T13: -0.0347 T23: 0.0023 REMARK 3 L TENSOR REMARK 3 L11: 5.3029 L22: 7.1230 REMARK 3 L33: 3.6786 L12: -3.4524 REMARK 3 L13: -0.7717 L23: 1.5783 REMARK 3 S TENSOR REMARK 3 S11: 0.4511 S12: 0.5663 S13: 0.1904 REMARK 3 S21: -0.8625 S22: -0.4932 S23: 0.1432 REMARK 3 S31: -0.5123 S32: 0.2202 S33: 0.1333 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 152 THROUGH 175 ) REMARK 3 ORIGIN FOR THE GROUP (A): -38.4193 -16.0849 -61.2629 REMARK 3 T TENSOR REMARK 3 T11: 0.4155 T22: 0.4451 REMARK 3 T33: 0.4212 T12: -0.0598 REMARK 3 T13: -0.0107 T23: -0.0242 REMARK 3 L TENSOR REMARK 3 L11: 4.0941 L22: 6.5630 REMARK 3 L33: 4.7784 L12: -1.8400 REMARK 3 L13: -0.3596 L23: 1.3455 REMARK 3 S TENSOR REMARK 3 S11: -0.0849 S12: 0.1880 S13: 0.0357 REMARK 3 S21: -0.3154 S22: 0.0376 S23: -0.0160 REMARK 3 S31: -0.2478 S32: 0.2958 S33: 0.0142 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 176 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): -46.0780 -9.6480 -69.4876 REMARK 3 T TENSOR REMARK 3 T11: 0.9012 T22: 0.5733 REMARK 3 T33: 0.4250 T12: 0.3383 REMARK 3 T13: -0.1719 T23: -0.0853 REMARK 3 L TENSOR REMARK 3 L11: 2.4171 L22: 2.2829 REMARK 3 L33: 1.8871 L12: 0.3949 REMARK 3 L13: 0.7032 L23: -1.7829 REMARK 3 S TENSOR REMARK 3 S11: 0.6168 S12: 0.8615 S13: 0.0632 REMARK 3 S21: -1.4186 S22: -0.8621 S23: 0.3488 REMARK 3 S31: -0.8876 S32: -0.6012 S33: 0.1308 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 6DG2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-18. REMARK 100 THE DEPOSITION ID IS D_1000234518. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-NOV-17 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 : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70193 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960 REMARK 200 RESOLUTION RANGE LOW (A) : 72.040 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2 REMARK 200 DATA REDUNDANCY : 3.300 REMARK 200 R MERGE (I) : 0.07000 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) : 1.96 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.30 REMARK 200 R MERGE FOR SHELL (I) : 1.00000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.300 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: 1I9R REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.71 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 7.6, 25% W/V PEG 6000, REMARK 280 VAPOR DIFFUSION, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 36.01900 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3170 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20280 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2980 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20150 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL 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 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 A 135 REMARK 465 THR A 136 REMARK 465 SER A 137 REMARK 465 CYS A 221 REMARK 465 ASP A 222 REMARK 465 LEU A 223 REMARK 465 GLU A 224 REMARK 465 VAL A 225 REMARK 465 ASP A 226 REMARK 465 ASP A 227 REMARK 465 ASP A 228 REMARK 465 ASP A 229 REMARK 465 LYS A 230 REMARK 465 ASP B 1 REMARK 465 GLU B 214 REMARK 465 CYS B 215 REMARK 465 LYS C 134 REMARK 465 SER C 135 REMARK 465 THR C 136 REMARK 465 SER C 137 REMARK 465 GLY C 138 REMARK 465 GLY C 139 REMARK 465 THR C 140 REMARK 465 ALA C 141 REMARK 465 SER C 220 REMARK 465 CYS C 221 REMARK 465 ASP C 222 REMARK 465 LEU C 223 REMARK 465 GLU C 224 REMARK 465 VAL C 225 REMARK 465 ASP C 226 REMARK 465 ASP C 227 REMARK 465 ASP C 228 REMARK 465 ASP C 229 REMARK 465 LYS C 230 REMARK 465 ASP D 1 REMARK 465 GLY D 213 REMARK 465 GLU D 214 REMARK 465 CYS D 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 GLN A 1 CG CD OE1 NE2 REMARK 470 LYS A 134 CG CD CE NZ REMARK 470 LYS C 219 CG CD CE NZ 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 GLY A 138 OG SER A 191 1.33 REMARK 500 N GLN C 1 O HOH C 301 1.65 REMARK 500 O SER B 77 N VAL B 78 1.79 REMARK 500 OG SER D 128 O HOH D 301 1.92 REMARK 500 O HOH D 318 O HOH D 345 1.99 REMARK 500 NH1 ARG B 203 O HOH B 301 1.99 REMARK 500 OG SER A 125 O HOH A 301 2.00 REMARK 500 O HOH D 335 O HOH D 354 2.04 REMARK 500 O HOH A 393 O HOH A 397 2.07 REMARK 500 O HOH C 368 O HOH D 325 2.10 REMARK 500 OE1 GLU B 106 O HOH B 302 2.15 REMARK 500 O GLY A 138 CB SER A 191 2.18 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 ILE A 200 C CYS A 201 N 0.144 REMARK 500 CYS A 201 C ASN A 202 N -0.219 REMARK 500 SER B 77 C VAL B 78 N -0.289 REMARK 500 ALA C 119 C SER C 120 N -0.406 REMARK 500 LYS D 208 C SER D 209 N 0.179 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 SER B 77 C - N - CA ANGL. DEV. = -17.9 DEGREES REMARK 500 SER B 77 O - C - N ANGL. DEV. = -19.9 DEGREES REMARK 500 VAL C 157 CB - CA - C ANGL. DEV. = -21.4 DEGREES REMARK 500 VAL C 157 N - CA - C ANGL. DEV. = 29.6 DEGREES REMARK 500 TRP D 97 N - CA - CB ANGL. DEV. = 11.7 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 85 60.07 39.43 REMARK 500 ALA A 92 171.71 179.68 REMARK 500 SER A 104 152.11 77.04 REMARK 500 THR A 196 -67.13 -140.77 REMARK 500 SER B 30 -127.01 46.53 REMARK 500 ALA B 51 -38.00 70.82 REMARK 500 HIS B 91 51.14 -143.69 REMARK 500 TYR B 92 -68.92 -94.23 REMARK 500 SER B 93 -49.46 -137.75 REMARK 500 SER C 104 151.56 78.63 REMARK 500 THR C 156 -63.55 -103.99 REMARK 500 SER C 191 -5.23 -56.44 REMARK 500 SER C 193 31.05 -84.92 REMARK 500 HIS D 8 67.17 62.06 REMARK 500 LYS D 9 -38.31 -35.55 REMARK 500 VAL D 31 14.70 -148.20 REMARK 500 LEU D 47 -31.33 -133.25 REMARK 500 SER D 50 65.43 -104.30 REMARK 500 ALA D 51 -38.80 64.48 REMARK 500 ALA D 84 175.51 178.21 REMARK 500 TYR D 92 -71.42 -81.93 REMARK 500 SER D 93 -50.50 -135.07 REMARK 500 ASN D 153 -0.75 75.10 REMARK 500 ALA D 185 -70.28 -60.43 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 SER B 77 -23.33 REMARK 500 REMARK 500 REMARK: NULL DBREF 6DG2 A 1 230 PDB 6DG2 6DG2 1 230 DBREF 6DG2 B 1 215 PDB 6DG2 6DG2 1 215 DBREF 6DG2 C 1 230 PDB 6DG2 6DG2 1 230 DBREF 6DG2 D 1 215 PDB 6DG2 6DG2 1 215 SEQRES 1 A 230 GLN VAL GLN LEU GLN GLN PRO GLY THR GLU LEU VAL LYS SEQRES 2 A 230 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY SEQRES 3 A 230 TYR THR PHE THR SER TYR TRP MET HIS TRP VAL LYS GLN SEQRES 4 A 230 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY GLU ILE ASN SEQRES 5 A 230 PRO ARG ASN GLY ARG THR ASP PHE SER GLU LYS PHE LYS SEQRES 6 A 230 SER LYS ALA THR LEU THR VAL ASP THR SER SER SER THR SEQRES 7 A 230 ALA PHE ILE GLN LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 A 230 ALA VAL TYR TYR CYS ALA ARG TRP GLY TYR TYR GLY SER SEQRES 9 A 230 SER ASP TYR TRP GLY GLN GLY THR ALA LEU THR VAL SER SEQRES 10 A 230 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 A 230 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 A 230 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 A 230 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 A 230 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 A 230 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 A 230 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 A 230 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 18 A 230 ASP LEU GLU VAL ASP ASP ASP ASP LYS SEQRES 1 B 215 ASP ILE VAL VAL THR GLN SER HIS LYS PHE MET SER THR SEQRES 2 B 215 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 B 215 GLN ASP VAL SER VAL ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 B 215 THR GLY GLN SER PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 B 215 TYR ARG ILE THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 B 215 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER VAL SEQRES 7 B 215 GLN ALA GLU ASP MET ALA VAL TYR TYR CYS GLN GLN HIS SEQRES 8 B 215 TYR SER THR PRO PRO TRP THR PHE GLY GLY GLY THR LYS SEQRES 9 B 215 LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 B 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 B 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 B 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 B 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 B 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 B 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 B 215 GLU VAL THR HIS GLN GLY LEU ARG SER PRO VAL THR LYS SEQRES 17 B 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 C 230 GLN VAL GLN LEU GLN GLN PRO GLY THR GLU LEU VAL LYS SEQRES 2 C 230 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY SEQRES 3 C 230 TYR THR PHE THR SER TYR TRP MET HIS TRP VAL LYS GLN SEQRES 4 C 230 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY GLU ILE ASN SEQRES 5 C 230 PRO ARG ASN GLY ARG THR ASP PHE SER GLU LYS PHE LYS SEQRES 6 C 230 SER LYS ALA THR LEU THR VAL ASP THR SER SER SER THR SEQRES 7 C 230 ALA PHE ILE GLN LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 C 230 ALA VAL TYR TYR CYS ALA ARG TRP GLY TYR TYR GLY SER SEQRES 9 C 230 SER ASP TYR TRP GLY GLN GLY THR ALA LEU THR VAL SER SEQRES 10 C 230 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 C 230 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 C 230 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 C 230 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 C 230 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 C 230 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 C 230 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 C 230 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 18 C 230 ASP LEU GLU VAL ASP ASP ASP ASP LYS SEQRES 1 D 215 ASP ILE VAL VAL THR GLN SER HIS LYS PHE MET SER THR SEQRES 2 D 215 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 D 215 GLN ASP VAL SER VAL ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 D 215 THR GLY GLN SER PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 D 215 TYR ARG ILE THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 D 215 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER VAL SEQRES 7 D 215 GLN ALA GLU ASP MET ALA VAL TYR TYR CYS GLN GLN HIS SEQRES 8 D 215 TYR SER THR PRO PRO TRP THR PHE GLY GLY GLY THR LYS SEQRES 9 D 215 LEU GLU ILE LYS 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 ARG SER PRO VAL THR LYS SEQRES 17 D 215 SER PHE ASN ARG GLY GLU CYS FORMUL 5 HOH *337(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 GLU A 62 LYS A 65 5 4 HELIX 3 AA3 THR A 74 SER A 76 5 3 HELIX 4 AA4 THR A 87 SER A 91 5 5 HELIX 5 AA5 SER A 161 ALA A 163 5 3 HELIX 6 AA6 SER A 192 LEU A 194 5 3 HELIX 7 AA7 LYS A 206 ASN A 209 5 4 HELIX 8 AA8 GLN B 79 MET B 83 5 5 HELIX 9 AA9 SER B 122 SER B 128 1 7 HELIX 10 AB1 LYS B 184 LYS B 189 1 6 HELIX 11 AB2 THR C 28 TYR C 32 5 5 HELIX 12 AB3 GLU C 62 LYS C 65 5 4 HELIX 13 AB4 THR C 74 SER C 76 5 3 HELIX 14 AB5 THR C 87 SER C 91 5 5 HELIX 15 AB6 SER C 161 ALA C 163 5 3 HELIX 16 AB7 LYS C 206 ASN C 209 5 4 HELIX 17 AB8 GLN D 79 MET D 83 5 5 HELIX 18 AB9 SER D 122 LYS D 127 1 6 HELIX 19 AC1 LYS D 184 LYS D 189 1 6 SHEET 1 AA1 4 GLN A 3 GLN A 5 0 SHEET 2 AA1 4 VAL A 18 SER A 25 -1 O LYS A 23 N GLN A 5 SHEET 3 AA1 4 THR A 78 LEU A 83 -1 O ILE A 81 N LEU A 20 SHEET 4 AA1 4 ALA A 68 ASP A 73 -1 N THR A 71 O PHE A 80 SHEET 1 AA2 6 THR A 9 VAL A 12 0 SHEET 2 AA2 6 THR A 112 VAL A 116 1 O THR A 115 N GLU A 10 SHEET 3 AA2 6 ALA A 92 TRP A 99 -1 N ALA A 92 O LEU A 114 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N HIS A 35 O ALA A 97 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O ILE A 51 N MET A 34 SHEET 6 AA2 6 THR A 58 PHE A 60 -1 O ASP A 59 N GLU A 50 SHEET 1 AA3 4 THR A 9 VAL A 12 0 SHEET 2 AA3 4 THR A 112 VAL A 116 1 O THR A 115 N GLU A 10 SHEET 3 AA3 4 ALA A 92 TRP A 99 -1 N ALA A 92 O LEU A 114 SHEET 4 AA3 4 SER A 105 TRP A 108 -1 O TYR A 107 N ARG A 98 SHEET 1 AA4 4 SER A 125 LEU A 129 0 SHEET 2 AA4 4 THR A 140 TYR A 150 -1 O LEU A 146 N PHE A 127 SHEET 3 AA4 4 TYR A 181 PRO A 190 -1 O LEU A 183 N VAL A 147 SHEET 4 AA4 4 VAL A 168 THR A 170 -1 N HIS A 169 O VAL A 186 SHEET 1 AA5 4 SER A 125 LEU A 129 0 SHEET 2 AA5 4 THR A 140 TYR A 150 -1 O LEU A 146 N PHE A 127 SHEET 3 AA5 4 TYR A 181 PRO A 190 -1 O LEU A 183 N VAL A 147 SHEET 4 AA5 4 VAL A 174 LEU A 175 -1 N VAL A 174 O SER A 182 SHEET 1 AA6 3 THR A 156 TRP A 159 0 SHEET 2 AA6 3 ILE A 200 HIS A 205 -1 O ASN A 202 N SER A 158 SHEET 3 AA6 3 THR A 210 LYS A 215 -1 O VAL A 212 N VAL A 203 SHEET 1 AA7 4 VAL B 4 THR B 5 0 SHEET 2 AA7 4 VAL B 19 ALA B 25 -1 O LYS B 24 N THR B 5 SHEET 3 AA7 4 ASP B 70 ILE B 75 -1 O PHE B 73 N ILE B 21 SHEET 4 AA7 4 PHE B 62 SER B 67 -1 N THR B 63 O THR B 74 SHEET 1 AA8 6 PHE B 10 THR B 13 0 SHEET 2 AA8 6 THR B 103 ILE B 107 1 O GLU B 106 N THR B 13 SHEET 3 AA8 6 VAL B 85 GLN B 90 -1 N TYR B 86 O THR B 103 SHEET 4 AA8 6 VAL B 33 GLN B 38 -1 N TYR B 36 O TYR B 87 SHEET 5 AA8 6 LYS B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AA8 6 TYR B 53 ARG B 54 -1 O TYR B 53 N TYR B 49 SHEET 1 AA9 4 SER B 115 PHE B 119 0 SHEET 2 AA9 4 THR B 130 PHE B 140 -1 O LEU B 136 N PHE B 117 SHEET 3 AA9 4 TYR B 174 SER B 183 -1 O LEU B 176 N LEU B 137 SHEET 4 AA9 4 SER B 160 VAL B 164 -1 N GLN B 161 O THR B 179 SHEET 1 AB1 4 ALA B 154 LEU B 155 0 SHEET 2 AB1 4 LYS B 146 VAL B 151 -1 N VAL B 151 O ALA B 154 SHEET 3 AB1 4 VAL B 192 THR B 198 -1 O GLU B 196 N GLN B 148 SHEET 4 AB1 4 VAL B 206 ASN B 211 -1 O VAL B 206 N VAL B 197 SHEET 1 AB2 4 GLN C 3 GLN C 5 0 SHEET 2 AB2 4 VAL C 18 SER C 25 -1 O LYS C 23 N GLN C 5 SHEET 3 AB2 4 THR C 78 LEU C 83 -1 O ILE C 81 N LEU C 20 SHEET 4 AB2 4 ALA C 68 ASP C 73 -1 N THR C 71 O PHE C 80 SHEET 1 AB3 6 THR C 9 VAL C 12 0 SHEET 2 AB3 6 THR C 112 VAL C 116 1 O THR C 115 N GLU C 10 SHEET 3 AB3 6 ALA C 92 TRP C 99 -1 N ALA C 92 O LEU C 114 SHEET 4 AB3 6 MET C 34 GLN C 39 -1 N HIS C 35 O ALA C 97 SHEET 5 AB3 6 LEU C 45 ILE C 51 -1 O ILE C 48 N TRP C 36 SHEET 6 AB3 6 THR C 58 PHE C 60 -1 O ASP C 59 N GLU C 50 SHEET 1 AB4 4 THR C 9 VAL C 12 0 SHEET 2 AB4 4 THR C 112 VAL C 116 1 O THR C 115 N GLU C 10 SHEET 3 AB4 4 ALA C 92 TRP C 99 -1 N ALA C 92 O LEU C 114 SHEET 4 AB4 4 SER C 105 TRP C 108 -1 O TYR C 107 N ARG C 98 SHEET 1 AB5 4 SER C 125 LEU C 129 0 SHEET 2 AB5 4 LEU C 143 TYR C 150 -1 O GLY C 144 N LEU C 129 SHEET 3 AB5 4 TYR C 181 VAL C 187 -1 O LEU C 183 N VAL C 147 SHEET 4 AB5 4 VAL C 168 THR C 170 -1 N HIS C 169 O VAL C 186 SHEET 1 AB6 4 SER C 125 LEU C 129 0 SHEET 2 AB6 4 LEU C 143 TYR C 150 -1 O GLY C 144 N LEU C 129 SHEET 3 AB6 4 TYR C 181 VAL C 187 -1 O LEU C 183 N VAL C 147 SHEET 4 AB6 4 VAL C 174 LEU C 175 -1 N VAL C 174 O SER C 182 SHEET 1 AB7 3 SER C 158 TRP C 159 0 SHEET 2 AB7 3 ILE C 200 HIS C 205 -1 O ASN C 202 N SER C 158 SHEET 3 AB7 3 THR C 210 LYS C 215 -1 O VAL C 212 N VAL C 203 SHEET 1 AB8 4 VAL D 4 THR D 5 0 SHEET 2 AB8 4 VAL D 19 ALA D 25 -1 O LYS D 24 N THR D 5 SHEET 3 AB8 4 ASP D 70 ILE D 75 -1 O PHE D 73 N ILE D 21 SHEET 4 AB8 4 PHE D 62 SER D 67 -1 N THR D 63 O THR D 74 SHEET 1 AB9 5 PHE D 10 THR D 13 0 SHEET 2 AB9 5 THR D 103 ILE D 107 1 O LYS D 104 N MET D 11 SHEET 3 AB9 5 VAL D 85 GLN D 90 -1 N TYR D 86 O THR D 103 SHEET 4 AB9 5 VAL D 33 GLN D 38 -1 N TYR D 36 O TYR D 87 SHEET 5 AB9 5 LYS D 45 ILE D 48 -1 O ILE D 48 N TRP D 35 SHEET 1 AC1 4 SER D 115 PHE D 119 0 SHEET 2 AC1 4 THR D 130 PHE D 140 -1 O ASN D 138 N SER D 115 SHEET 3 AC1 4 TYR D 174 SER D 183 -1 O LEU D 176 N LEU D 137 SHEET 4 AC1 4 SER D 160 VAL D 164 -1 N GLN D 161 O THR D 179 SHEET 1 AC2 4 ALA D 154 LEU D 155 0 SHEET 2 AC2 4 LYS D 146 VAL D 151 -1 N VAL D 151 O ALA D 154 SHEET 3 AC2 4 VAL D 192 THR D 198 -1 O THR D 198 N LYS D 146 SHEET 4 AC2 4 VAL D 206 ASN D 211 -1 O VAL D 206 N VAL D 197 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.03 SSBOND 2 CYS A 145 CYS A 201 1555 1555 2.18 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.10 SSBOND 4 CYS B 135 CYS B 195 1555 1555 2.07 SSBOND 5 CYS C 22 CYS C 96 1555 1555 2.04 SSBOND 6 CYS C 145 CYS C 201 1555 1555 2.00 SSBOND 7 CYS D 23 CYS D 88 1555 1555 2.09 SSBOND 8 CYS D 135 CYS D 195 1555 1555 2.03 CISPEP 1 PHE A 151 PRO A 152 0 -8.59 CISPEP 2 GLU A 153 PRO A 154 0 -4.03 CISPEP 3 PRO B 95 PRO B 96 0 4.77 CISPEP 4 TYR B 141 PRO B 142 0 4.28 CISPEP 5 PHE C 151 PRO C 152 0 -8.57 CISPEP 6 GLU C 153 PRO C 154 0 2.88 CISPEP 7 TYR D 141 PRO D 142 0 5.24 CRYST1 70.226 72.038 107.149 90.00 104.20 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.014240 0.000000 0.003604 0.00000 SCALE2 0.000000 0.013882 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009627 0.00000