HEADER TOXIN 03-JUL-24 9FYS TITLE D11 MABS BOUND TO ALPHA-BUNGAROTOXIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN; COMPND 3 CHAIN: C, M; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: HEAVY CHAIN D11; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ALPHA-BUNGAROTOXIN; COMPND 8 CHAIN: X, Z; COMPND 9 SYNONYM: ALPHA-BGTX,ALPHA-BTX,ALPHA-BUNGAROTOXIN,ISOFORM A31,ALPHA- COMPND 10 BTX A31,ALPHA-BGTX(A31),ALPHA-BUNGAROTOXIN (A31),BGTX A31,ALPHA- COMPND 11 ELAPITOXIN-BM2A,ALPHA-EPTX-BM2A,LONG NEUROTOXIN 1; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: D11 MABS LIGHT CHAIN; COMPND 15 CHAIN: I, B; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: BUNGARUS MULTICINCTUS; SOURCE 8 ORGANISM_COMMON: MANY-BANDED KRAIT; SOURCE 9 ORGANISM_TAXID: 8616; SOURCE 10 EXPRESSION_SYSTEM: BUNGARUS MULTICINCTUS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 8616; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS MABS, BUNGAROTOXIN, ANTIBODY:TOXIN COMPLEX, TOXIN EXPDTA X-RAY DIFFRACTION AUTHOR J.WADE,M.F.BOHN,A.H.LAUSTSEN,J.P.MORTH REVDAT 1 16-JUL-25 9FYS 0 JRNL AUTH J.WADE JRNL TITL STRUCTURAL MECHANISMS OF A-NEUROTOXIN-NEUTRALIZING JRNL TITL 2 ANTIBODIES ENABLE RATIONAL DESIGN OF PH-DEPENDENT ANTIGEN JRNL TITL 3 BINDING JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.32 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.32 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.17 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2 REMARK 3 NUMBER OF REFLECTIONS : 149352 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.169 REMARK 3 R VALUE (WORKING SET) : 0.167 REMARK 3 FREE R VALUE : 0.192 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060 REMARK 3 FREE R VALUE TEST SET COUNT : 15121 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 25.1700 - 4.0900 1.00 9879 530 0.1405 0.1469 REMARK 3 2 4.0900 - 3.2500 1.00 9978 485 0.1380 0.1716 REMARK 3 3 3.2500 - 2.8400 1.00 9958 498 0.1399 0.1672 REMARK 3 4 2.8400 - 2.5800 1.00 9963 474 0.1383 0.1610 REMARK 3 5 2.5800 - 2.4000 1.00 9886 567 0.1394 0.1659 REMARK 3 6 2.4000 - 2.2600 1.00 9876 570 0.1406 0.1722 REMARK 3 7 2.2600 - 2.1400 1.00 9879 506 0.1526 0.1798 REMARK 3 8 2.1400 - 2.0500 0.99 9918 527 0.1511 0.1799 REMARK 3 9 2.0500 - 1.9700 0.99 9908 511 0.1527 0.1765 REMARK 3 10 1.9700 - 1.9000 0.99 9867 475 0.1572 0.1859 REMARK 3 11 1.9000 - 1.8400 0.99 9881 499 0.1587 0.1887 REMARK 3 12 1.8400 - 1.7900 0.99 9938 456 0.1569 0.1860 REMARK 3 13 1.7900 - 1.7400 0.99 9844 484 0.1644 0.2012 REMARK 3 14 1.7400 - 1.7000 0.99 9826 495 0.1696 0.1980 REMARK 3 15 1.7000 - 1.6600 0.99 9767 589 0.1902 0.2190 REMARK 3 16 1.6600 - 1.6300 0.99 9772 555 0.2100 0.2412 REMARK 3 17 1.6300 - 1.5900 0.98 9757 548 0.2201 0.2385 REMARK 3 18 1.5900 - 1.5600 0.98 9728 509 0.2352 0.2668 REMARK 3 19 1.5600 - 1.5400 0.98 9840 496 0.2436 0.2672 REMARK 3 20 1.5400 - 1.5100 0.98 9755 534 0.2507 0.2623 REMARK 3 21 1.5100 - 1.4900 0.98 9676 577 0.2714 0.3014 REMARK 3 22 1.4900 - 1.4600 0.98 9626 533 0.3010 0.3189 REMARK 3 23 1.4600 - 1.4400 0.98 9713 472 0.3213 0.3451 REMARK 3 24 1.4400 - 1.4200 0.98 9683 546 0.3479 0.3757 REMARK 3 25 1.4200 - 1.4000 0.97 9685 536 0.3593 0.3439 REMARK 3 26 1.4000 - 1.3800 0.97 9464 581 0.3757 0.3831 REMARK 3 27 1.3800 - 1.3700 0.94 9355 509 0.3890 0.4132 REMARK 3 28 1.3700 - 1.3500 0.86 8522 513 0.4096 0.4289 REMARK 3 29 1.3500 - 1.3300 0.64 6350 311 0.4265 0.4091 REMARK 3 30 1.3300 - 1.3200 0.43 4289 235 0.4318 0.4252 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) : 0.232 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.049 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 18.55 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.22 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 : 0.018 5177 REMARK 3 ANGLE : 1.507 7045 REMARK 3 CHIRALITY : 0.112 756 REMARK 3 PLANARITY : 0.017 919 REMARK 3 DIHEDRAL : 7.579 755 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 32 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 145 THROUGH 154 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.2780 -40.1797 27.7412 REMARK 3 T TENSOR REMARK 3 T11: 0.1973 T22: 0.3230 REMARK 3 T33: 0.2586 T12: -0.0783 REMARK 3 T13: -0.0159 T23: 0.0115 REMARK 3 L TENSOR REMARK 3 L11: 3.8340 L22: 5.9182 REMARK 3 L33: 5.2224 L12: -2.8523 REMARK 3 L13: 2.9448 L23: -2.4238 REMARK 3 S TENSOR REMARK 3 S11: -0.0686 S12: -0.2556 S13: 0.3788 REMARK 3 S21: 0.1591 S22: -0.3236 S23: -0.5655 REMARK 3 S31: -0.3688 S32: 0.4445 S33: 0.4418 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 155 THROUGH 163 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.2061 -58.2394 42.1837 REMARK 3 T TENSOR REMARK 3 T11: 0.2215 T22: 0.2740 REMARK 3 T33: 0.2037 T12: 0.0032 REMARK 3 T13: -0.0328 T23: 0.0290 REMARK 3 L TENSOR REMARK 3 L11: 7.7065 L22: 3.6312 REMARK 3 L33: 2.7284 L12: 0.4431 REMARK 3 L13: -1.4838 L23: 1.0987 REMARK 3 S TENSOR REMARK 3 S11: -0.0978 S12: -0.3674 S13: -0.3110 REMARK 3 S21: 0.2180 S22: -0.0235 S23: 0.0061 REMARK 3 S31: -0.1164 S32: 0.2337 S33: 0.1273 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 164 THROUGH 224 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.0025 -48.3711 32.2619 REMARK 3 T TENSOR REMARK 3 T11: 0.1466 T22: 0.3086 REMARK 3 T33: 0.1686 T12: -0.0041 REMARK 3 T13: 0.0046 T23: 0.0291 REMARK 3 L TENSOR REMARK 3 L11: 1.6261 L22: 2.4446 REMARK 3 L33: 2.3936 L12: -0.4255 REMARK 3 L13: 0.7254 L23: -0.4903 REMARK 3 S TENSOR REMARK 3 S11: -0.0227 S12: -0.3427 S13: -0.0641 REMARK 3 S21: 0.1037 S22: 0.0552 S23: 0.0976 REMARK 3 S31: -0.0299 S32: -0.1091 S33: -0.0427 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 225 THROUGH 232 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.2328 -62.9821 36.9250 REMARK 3 T TENSOR REMARK 3 T11: 0.2338 T22: 0.2575 REMARK 3 T33: 0.2885 T12: -0.0362 REMARK 3 T13: -0.0197 T23: 0.0079 REMARK 3 L TENSOR REMARK 3 L11: 6.6638 L22: 6.1365 REMARK 3 L33: 2.2896 L12: -1.6942 REMARK 3 L13: -3.8697 L23: 1.3634 REMARK 3 S TENSOR REMARK 3 S11: -0.1704 S12: -0.0534 S13: -1.1588 REMARK 3 S21: 0.0420 S22: 0.0433 S23: 0.2299 REMARK 3 S31: 0.5550 S32: -0.5841 S33: 0.0833 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 233 THROUGH 252 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.7293 -42.8164 23.7747 REMARK 3 T TENSOR REMARK 3 T11: 0.1687 T22: 0.2402 REMARK 3 T33: 0.1610 T12: -0.0105 REMARK 3 T13: -0.0098 T23: 0.0018 REMARK 3 L TENSOR REMARK 3 L11: 1.0788 L22: 1.3000 REMARK 3 L33: 2.0969 L12: 0.4095 REMARK 3 L13: -0.6678 L23: -0.5298 REMARK 3 S TENSOR REMARK 3 S11: 0.0841 S12: -0.0755 S13: 0.0334 REMARK 3 S21: 0.1213 S22: -0.0649 S23: -0.0154 REMARK 3 S31: -0.1910 S32: 0.2074 S33: -0.0136 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 253 THROUGH 258 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.7379 -58.1928 35.4219 REMARK 3 T TENSOR REMARK 3 T11: 0.1717 T22: 0.2710 REMARK 3 T33: 0.1844 T12: 0.0067 REMARK 3 T13: -0.0006 T23: 0.0219 REMARK 3 L TENSOR REMARK 3 L11: 6.0648 L22: 2.7708 REMARK 3 L33: 2.6349 L12: -2.4409 REMARK 3 L13: 1.6118 L23: 1.2882 REMARK 3 S TENSOR REMARK 3 S11: 0.0805 S12: 0.5684 S13: -0.2434 REMARK 3 S21: -0.2781 S22: -0.2896 S23: -0.4111 REMARK 3 S31: 0.3572 S32: 0.1653 S33: 0.3486 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 259 THROUGH 263 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.4931 -63.6652 47.1288 REMARK 3 T TENSOR REMARK 3 T11: 0.3583 T22: 0.3183 REMARK 3 T33: 0.3010 T12: 0.0066 REMARK 3 T13: -0.0572 T23: 0.0376 REMARK 3 L TENSOR REMARK 3 L11: 3.5854 L22: 3.7206 REMARK 3 L33: 9.5232 L12: -2.7546 REMARK 3 L13: -1.6830 L23: -2.4536 REMARK 3 S TENSOR REMARK 3 S11: -0.4556 S12: -0.6947 S13: -0.0552 REMARK 3 S21: 0.7719 S22: -0.0550 S23: -0.4394 REMARK 3 S31: -0.7203 S32: 0.3735 S33: 0.4598 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'X' AND (RESID 1 THROUGH 45 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.2507 -35.6764 8.8863 REMARK 3 T TENSOR REMARK 3 T11: 0.1405 T22: 0.1565 REMARK 3 T33: 0.1538 T12: 0.0034 REMARK 3 T13: -0.0148 T23: -0.0361 REMARK 3 L TENSOR REMARK 3 L11: 2.2767 L22: 2.3101 REMARK 3 L33: 1.8278 L12: -1.1945 REMARK 3 L13: -0.9375 L23: -0.0369 REMARK 3 S TENSOR REMARK 3 S11: 0.0270 S12: 0.1928 S13: -0.1205 REMARK 3 S21: -0.1884 S22: -0.1067 S23: 0.2404 REMARK 3 S31: -0.0932 S32: -0.3547 S33: 0.0365 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'X' AND (RESID 46 THROUGH 60 ) REMARK 3 ORIGIN FOR THE GROUP (A): -28.3635 -29.1236 14.8510 REMARK 3 T TENSOR REMARK 3 T11: 0.2697 T22: 0.2647 REMARK 3 T33: 0.2398 T12: 0.0571 REMARK 3 T13: -0.0131 T23: -0.0415 REMARK 3 L TENSOR REMARK 3 L11: 0.8270 L22: 1.7982 REMARK 3 L33: 8.7195 L12: -0.4520 REMARK 3 L13: -0.0159 L23: -2.1415 REMARK 3 S TENSOR REMARK 3 S11: 0.0521 S12: 0.0476 S13: 0.0532 REMARK 3 S21: -0.1996 S22: -0.1234 S23: 0.2743 REMARK 3 S31: -0.4566 S32: -0.5716 S33: 0.0732 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'X' AND (RESID 61 THROUGH 72 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.3570 -30.0092 3.8860 REMARK 3 T TENSOR REMARK 3 T11: 0.3025 T22: 0.2593 REMARK 3 T33: 0.1862 T12: -0.0034 REMARK 3 T13: -0.0063 T23: -0.0104 REMARK 3 L TENSOR REMARK 3 L11: 4.3048 L22: 8.4480 REMARK 3 L33: 4.1996 L12: -5.9958 REMARK 3 L13: 4.0780 L23: -5.7990 REMARK 3 S TENSOR REMARK 3 S11: -0.0105 S12: 0.6099 S13: 0.1874 REMARK 3 S21: -0.2828 S22: -0.1914 S23: -0.2386 REMARK 3 S31: -0.5982 S32: 0.3035 S33: 0.3282 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'Z' AND (RESID 1 THROUGH 21 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.1218 -35.5972 50.5173 REMARK 3 T TENSOR REMARK 3 T11: 0.1991 T22: 0.2361 REMARK 3 T33: 0.1867 T12: 0.0205 REMARK 3 T13: 0.0062 T23: 0.0416 REMARK 3 L TENSOR REMARK 3 L11: 1.4739 L22: 2.0657 REMARK 3 L33: 2.3021 L12: 0.7450 REMARK 3 L13: 0.1685 L23: -0.0646 REMARK 3 S TENSOR REMARK 3 S11: -0.0861 S12: 0.0268 S13: -0.1664 REMARK 3 S21: 0.1327 S22: 0.0508 S23: -0.2422 REMARK 3 S31: -0.0473 S32: 0.3447 S33: 0.0478 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'Z' AND (RESID 22 THROUGH 28 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.4422 -31.1693 39.5936 REMARK 3 T TENSOR REMARK 3 T11: 0.1982 T22: 0.2132 REMARK 3 T33: 0.1532 T12: -0.0561 REMARK 3 T13: 0.0120 T23: 0.0092 REMARK 3 L TENSOR REMARK 3 L11: 5.1012 L22: 3.3606 REMARK 3 L33: 4.4049 L12: 2.9089 REMARK 3 L13: 4.5802 L23: 3.2712 REMARK 3 S TENSOR REMARK 3 S11: -0.2927 S12: 0.3737 S13: -0.0501 REMARK 3 S21: -0.1776 S22: 0.1627 S23: 0.0217 REMARK 3 S31: -0.2709 S32: 0.3185 S33: 0.1194 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'Z' AND (RESID 29 THROUGH 45 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.6367 -35.7160 33.4456 REMARK 3 T TENSOR REMARK 3 T11: 0.1684 T22: 0.1988 REMARK 3 T33: 0.1635 T12: -0.0348 REMARK 3 T13: 0.0141 T23: -0.0074 REMARK 3 L TENSOR REMARK 3 L11: 0.8062 L22: 0.5651 REMARK 3 L33: 3.8016 L12: 0.1055 REMARK 3 L13: 0.9516 L23: 0.0380 REMARK 3 S TENSOR REMARK 3 S11: -0.1329 S12: 0.1424 S13: -0.1144 REMARK 3 S21: -0.0822 S22: 0.1043 S23: -0.0150 REMARK 3 S31: -0.1257 S32: 0.1501 S33: 0.0687 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'Z' AND (RESID 46 THROUGH 55 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.0840 -30.0915 33.9850 REMARK 3 T TENSOR REMARK 3 T11: 0.3029 T22: 0.4295 REMARK 3 T33: 0.2554 T12: -0.0841 REMARK 3 T13: 0.0051 T23: 0.0088 REMARK 3 L TENSOR REMARK 3 L11: 0.2410 L22: 0.1395 REMARK 3 L33: 7.7298 L12: 0.2033 REMARK 3 L13: 1.4142 L23: 1.0953 REMARK 3 S TENSOR REMARK 3 S11: 0.0234 S12: 0.0255 S13: -0.2919 REMARK 3 S21: -0.0990 S22: 0.1607 S23: -0.1927 REMARK 3 S31: 0.0476 S32: 0.9034 S33: 0.0520 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'Z' AND (RESID 56 THROUGH 68 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.7688 -27.1972 45.0959 REMARK 3 T TENSOR REMARK 3 T11: 0.2129 T22: 0.1870 REMARK 3 T33: 0.1407 T12: -0.0323 REMARK 3 T13: -0.0064 T23: 0.0195 REMARK 3 L TENSOR REMARK 3 L11: 3.5160 L22: 2.9043 REMARK 3 L33: 1.7068 L12: 1.2831 REMARK 3 L13: 0.7050 L23: 1.0515 REMARK 3 S TENSOR REMARK 3 S11: -0.1406 S12: 0.1281 S13: 0.0157 REMARK 3 S21: -0.0799 S22: 0.1441 S23: -0.0352 REMARK 3 S31: -0.3569 S32: 0.0987 S33: -0.0219 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'Z' AND (RESID 69 THROUGH 74 ) REMARK 3 ORIGIN FOR THE GROUP (A): -28.9855 -28.7974 44.2869 REMARK 3 T TENSOR REMARK 3 T11: 0.2600 T22: 0.2693 REMARK 3 T33: 0.2852 T12: 0.0130 REMARK 3 T13: 0.0507 T23: 0.0338 REMARK 3 L TENSOR REMARK 3 L11: 5.4685 L22: 6.5194 REMARK 3 L33: 7.8004 L12: 1.0657 REMARK 3 L13: 0.9914 L23: 0.8417 REMARK 3 S TENSOR REMARK 3 S11: 0.3841 S12: 0.0163 S13: 0.2356 REMARK 3 S21: -0.0116 S22: -0.3049 S23: 0.6178 REMARK 3 S31: -0.4434 S32: -0.3478 S33: 0.1037 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -47.2444 -57.3776 42.4572 REMARK 3 T TENSOR REMARK 3 T11: 0.2050 T22: 0.1820 REMARK 3 T33: 0.1259 T12: -0.0177 REMARK 3 T13: -0.0249 T23: 0.0293 REMARK 3 L TENSOR REMARK 3 L11: 6.5860 L22: 3.5109 REMARK 3 L33: 0.5582 L12: 0.2482 REMARK 3 L13: 1.4803 L23: -0.7383 REMARK 3 S TENSOR REMARK 3 S11: -0.0280 S12: 0.0039 S13: -0.3106 REMARK 3 S21: 0.1082 S22: -0.0585 S23: -0.1216 REMARK 3 S31: 0.1925 S32: -0.0831 S33: 0.1793 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 18 THROUGH 60 ) REMARK 3 ORIGIN FOR THE GROUP (A): -39.9192 -48.5621 38.5323 REMARK 3 T TENSOR REMARK 3 T11: 0.1412 T22: 0.2159 REMARK 3 T33: 0.1454 T12: -0.0076 REMARK 3 T13: -0.0081 T23: -0.0121 REMARK 3 L TENSOR REMARK 3 L11: 1.9194 L22: 2.6503 REMARK 3 L33: 3.3166 L12: 1.1201 REMARK 3 L13: -0.7748 L23: -0.1450 REMARK 3 S TENSOR REMARK 3 S11: 0.0350 S12: -0.1753 S13: -0.0677 REMARK 3 S21: 0.1820 S22: -0.0544 S23: -0.1823 REMARK 3 S31: -0.0352 S32: 0.3186 S33: 0.0096 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 61 THROUGH 76 ) REMARK 3 ORIGIN FOR THE GROUP (A): -43.0461 -44.9396 44.0321 REMARK 3 T TENSOR REMARK 3 T11: 0.2404 T22: 0.2323 REMARK 3 T33: 0.1715 T12: -0.0624 REMARK 3 T13: -0.0189 T23: -0.0302 REMARK 3 L TENSOR REMARK 3 L11: 5.2352 L22: 5.7646 REMARK 3 L33: 3.6909 L12: -2.5297 REMARK 3 L13: -0.1396 L23: -1.1461 REMARK 3 S TENSOR REMARK 3 S11: 0.1136 S12: -0.0800 S13: 0.1749 REMARK 3 S21: 0.4917 S22: -0.1548 S23: -0.3303 REMARK 3 S31: -0.2489 S32: 0.1761 S33: 0.0419 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 77 THROUGH 133 ) REMARK 3 ORIGIN FOR THE GROUP (A): -41.3617 -48.6767 37.3763 REMARK 3 T TENSOR REMARK 3 T11: 0.1619 T22: 0.1954 REMARK 3 T33: 0.1567 T12: -0.0076 REMARK 3 T13: -0.0139 T23: 0.0038 REMARK 3 L TENSOR REMARK 3 L11: 1.9576 L22: 1.2124 REMARK 3 L33: 0.4741 L12: 1.3585 REMARK 3 L13: -0.5060 L23: -0.1422 REMARK 3 S TENSOR REMARK 3 S11: 0.0507 S12: -0.0881 S13: -0.0570 REMARK 3 S21: 0.0224 S22: -0.0512 S23: -0.0695 REMARK 3 S31: -0.0367 S32: 0.0388 S33: -0.0024 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 145 THROUGH 154 ) REMARK 3 ORIGIN FOR THE GROUP (A): -49.9063 -39.7284 22.4269 REMARK 3 T TENSOR REMARK 3 T11: 0.1575 T22: 0.2490 REMARK 3 T33: 0.1953 T12: 0.0579 REMARK 3 T13: -0.0076 T23: -0.0049 REMARK 3 L TENSOR REMARK 3 L11: 1.8015 L22: 4.3731 REMARK 3 L33: 5.5573 L12: 1.2035 REMARK 3 L13: 0.9628 L23: 3.3231 REMARK 3 S TENSOR REMARK 3 S11: -0.0697 S12: -0.1048 S13: 0.2453 REMARK 3 S21: 0.0519 S22: -0.1096 S23: 0.4350 REMARK 3 S31: -0.1189 S32: -0.5657 S33: 0.0481 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 155 THROUGH 163 ) REMARK 3 ORIGIN FOR THE GROUP (A): -49.6394 -55.8743 6.1260 REMARK 3 T TENSOR REMARK 3 T11: 0.2304 T22: 0.2976 REMARK 3 T33: 0.2672 T12: 0.0116 REMARK 3 T13: -0.0568 T23: -0.0755 REMARK 3 L TENSOR REMARK 3 L11: 4.0170 L22: 3.1911 REMARK 3 L33: 0.6892 L12: -0.3117 REMARK 3 L13: -0.6859 L23: 1.0039 REMARK 3 S TENSOR REMARK 3 S11: 0.0046 S12: 0.4473 S13: -0.4072 REMARK 3 S21: -0.2652 S22: -0.0634 S23: 0.0028 REMARK 3 S31: -0.2675 S32: -0.1684 S33: 0.0468 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 164 THROUGH 252 ) REMARK 3 ORIGIN FOR THE GROUP (A): -40.9960 -46.9941 18.5625 REMARK 3 T TENSOR REMARK 3 T11: 0.1364 T22: 0.1896 REMARK 3 T33: 0.1537 T12: 0.0106 REMARK 3 T13: -0.0023 T23: -0.0102 REMARK 3 L TENSOR REMARK 3 L11: 2.0248 L22: 1.5359 REMARK 3 L33: 2.0286 L12: 0.3536 REMARK 3 L13: 0.5273 L23: 0.7690 REMARK 3 S TENSOR REMARK 3 S11: 0.0399 S12: 0.0789 S13: -0.1116 REMARK 3 S21: -0.0770 S22: -0.0182 S23: -0.0283 REMARK 3 S31: -0.0706 S32: -0.0025 S33: -0.0247 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 253 THROUGH 264 ) REMARK 3 ORIGIN FOR THE GROUP (A): -55.4902 -59.8872 5.9991 REMARK 3 T TENSOR REMARK 3 T11: 0.1830 T22: 0.2074 REMARK 3 T33: 0.2159 T12: 0.0001 REMARK 3 T13: 0.0034 T23: -0.0495 REMARK 3 L TENSOR REMARK 3 L11: 2.6063 L22: 2.7329 REMARK 3 L33: 4.1610 L12: 2.0630 REMARK 3 L13: 2.6920 L23: 1.8120 REMARK 3 S TENSOR REMARK 3 S11: 0.1135 S12: 0.0000 S13: -0.2274 REMARK 3 S21: -0.2017 S22: -0.0209 S23: -0.1774 REMARK 3 S31: 0.2385 S32: -0.1458 S33: -0.1624 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.4657 -56.7162 6.3233 REMARK 3 T TENSOR REMARK 3 T11: 0.1530 T22: 0.1314 REMARK 3 T33: 0.1485 T12: 0.0235 REMARK 3 T13: -0.0278 T23: -0.0159 REMARK 3 L TENSOR REMARK 3 L11: 6.7389 L22: 2.0901 REMARK 3 L33: 0.6439 L12: -0.0142 REMARK 3 L13: 0.2147 L23: 0.9088 REMARK 3 S TENSOR REMARK 3 S11: -0.0677 S12: 0.0113 S13: -0.3801 REMARK 3 S21: -0.0169 S22: -0.0232 S23: 0.1496 REMARK 3 S31: 0.1280 S32: 0.0493 S33: 0.1350 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 18 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.2001 -53.8395 7.0586 REMARK 3 T TENSOR REMARK 3 T11: 0.1905 T22: 0.1924 REMARK 3 T33: 0.1928 T12: 0.0095 REMARK 3 T13: -0.0247 T23: -0.0186 REMARK 3 L TENSOR REMARK 3 L11: 2.9595 L22: 1.1986 REMARK 3 L33: 0.6303 L12: 0.2074 REMARK 3 L13: -0.8907 L23: -0.1050 REMARK 3 S TENSOR REMARK 3 S11: 0.0159 S12: 0.0028 S13: -0.3954 REMARK 3 S21: -0.0702 S22: -0.1120 S23: 0.0665 REMARK 3 S31: 0.1253 S32: -0.0467 S33: 0.0916 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 33 THROUGH 60 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.3782 -45.9827 13.0883 REMARK 3 T TENSOR REMARK 3 T11: 0.1460 T22: 0.1689 REMARK 3 T33: 0.1480 T12: -0.0053 REMARK 3 T13: -0.0051 T23: -0.0023 REMARK 3 L TENSOR REMARK 3 L11: 1.3342 L22: 1.1596 REMARK 3 L33: 1.9539 L12: -0.5438 REMARK 3 L13: -0.3343 L23: -0.1102 REMARK 3 S TENSOR REMARK 3 S11: 0.0003 S12: -0.0452 S13: 0.0022 REMARK 3 S21: 0.0126 S22: -0.0245 S23: -0.0448 REMARK 3 S31: 0.0131 S32: 0.1890 S33: 0.0107 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 61 THROUGH 67 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.5938 -38.4333 9.8512 REMARK 3 T TENSOR REMARK 3 T11: 0.2768 T22: 0.2188 REMARK 3 T33: 0.2283 T12: -0.0219 REMARK 3 T13: 0.0294 T23: 0.0156 REMARK 3 L TENSOR REMARK 3 L11: 6.0574 L22: 3.3567 REMARK 3 L33: 6.1383 L12: -0.3444 REMARK 3 L13: -2.4053 L23: 1.7296 REMARK 3 S TENSOR REMARK 3 S11: 0.3741 S12: -0.1453 S13: 0.4602 REMARK 3 S21: -0.1264 S22: -0.2315 S23: -0.1839 REMARK 3 S31: -0.6144 S32: 0.1356 S33: -0.0451 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 68 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.3936 -49.9272 3.0412 REMARK 3 T TENSOR REMARK 3 T11: 0.1889 T22: 0.1963 REMARK 3 T33: 0.1979 T12: 0.0128 REMARK 3 T13: -0.0194 T23: -0.0219 REMARK 3 L TENSOR REMARK 3 L11: 5.4029 L22: 1.9406 REMARK 3 L33: 1.1579 L12: 1.8963 REMARK 3 L13: -0.8205 L23: -0.4551 REMARK 3 S TENSOR REMARK 3 S11: -0.1073 S12: 0.2960 S13: -0.1876 REMARK 3 S21: -0.1802 S22: 0.0563 S23: 0.0885 REMARK 3 S31: 0.0054 S32: -0.1699 S33: 0.0515 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 84 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.1107 -46.7142 6.2656 REMARK 3 T TENSOR REMARK 3 T11: 0.1836 T22: 0.2427 REMARK 3 T33: 0.1989 T12: -0.0113 REMARK 3 T13: -0.0093 T23: -0.0018 REMARK 3 L TENSOR REMARK 3 L11: 2.9261 L22: 5.2278 REMARK 3 L33: 2.8934 L12: -3.8872 REMARK 3 L13: 2.8289 L23: -3.8484 REMARK 3 S TENSOR REMARK 3 S11: -0.2028 S12: -0.0904 S13: 0.3343 REMARK 3 S21: 0.1746 S22: 0.1072 S23: -0.3122 REMARK 3 S31: -0.4123 S32: 0.1943 S33: 0.2551 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 92 THROUGH 118 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.9175 -45.4180 16.2123 REMARK 3 T TENSOR REMARK 3 T11: 0.1682 T22: 0.1688 REMARK 3 T33: 0.1739 T12: 0.0019 REMARK 3 T13: 0.0044 T23: -0.0075 REMARK 3 L TENSOR REMARK 3 L11: 2.3614 L22: 0.5882 REMARK 3 L33: 0.5963 L12: -0.8480 REMARK 3 L13: -0.0137 L23: -0.0754 REMARK 3 S TENSOR REMARK 3 S11: 0.0472 S12: -0.2045 S13: -0.0678 REMARK 3 S21: -0.0115 S22: -0.0021 S23: 0.0595 REMARK 3 S31: -0.0182 S32: 0.0048 S33: -0.0389 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 119 THROUGH 133 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.2697 -54.7187 11.1212 REMARK 3 T TENSOR REMARK 3 T11: 0.1632 T22: 0.1466 REMARK 3 T33: 0.1911 T12: 0.0386 REMARK 3 T13: -0.0106 T23: 0.0117 REMARK 3 L TENSOR REMARK 3 L11: 9.5594 L22: 0.2119 REMARK 3 L33: 2.4517 L12: -0.1283 REMARK 3 L13: -2.6885 L23: 0.1426 REMARK 3 S TENSOR REMARK 3 S11: -0.1049 S12: 0.0939 S13: -0.0101 REMARK 3 S21: -0.0057 S22: 0.0864 S23: 0.0239 REMARK 3 S31: 0.0789 S32: 0.1018 S33: 0.0112 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 9FYS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1292139980. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-MAY-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID23-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS V1.0 REMARK 200 DATA SCALING SOFTWARE : DIALS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 158875 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.320 REMARK 200 RESOLUTION RANGE LOW (A) : 38.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2 REMARK 200 DATA REDUNDANCY : 13.40 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.9900 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.32 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.37 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 44.83 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES: NAOH, 12 % PEG 20000, PH REMARK 280 6.5, VAPOR DIFFUSION, SITTING DROP, 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 39.92350 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.38950 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.90200 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.38950 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.92350 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.90200 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 9100 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 28740 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, X, Z, I, M, 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY C 144 REMARK 465 GLN C 264 REMARK 465 MET X -20 REMARK 465 LYS X -19 REMARK 465 THR X -18 REMARK 465 LEU X -17 REMARK 465 LEU X -16 REMARK 465 LEU X -15 REMARK 465 THR X -14 REMARK 465 LEU X -13 REMARK 465 VAL X -12 REMARK 465 VAL X -11 REMARK 465 VAL X -10 REMARK 465 THR X -9 REMARK 465 ILE X -8 REMARK 465 VAL X -7 REMARK 465 CYS X -6 REMARK 465 LEU X -5 REMARK 465 ASP X -4 REMARK 465 LEU X -3 REMARK 465 GLY X -2 REMARK 465 TYR X -1 REMARK 465 THR X 0 REMARK 465 PRO X 73 REMARK 465 GLY X 74 REMARK 465 MET Z -20 REMARK 465 LYS Z -19 REMARK 465 THR Z -18 REMARK 465 LEU Z -17 REMARK 465 LEU Z -16 REMARK 465 LEU Z -15 REMARK 465 THR Z -14 REMARK 465 LEU Z -13 REMARK 465 VAL Z -12 REMARK 465 VAL Z -11 REMARK 465 VAL Z -10 REMARK 465 THR Z -9 REMARK 465 ILE Z -8 REMARK 465 VAL Z -7 REMARK 465 CYS Z -6 REMARK 465 LEU Z -5 REMARK 465 ASP Z -4 REMARK 465 LEU Z -3 REMARK 465 GLY Z -2 REMARK 465 TYR Z -1 REMARK 465 THR Z 0 REMARK 465 ALA I 0 REMARK 465 GLY I 134 REMARK 465 GLY I 135 REMARK 465 SER I 136 REMARK 465 GLY I 137 REMARK 465 GLY I 138 REMARK 465 GLY I 139 REMARK 465 GLY I 140 REMARK 465 SER I 141 REMARK 465 GLY I 142 REMARK 465 GLY I 143 REMARK 465 GLY M 144 REMARK 465 ALA B 0 REMARK 465 GLY B 134 REMARK 465 GLY B 135 REMARK 465 SER B 136 REMARK 465 GLY B 137 REMARK 465 GLY B 138 REMARK 465 GLY B 139 REMARK 465 GLY B 140 REMARK 465 SER B 141 REMARK 465 GLY B 142 REMARK 465 GLY B 143 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 ALA M 145 CB REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 CYS M 237 N CA C O CB SG 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 HZ3 LYS Z 38 OE2 GLU Z 56 1.56 REMARK 500 OD1 ASP I 73 HG SER I 75 1.59 REMARK 500 O HOH I 260 O HOH M 433 1.86 REMARK 500 O HOH Z 225 O HOH Z 252 1.88 REMARK 500 O HOH B 231 O HOH B 384 1.95 REMARK 500 OXT GLY Z 74 O HOH Z 201 1.99 REMARK 500 O HOH M 331 O HOH M 467 2.10 REMARK 500 O HOH Z 270 O HOH Z 282 2.14 REMARK 500 O HOH B 310 O HOH B 337 2.17 REMARK 500 O HOH I 306 O HOH I 335 2.19 REMARK 500 O HOH M 472 O HOH M 473 2.19 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 GLU I 10 CD GLU I 10 OE1 0.070 REMARK 500 TYR I 117 CE1 TYR I 117 CZ -0.125 REMARK 500 GLU M 259 CB GLU M 259 CG -0.140 REMARK 500 LYS B 12 CE LYS B 12 NZ 0.160 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 CYS X 29 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 ASP I 119 CB - CG - OD1 ANGL. DEV. = 7.6 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 ASP C 198 -41.33 74.08 REMARK 500 ASN C 199 13.68 -152.32 REMARK 500 ALA C 233 173.83 178.75 REMARK 500 SER C 239 -157.40 -143.90 REMARK 500 ASP X 30 -168.87 -111.94 REMARK 500 SER X 35 -51.50 -120.28 REMARK 500 ASN Z 66 58.82 -118.05 REMARK 500 ASP M 198 -47.46 79.11 REMARK 500 ASN M 199 14.69 -149.42 REMARK 500 SER M 239 -159.59 -145.54 REMARK 500 SER B 30 -135.87 51.36 REMARK 500 SER B 77 51.61 28.59 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 87 0.13 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH C 447 DISTANCE = 6.36 ANGSTROMS REMARK 525 HOH I 366 DISTANCE = 6.06 ANGSTROMS REMARK 525 HOH I 367 DISTANCE = 6.44 ANGSTROMS REMARK 525 HOH B 397 DISTANCE = 5.90 ANGSTROMS REMARK 525 HOH B 398 DISTANCE = 6.37 ANGSTROMS DBREF 9FYS C 144 264 PDB 9FYS 9FYS 144 264 DBREF 9FYS X -20 74 UNP P60615 3L21A_BUNMU 1 95 DBREF 9FYS Z -20 74 UNP P60615 3L21A_BUNMU 1 95 DBREF 9FYS I 0 143 PDB 9FYS 9FYS 0 143 DBREF 9FYS M 144 264 PDB 9FYS 9FYS 144 264 DBREF 9FYS B 0 143 PDB 9FYS 9FYS 0 143 SEQRES 1 C 121 GLY ALA SER ASN PHE MET LEU THR GLN PRO ARG SER VAL SEQRES 2 C 121 SER GLU SER PRO GLY LYS THR VAL THR ILE SER CYS THR SEQRES 3 C 121 ARG SER SER GLY SER ILE GLY SER ASP TYR VAL HIS TRP SEQRES 4 C 121 TYR GLN GLN ARG PRO GLY SER SER PRO THR THR VAL ILE SEQRES 5 C 121 TYR GLU ASP ASN GLN ARG PRO SER GLY VAL PRO ASP ARG SEQRES 6 C 121 PHE SER GLY SER ILE ASP SER SER SER ASN SER ALA SER SEQRES 7 C 121 LEU THR ILE SER GLY LEU LYS THR GLU ASP GLU ALA ASP SEQRES 8 C 121 TYR TYR CYS GLN SER TYR ASP ARG SER ASN HIS GLU VAL SEQRES 9 C 121 VAL PHE GLY GLY GLY THR LYS LEU THR VAL LEU GLU ASN SEQRES 10 C 121 LEU TYR PHE GLN SEQRES 1 X 95 MET LYS THR LEU LEU LEU THR LEU VAL VAL VAL THR ILE SEQRES 2 X 95 VAL CYS LEU ASP LEU GLY TYR THR ILE VAL CYS HIS THR SEQRES 3 X 95 THR ALA THR SER PRO ILE SER ALA VAL THR CYS PRO PRO SEQRES 4 X 95 GLY GLU ASN LEU CYS TYR ARG LYS MET TRP CYS ASP ALA SEQRES 5 X 95 PHE CYS SER SER ARG GLY LYS VAL VAL GLU LEU GLY CYS SEQRES 6 X 95 ALA ALA THR CYS PRO SER LYS LYS PRO TYR GLU GLU VAL SEQRES 7 X 95 THR CYS CYS SER THR ASP LYS CYS ASN PRO HIS PRO LYS SEQRES 8 X 95 GLN ARG PRO GLY SEQRES 1 Z 95 MET LYS THR LEU LEU LEU THR LEU VAL VAL VAL THR ILE SEQRES 2 Z 95 VAL CYS LEU ASP LEU GLY TYR THR ILE VAL CYS HIS THR SEQRES 3 Z 95 THR ALA THR SER PRO ILE SER ALA VAL THR CYS PRO PRO SEQRES 4 Z 95 GLY GLU ASN LEU CYS TYR ARG LYS MET TRP CYS ASP ALA SEQRES 5 Z 95 PHE CYS SER SER ARG GLY LYS VAL VAL GLU LEU GLY CYS SEQRES 6 Z 95 ALA ALA THR CYS PRO SER LYS LYS PRO TYR GLU GLU VAL SEQRES 7 Z 95 THR CYS CYS SER THR ASP LYS CYS ASN PRO HIS PRO LYS SEQRES 8 Z 95 GLN ARG PRO GLY 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 121 GLY ALA SER ASN PHE MET LEU THR GLN PRO ARG SER VAL SEQRES 2 M 121 SER GLU SER PRO GLY LYS THR VAL THR ILE SER CYS THR SEQRES 3 M 121 ARG SER SER GLY SER ILE GLY SER ASP TYR VAL HIS TRP SEQRES 4 M 121 TYR GLN GLN ARG PRO GLY SER SER PRO THR THR VAL ILE SEQRES 5 M 121 TYR GLU ASP ASN GLN ARG PRO SER GLY VAL PRO ASP ARG SEQRES 6 M 121 PHE SER GLY SER ILE ASP SER SER SER ASN SER ALA SER SEQRES 7 M 121 LEU THR ILE SER GLY LEU LYS THR GLU ASP GLU ALA ASP SEQRES 8 M 121 TYR TYR CYS GLN SER TYR ASP ARG SER ASN HIS GLU VAL SEQRES 9 M 121 VAL PHE GLY GLY GLY THR LYS LEU THR VAL LEU GLU ASN SEQRES 10 M 121 LEU TYR PHE GLN SEQRES 1 B 144 ALA GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS SEQRES 2 B 144 LYS PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER SEQRES 3 B 144 GLY GLY THR PHE SER SER TYR ALA ILE SER TRP VAL ARG SEQRES 4 B 144 GLN ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE SEQRES 5 B 144 ILE PRO ILE PHE GLY THR ALA ASN TYR ALA GLN LYS PHE SEQRES 6 B 144 GLN GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER SEQRES 7 B 144 THR ALA TYR MET GLU LEU ARG SER LEU ARG SER ASP ASP SEQRES 8 B 144 THR ALA VAL TYR TYR CYS ALA ARG ASP ASN LEU GLY TYR SEQRES 9 B 144 CYS SER GLY GLY SER CYS TYR SER ASP TYR TYR TYR TYR SEQRES 10 B 144 TYR MET ASP VAL TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 11 B 144 SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY SEQRES 12 B 144 GLY HET MES Z 101 25 HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID FORMUL 7 MES C6 H13 N O4 S FORMUL 8 HOH *877(H2 O) HELIX 1 AA1 SER C 174 ASP C 178 5 5 HELIX 2 AA2 LYS C 228 GLU C 232 5 5 HELIX 3 AA3 PHE X 32 GLY X 37 1 6 HELIX 4 AA4 HIS X 68 ARG X 72 5 5 HELIX 5 AA5 PHE Z 32 GLY Z 37 1 6 HELIX 6 AA6 HIS Z 68 ARG Z 72 5 5 HELIX 7 AA7 GLU I 74 THR I 76 5 3 HELIX 8 AA8 ARG I 87 THR I 91 5 5 HELIX 9 AA9 SER M 174 ASP M 178 5 5 HELIX 10 AB1 LYS M 228 GLU M 232 5 5 HELIX 11 AB2 GLU B 74 THR B 76 5 3 HELIX 12 AB3 ARG B 87 THR B 91 5 5 SHEET 1 AA1 4 LEU C 150 THR C 151 0 SHEET 2 AA1 4 VAL C 164 ARG C 170 -1 O THR C 169 N THR C 151 SHEET 3 AA1 4 SER C 219 ILE C 224 -1 O ILE C 224 N VAL C 164 SHEET 4 AA1 4 PHE C 209 ASP C 214 -1 N ASP C 214 O SER C 219 SHEET 1 AA2 5 SER C 155 GLU C 158 0 SHEET 2 AA2 5 THR C 253 VAL C 257 1 O THR C 256 N VAL C 156 SHEET 3 AA2 5 ALA C 233 ASP C 241 -1 N ALA C 233 O LEU C 255 SHEET 4 AA2 5 HIS C 181 GLN C 185 -1 N GLN C 185 O ASP C 234 SHEET 5 AA2 5 THR C 192 ILE C 195 -1 O ILE C 195 N TRP C 182 SHEET 1 AA3 4 SER C 155 GLU C 158 0 SHEET 2 AA3 4 THR C 253 VAL C 257 1 O THR C 256 N VAL C 156 SHEET 3 AA3 4 ALA C 233 ASP C 241 -1 N ALA C 233 O LEU C 255 SHEET 4 AA3 4 GLU C 246 PHE C 249 -1 O GLU C 246 N ASP C 241 SHEET 1 AA4 2 VAL X 2 THR X 5 0 SHEET 2 AA4 2 SER X 12 THR X 15 -1 O SER X 12 N THR X 5 SHEET 1 AA5 5 GLU X 56 CYS X 60 0 SHEET 2 AA5 5 LEU X 22 TRP X 28 -1 N CYS X 23 O CYS X 60 SHEET 3 AA5 5 VAL X 39 ALA X 45 -1 O GLU X 41 N LYS X 26 SHEET 4 AA5 5 SER B 108 TYR B 110 -1 O CYS B 109 N VAL X 40 SHEET 5 AA5 5 CYS B 104 SER B 105 -1 N SER B 105 O SER B 108 SHEET 1 AA6 2 VAL Z 2 THR Z 5 0 SHEET 2 AA6 2 SER Z 12 THR Z 15 -1 O SER Z 12 N THR Z 5 SHEET 1 AA7 5 GLU Z 56 CYS Z 60 0 SHEET 2 AA7 5 LEU Z 22 TRP Z 28 -1 N CYS Z 23 O CYS Z 60 SHEET 3 AA7 5 VAL Z 39 ALA Z 45 -1 O VAL Z 39 N TRP Z 28 SHEET 4 AA7 5 SER I 108 TYR I 110 -1 O CYS I 109 N VAL Z 40 SHEET 5 AA7 5 CYS I 104 SER I 105 -1 N SER I 105 O SER I 108 SHEET 1 AA8 4 GLN I 3 GLN I 6 0 SHEET 2 AA8 4 VAL I 18 SER I 25 -1 O LYS I 23 N VAL I 5 SHEET 3 AA8 4 THR I 78 LEU I 83 -1 O ALA I 79 N CYS I 22 SHEET 4 AA8 4 VAL I 68 ASP I 73 -1 N ASP I 73 O THR I 78 SHEET 1 AA9 6 GLU I 10 LYS I 12 0 SHEET 2 AA9 6 THR I 125 VAL I 129 1 O THR I 128 N LYS I 12 SHEET 3 AA9 6 ALA I 92 ASP I 99 -1 N ALA I 92 O VAL I 127 SHEET 4 AA9 6 ILE I 34 GLN I 39 -1 N VAL I 37 O TYR I 95 SHEET 5 AA9 6 LEU I 45 ILE I 51 -1 O MET I 48 N TRP I 36 SHEET 6 AA9 6 ALA I 58 TYR I 60 -1 O ASN I 59 N GLY I 50 SHEET 1 AB1 4 GLU I 10 LYS I 12 0 SHEET 2 AB1 4 THR I 125 VAL I 129 1 O THR I 128 N LYS I 12 SHEET 3 AB1 4 ALA I 92 ASP I 99 -1 N ALA I 92 O VAL I 127 SHEET 4 AB1 4 MET I 118 TRP I 121 -1 O VAL I 120 N ARG I 98 SHEET 1 AB2 4 LEU M 150 THR M 151 0 SHEET 2 AB2 4 VAL M 164 ARG M 170 -1 O THR M 169 N THR M 151 SHEET 3 AB2 4 SER M 219 ILE M 224 -1 O ALA M 220 N CYS M 168 SHEET 4 AB2 4 PHE M 209 ASP M 214 -1 N ASP M 214 O SER M 219 SHEET 1 AB3 5 SER M 155 GLU M 158 0 SHEET 2 AB3 5 THR M 253 VAL M 257 1 O LYS M 254 N VAL M 156 SHEET 3 AB3 5 ALA M 233 ASP M 241 -1 N ALA M 233 O LEU M 255 SHEET 4 AB3 5 HIS M 181 GLN M 185 -1 N GLN M 185 O ASP M 234 SHEET 5 AB3 5 THR M 192 ILE M 195 -1 O ILE M 195 N TRP M 182 SHEET 1 AB4 4 SER M 155 GLU M 158 0 SHEET 2 AB4 4 THR M 253 VAL M 257 1 O LYS M 254 N VAL M 156 SHEET 3 AB4 4 ALA M 233 ASP M 241 -1 N ALA M 233 O LEU M 255 SHEET 4 AB4 4 GLU M 246 PHE M 249 -1 O GLU M 246 N ASP M 241 SHEET 1 AB5 4 LEU B 4 GLN B 6 0 SHEET 2 AB5 4 VAL B 18 ALA B 24 -1 O LYS B 23 N VAL B 5 SHEET 3 AB5 4 THR B 78 LEU B 83 -1 O ALA B 79 N CYS B 22 SHEET 4 AB5 4 VAL B 68 ASP B 73 -1 N THR B 71 O TYR B 80 SHEET 1 AB6 6 GLU B 10 LYS B 12 0 SHEET 2 AB6 6 THR B 125 VAL B 129 1 O THR B 128 N LYS B 12 SHEET 3 AB6 6 ALA B 92 ASP B 99 -1 N TYR B 94 O THR B 125 SHEET 4 AB6 6 ILE B 34 GLN B 39 -1 N VAL B 37 O TYR B 95 SHEET 5 AB6 6 LEU B 45 ILE B 51 -1 O MET B 48 N TRP B 36 SHEET 6 AB6 6 ALA B 58 TYR B 60 -1 O ASN B 59 N GLY B 50 SHEET 1 AB7 4 GLU B 10 LYS B 12 0 SHEET 2 AB7 4 THR B 125 VAL B 129 1 O THR B 128 N LYS B 12 SHEET 3 AB7 4 ALA B 92 ASP B 99 -1 N TYR B 94 O THR B 125 SHEET 4 AB7 4 MET B 118 TRP B 121 -1 O VAL B 120 N ARG B 98 SSBOND 1 CYS C 168 CYS C 237 1555 1555 2.03 SSBOND 2 CYS X 3 CYS X 23 1555 1555 2.05 SSBOND 3 CYS X 16 CYS X 44 1555 1555 2.05 SSBOND 4 CYS X 29 CYS X 33 1555 1555 2.07 SSBOND 5 CYS X 48 CYS X 59 1555 1555 2.09 SSBOND 6 CYS X 60 CYS X 65 1555 1555 2.05 SSBOND 7 CYS Z 3 CYS Z 23 1555 1555 2.02 SSBOND 8 CYS Z 16 CYS Z 44 1555 1555 2.05 SSBOND 9 CYS Z 29 CYS Z 33 1555 1555 2.05 SSBOND 10 CYS Z 48 CYS Z 59 1555 1555 2.06 SSBOND 11 CYS Z 60 CYS Z 65 1555 1555 2.04 SSBOND 12 CYS I 22 CYS I 96 1555 1555 2.05 SSBOND 13 CYS I 104 CYS I 109 1555 1555 2.08 SSBOND 14 CYS M 168 CYS M 237 1555 1555 2.05 SSBOND 15 CYS B 22 CYS B 96 1555 1555 2.07 SSBOND 16 CYS B 104 CYS B 109 1555 1555 2.08 CISPEP 1 SER X 9 PRO X 10 0 -0.05 CISPEP 2 SER Z 9 PRO Z 10 0 -7.59 CRYST1 79.847 83.804 102.779 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 0.012524 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011933 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009730 0.00000