HEADER TOXIN 23-DEC-24 9HUO TITLE A01 MABS BOUND TO COBRATOXIN AT PH 5.5 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-COBRATOXIN; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: ALPHA-CT,ALPHA-CBT,ALPHA-CBTX,ALPHA-CTX,ALPHA-ELAPITOXIN- COMPND 5 NK2A,ALPHA-EPTX-NK2A,LONG NEUROTOXIN 1,SIAMENSIS 3; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: LIGHT CHAIN; COMPND 8 CHAIN: I, C; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: HEAVY CHAIN; COMPND 12 CHAIN: M, D; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: NAJA KAOUTHIA; SOURCE 3 ORGANISM_COMMON: MONOCLED COBRA; SOURCE 4 ORGANISM_TAXID: 8649; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 7 ORGANISM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 10 MOL_ID: 3; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS COBRATOXIN, MAB, PH SENSITIVITY, TOXIN EXPDTA X-RAY DIFFRACTION AUTHOR J.W.WADE,M.F.BOHN,A.H.LAUSTSEN,J.P.MORTH REVDAT 1 19-NOV-25 9HUO 0 JRNL AUTH J.WADE,N.STRANCAR,M.L.FERNANDEZ-QUINTERO,S.SIEBENHAAR, JRNL AUTH 2 T.JANSEN,E.P.W.MEIER,T.P.JENKINS,S.P.BJORN,G.T.T.NGUYEN, JRNL AUTH 3 B.LOMONTE,J.M.GUTIERREZ,C.V.SORENSEN,J.R.LOEFFLER,A.PAUL, JRNL AUTH 4 T.TULIKA,J.ARNSDORF,S.SCHOFFELEN,E.V.S.LUNDQUIST,J.SORENSEN, JRNL AUTH 5 A.B.WARD,B.G.VOLDBORG,M.F.BOHN,E.RIVERA-DE-TORRE,J.P.MORTH, JRNL AUTH 6 A.H.LAUSTSEN JRNL TITL RATIONAL DESIGN OF ANTIBODIES WITH PH-DEPENDENT JRNL TITL 2 ANTIGEN-BINDING PROPERTIES USING STRUCTURAL INSIGHTS FROM JRNL TITL 3 BROADLY NEUTRALIZING ANTIBODIES AGAINST ALPHA-NEUROTOXINS. JRNL REF MABS V. 17 53624 2025 JRNL REFN ESSN 1942-0870 JRNL PMID 40936197 JRNL DOI 10.1080/19420862.2025.2553624 REMARK 2 REMARK 2 RESOLUTION. 1.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21RC1_5156 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.58 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 3 NUMBER OF REFLECTIONS : 83128 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.185 REMARK 3 R VALUE (WORKING SET) : 0.183 REMARK 3 FREE R VALUE : 0.225 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 4075 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 41.5800 - 4.9100 0.98 2902 158 0.1824 0.2181 REMARK 3 2 4.9100 - 3.9000 0.99 2814 128 0.1302 0.1562 REMARK 3 3 3.9000 - 3.4100 1.00 2789 148 0.1582 0.2134 REMARK 3 4 3.4100 - 3.1000 0.99 2736 163 0.1733 0.2000 REMARK 3 5 3.1000 - 2.8700 0.99 2751 136 0.1880 0.2363 REMARK 3 6 2.8700 - 2.7100 0.99 2781 120 0.1790 0.2143 REMARK 3 7 2.7000 - 2.5700 0.99 2727 131 0.1802 0.2149 REMARK 3 8 2.5700 - 2.4600 1.00 2730 145 0.1792 0.2232 REMARK 3 9 2.4600 - 2.3600 1.00 2751 132 0.1763 0.2183 REMARK 3 10 2.3600 - 2.2800 1.00 2749 144 0.1742 0.2199 REMARK 3 11 2.2800 - 2.2100 1.00 2717 146 0.1745 0.2311 REMARK 3 12 2.2100 - 2.1500 1.00 2702 124 0.1710 0.2786 REMARK 3 13 2.1500 - 2.0900 1.00 2756 131 0.1696 0.1877 REMARK 3 14 2.0900 - 2.0400 1.00 2721 163 0.1781 0.2281 REMARK 3 15 2.0400 - 1.9900 1.00 2664 176 0.1797 0.2072 REMARK 3 16 1.9900 - 1.9500 1.00 2757 115 0.1789 0.2478 REMARK 3 17 1.9500 - 1.9100 0.99 2727 132 0.1882 0.2295 REMARK 3 18 1.9100 - 1.8800 0.99 2688 145 0.2013 0.2400 REMARK 3 19 1.8800 - 1.8400 1.00 2691 149 0.2161 0.2712 REMARK 3 20 1.8400 - 1.8100 1.00 2727 134 0.2116 0.2194 REMARK 3 21 1.8100 - 1.7800 1.00 2705 159 0.2225 0.2463 REMARK 3 22 1.7800 - 1.7500 1.00 2687 149 0.2278 0.2821 REMARK 3 23 1.7500 - 1.7300 1.00 2703 125 0.2409 0.3120 REMARK 3 24 1.7300 - 1.7000 1.00 2715 129 0.2599 0.2891 REMARK 3 25 1.7000 - 1.6800 0.99 2691 156 0.2904 0.3284 REMARK 3 26 1.6800 - 1.6600 0.99 2708 145 0.3165 0.3891 REMARK 3 27 1.6600 - 1.6400 0.99 2673 123 0.3338 0.3679 REMARK 3 28 1.6400 - 1.6200 0.99 2706 118 0.3686 0.3824 REMARK 3 29 1.6200 - 1.6000 0.98 2585 151 0.4115 0.4226 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.197 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.659 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 20.72 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.83 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 : 0.009 5067 REMARK 3 ANGLE : 1.077 6903 REMARK 3 CHIRALITY : 0.064 746 REMARK 3 PLANARITY : 0.011 903 REMARK 3 DIHEDRAL : 14.479 1817 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 34 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 13 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.2596 8.9855 25.7371 REMARK 3 T TENSOR REMARK 3 T11: 0.3957 T22: 0.3763 REMARK 3 T33: 0.2212 T12: -0.0743 REMARK 3 T13: 0.0345 T23: -0.0362 REMARK 3 L TENSOR REMARK 3 L11: 2.2144 L22: 1.2985 REMARK 3 L33: 3.7108 L12: 0.0136 REMARK 3 L13: -1.4461 L23: -0.3172 REMARK 3 S TENSOR REMARK 3 S11: 0.4948 S12: -0.9063 S13: 0.2538 REMARK 3 S21: 0.6949 S22: -0.2384 S23: -0.0109 REMARK 3 S31: -0.3952 S32: 0.7587 S33: -0.3551 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 14 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.9182 16.4110 32.2143 REMARK 3 T TENSOR REMARK 3 T11: 0.6427 T22: 0.5181 REMARK 3 T33: 0.4129 T12: -0.1915 REMARK 3 T13: 0.2361 T23: -0.1822 REMARK 3 L TENSOR REMARK 3 L11: 0.0743 L22: 8.4751 REMARK 3 L33: 7.6942 L12: 0.7473 REMARK 3 L13: 0.0816 L23: 3.5511 REMARK 3 S TENSOR REMARK 3 S11: 0.3568 S12: -0.9034 S13: 1.2532 REMARK 3 S21: 0.6237 S22: 0.1242 S23: 0.1327 REMARK 3 S31: -0.5076 S32: 0.4403 S33: -0.1624 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 19 THROUGH 52 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.6858 13.7594 12.5760 REMARK 3 T TENSOR REMARK 3 T11: 0.3039 T22: 0.2535 REMARK 3 T33: 0.2665 T12: 0.0509 REMARK 3 T13: 0.0468 T23: 0.0148 REMARK 3 L TENSOR REMARK 3 L11: 0.9262 L22: 1.5005 REMARK 3 L33: 3.0355 L12: 0.7592 REMARK 3 L13: -0.2867 L23: -0.5890 REMARK 3 S TENSOR REMARK 3 S11: 0.2000 S12: 0.0152 S13: 0.2843 REMARK 3 S21: 0.0671 S22: 0.1012 S23: 0.2140 REMARK 3 S31: -0.7543 S32: -0.1757 S33: -0.2404 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 53 THROUGH 71 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.3620 4.9662 17.1036 REMARK 3 T TENSOR REMARK 3 T11: 0.2354 T22: 0.2969 REMARK 3 T33: 0.2722 T12: -0.0045 REMARK 3 T13: 0.0192 T23: 0.0118 REMARK 3 L TENSOR REMARK 3 L11: 2.9793 L22: 2.0483 REMARK 3 L33: 2.7180 L12: 0.7708 REMARK 3 L13: -0.8443 L23: -0.3173 REMARK 3 S TENSOR REMARK 3 S11: 0.0360 S12: 0.4489 S13: -0.0540 REMARK 3 S21: 0.0798 S22: 0.1007 S23: 0.1177 REMARK 3 S31: 0.0103 S32: -0.4631 S33: -0.0149 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.9458 -7.1454 10.3111 REMARK 3 T TENSOR REMARK 3 T11: 0.2084 T22: 0.2505 REMARK 3 T33: 0.3027 T12: -0.0023 REMARK 3 T13: -0.0577 T23: -0.0209 REMARK 3 L TENSOR REMARK 3 L11: 2.5713 L22: 4.0534 REMARK 3 L33: 2.1800 L12: 0.3499 REMARK 3 L13: -0.0801 L23: 1.1095 REMARK 3 S TENSOR REMARK 3 S11: 0.1063 S12: -0.2618 S13: -0.1629 REMARK 3 S21: 0.4985 S22: 0.0448 S23: -0.5336 REMARK 3 S31: 0.0454 S32: 0.0640 S33: -0.1307 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 18 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.3289 -2.7965 13.8617 REMARK 3 T TENSOR REMARK 3 T11: 0.2708 T22: 0.3726 REMARK 3 T33: 0.2727 T12: -0.0039 REMARK 3 T13: -0.0418 T23: -0.0505 REMARK 3 L TENSOR REMARK 3 L11: 5.6064 L22: 5.2218 REMARK 3 L33: 6.2812 L12: -1.2039 REMARK 3 L13: 0.1668 L23: 0.8137 REMARK 3 S TENSOR REMARK 3 S11: 0.0082 S12: -0.7327 S13: 0.3658 REMARK 3 S21: 0.7198 S22: 0.2949 S23: -0.3743 REMARK 3 S31: -0.3072 S32: -0.2787 S33: -0.1403 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 26 THROUGH 33 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.7775 7.0820 13.2898 REMARK 3 T TENSOR REMARK 3 T11: 0.4115 T22: 0.5144 REMARK 3 T33: 0.4563 T12: 0.0334 REMARK 3 T13: -0.0893 T23: -0.1890 REMARK 3 L TENSOR REMARK 3 L11: 1.4000 L22: 0.0109 REMARK 3 L33: 3.1913 L12: -0.0419 REMARK 3 L13: 2.0392 L23: -0.0955 REMARK 3 S TENSOR REMARK 3 S11: 0.0454 S12: -1.2680 S13: 1.0213 REMARK 3 S21: 0.8363 S22: 0.1016 S23: -0.8750 REMARK 3 S31: -1.0264 S32: -0.1485 S33: 0.1426 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 34 THROUGH 72 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.5051 -8.2458 6.3482 REMARK 3 T TENSOR REMARK 3 T11: 0.1955 T22: 0.2293 REMARK 3 T33: 0.2217 T12: -0.0269 REMARK 3 T13: -0.0036 T23: 0.0171 REMARK 3 L TENSOR REMARK 3 L11: 3.0906 L22: 1.8151 REMARK 3 L33: 2.0897 L12: -0.1822 REMARK 3 L13: 0.4657 L23: -0.5823 REMARK 3 S TENSOR REMARK 3 S11: 0.1449 S12: -0.2154 S13: -0.1845 REMARK 3 S21: 0.0612 S22: 0.0334 S23: 0.1305 REMARK 3 S31: -0.0009 S32: -0.1104 S33: -0.1427 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 73 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.5136 -10.8273 11.2574 REMARK 3 T TENSOR REMARK 3 T11: 0.1925 T22: 0.2862 REMARK 3 T33: 0.2031 T12: -0.0584 REMARK 3 T13: -0.0521 T23: 0.0488 REMARK 3 L TENSOR REMARK 3 L11: 3.1149 L22: 2.9805 REMARK 3 L33: 2.3989 L12: 0.4971 REMARK 3 L13: 0.3577 L23: -0.1101 REMARK 3 S TENSOR REMARK 3 S11: 0.2227 S12: -0.5455 S13: -0.2477 REMARK 3 S21: 0.3671 S22: -0.0436 S23: -0.0664 REMARK 3 S31: 0.3111 S32: -0.1945 S33: -0.0601 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 91 THROUGH 130 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.7500 0.6187 5.3489 REMARK 3 T TENSOR REMARK 3 T11: 0.2084 T22: 0.2209 REMARK 3 T33: 0.1950 T12: 0.0016 REMARK 3 T13: 0.0080 T23: 0.0019 REMARK 3 L TENSOR REMARK 3 L11: 2.6688 L22: 0.4945 REMARK 3 L33: 0.5494 L12: -0.6838 REMARK 3 L13: -0.2974 L23: 0.3941 REMARK 3 S TENSOR REMARK 3 S11: 0.0500 S12: -0.1422 S13: -0.0358 REMARK 3 S21: -0.0178 S22: -0.0144 S23: -0.0418 REMARK 3 S31: -0.0702 S32: 0.0105 S33: -0.0402 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 0 THROUGH 8 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.3091 -8.7295 -11.9547 REMARK 3 T TENSOR REMARK 3 T11: 0.3189 T22: 0.2841 REMARK 3 T33: 0.3045 T12: -0.0322 REMARK 3 T13: 0.0161 T23: -0.0190 REMARK 3 L TENSOR REMARK 3 L11: 7.9997 L22: 1.8757 REMARK 3 L33: 4.1956 L12: 0.0496 REMARK 3 L13: -2.3799 L23: 1.2937 REMARK 3 S TENSOR REMARK 3 S11: -0.1660 S12: 0.0060 S13: -0.7236 REMARK 3 S21: 0.1237 S22: -0.0421 S23: 0.1118 REMARK 3 S31: 0.6684 S32: -0.1590 S33: 0.2528 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 9 THROUGH 24 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.2307 2.3067 -22.1800 REMARK 3 T TENSOR REMARK 3 T11: 0.3038 T22: 0.4780 REMARK 3 T33: 0.2433 T12: -0.0048 REMARK 3 T13: 0.0354 T23: 0.0208 REMARK 3 L TENSOR REMARK 3 L11: 2.7875 L22: 2.1068 REMARK 3 L33: 1.3678 L12: 0.8421 REMARK 3 L13: -0.7521 L23: -0.4703 REMARK 3 S TENSOR REMARK 3 S11: -0.1989 S12: 0.6820 S13: -0.0801 REMARK 3 S21: -0.3651 S22: 0.0163 S23: -0.2313 REMARK 3 S31: -0.1130 S32: 0.0022 S33: 0.1629 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 25 THROUGH 48 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.9991 1.1366 -8.6372 REMARK 3 T TENSOR REMARK 3 T11: 0.2469 T22: 0.2449 REMARK 3 T33: 0.2157 T12: 0.0155 REMARK 3 T13: 0.0229 T23: -0.0043 REMARK 3 L TENSOR REMARK 3 L11: 1.7189 L22: 1.0474 REMARK 3 L33: 1.2422 L12: -0.6578 REMARK 3 L13: 0.3129 L23: -0.1872 REMARK 3 S TENSOR REMARK 3 S11: 0.0240 S12: 0.1780 S13: -0.1209 REMARK 3 S21: -0.0419 S22: -0.0338 S23: -0.0362 REMARK 3 S31: 0.0634 S32: -0.0435 S33: 0.0157 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 49 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.7356 9.0422 -13.1347 REMARK 3 T TENSOR REMARK 3 T11: 0.2876 T22: 0.2889 REMARK 3 T33: 0.3004 T12: 0.0208 REMARK 3 T13: 0.0112 T23: 0.0319 REMARK 3 L TENSOR REMARK 3 L11: 3.0237 L22: 1.5584 REMARK 3 L33: 2.1625 L12: -0.5191 REMARK 3 L13: -0.5393 L23: -0.1803 REMARK 3 S TENSOR REMARK 3 S11: 0.0798 S12: 0.2738 S13: 0.4956 REMARK 3 S21: -0.0589 S22: -0.0631 S23: 0.0225 REMARK 3 S31: -0.2299 S32: -0.2111 S33: 0.0004 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 76 THROUGH 117 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.5784 -0.3108 -9.2347 REMARK 3 T TENSOR REMARK 3 T11: 0.1873 T22: 0.1896 REMARK 3 T33: 0.1817 T12: -0.0046 REMARK 3 T13: 0.0057 T23: -0.0234 REMARK 3 L TENSOR REMARK 3 L11: 2.8159 L22: 1.2067 REMARK 3 L33: 2.0391 L12: 0.5164 REMARK 3 L13: -0.3237 L23: -0.2914 REMARK 3 S TENSOR REMARK 3 S11: 0.0556 S12: 0.0417 S13: 0.0562 REMARK 3 S21: 0.0032 S22: -0.0053 S23: 0.0793 REMARK 3 S31: 0.0326 S32: 0.0219 S33: -0.0424 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 118 THROUGH 1022 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.2600 2.4756 -26.3098 REMARK 3 T TENSOR REMARK 3 T11: 0.3558 T22: 0.3716 REMARK 3 T33: 0.3034 T12: -0.0293 REMARK 3 T13: 0.0159 T23: -0.0185 REMARK 3 L TENSOR REMARK 3 L11: 2.3994 L22: 0.6931 REMARK 3 L33: 3.1269 L12: 0.7104 REMARK 3 L13: -1.3865 L23: 0.6616 REMARK 3 S TENSOR REMARK 3 S11: 0.0314 S12: -0.1049 S13: 0.1946 REMARK 3 S21: -0.1983 S22: 0.0371 S23: -0.0445 REMARK 3 S31: -0.3760 S32: 0.7870 S33: -0.0001 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 5 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.3321 10.1771 -25.8301 REMARK 3 T TENSOR REMARK 3 T11: 0.3417 T22: 0.4578 REMARK 3 T33: 0.1923 T12: -0.0482 REMARK 3 T13: -0.0074 T23: 0.0766 REMARK 3 L TENSOR REMARK 3 L11: 0.2467 L22: 2.8889 REMARK 3 L33: 3.2483 L12: 0.6975 REMARK 3 L13: -0.7951 L23: -1.4564 REMARK 3 S TENSOR REMARK 3 S11: -0.0192 S12: 1.2044 S13: 0.2426 REMARK 3 S21: -0.4287 S22: 0.0996 S23: 0.0535 REMARK 3 S31: -0.2684 S32: 0.4307 S33: -0.0431 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 6 THROUGH 13 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.3315 10.3011 -22.7123 REMARK 3 T TENSOR REMARK 3 T11: 0.2768 T22: 0.4413 REMARK 3 T33: 0.2393 T12: -0.0082 REMARK 3 T13: -0.0491 T23: 0.0964 REMARK 3 L TENSOR REMARK 3 L11: 1.2826 L22: 0.6856 REMARK 3 L33: 3.5624 L12: -0.6310 REMARK 3 L13: -2.1257 L23: 1.0412 REMARK 3 S TENSOR REMARK 3 S11: -0.2072 S12: 0.8423 S13: 0.4630 REMARK 3 S21: -0.1115 S22: 0.0710 S23: 0.1029 REMARK 3 S31: -0.4100 S32: 0.4565 S33: 0.1232 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 14 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.8149 18.0915 -30.1441 REMARK 3 T TENSOR REMARK 3 T11: 0.5687 T22: 0.8205 REMARK 3 T33: 0.3620 T12: -0.1560 REMARK 3 T13: -0.0103 T23: 0.1698 REMARK 3 L TENSOR REMARK 3 L11: 0.1065 L22: 3.4587 REMARK 3 L33: 2.1653 L12: 0.3702 REMARK 3 L13: -0.3005 L23: -2.0536 REMARK 3 S TENSOR REMARK 3 S11: -0.5021 S12: 0.6437 S13: 0.6410 REMARK 3 S21: -1.0008 S22: 0.1760 S23: -0.1733 REMARK 3 S31: -0.0026 S32: 0.3725 S33: 0.2675 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 19 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.6034 14.0186 -14.7508 REMARK 3 T TENSOR REMARK 3 T11: 0.2741 T22: 0.3105 REMARK 3 T33: 0.2659 T12: -0.0386 REMARK 3 T13: -0.0011 T23: 0.0400 REMARK 3 L TENSOR REMARK 3 L11: 1.6848 L22: 0.8555 REMARK 3 L33: 9.8544 L12: -0.1257 REMARK 3 L13: -3.1439 L23: 0.2984 REMARK 3 S TENSOR REMARK 3 S11: 0.1349 S12: 0.1512 S13: 0.4474 REMARK 3 S21: -0.0795 S22: 0.0876 S23: -0.0691 REMARK 3 S31: -0.5075 S32: 0.4064 S33: -0.2654 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 26 THROUGH 35 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.8670 8.7518 -1.1502 REMARK 3 T TENSOR REMARK 3 T11: 0.2630 T22: 0.2836 REMARK 3 T33: 0.2338 T12: -0.0036 REMARK 3 T13: 0.0064 T23: 0.0155 REMARK 3 L TENSOR REMARK 3 L11: 1.5712 L22: 2.5007 REMARK 3 L33: 1.3129 L12: 0.7797 REMARK 3 L13: 1.0237 L23: 0.4649 REMARK 3 S TENSOR REMARK 3 S11: -0.1393 S12: 0.2028 S13: 0.1564 REMARK 3 S21: 0.0288 S22: 0.1238 S23: 0.1234 REMARK 3 S31: -0.1660 S32: 0.0698 S33: 0.0274 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 36 THROUGH 52 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.2671 17.6400 -14.1368 REMARK 3 T TENSOR REMARK 3 T11: 0.4014 T22: 0.3992 REMARK 3 T33: 0.2897 T12: -0.0753 REMARK 3 T13: 0.0189 T23: 0.0519 REMARK 3 L TENSOR REMARK 3 L11: 1.3500 L22: 0.7340 REMARK 3 L33: 1.3329 L12: 0.1718 REMARK 3 L13: -0.3088 L23: -0.6519 REMARK 3 S TENSOR REMARK 3 S11: 0.0678 S12: 0.1453 S13: 0.5179 REMARK 3 S21: 0.0166 S22: 0.0368 S23: 0.0885 REMARK 3 S31: -0.7945 S32: 0.0902 S33: -0.1282 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 53 THROUGH 71 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.8489 5.9036 -15.3374 REMARK 3 T TENSOR REMARK 3 T11: 0.2424 T22: 0.3641 REMARK 3 T33: 0.2321 T12: -0.0209 REMARK 3 T13: -0.0022 T23: 0.0196 REMARK 3 L TENSOR REMARK 3 L11: 2.1453 L22: 1.1346 REMARK 3 L33: 1.5071 L12: -0.3835 REMARK 3 L13: -0.5410 L23: 0.3762 REMARK 3 S TENSOR REMARK 3 S11: -0.0195 S12: -0.1983 S13: -0.1710 REMARK 3 S21: 0.0282 S22: -0.0572 S23: -0.0924 REMARK 3 S31: 0.0293 S32: 0.4023 S33: 0.1159 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.8296 -6.7341 -8.8681 REMARK 3 T TENSOR REMARK 3 T11: 0.2016 T22: 0.2409 REMARK 3 T33: 0.2042 T12: 0.0294 REMARK 3 T13: -0.0367 T23: 0.0233 REMARK 3 L TENSOR REMARK 3 L11: 2.2822 L22: 5.0692 REMARK 3 L33: 1.4882 L12: 0.7550 REMARK 3 L13: -0.2498 L23: -0.3301 REMARK 3 S TENSOR REMARK 3 S11: 0.1009 S12: 0.1731 S13: -0.0018 REMARK 3 S21: -0.2635 S22: 0.0015 S23: 0.4296 REMARK 3 S31: 0.0069 S32: -0.1039 S33: -0.1314 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 18 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): -29.2122 -2.1422 -12.2668 REMARK 3 T TENSOR REMARK 3 T11: 0.2888 T22: 0.2988 REMARK 3 T33: 0.2489 T12: 0.0194 REMARK 3 T13: 0.0098 T23: 0.0544 REMARK 3 L TENSOR REMARK 3 L11: 3.8062 L22: 5.6813 REMARK 3 L33: 4.7184 L12: 1.1156 REMARK 3 L13: 0.8055 L23: 0.4637 REMARK 3 S TENSOR REMARK 3 S11: 0.0910 S12: 0.6161 S13: 0.2227 REMARK 3 S21: -0.5546 S22: 0.1863 S23: 0.1603 REMARK 3 S31: -0.5626 S32: 0.0835 S33: -0.0957 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 26 THROUGH 33 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.3602 8.4372 -11.2817 REMARK 3 T TENSOR REMARK 3 T11: 0.4241 T22: 0.5394 REMARK 3 T33: 0.3291 T12: 0.0195 REMARK 3 T13: -0.0430 T23: 0.1666 REMARK 3 L TENSOR REMARK 3 L11: 0.0431 L22: 0.2395 REMARK 3 L33: 0.0679 L12: 0.1040 REMARK 3 L13: 0.0582 L23: 0.1255 REMARK 3 S TENSOR REMARK 3 S11: 0.0660 S12: 1.0087 S13: 0.6458 REMARK 3 S21: -0.7007 S22: 0.0537 S23: 0.4090 REMARK 3 S31: -0.7887 S32: -0.2646 S33: 0.1277 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 34 THROUGH 97 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.6856 -8.0605 -6.3058 REMARK 3 T TENSOR REMARK 3 T11: 0.1917 T22: 0.2282 REMARK 3 T33: 0.1733 T12: 0.0288 REMARK 3 T13: -0.0060 T23: 0.0025 REMARK 3 L TENSOR REMARK 3 L11: 2.3779 L22: 1.1760 REMARK 3 L33: 1.1160 L12: 0.1911 REMARK 3 L13: 0.2231 L23: 0.4007 REMARK 3 S TENSOR REMARK 3 S11: 0.0658 S12: 0.1567 S13: -0.0966 REMARK 3 S21: -0.0577 S22: -0.0114 S23: -0.0278 REMARK 3 S31: 0.0327 S32: 0.1327 S33: -0.0607 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 98 THROUGH 130 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.9662 1.6770 -4.0095 REMARK 3 T TENSOR REMARK 3 T11: 0.2047 T22: 0.2245 REMARK 3 T33: 0.2178 T12: 0.0015 REMARK 3 T13: 0.0017 T23: 0.0187 REMARK 3 L TENSOR REMARK 3 L11: 1.7803 L22: 0.2116 REMARK 3 L33: 0.2669 L12: 0.4435 REMARK 3 L13: -0.1195 L23: -0.1463 REMARK 3 S TENSOR REMARK 3 S11: 0.0503 S12: -0.0354 S13: -0.0223 REMARK 3 S21: -0.0165 S22: -0.0378 S23: 0.0716 REMARK 3 S31: -0.0114 S32: 0.0431 S33: -0.0398 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 0 THROUGH 8 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.2525 -9.1194 13.3185 REMARK 3 T TENSOR REMARK 3 T11: 0.2586 T22: 0.2586 REMARK 3 T33: 0.3190 T12: 0.0090 REMARK 3 T13: 0.0387 T23: -0.0022 REMARK 3 L TENSOR REMARK 3 L11: 7.9170 L22: 1.3745 REMARK 3 L33: 4.0906 L12: -0.1784 REMARK 3 L13: -2.1775 L23: -1.4903 REMARK 3 S TENSOR REMARK 3 S11: -0.3083 S12: 0.0407 S13: -0.8370 REMARK 3 S21: -0.0585 S22: -0.0475 S23: -0.1155 REMARK 3 S31: 0.2345 S32: 0.3349 S33: 0.3517 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 9 THROUGH 30 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.4169 -0.4629 20.9821 REMARK 3 T TENSOR REMARK 3 T11: 0.2571 T22: 0.3740 REMARK 3 T33: 0.2128 T12: 0.0169 REMARK 3 T13: 0.0050 T23: 0.0104 REMARK 3 L TENSOR REMARK 3 L11: 2.1858 L22: 1.2562 REMARK 3 L33: 0.3754 L12: -0.1868 REMARK 3 L13: -0.6651 L23: -0.0737 REMARK 3 S TENSOR REMARK 3 S11: -0.1645 S12: -0.3471 S13: -0.0966 REMARK 3 S21: 0.1474 S22: 0.0494 S23: -0.0657 REMARK 3 S31: 0.0000 S32: 0.1820 S33: 0.1318 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 31 THROUGH 48 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.4344 2.6583 8.8036 REMARK 3 T TENSOR REMARK 3 T11: 0.2162 T22: 0.2282 REMARK 3 T33: 0.2153 T12: -0.0055 REMARK 3 T13: 0.0127 T23: 0.0073 REMARK 3 L TENSOR REMARK 3 L11: 1.3115 L22: 0.9270 REMARK 3 L33: 1.2304 L12: 0.4706 REMARK 3 L13: 0.2845 L23: -0.0075 REMARK 3 S TENSOR REMARK 3 S11: 0.0176 S12: 0.1812 S13: 0.1198 REMARK 3 S21: -0.0961 S22: -0.0638 S23: 0.0530 REMARK 3 S31: 0.0558 S32: -0.0371 S33: 0.0558 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 49 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.6390 8.2474 15.3917 REMARK 3 T TENSOR REMARK 3 T11: 0.2273 T22: 0.2713 REMARK 3 T33: 0.2629 T12: -0.0317 REMARK 3 T13: 0.0114 T23: -0.0044 REMARK 3 L TENSOR REMARK 3 L11: 2.8454 L22: 1.4587 REMARK 3 L33: 1.8239 L12: 0.5185 REMARK 3 L13: -0.3666 L23: 0.1349 REMARK 3 S TENSOR REMARK 3 S11: -0.0056 S12: -0.1624 S13: 0.5009 REMARK 3 S21: -0.0405 S22: 0.0397 S23: -0.1102 REMARK 3 S31: -0.2067 S32: 0.1451 S33: -0.0060 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 76 THROUGH 103 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.1654 -1.0729 10.3877 REMARK 3 T TENSOR REMARK 3 T11: 0.1882 T22: 0.2402 REMARK 3 T33: 0.1998 T12: 0.0131 REMARK 3 T13: -0.0045 T23: 0.0126 REMARK 3 L TENSOR REMARK 3 L11: 1.9522 L22: 1.4124 REMARK 3 L33: 2.2512 L12: 0.0676 REMARK 3 L13: -0.7412 L23: 0.3520 REMARK 3 S TENSOR REMARK 3 S11: 0.0358 S12: -0.0486 S13: 0.1267 REMARK 3 S21: -0.0723 S22: 0.0352 S23: -0.1420 REMARK 3 S31: -0.0023 S32: 0.0173 S33: -0.0400 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 104 THROUGH 1008 ) REMARK 3 ORIGIN FOR THE GROUP (A): -34.2948 1.7672 27.8860 REMARK 3 T TENSOR REMARK 3 T11: 0.2498 T22: 0.3346 REMARK 3 T33: 0.2031 T12: 0.0147 REMARK 3 T13: -0.0048 T23: -0.0133 REMARK 3 L TENSOR REMARK 3 L11: 3.1084 L22: 0.9455 REMARK 3 L33: 2.4297 L12: -0.7469 REMARK 3 L13: -1.3075 L23: -0.7103 REMARK 3 S TENSOR REMARK 3 S11: -0.1080 S12: -0.0700 S13: 0.1983 REMARK 3 S21: 0.2253 S22: 0.0431 S23: 0.0247 REMARK 3 S31: -0.1329 S32: -0.6556 S33: 0.0782 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 9HUO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1292144274. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-OCT-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY REMARK 200 BEAMLINE : P14 (MX2) REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : DIALS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83281 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600 REMARK 200 RESOLUTION RANGE LOW (A) : 41.580 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : 5.000 REMARK 200 R MERGE (I) : 0.06727 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.62 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.88840 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 44.68 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.1M BIS-TRIS PH5.5, 0.25 REMARK 280 M AMS, VAPOR DIFFUSION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 38.43500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.17000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.57500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.17000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.43500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.57500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4800 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 14690 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I, M 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4430 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15040 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 ALA I 0 REMARK 465 GLY I 131 REMARK 465 GLY I 132 REMARK 465 GLY I 133 REMARK 465 GLY I 134 REMARK 465 SER I 135 REMARK 465 GLY I 136 REMARK 465 GLY I 137 REMARK 465 GLY I 138 REMARK 465 GLY I 139 REMARK 465 SER I 140 REMARK 465 GLY I 141 REMARK 465 GLY I 142 REMARK 465 GLY M -2 REMARK 465 ALA M -1 REMARK 465 ALA C 0 REMARK 465 GLY C 131 REMARK 465 GLY C 132 REMARK 465 GLY C 133 REMARK 465 GLY C 134 REMARK 465 SER C 135 REMARK 465 GLY C 136 REMARK 465 GLY C 137 REMARK 465 GLY C 138 REMARK 465 GLY C 139 REMARK 465 SER C 140 REMARK 465 GLY C 141 REMARK 465 GLY C 142 REMARK 465 GLY D -2 REMARK 465 ALA D -1 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 M1022 CG CD OE1 NE2 REMARK 470 GLN D1008 CG CD OE1 NE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OG SER M 52 HE22 GLN B 55 1.38 REMARK 500 O HOH C 306 O HOH C 382 1.82 REMARK 500 O HOH A 218 O HOH A 248 1.87 REMARK 500 O HOH M 1303 O HOH M 1393 1.95 REMARK 500 O HOH C 302 O HOH C 390 1.97 REMARK 500 O HOH D 1295 O HOH D 1298 1.99 REMARK 500 O HOH C 317 O HOH C 402 2.02 REMARK 500 O HOH C 383 O HOH C 394 2.05 REMARK 500 O HOH C 346 O HOH C 397 2.15 REMARK 500 O HOH D 1269 O HOH D 1316 2.17 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 ASP A 27 -168.62 -101.78 REMARK 500 ASN A 63 58.20 -116.46 REMARK 500 PHE I 29 -132.98 -112.03 REMARK 500 SER I 30 -78.70 105.26 REMARK 500 SER I 30 -78.81 105.26 REMARK 500 TYR I 113 116.52 -167.33 REMARK 500 ASP M 51 -45.44 75.51 REMARK 500 ALA M 84 170.93 179.29 REMARK 500 ASP B 27 -166.17 -100.42 REMARK 500 ASN B 63 55.81 -119.41 REMARK 500 THR C 28 -137.62 -155.09 REMARK 500 PHE C 29 114.73 124.61 REMARK 500 TYR C 113 117.79 -166.40 REMARK 500 ASP D 51 -44.12 67.66 REMARK 500 ALA D 84 174.28 178.66 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG I 66 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 K I 201 K REMARK 620 N RES CSSEQI ATOM REMARK 620 1 TRP I 120 O REMARK 620 2 GLY I 121 O 64.4 REMARK 620 3 HOH I 372 O 82.2 132.3 REMARK 620 4 HOH I 375 O 85.8 107.4 102.6 REMARK 620 5 HOH I 379 O 163.4 101.6 114.4 90.6 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA C 201 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 TRP C 120 O REMARK 620 2 GLY C 121 O 63.5 REMARK 620 3 HOH C 395 O 73.9 122.5 REMARK 620 4 HOH C 401 O 85.6 109.8 103.2 REMARK 620 5 HOH D1317 O 168.7 105.6 116.2 96.2 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA D1102 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ARG D 61 O REMARK 620 2 SER D 63 OG 117.5 REMARK 620 3 SER D 76 OG 93.4 147.9 REMARK 620 4 HOH D1287 O 88.0 91.1 99.3 REMARK 620 N 1 2 3 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9FYT RELATED DB: PDB DBREF 9HUO A 1 71 UNP P01391 3L21_NAJKA 1 71 DBREF 9HUO I 0 142 PDB 9HUO 9HUO 0 142 DBREF 9HUO M -2 1022 PDB 9HUO 9HUO -2 1022 DBREF 9HUO B 1 71 UNP P01391 3L21_NAJKA 1 71 DBREF 9HUO C 0 142 PDB 9HUO 9HUO 0 142 DBREF 9HUO D -2 1008 PDB 9HUO 9HUO -2 1008 SEQRES 1 A 71 ILE ARG CYS PHE ILE THR PRO ASP ILE THR SER LYS ASP SEQRES 2 A 71 CYS PRO ASN GLY HIS VAL CYS TYR THR LYS THR TRP CYS SEQRES 3 A 71 ASP ALA PHE CYS SER ILE ARG GLY LYS ARG VAL ASP LEU SEQRES 4 A 71 GLY CYS ALA ALA THR CYS PRO THR VAL LYS THR GLY VAL SEQRES 5 A 71 ASP ILE GLN CYS CYS SER THR ASP ASN CYS ASN PRO PHE SEQRES 6 A 71 PRO THR ARG LYS ARG PRO SEQRES 1 I 144 ALA GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS SEQRES 2 I 144 LYS PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER SEQRES 3 I 144 GLY GLY THR PHE SER SER TYR ALA ILE SER TRP VAL ARG SEQRES 4 I 144 GLN ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE SEQRES 5 I 144 ILE PRO ILE PHE GLY THR ALA ASN TYR ALA GLN LYS PHE SEQRES 6 I 144 GLN GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER SEQRES 7 I 144 THR ALA TYR MET GLU LEU ARG SER LEU ARG SER ASP ASP SEQRES 8 I 144 THR ALA VAL TYR TYR CYS ALA ARG ASP ASN LEU GLY TYR SEQRES 9 I 144 CYS SER GLY GLY SER CYS TYR SER ASP TYR TYR TYR TYR SEQRES 10 I 144 TYR MET ASP VAL TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 11 I 144 SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY SEQRES 12 I 144 GLY SEQRES 1 M 117 GLY ALA SER SER TYR GLU LEU THR GLN PRO PRO SER VAL SEQRES 2 M 117 SER VAL ALA PRO GLY ARG THR ALA THR ILE THR CYS GLU SEQRES 3 M 117 GLY ASP ASN ILE GLY GLN GLN ILE VAL HIS TRP TYR GLN SEQRES 4 M 117 GLN LYS PRO GLY GLN ALA PRO VAL ALA VAL ILE SER SER SEQRES 5 M 117 ASP SER ASP ARG PRO SER GLY ILE PRO GLU ARG PHE SER SEQRES 6 M 117 GLY SER ASN SER GLY ASN THR ALA THR LEU THR ILE SER SEQRES 7 M 117 ARG VAL GLU ALA GLY ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 M 117 VAL TRP ASP SER GLY SER ASP HIS VAL VAL PHE GLY GLY SEQRES 9 M 117 GLY THR LYS VAL THR VAL LEU GLU ASN LEU TYR PHE GLN SEQRES 1 B 71 ILE ARG CYS PHE ILE THR PRO ASP ILE THR SER LYS ASP SEQRES 2 B 71 CYS PRO ASN GLY HIS VAL CYS TYR THR LYS THR TRP CYS SEQRES 3 B 71 ASP ALA PHE CYS SER ILE ARG GLY LYS ARG VAL ASP LEU SEQRES 4 B 71 GLY CYS ALA ALA THR CYS PRO THR VAL LYS THR GLY VAL SEQRES 5 B 71 ASP ILE GLN CYS CYS SER THR ASP ASN CYS ASN PRO PHE SEQRES 6 B 71 PRO THR ARG LYS ARG PRO SEQRES 1 C 144 ALA GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS SEQRES 2 C 144 LYS PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER SEQRES 3 C 144 GLY GLY THR PHE SER SER TYR ALA ILE SER TRP VAL ARG SEQRES 4 C 144 GLN ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE SEQRES 5 C 144 ILE PRO ILE PHE GLY THR ALA ASN TYR ALA GLN LYS PHE SEQRES 6 C 144 GLN GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER SEQRES 7 C 144 THR ALA TYR MET GLU LEU ARG SER LEU ARG SER ASP ASP SEQRES 8 C 144 THR ALA VAL TYR TYR CYS ALA ARG ASP ASN LEU GLY TYR SEQRES 9 C 144 CYS SER GLY GLY SER CYS TYR SER ASP TYR TYR TYR TYR SEQRES 10 C 144 TYR MET ASP VAL TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 11 C 144 SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY SEQRES 12 C 144 GLY SEQRES 1 D 117 GLY ALA SER SER TYR GLU LEU THR GLN PRO PRO SER VAL SEQRES 2 D 117 SER VAL ALA PRO GLY ARG THR ALA THR ILE THR CYS GLU SEQRES 3 D 117 GLY ASP ASN ILE GLY GLN GLN ILE VAL HIS TRP TYR GLN SEQRES 4 D 117 GLN LYS PRO GLY GLN ALA PRO VAL ALA VAL ILE SER SER SEQRES 5 D 117 ASP SER ASP ARG PRO SER GLY ILE PRO GLU ARG PHE SER SEQRES 6 D 117 GLY SER ASN SER GLY ASN THR ALA THR LEU THR ILE SER SEQRES 7 D 117 ARG VAL GLU ALA GLY ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 D 117 VAL TRP ASP SER GLY SER ASP HIS VAL VAL PHE GLY GLY SEQRES 9 D 117 GLY THR LYS VAL THR VAL LEU GLU ASN LEU TYR PHE GLN HET GOL A 101 14 HET CL A 102 1 HET K I 201 1 HET GOL M1201 14 HET GOL B 101 14 HET GOL B 102 14 HET NA C 201 1 HET SO4 C 202 5 HET GOL D1101 12 HET NA D1102 1 HETNAM GOL GLYCEROL HETNAM CL CHLORIDE ION HETNAM K POTASSIUM ION HETNAM NA SODIUM ION HETNAM SO4 SULFATE ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 7 GOL 5(C3 H8 O3) FORMUL 8 CL CL 1- FORMUL 9 K K 1+ FORMUL 13 NA 2(NA 1+) FORMUL 14 SO4 O4 S 2- FORMUL 17 HOH *552(H2 O) HELIX 1 AA1 PHE A 29 GLY A 34 1 6 HELIX 2 AA2 PRO I 52A GLY I 55 5 4 HELIX 3 AA3 ARG I 86 THR I 90 5 5 HELIX 4 AA4 ASN M 27 GLN M 31 5 5 HELIX 5 AA5 GLU M 79 GLU M 83 5 5 HELIX 6 AA6 PHE B 29 GLY B 34 1 6 HELIX 7 AA7 PRO C 52A GLY C 55 5 4 HELIX 8 AA8 ARG C 86 THR C 90 5 5 HELIX 9 AA9 ASN D 27 GLN D 31 5 5 HELIX 10 AB1 GLU D 79 GLU D 83 5 5 SHEET 1 AA1 2 ARG A 2 ILE A 5 0 SHEET 2 AA1 2 THR A 10 ASP A 13 -1 O LYS A 12 N CYS A 3 SHEET 1 AA2 3 ARG A 36 ALA A 42 0 SHEET 2 AA2 3 VAL A 19 TRP A 25 -1 N LYS A 23 O ASP A 38 SHEET 3 AA2 3 ASP A 53 CYS A 57 -1 O ASP A 53 N THR A 24 SHEET 1 AA3 4 GLN I 3 GLN I 6 0 SHEET 2 AA3 4 VAL I 18 SER I 25 -1 O SER I 25 N GLN I 3 SHEET 3 AA3 4 THR I 77 LEU I 82 -1 O ALA I 78 N CYS I 22 SHEET 4 AA3 4 VAL I 67 ASP I 72 -1 N ASP I 72 O THR I 77 SHEET 1 AA4 6 GLU I 10 LYS I 12 0 SHEET 2 AA4 6 THR I 124 VAL I 128 1 O THR I 127 N LYS I 12 SHEET 3 AA4 6 ALA I 91 ASP I 98 -1 N TYR I 93 O THR I 124 SHEET 4 AA4 6 ILE I 34 GLN I 39 -1 N VAL I 37 O TYR I 94 SHEET 5 AA4 6 LEU I 45 ILE I 52 -1 O GLU I 46 N ARG I 38 SHEET 6 AA4 6 THR I 56 TYR I 59 -1 O ASN I 58 N GLY I 50 SHEET 1 AA5 4 GLU I 10 LYS I 12 0 SHEET 2 AA5 4 THR I 124 VAL I 128 1 O THR I 127 N LYS I 12 SHEET 3 AA5 4 ALA I 91 ASP I 98 -1 N TYR I 93 O THR I 124 SHEET 4 AA5 4 MET I 117 TRP I 120 -1 O VAL I 119 N ARG I 97 SHEET 1 AA6 2 CYS I 103 SER I 104 0 SHEET 2 AA6 2 SER I 107 CYS I 108 -1 O SER I 107 N SER I 104 SHEET 1 AA7 5 SER M 9 VAL M 13 0 SHEET 2 AA7 5 THR M 118 VAL M 122 1 O THR M 121 N VAL M 11 SHEET 3 AA7 5 ALA M 84 ASP M 92 -1 N ALA M 84 O VAL M 120 SHEET 4 AA7 5 HIS M 34 GLN M 38 -1 N GLN M 38 O ASP M 85 SHEET 5 AA7 5 VAL M 45 ILE M 48 -1 O VAL M 45 N GLN M 37 SHEET 1 AA8 4 SER M 9 VAL M 13 0 SHEET 2 AA8 4 THR M 118 VAL M 122 1 O THR M 121 N VAL M 11 SHEET 3 AA8 4 ALA M 84 ASP M 92 -1 N ALA M 84 O VAL M 120 SHEET 4 AA8 4 HIS M 97 PHE M 100 -1 O HIS M 97 N ASP M 92 SHEET 1 AA9 3 ALA M 19 GLU M 24 0 SHEET 2 AA9 3 THR M 70 ILE M 75 -1 O LEU M 73 N ILE M 21 SHEET 3 AA9 3 PHE M 62 SER M 67 -1 N SER M 65 O THR M 72 SHEET 1 AB1 2 ARG B 2 ILE B 5 0 SHEET 2 AB1 2 THR B 10 ASP B 13 -1 O LYS B 12 N CYS B 3 SHEET 1 AB2 5 ASP B 53 CYS B 57 0 SHEET 2 AB2 5 VAL B 19 TRP B 25 -1 N CYS B 20 O CYS B 57 SHEET 3 AB2 5 ARG B 36 ALA B 42 -1 O ARG B 36 N TRP B 25 SHEET 4 AB2 5 SER C 107 TYR C 109 -1 O CYS C 108 N VAL B 37 SHEET 5 AB2 5 CYS C 103 SER C 104 -1 N SER C 104 O SER C 107 SHEET 1 AB3 4 GLN C 3 GLN C 6 0 SHEET 2 AB3 4 VAL C 18 SER C 25 -1 O LYS C 23 N VAL C 5 SHEET 3 AB3 4 THR C 77 LEU C 82 -1 O ALA C 78 N CYS C 22 SHEET 4 AB3 4 VAL C 67 ASP C 72 -1 N ASP C 72 O THR C 77 SHEET 1 AB4 6 GLU C 10 LYS C 12 0 SHEET 2 AB4 6 THR C 124 VAL C 128 1 O THR C 127 N LYS C 12 SHEET 3 AB4 6 ALA C 91 ASP C 98 -1 N TYR C 93 O THR C 124 SHEET 4 AB4 6 ILE C 34 GLN C 39 -1 N VAL C 37 O TYR C 94 SHEET 5 AB4 6 LEU C 45 ILE C 52 -1 O MET C 48 N TRP C 36 SHEET 6 AB4 6 THR C 56 TYR C 59 -1 O ASN C 58 N GLY C 50 SHEET 1 AB5 4 GLU C 10 LYS C 12 0 SHEET 2 AB5 4 THR C 124 VAL C 128 1 O THR C 127 N LYS C 12 SHEET 3 AB5 4 ALA C 91 ASP C 98 -1 N TYR C 93 O THR C 124 SHEET 4 AB5 4 MET C 117 TRP C 120 -1 O VAL C 119 N ARG C 97 SHEET 1 AB6 5 SER D 9 VAL D 13 0 SHEET 2 AB6 5 THR D 104 VAL D 108 1 O THR D 107 N VAL D 11 SHEET 3 AB6 5 ALA D 84 ASP D 92 -1 N ALA D 84 O VAL D 106 SHEET 4 AB6 5 HIS D 34 GLN D 38 -1 N GLN D 38 O ASP D 85 SHEET 5 AB6 5 VAL D 45 ILE D 48 -1 O ILE D 48 N TRP D 35 SHEET 1 AB7 4 SER D 9 VAL D 13 0 SHEET 2 AB7 4 THR D 104 VAL D 108 1 O THR D 107 N VAL D 11 SHEET 3 AB7 4 ALA D 84 ASP D 92 -1 N ALA D 84 O VAL D 106 SHEET 4 AB7 4 HIS D 97 PHE D 100 -1 O HIS D 97 N ASP D 92 SHEET 1 AB8 3 ALA D 19 GLU D 24 0 SHEET 2 AB8 3 THR D 70 ILE D 75 -1 O LEU D 73 N ILE D 21 SHEET 3 AB8 3 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74 SSBOND 1 CYS A 3 CYS A 20 1555 1555 2.03 SSBOND 2 CYS A 14 CYS A 41 1555 1555 2.05 SSBOND 3 CYS A 26 CYS A 30 1555 1555 2.04 SSBOND 4 CYS A 45 CYS A 56 1555 1555 2.02 SSBOND 5 CYS A 57 CYS A 62 1555 1555 2.04 SSBOND 6 CYS I 22 CYS I 95 1555 1555 2.05 SSBOND 7 CYS I 103 CYS I 108 1555 1555 2.02 SSBOND 8 CYS M 23 CYS M 88 1555 1555 2.07 SSBOND 9 CYS B 3 CYS B 20 1555 1555 2.02 SSBOND 10 CYS B 14 CYS B 41 1555 1555 2.04 SSBOND 11 CYS B 26 CYS B 30 1555 1555 2.06 SSBOND 12 CYS B 45 CYS B 56 1555 1555 2.03 SSBOND 13 CYS B 57 CYS B 62 1555 1555 2.06 SSBOND 14 CYS C 22 CYS C 95 1555 1555 2.05 SSBOND 15 CYS C 103 CYS C 108 1555 1555 2.06 SSBOND 16 CYS D 23 CYS D 88 1555 1555 2.07 LINK O TRP I 120 K K I 201 1555 1555 2.91 LINK O GLY I 121 K K I 201 1555 1555 3.04 LINK K K I 201 O HOH I 372 1555 1555 2.59 LINK K K I 201 O HOH I 375 1555 1555 2.86 LINK K K I 201 O HOH I 379 1555 1555 2.66 LINK O TRP C 120 NA NA C 201 1555 1555 3.11 LINK O GLY C 121 NA NA C 201 1555 1555 3.14 LINK NA NA C 201 O HOH C 395 1555 1555 2.50 LINK NA NA C 201 O HOH C 401 1555 1555 2.78 LINK NA NA C 201 O HOH D1317 1555 1555 2.50 LINK O ARG D 61 NA NA D1102 1555 1555 2.90 LINK OG SER D 63 NA NA D1102 1555 1555 2.80 LINK OG SER D 76 NA NA D1102 1555 1555 2.88 LINK NA NA D1102 O HOH D1287 1555 1555 2.36 CISPEP 1 THR A 6 PRO A 7 0 7.43 CISPEP 2 THR B 6 PRO B 7 0 7.47 CRYST1 76.870 83.150 98.340 90.00 90.00 90.00 P 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.013009 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012026 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010169 0.00000