HEADER PROTEIN BINDING 07-AUG-25 9PYF TITLE UPA INHIBITORY FAB AB2 COMPLEX CAVEAT 9PYF RESIDUES ILE A 111 AND ARG A 113 THAT ARE NEXT TO EACH OTHER CAVEAT 2 9PYF IN THE SAMPLE SEQUENCE ARE NOT PROPERLY LINKED: DISTANCE CAVEAT 3 9PYF BETWEEN C AND N IS 3.68 A. RESIDUES GLN I 27 AND LEU I 29 CAVEAT 4 9PYF THAT ARE NEXT TO EACH OTHER IN THE SAMPLE SEQUENCE ARE NOT CAVEAT 5 9PYF PROPERLY LINKED: DISTANCE BETWEEN C AND N IS 3.62 A. CAVEAT 6 9PYF RESIDUES ILE I 111 AND ARG I 113 THAT ARE NEXT TO EACH CAVEAT 7 9PYF OTHER IN THE SAMPLE SEQUENCE ARE NOT PROPERLY LINKED: CAVEAT 8 9PYF DISTANCE BETWEEN C AND N IS 5.25 A. COMPND MOL_ID: 1; COMPND 2 MOLECULE: AB2 FAB LIGHT CHAIN; COMPND 3 CHAIN: A, I; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: UROKINASE-TYPE PLASMINOGEN ACTIVATOR; COMPND 7 CHAIN: F; COMPND 8 SYNONYM: U-PLASMINOGEN ACTIVATOR,UPA; COMPND 9 EC: 3.4.21.73; COMPND 10 ENGINEERED: YES; COMPND 11 MUTATION: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: AB2 FAB HEAVY CHAIN; COMPND 14 CHAIN: D, H; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_COMMON: HUMAN; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 GENE: PLAU; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008 KEYWDS INHIBITORY ANTIBODY, SERINE PROTEASE, UROKINASE PLASMINOGEN KEYWDS 2 ACTIVATOR, SITE DIRECTED, PROTEIN BINDING EXPDTA X-RAY DIFFRACTION AUTHOR K.J.ANDERSON,M.F.BOHN REVDAT 1 27-AUG-25 9PYF 0 JRNL AUTH N.SEVILLANO,M.F.BOHN,M.ZIMANYI,Y.CHEN,C.PETZOLD,S.GUPTA, JRNL AUTH 2 C.Y.RALSTON,C.S.CRAIK JRNL TITL STRUCTURE OF AN AFFINITY-MATURED INHIBITORY RECOMBINANT FAB JRNL TITL 2 AGAINST UROKINASE PLASMINOGEN ACTIVATOR REVEALS BASIS OF JRNL TITL 3 POTENCY AND SPECIFICITY. JRNL REF BIOCHIM BIOPHYS ACTA V.1869 40562 2021 JRNL REF 2 PROTEINS PROTEOM JRNL REFN ISSN 1878-1454 JRNL PMID 33221341 JRNL DOI 10.1016/J.BBAPAP.2020.140562 REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.11.1_2575 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 86.75 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.6 REMARK 3 NUMBER OF REFLECTIONS : 26386 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.231 REMARK 3 R VALUE (WORKING SET) : 0.228 REMARK 3 FREE R VALUE : 0.300 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.810 REMARK 3 FREE R VALUE TEST SET COUNT : 1270 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 86.7450 - 6.0320 0.99 3003 150 0.1824 0.2502 REMARK 3 2 6.0320 - 4.7879 0.96 2864 166 0.1907 0.2745 REMARK 3 3 4.7879 - 4.1827 0.94 2796 147 0.1825 0.2385 REMARK 3 4 4.1827 - 3.8003 0.89 2656 119 0.2386 0.3082 REMARK 3 5 3.8003 - 3.5279 0.93 2765 134 0.2588 0.3412 REMARK 3 6 3.5279 - 3.3199 0.94 2784 146 0.2706 0.3540 REMARK 3 7 3.3199 - 3.1536 0.94 2805 141 0.2982 0.3576 REMARK 3 8 3.1536 - 3.0163 0.89 2653 121 0.3743 0.5045 REMARK 3 9 3.0163 - 2.9002 0.94 2790 146 0.3962 0.4702 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.560 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.730 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 69.50 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 : 0.011 7767 REMARK 3 ANGLE : 1.394 10472 REMARK 3 CHIRALITY : 0.067 1048 REMARK 3 PLANARITY : 0.008 1417 REMARK 3 DIHEDRAL : 18.573 4336 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 31 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 118 ) REMARK 3 ORIGIN FOR THE GROUP (A): 44.2853 77.6445 15.2259 REMARK 3 T TENSOR REMARK 3 T11: 0.4507 T22: 0.4809 REMARK 3 T33: 0.4610 T12: 0.0650 REMARK 3 T13: 0.0029 T23: 0.0459 REMARK 3 L TENSOR REMARK 3 L11: 1.1316 L22: 0.1315 REMARK 3 L33: 2.9257 L12: -0.4345 REMARK 3 L13: 0.8256 L23: 0.1610 REMARK 3 S TENSOR REMARK 3 S11: 0.0941 S12: 0.2185 S13: 0.1960 REMARK 3 S21: -0.1913 S22: -0.2776 S23: -0.1055 REMARK 3 S31: -0.0192 S32: 0.5612 S33: 0.0002 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 119 THROUGH 155 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.4915 84.5910 -15.6357 REMARK 3 T TENSOR REMARK 3 T11: 0.3290 T22: 0.3261 REMARK 3 T33: 0.4068 T12: 0.0427 REMARK 3 T13: 0.0829 T23: 0.0893 REMARK 3 L TENSOR REMARK 3 L11: 0.7854 L22: 0.2098 REMARK 3 L33: 2.4622 L12: -0.9462 REMARK 3 L13: 0.3309 L23: -0.2945 REMARK 3 S TENSOR REMARK 3 S11: -0.0411 S12: 0.2343 S13: -0.2373 REMARK 3 S21: 0.3633 S22: 0.0302 S23: 0.1349 REMARK 3 S31: 0.0117 S32: 0.1837 S33: 0.0003 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 156 THROUGH 218 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.1725 85.8976 -17.9495 REMARK 3 T TENSOR REMARK 3 T11: 0.4123 T22: 0.5688 REMARK 3 T33: 0.4728 T12: 0.0789 REMARK 3 T13: 0.0282 T23: 0.0423 REMARK 3 L TENSOR REMARK 3 L11: 2.5761 L22: 0.0891 REMARK 3 L33: 1.4753 L12: 0.6515 REMARK 3 L13: -0.0931 L23: -0.4913 REMARK 3 S TENSOR REMARK 3 S11: 0.1121 S12: 0.4025 S13: 0.1739 REMARK 3 S21: -0.2206 S22: -0.1504 S23: 0.1031 REMARK 3 S31: 0.3710 S32: 0.3622 S33: 0.0001 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 16 THROUGH 37D) REMARK 3 ORIGIN FOR THE GROUP (A): 22.2168 54.9064 4.5198 REMARK 3 T TENSOR REMARK 3 T11: 0.7327 T22: 0.4070 REMARK 3 T33: 0.5612 T12: 0.0679 REMARK 3 T13: 0.0644 T23: 0.0263 REMARK 3 L TENSOR REMARK 3 L11: 0.5098 L22: 0.5602 REMARK 3 L33: 0.1913 L12: -0.4388 REMARK 3 L13: 0.3715 L23: -0.1751 REMARK 3 S TENSOR REMARK 3 S11: 0.3934 S12: -0.2482 S13: -0.1220 REMARK 3 S21: 0.3024 S22: -0.2249 S23: -0.0420 REMARK 3 S31: -0.1107 S32: -0.0142 S33: 0.0129 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 38 THROUGH 140 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.8694 45.2858 6.6541 REMARK 3 T TENSOR REMARK 3 T11: 0.5831 T22: 0.3302 REMARK 3 T33: 0.3634 T12: -0.0023 REMARK 3 T13: -0.0104 T23: 0.0332 REMARK 3 L TENSOR REMARK 3 L11: 2.9355 L22: 2.2313 REMARK 3 L33: 1.0780 L12: 0.4494 REMARK 3 L13: 0.4448 L23: 0.9958 REMARK 3 S TENSOR REMARK 3 S11: 0.0906 S12: -0.1036 S13: -0.0877 REMARK 3 S21: 0.3398 S22: -0.0200 S23: -0.2951 REMARK 3 S31: 0.0010 S32: 0.1465 S33: -0.0001 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 141 THROUGH 244 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.1237 46.5175 4.7804 REMARK 3 T TENSOR REMARK 3 T11: 0.5706 T22: 0.3399 REMARK 3 T33: 0.4190 T12: 0.0210 REMARK 3 T13: 0.0775 T23: 0.0233 REMARK 3 L TENSOR REMARK 3 L11: 1.6043 L22: 2.6056 REMARK 3 L33: 3.3508 L12: 0.2103 REMARK 3 L13: -0.8409 L23: 0.4648 REMARK 3 S TENSOR REMARK 3 S11: 0.0182 S12: -0.1586 S13: -0.1299 REMARK 3 S21: 0.2988 S22: -0.2401 S23: 0.0400 REMARK 3 S31: 0.1027 S32: 0.0131 S33: -0.0002 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 61.5015 128.6289 3.4092 REMARK 3 T TENSOR REMARK 3 T11: 1.6811 T22: 1.0344 REMARK 3 T33: 1.4829 T12: -0.0738 REMARK 3 T13: -0.2720 T23: -0.0358 REMARK 3 L TENSOR REMARK 3 L11: 0.6187 L22: 0.2932 REMARK 3 L33: 0.2357 L12: -0.1602 REMARK 3 L13: -0.3913 L23: -0.0906 REMARK 3 S TENSOR REMARK 3 S11: 0.5954 S12: 0.1421 S13: -0.2352 REMARK 3 S21: 0.5198 S22: -0.4734 S23: 0.0375 REMARK 3 S31: -0.2922 S32: -0.3466 S33: 0.0041 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 19 THROUGH 37 ) REMARK 3 ORIGIN FOR THE GROUP (A): 47.9556 131.5789 -5.7280 REMARK 3 T TENSOR REMARK 3 T11: 1.5413 T22: 1.3448 REMARK 3 T33: 1.8228 T12: 0.2324 REMARK 3 T13: 0.0501 T23: 0.2633 REMARK 3 L TENSOR REMARK 3 L11: 0.0597 L22: 0.3359 REMARK 3 L33: 0.6310 L12: -0.1628 REMARK 3 L13: -0.0615 L23: 0.0079 REMARK 3 S TENSOR REMARK 3 S11: 2.3657 S12: 0.5934 S13: 1.5849 REMARK 3 S21: 0.7345 S22: -0.2445 S23: 0.4114 REMARK 3 S31: -1.5190 S32: 0.7164 S33: 0.0712 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 38 THROUGH 73 ) REMARK 3 ORIGIN FOR THE GROUP (A): 49.3830 126.9751 8.1472 REMARK 3 T TENSOR REMARK 3 T11: 1.1200 T22: 0.9851 REMARK 3 T33: 1.5876 T12: -0.1443 REMARK 3 T13: -0.2882 T23: 0.2587 REMARK 3 L TENSOR REMARK 3 L11: 0.4480 L22: 0.3290 REMARK 3 L33: 0.6240 L12: -0.2982 REMARK 3 L13: -0.2572 L23: 0.4753 REMARK 3 S TENSOR REMARK 3 S11: 0.7918 S12: -1.1770 S13: -0.4869 REMARK 3 S21: -0.1181 S22: -0.1959 S23: -1.2414 REMARK 3 S31: -0.4308 S32: 0.6439 S33: 0.0014 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 74 THROUGH 88 ) REMARK 3 ORIGIN FOR THE GROUP (A): 56.2179 131.8355 9.9625 REMARK 3 T TENSOR REMARK 3 T11: 1.9712 T22: 1.4797 REMARK 3 T33: 1.6076 T12: -0.6483 REMARK 3 T13: 0.0594 T23: 0.1678 REMARK 3 L TENSOR REMARK 3 L11: 0.4163 L22: 0.3067 REMARK 3 L33: 0.2749 L12: -0.3327 REMARK 3 L13: 0.2173 L23: 0.0059 REMARK 3 S TENSOR REMARK 3 S11: 1.8717 S12: 0.1625 S13: -0.6073 REMARK 3 S21: 0.8828 S22: -0.2265 S23: -0.0743 REMARK 3 S31: 0.9838 S32: -0.8410 S33: -0.0244 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 89 THROUGH 106 ) REMARK 3 ORIGIN FOR THE GROUP (A): 51.8300 121.4552 -1.3995 REMARK 3 T TENSOR REMARK 3 T11: 1.2644 T22: 0.9887 REMARK 3 T33: 1.6075 T12: 0.0016 REMARK 3 T13: -0.3601 T23: -0.0237 REMARK 3 L TENSOR REMARK 3 L11: -0.0119 L22: 0.0256 REMARK 3 L33: 0.0641 L12: 0.0395 REMARK 3 L13: 0.0334 L23: 0.1111 REMARK 3 S TENSOR REMARK 3 S11: 0.2978 S12: 0.5722 S13: -1.3176 REMARK 3 S21: -0.1331 S22: -0.9145 S23: -0.2928 REMARK 3 S31: 0.0336 S32: 0.2922 S33: -0.0018 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 107 THROUGH 125 ) REMARK 3 ORIGIN FOR THE GROUP (A): 70.9148 118.4580 20.2374 REMARK 3 T TENSOR REMARK 3 T11: 1.1530 T22: 0.3720 REMARK 3 T33: 1.9523 T12: -0.5556 REMARK 3 T13: -0.4139 T23: -0.0886 REMARK 3 L TENSOR REMARK 3 L11: 2.6432 L22: 0.1981 REMARK 3 L33: 0.2712 L12: -0.6965 REMARK 3 L13: -1.0037 L23: 0.2012 REMARK 3 S TENSOR REMARK 3 S11: -0.0768 S12: 1.2083 S13: 0.8275 REMARK 3 S21: -0.0675 S22: -0.4343 S23: -0.8543 REMARK 3 S31: -0.1511 S32: -0.0832 S33: 0.1796 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 126 THROUGH 155 ) REMARK 3 ORIGIN FOR THE GROUP (A): 77.0555 103.8474 23.5028 REMARK 3 T TENSOR REMARK 3 T11: 2.0335 T22: 1.4308 REMARK 3 T33: 1.8942 T12: -0.4193 REMARK 3 T13: -0.0309 T23: 0.5101 REMARK 3 L TENSOR REMARK 3 L11: -0.0047 L22: 0.0640 REMARK 3 L33: 0.8755 L12: 0.0060 REMARK 3 L13: 0.1884 L23: 0.0433 REMARK 3 S TENSOR REMARK 3 S11: 0.4520 S12: -0.2563 S13: 0.8541 REMARK 3 S21: 0.4214 S22: -0.2536 S23: -1.5684 REMARK 3 S31: 2.2797 S32: 1.2115 S33: 0.0702 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 156 THROUGH 187 ) REMARK 3 ORIGIN FOR THE GROUP (A): 75.6928 108.0654 19.1594 REMARK 3 T TENSOR REMARK 3 T11: 0.8945 T22: 1.4725 REMARK 3 T33: 1.7365 T12: -0.0130 REMARK 3 T13: -0.0711 T23: -0.2457 REMARK 3 L TENSOR REMARK 3 L11: 0.1734 L22: 0.2580 REMARK 3 L33: 0.5141 L12: -0.1178 REMARK 3 L13: -0.2443 L23: 0.4574 REMARK 3 S TENSOR REMARK 3 S11: 0.9638 S12: -1.0821 S13: -0.5750 REMARK 3 S21: -0.2306 S22: 0.1798 S23: 0.2072 REMARK 3 S31: -0.3431 S32: 1.3303 S33: 0.0017 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 188 THROUGH 206 ) REMARK 3 ORIGIN FOR THE GROUP (A): 84.8298 103.2372 25.6571 REMARK 3 T TENSOR REMARK 3 T11: 1.0728 T22: 1.4844 REMARK 3 T33: 3.2723 T12: -0.0931 REMARK 3 T13: 0.7647 T23: -0.2110 REMARK 3 L TENSOR REMARK 3 L11: 1.1839 L22: 1.1783 REMARK 3 L33: 4.5515 L12: 0.4471 REMARK 3 L13: 2.2758 L23: 0.6230 REMARK 3 S TENSOR REMARK 3 S11: 1.8281 S12: -0.1733 S13: 0.4570 REMARK 3 S21: -0.2808 S22: 1.0790 S23: -0.5848 REMARK 3 S31: 0.4213 S32: 1.4865 S33: 0.7406 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 207 THROUGH 218 ) REMARK 3 ORIGIN FOR THE GROUP (A): 82.6142 106.2679 32.6593 REMARK 3 T TENSOR REMARK 3 T11: 0.9227 T22: 1.3977 REMARK 3 T33: 1.7668 T12: -0.7450 REMARK 3 T13: 0.5655 T23: -0.0450 REMARK 3 L TENSOR REMARK 3 L11: 0.1565 L22: 0.8495 REMARK 3 L33: 1.8144 L12: 0.1444 REMARK 3 L13: -0.4322 L23: 0.2059 REMARK 3 S TENSOR REMARK 3 S11: -0.6890 S12: -0.1338 S13: -0.0906 REMARK 3 S21: 0.8638 S22: -0.1081 S23: 0.1590 REMARK 3 S31: 0.8278 S32: 0.3419 S33: -0.0332 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 2 THROUGH 121 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.3432 86.2715 22.6580 REMARK 3 T TENSOR REMARK 3 T11: 0.4200 T22: 0.5715 REMARK 3 T33: 0.4388 T12: 0.1138 REMARK 3 T13: -0.0322 T23: -0.1625 REMARK 3 L TENSOR REMARK 3 L11: 2.5283 L22: 1.9661 REMARK 3 L33: 1.2609 L12: -0.8678 REMARK 3 L13: 1.1919 L23: -1.5781 REMARK 3 S TENSOR REMARK 3 S11: 0.0543 S12: -0.1829 S13: 0.0514 REMARK 3 S21: 0.1887 S22: -0.1696 S23: 0.0596 REMARK 3 S31: -0.3020 S32: -0.3785 S33: -0.0000 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 122 THROUGH 136 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.6692 75.8608 -16.0030 REMARK 3 T TENSOR REMARK 3 T11: 0.5944 T22: 0.5651 REMARK 3 T33: 0.4879 T12: 0.0060 REMARK 3 T13: 0.0285 T23: -0.0297 REMARK 3 L TENSOR REMARK 3 L11: -0.0334 L22: 0.3111 REMARK 3 L33: 0.6867 L12: -0.0777 REMARK 3 L13: -0.0551 L23: -0.4362 REMARK 3 S TENSOR REMARK 3 S11: 0.3417 S12: 0.1145 S13: 0.3282 REMARK 3 S21: 0.0315 S22: 0.0613 S23: -0.2099 REMARK 3 S31: 0.4232 S32: 0.3318 S33: -0.0007 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 137 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.4111 79.5145 -4.3895 REMARK 3 T TENSOR REMARK 3 T11: 0.3465 T22: 0.2884 REMARK 3 T33: 0.3341 T12: 0.0673 REMARK 3 T13: 0.0514 T23: -0.0048 REMARK 3 L TENSOR REMARK 3 L11: 1.6028 L22: 2.6189 REMARK 3 L33: 1.5977 L12: -0.3645 REMARK 3 L13: 0.0517 L23: -1.0054 REMARK 3 S TENSOR REMARK 3 S11: -0.2367 S12: -0.1023 S13: 0.0818 REMARK 3 S21: 0.4387 S22: 0.2498 S23: 0.1740 REMARK 3 S31: 0.2793 S32: -0.2143 S33: 0.0003 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 2 THROUGH 34 ) REMARK 3 ORIGIN FOR THE GROUP (A): 41.6804 105.0669 6.0975 REMARK 3 T TENSOR REMARK 3 T11: 1.2822 T22: 0.9476 REMARK 3 T33: 1.5409 T12: -0.0598 REMARK 3 T13: -0.3775 T23: 0.2655 REMARK 3 L TENSOR REMARK 3 L11: 0.6876 L22: 0.4511 REMARK 3 L33: 0.8212 L12: 0.3601 REMARK 3 L13: -0.1280 L23: -0.6900 REMARK 3 S TENSOR REMARK 3 S11: 0.8097 S12: -0.1400 S13: -0.6347 REMARK 3 S21: -0.6764 S22: -0.6749 S23: -0.1269 REMARK 3 S31: -0.3492 S32: 0.2681 S33: -0.0001 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 35 THROUGH 47 ) REMARK 3 ORIGIN FOR THE GROUP (A): 53.0571 111.4004 0.2918 REMARK 3 T TENSOR REMARK 3 T11: 1.5601 T22: 1.2826 REMARK 3 T33: 2.2955 T12: -0.0563 REMARK 3 T13: -1.0065 T23: 0.4349 REMARK 3 L TENSOR REMARK 3 L11: 0.2366 L22: 0.0032 REMARK 3 L33: 0.6415 L12: 0.0008 REMARK 3 L13: -0.3987 L23: -0.0204 REMARK 3 S TENSOR REMARK 3 S11: -1.4531 S12: -0.1654 S13: 0.1908 REMARK 3 S21: -0.5517 S22: 0.0300 S23: -0.3802 REMARK 3 S31: 1.6403 S32: 0.4474 S33: -0.1369 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 48 THROUGH 58 ) REMARK 3 ORIGIN FOR THE GROUP (A): 33.8196 113.2200 -4.1136 REMARK 3 T TENSOR REMARK 3 T11: 1.5397 T22: 1.5027 REMARK 3 T33: 1.4386 T12: 0.3102 REMARK 3 T13: -0.5753 T23: -0.4488 REMARK 3 L TENSOR REMARK 3 L11: 0.1425 L22: 0.0975 REMARK 3 L33: 0.0673 L12: -0.0879 REMARK 3 L13: -0.0882 L23: 0.0166 REMARK 3 S TENSOR REMARK 3 S11: 0.2657 S12: -0.1108 S13: -1.0324 REMARK 3 S21: 0.1222 S22: -0.8885 S23: 0.3598 REMARK 3 S31: -0.8353 S32: -2.5267 S33: 0.0031 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 59 THROUGH 69 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.0044 107.4810 -9.5754 REMARK 3 T TENSOR REMARK 3 T11: 1.1476 T22: 0.8989 REMARK 3 T33: 2.0439 T12: -0.1768 REMARK 3 T13: -0.0583 T23: -0.0487 REMARK 3 L TENSOR REMARK 3 L11: 0.0218 L22: 0.0047 REMARK 3 L33: 0.0219 L12: -0.0281 REMARK 3 L13: 0.0267 L23: -0.0261 REMARK 3 S TENSOR REMARK 3 S11: -0.0760 S12: -0.3015 S13: -1.0337 REMARK 3 S21: -0.2367 S22: 1.1518 S23: -0.5411 REMARK 3 S31: 0.2825 S32: 0.0550 S33: -0.0018 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 70 THROUGH 94 ) REMARK 3 ORIGIN FOR THE GROUP (A): 43.3386 102.8290 0.0254 REMARK 3 T TENSOR REMARK 3 T11: 1.0211 T22: 0.8557 REMARK 3 T33: 1.8806 T12: 0.1954 REMARK 3 T13: -0.5162 T23: 0.1264 REMARK 3 L TENSOR REMARK 3 L11: 2.7727 L22: 0.3345 REMARK 3 L33: 1.2257 L12: -0.8891 REMARK 3 L13: -1.0591 L23: 0.6979 REMARK 3 S TENSOR REMARK 3 S11: 0.0677 S12: 0.1914 S13: -3.0838 REMARK 3 S21: 1.7605 S22: 0.1038 S23: -0.6443 REMARK 3 S31: 1.4055 S32: 0.8352 S33: -0.1582 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 95 THROUGH 112 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.4523 111.8927 6.9719 REMARK 3 T TENSOR REMARK 3 T11: 1.7200 T22: 0.7962 REMARK 3 T33: 1.7334 T12: -0.1194 REMARK 3 T13: -0.5732 T23: 0.3146 REMARK 3 L TENSOR REMARK 3 L11: 1.4523 L22: 0.3755 REMARK 3 L33: 0.3454 L12: -0.6107 REMARK 3 L13: -0.0613 L23: 0.2243 REMARK 3 S TENSOR REMARK 3 S11: -0.6383 S12: -1.1662 S13: -1.0382 REMARK 3 S21: -0.3455 S22: 1.1486 S23: -0.4103 REMARK 3 S31: 1.6570 S32: -0.0483 S33: 0.1264 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 113 THROUGH 133 ) REMARK 3 ORIGIN FOR THE GROUP (A): 65.6766 96.6294 19.8538 REMARK 3 T TENSOR REMARK 3 T11: 1.8691 T22: 0.8999 REMARK 3 T33: 2.3149 T12: -0.0096 REMARK 3 T13: -0.6820 T23: 0.1055 REMARK 3 L TENSOR REMARK 3 L11: 0.2116 L22: 0.0221 REMARK 3 L33: 1.6541 L12: 0.2588 REMARK 3 L13: 0.1668 L23: 0.0702 REMARK 3 S TENSOR REMARK 3 S11: 0.6728 S12: -0.1301 S13: 0.5517 REMARK 3 S21: 0.3338 S22: 1.8562 S23: 0.1470 REMARK 3 S31: 0.6976 S32: -0.7902 S33: 0.1746 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 134 THROUGH 150 ) REMARK 3 ORIGIN FOR THE GROUP (A): 66.7808 102.7256 25.8618 REMARK 3 T TENSOR REMARK 3 T11: 2.2297 T22: 1.3249 REMARK 3 T33: 1.2653 T12: -0.1237 REMARK 3 T13: -0.4723 T23: -0.1731 REMARK 3 L TENSOR REMARK 3 L11: 0.4460 L22: 0.1121 REMARK 3 L33: 0.1250 L12: -0.1201 REMARK 3 L13: -0.1776 L23: -0.0421 REMARK 3 S TENSOR REMARK 3 S11: -0.5970 S12: -0.5825 S13: -0.0701 REMARK 3 S21: 1.7533 S22: -0.6199 S23: 0.6735 REMARK 3 S31: -1.2924 S32: -0.2864 S33: -0.0008 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 151 THROUGH 170 ) REMARK 3 ORIGIN FOR THE GROUP (A): 59.6330 106.7402 25.0910 REMARK 3 T TENSOR REMARK 3 T11: 2.1848 T22: 1.7308 REMARK 3 T33: 1.2661 T12: -0.1922 REMARK 3 T13: -0.0733 T23: -0.1572 REMARK 3 L TENSOR REMARK 3 L11: 0.1088 L22: 0.0139 REMARK 3 L33: 0.0590 L12: -0.0538 REMARK 3 L13: 0.0708 L23: -0.0247 REMARK 3 S TENSOR REMARK 3 S11: -1.1036 S12: -2.1821 S13: 0.3771 REMARK 3 S21: 2.3025 S22: -0.2588 S23: 0.5437 REMARK 3 S31: -0.5155 S32: -0.7480 S33: -0.0053 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 171 THROUGH 180 ) REMARK 3 ORIGIN FOR THE GROUP (A): 69.2988 97.1626 11.6175 REMARK 3 T TENSOR REMARK 3 T11: 1.6151 T22: 1.0821 REMARK 3 T33: 3.9760 T12: 0.0875 REMARK 3 T13: -0.0853 T23: -0.6553 REMARK 3 L TENSOR REMARK 3 L11: 0.2980 L22: 0.3296 REMARK 3 L33: 0.0417 L12: 0.3020 REMARK 3 L13: -0.0169 L23: -0.0420 REMARK 3 S TENSOR REMARK 3 S11: 0.7211 S12: -0.2974 S13: 0.1461 REMARK 3 S21: -0.2585 S22: -0.4108 S23: -0.3882 REMARK 3 S31: 0.8264 S32: 0.2025 S33: -0.0193 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 181 THROUGH 198 ) REMARK 3 ORIGIN FOR THE GROUP (A): 64.1378 106.1266 35.1908 REMARK 3 T TENSOR REMARK 3 T11: 3.4080 T22: 1.8872 REMARK 3 T33: 1.3526 T12: -0.5912 REMARK 3 T13: 0.2414 T23: -0.5563 REMARK 3 L TENSOR REMARK 3 L11: 1.0440 L22: 0.0111 REMARK 3 L33: 0.3846 L12: -0.0216 REMARK 3 L13: 0.4293 L23: 0.0702 REMARK 3 S TENSOR REMARK 3 S11: 0.8247 S12: -3.7823 S13: 0.6149 REMARK 3 S21: 2.5447 S22: -0.6057 S23: -0.1967 REMARK 3 S31: -0.7640 S32: -0.4453 S33: 0.0008 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 199 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): 58.5913 95.8420 24.7806 REMARK 3 T TENSOR REMARK 3 T11: 1.1969 T22: 0.4303 REMARK 3 T33: 1.1876 T12: -1.4017 REMARK 3 T13: -0.0751 T23: 0.0112 REMARK 3 L TENSOR REMARK 3 L11: 4.1699 L22: 4.0159 REMARK 3 L33: 2.3344 L12: -1.9745 REMARK 3 L13: -2.3112 L23: -0.6570 REMARK 3 S TENSOR REMARK 3 S11: 0.3730 S12: 2.0476 S13: 0.4197 REMARK 3 S21: -1.9297 S22: -0.2138 S23: 0.0578 REMARK 3 S31: 0.0298 S32: -0.6897 S33: 0.1362 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 9PYF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-25. REMARK 100 THE DEPOSITION ID IS D_1000298041. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-JUN-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 : ALS REMARK 200 BEAMLINE : 8.3.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.1158 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 : XIA2 REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28202 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 86.745 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6 REMARK 200 DATA REDUNDANCY : 73.10 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.8100 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3 REMARK 200 DATA REDUNDANCY IN SHELL : 34.30 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: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.84 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: FOR CRYSTALLIZATION PURPOSES, UPA WAS REMARK 280 CO-INCUBATED WITH AB2 IN A 1:1 STOICHIOMETRIC RATIO FOR 1H AND REMARK 280 CO-PURIFIED USING SIZE-EXCLUSION CHROMATOGRAPHY. THE COMPLEX CO- REMARK 280 ELUTED WAS CONCENTRATED TO 15 MG/ML.CRYSTALLIZATION DROPS WERE REMARK 280 PRODUCED BY MIXING 0.1 UL OF UPA-AB2 SOLUTION WITH 0.1 UL OF THE REMARK 280 RESPECTIVE CRYSTALLIZATION SOLUTION. A SINGLE CRYSTAL WAS REMARK 280 PRODUCED USING A SOLUTION CONTAINING 0.2 M DIAMMONIUM HYDROGEN REMARK 280 CITRATE (SALT) AND 20 PERCENT PEG 3350 AND INCUBATING THE REMARK 280 EXPERIMENT FOR 14 DAYS AT ROOM TEMPERATURE., VAPOR DIFFUSION, REMARK 280 TEMPERATURE 298.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y,X,Z+3/4 REMARK 290 4555 Y,-X,Z+1/4 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 86.21000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 129.31500 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 43.10500 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 APPLY THE FOLLOWING TO CHAINS: A, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: F REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 86.74500 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 43.10500 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, H REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET F -21 REMARK 465 ARG F -20 REMARK 465 GLY F -19 REMARK 465 SER F -18 REMARK 465 HIS F -17 REMARK 465 HIS F -16 REMARK 465 HIS F -15 REMARK 465 HIS F -14 REMARK 465 HIS F -13 REMARK 465 HIS F -12 REMARK 465 GLY F -11 REMARK 465 SER F -10 REMARK 465 ALA F -9 REMARK 465 CYS F -8 REMARK 465 LYS F -7 REMARK 465 PRO F -6 REMARK 465 SER F -5 REMARK 465 SER F -4 REMARK 465 PRO F -3 REMARK 465 PRO F -2 REMARK 465 GLU F -1 REMARK 465 GLU F 0 REMARK 465 LEU F 1 REMARK 465 LYS F 2 REMARK 465 PHE F 3 REMARK 465 GLN F 4 REMARK 465 CYS F 5 REMARK 465 GLY F 6 REMARK 465 GLN F 7 REMARK 465 LYS F 8 REMARK 465 THR F 9 REMARK 465 LEU F 10 REMARK 465 ARG F 11 REMARK 465 PRO F 12 REMARK 465 ARG F 13 REMARK 465 PHE F 14 REMARK 465 LYS F 15 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 ARG A 24 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 65 CG OD1 OD2 REMARK 470 VAL A 97 CG1 CG2 REMARK 470 GLU A 98 CG CD OE1 OE2 REMARK 470 GLU A 110 CG CD OE1 OE2 REMARK 470 GLU A 148 CG CD OE1 OE2 REMARK 470 GLU A 166 CG CD OE1 OE2 REMARK 470 LYS A 193 CG CD CE NZ REMARK 470 GLN A 204 CG CD OE1 NE2 REMARK 470 GLU A 218 CG CD OE1 OE2 REMARK 470 SER F 195 OG REMARK 470 GLU F 244 O REMARK 470 ARG I 24 CG CD NE CZ NH1 NH2 REMARK 470 ASP I 65 CG OD1 OD2 REMARK 470 VAL I 97 CG1 CG2 REMARK 470 GLU I 98 CG CD OE1 OE2 REMARK 470 GLU I 110 CG CD OE1 OE2 REMARK 470 ARG I 113 CB CG CD NE CZ NH1 NH2 REMARK 470 THR I 114 CB OG1 CG2 REMARK 470 VAL I 115 CB CG1 CG2 REMARK 470 VAL I 116 CB CG1 CG2 REMARK 470 ALA I 117 CB REMARK 470 PRO I 118 CB CG CD REMARK 470 SER I 119 CB OG REMARK 470 VAL I 120 CB CG1 CG2 REMARK 470 PHE I 121 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 ILE I 122 CB CG1 CG2 CD1 REMARK 470 PHE I 123 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 PRO I 124 CB CG CD REMARK 470 PRO I 125 CB CG CD REMARK 470 SER I 126 CB OG REMARK 470 ASP I 127 CB CG OD1 OD2 REMARK 470 GLU I 128 CB CG CD OE1 OE2 REMARK 470 GLN I 129 CB CG CD OE1 NE2 REMARK 470 LEU I 130 CB CG CD1 CD2 REMARK 470 LYS I 131 CB CG CD CE NZ REMARK 470 SER I 132 CB OG REMARK 470 THR I 134 CB OG1 CG2 REMARK 470 ALA I 135 CB REMARK 470 SER I 136 CB OG REMARK 470 VAL I 137 CB CG1 CG2 REMARK 470 VAL I 138 CB CG1 CG2 REMARK 470 CYS I 139 CB SG REMARK 470 LEU I 140 CB CG CD1 CD2 REMARK 470 LEU I 141 CB CG CD1 CD2 REMARK 470 ASN I 142 CB CG OD1 ND2 REMARK 470 ASN I 143 CB CG OD1 ND2 REMARK 470 PHE I 144 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR I 145 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR I 145 OH REMARK 470 PRO I 146 CB CG CD REMARK 470 ARG I 147 CB CG CD NE CZ NH1 NH2 REMARK 470 GLU I 148 CB CG CD OE1 OE2 REMARK 470 ALA I 149 CB REMARK 470 LYS I 150 CB CG CD CE NZ REMARK 470 VAL I 151 CB CG1 CG2 REMARK 470 GLN I 152 CB CG CD OE1 NE2 REMARK 470 TRP I 153 CB CG CD1 CD2 NE1 CE2 CE3 REMARK 470 TRP I 153 CZ2 CZ3 CH2 REMARK 470 LYS I 154 CB CG CD CE NZ REMARK 470 VAL I 155 CB CG1 CG2 REMARK 470 ASP I 156 CB CG OD1 OD2 REMARK 470 ASN I 157 CB CG OD1 ND2 REMARK 470 ALA I 158 CB REMARK 470 LEU I 159 CB CG CD1 CD2 REMARK 470 GLN I 160 CB CG CD OE1 NE2 REMARK 470 SER I 161 CB OG REMARK 470 ASN I 163 CB CG OD1 ND2 REMARK 470 SER I 164 CB OG REMARK 470 GLN I 165 CB CG CD OE1 NE2 REMARK 470 GLU I 166 CB CG CD OE1 OE2 REMARK 470 SER I 167 CB OG REMARK 470 VAL I 168 CB CG1 CG2 REMARK 470 THR I 169 CB OG1 CG2 REMARK 470 GLU I 170 CB CG CD OE1 OE2 REMARK 470 GLN I 171 CB CG CD OE1 NE2 REMARK 470 ASP I 172 CB CG OD1 OD2 REMARK 470 SER I 173 CB OG REMARK 470 LYS I 174 CB CG CD CE NZ REMARK 470 ASP I 175 CB CG OD1 OD2 REMARK 470 SER I 176 CB OG REMARK 470 THR I 177 CB OG1 CG2 REMARK 470 TYR I 178 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR I 178 OH REMARK 470 SER I 179 CB OG REMARK 470 LEU I 180 CB CG CD1 CD2 REMARK 470 SER I 181 CB OG REMARK 470 SER I 182 CB OG REMARK 470 THR I 183 CB OG1 CG2 REMARK 470 LEU I 184 CB CG CD1 CD2 REMARK 470 THR I 185 CB OG1 CG2 REMARK 470 LEU I 186 CB CG CD1 CD2 REMARK 470 SER I 187 CB OG REMARK 470 LYS I 188 CB CG CD CE NZ REMARK 470 ALA I 189 CB REMARK 470 ASP I 190 CB CG OD1 OD2 REMARK 470 TYR I 191 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR I 191 OH REMARK 470 GLU I 192 CB CG CD OE1 OE2 REMARK 470 LYS I 193 CB CG CD CE NZ REMARK 470 HIS I 194 CB CG ND1 CD2 CE1 NE2 REMARK 470 LYS I 195 CB CG CD CE NZ REMARK 470 VAL I 196 CB CG1 CG2 REMARK 470 TYR I 197 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR I 197 OH REMARK 470 ALA I 198 CB REMARK 470 CYS I 199 CB SG REMARK 470 GLU I 200 CB CG CD OE1 OE2 REMARK 470 VAL I 201 CB CG1 CG2 REMARK 470 THR I 202 CB OG1 CG2 REMARK 470 HIS I 203 CB CG ND1 CD2 CE1 NE2 REMARK 470 GLN I 204 CB CG CD OE1 NE2 REMARK 470 LEU I 206 CB CG CD1 CD2 REMARK 470 SER I 207 CB OG REMARK 470 SER I 208 CB OG REMARK 470 PRO I 209 CB CG CD REMARK 470 VAL I 210 CB CG1 CG2 REMARK 470 THR I 211 CB OG1 CG2 REMARK 470 LYS I 212 CB CG CD CE NZ REMARK 470 SER I 213 CB OG REMARK 470 PHE I 214 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASN I 215 CB CG OD1 ND2 REMARK 470 ARG I 216 CB CG CD NE CZ NH1 NH2 REMARK 470 GLU I 218 CB CG CD OE1 OE2 REMARK 470 LEU D 3 CG CD1 CD2 REMARK 470 ARG D 15 CG CD NE CZ NH1 NH2 REMARK 470 SER D 52 OG REMARK 470 ASP D 74 CG OD1 OD2 REMARK 470 ASN D 85 CG OD1 ND2 REMARK 470 LEU D 87 CG CD1 CD2 REMARK 470 LYS D 88 CG CD CE NZ REMARK 470 THR D 133 OG1 CG2 REMARK 470 LYS D 203 CG CD CE NZ REMARK 470 LYS D 208 CG CD CE NZ REMARK 470 LEU H 3 CG CD1 CD2 REMARK 470 ARG H 15 CG CD NE CZ NH1 NH2 REMARK 470 SER H 52 OG REMARK 470 ASP H 74 CG OD1 OD2 REMARK 470 ASN H 85 CG OD1 ND2 REMARK 470 LEU H 87 CG CD1 CD2 REMARK 470 LYS H 88 CG CD CE NZ REMARK 470 SER H 115 CB OG REMARK 470 ALA H 116 CB REMARK 470 SER H 117 CB OG REMARK 470 THR H 118 CB OG1 CG2 REMARK 470 LYS H 119 CB CG CD CE NZ REMARK 470 PRO H 121 CB CG CD REMARK 470 SER H 122 CB OG REMARK 470 VAL H 123 CB CG1 CG2 REMARK 470 PHE H 124 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 PRO H 125 CB CG CD REMARK 470 LEU H 126 CB CG CD1 CD2 REMARK 470 ALA H 127 CB REMARK 470 PRO H 128 CB CG CD REMARK 470 SER H 129 CB OG REMARK 470 SER H 130 CB OG REMARK 470 LYS H 131 CB CG CD CE NZ REMARK 470 THR H 133 CB OG1 CG2 REMARK 470 SER H 134 CB OG REMARK 470 THR H 137 CB OG1 CG2 REMARK 470 ALA H 138 CB REMARK 470 ALA H 139 CB REMARK 470 LEU H 140 CB CG CD1 CD2 REMARK 470 CYS H 142 CB SG REMARK 470 LEU H 143 CB CG CD1 CD2 REMARK 470 VAL H 144 CB CG1 CG2 REMARK 470 LYS H 145 CB CG CD CE NZ REMARK 470 ASP H 146 CB CG OD1 OD2 REMARK 470 TYR H 147 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR H 147 OH REMARK 470 PHE H 148 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 PRO H 149 CB CG CD REMARK 470 GLU H 150 CB CG CD OE1 OE2 REMARK 470 PRO H 151 CB CG CD REMARK 470 VAL H 152 CB CG1 CG2 REMARK 470 THR H 153 CB OG1 CG2 REMARK 470 VAL H 154 CB CG1 CG2 REMARK 470 SER H 155 CB OG REMARK 470 TRP H 156 CB CG CD1 CD2 NE1 CE2 CE3 REMARK 470 TRP H 156 CZ2 CZ3 CH2 REMARK 470 ASN H 157 CB CG OD1 ND2 REMARK 470 SER H 158 CB OG REMARK 470 ALA H 160 CB REMARK 470 LEU H 161 CB CG CD1 CD2 REMARK 470 THR H 162 CB OG1 CG2 REMARK 470 SER H 163 CB OG REMARK 470 VAL H 165 CB CG1 CG2 REMARK 470 HIS H 166 CB CG ND1 CD2 CE1 NE2 REMARK 470 THR H 167 CB OG1 CG2 REMARK 470 PHE H 168 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 PRO H 169 CB CG CD REMARK 470 ALA H 170 CB REMARK 470 VAL H 171 CB CG1 CG2 REMARK 470 LEU H 172 CB CG CD1 CD2 REMARK 470 GLN H 173 CB CG CD OE1 NE2 REMARK 470 SER H 174 CB OG REMARK 470 SER H 175 CB OG REMARK 470 LEU H 177 CB CG CD1 CD2 REMARK 470 TYR H 178 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR H 178 OH REMARK 470 SER H 179 CB OG REMARK 470 LEU H 180 CB CG CD1 CD2 REMARK 470 SER H 181 CB OG REMARK 470 SER H 182 CB OG REMARK 470 VAL H 183 CB CG1 CG2 REMARK 470 VAL H 184 CB CG1 CG2 REMARK 470 THR H 185 CB OG1 CG2 REMARK 470 VAL H 186 CB CG1 CG2 REMARK 470 PRO H 187 CB CG CD REMARK 470 SER H 188 CB OG REMARK 470 SER H 189 CB OG REMARK 470 SER H 190 CB OG REMARK 470 LEU H 191 CB CG CD1 CD2 REMARK 470 THR H 193 CB OG1 CG2 REMARK 470 GLN H 194 CB CG CD OE1 NE2 REMARK 470 THR H 195 CB OG1 CG2 REMARK 470 TYR H 196 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR H 196 OH REMARK 470 ILE H 197 CB CG1 CG2 CD1 REMARK 470 CYS H 198 CB SG REMARK 470 ASN H 199 CB CG OD1 ND2 REMARK 470 VAL H 200 CB CG1 CG2 REMARK 470 ASN H 201 CB CG OD1 ND2 REMARK 470 HIS H 202 CB CG ND1 CD2 CE1 NE2 REMARK 470 LYS H 203 CB CG CD CE NZ REMARK 470 PRO H 204 CB CG CD REMARK 470 SER H 205 CB OG REMARK 470 ASN H 206 CB CG OD1 ND2 REMARK 470 THR H 207 CB OG1 CG2 REMARK 470 LYS H 208 CB CG CD CE NZ REMARK 470 VAL H 209 CB CG1 CG2 REMARK 470 ASP H 210 CB CG OD1 OD2 REMARK 470 LYS H 211 CB CG CD CE NZ REMARK 470 LYS H 212 CB CG CD CE NZ REMARK 470 VAL H 213 CB CG1 CG2 REMARK 470 GLU H 214 CB CG CD OE1 OE2 REMARK 470 PRO H 215 CB CG CD 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 THR A 183 O HOH A 301 1.91 REMARK 500 OD2 ASP I 39 ND2 ASN H 102 1.92 REMARK 500 O TYR D 31 NH2 ARG D 73 1.93 REMARK 500 OE1 GLU F 86 NZ LYS F 107 2.08 REMARK 500 NE2 GLN D 2 O HOH D 301 2.11 REMARK 500 NZ LYS F 143 OE1 GLN F 192 2.12 REMARK 500 O THR F 77 O HOH F 301 2.16 REMARK 500 NH1 ARG F 70 OE1 GLU F 80 2.16 REMARK 500 OE1 GLN H 38 OH TYR H 96 2.17 REMARK 500 OE1 GLN D 2 O HOH D 302 2.18 REMARK 500 NH1 ARG A 66 OD2 ASP A 87 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OE2 GLU F 244 OH TYR H 31 1545 2.03 REMARK 500 N GLY F 37B O ARG I 32 1545 2.07 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 ARG F 37A CG ARG F 37A CD 0.199 REMARK 500 GLU D 45 CG GLU D 45 CD 0.112 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 LEU A 29 N - CA - C ANGL. DEV. = 21.4 DEGREES REMARK 500 SER A 48 C - N - CA ANGL. DEV. = 15.6 DEGREES REMARK 500 ARG F 37A CB - CG - CD ANGL. DEV. = 19.8 DEGREES REMARK 500 ARG F 37A NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 CYS I 23 CA - CB - SG ANGL. DEV. = 8.2 DEGREES REMARK 500 LEU I 42 CA - CB - CG ANGL. DEV. = -15.7 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 LEU A 11 105.00 -165.33 REMARK 500 SER A 20 111.49 -164.85 REMARK 500 SER A 25 -145.46 -119.26 REMARK 500 SER A 26 34.10 -163.86 REMARK 500 GLN A 27 -142.63 -165.63 REMARK 500 LEU A 29 -11.36 107.46 REMARK 500 SER A 48 105.68 78.42 REMARK 500 LEU A 52 -62.68 -101.21 REMARK 500 ALA A 60 164.27 -48.29 REMARK 500 SER A 72 149.82 -173.92 REMARK 500 ALA A 99 -142.03 63.66 REMARK 500 PRO A 146 -166.78 -74.04 REMARK 500 ASP A 156 -107.62 61.59 REMARK 500 SER A 187 153.31 -48.19 REMARK 500 SER A 207 -72.18 -42.74 REMARK 500 PRO A 209 153.91 -47.14 REMARK 500 GLN F 27 57.61 -152.22 REMARK 500 ARG F 37A -158.02 113.51 REMARK 500 VAL F 41 -64.43 -105.34 REMARK 500 SER F 54 -158.17 -149.47 REMARK 500 GLU F 62A 40.22 -72.85 REMARK 500 ASP F 63 -11.67 -159.07 REMARK 500 ASP F 93 39.59 -93.25 REMARK 500 ALA F 96 48.23 -161.34 REMARK 500 ASP F 97 10.71 -68.90 REMARK 500 SER F 115 -167.58 -175.58 REMARK 500 PRO F 124 -166.75 -71.54 REMARK 500 GLN F 169 10.16 -60.26 REMARK 500 TYR F 171 -104.53 -98.73 REMARK 500 SER F 174 -3.31 -58.40 REMARK 500 ALA F 183 119.03 -168.50 REMARK 500 SER F 214 -61.88 -120.54 REMARK 500 ARG F 217 -74.00 -72.56 REMARK 500 ALA F 221 54.78 74.89 REMARK 500 ILE F 238 -84.19 -50.09 REMARK 500 ARG F 239 -64.93 -21.20 REMARK 500 LEU I 9 -37.51 -37.56 REMARK 500 SER I 10 130.62 -172.38 REMARK 500 PRO I 15 101.12 -57.15 REMARK 500 ASN I 31 -119.53 -75.36 REMARK 500 PRO I 45 72.40 -69.68 REMARK 500 SER I 48 105.03 64.34 REMARK 500 SER I 57 21.13 -148.87 REMARK 500 ASP I 65 -0.65 -59.74 REMARK 500 SER I 70 144.21 -171.84 REMARK 500 THR I 74 -55.15 -122.83 REMARK 500 SER I 81 -111.16 -100.84 REMARK 500 ARG I 96 38.35 -153.79 REMARK 500 VAL I 97 -82.54 -93.72 REMARK 500 ALA I 99 -141.03 59.09 REMARK 500 REMARK 500 THIS ENTRY HAS 139 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLN A 27 LEU A 29 137.43 REMARK 500 LYS D 131 THR D 133 148.97 REMARK 500 THR D 133 SER D 134 146.62 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 D 317 DISTANCE = 5.91 ANGSTROMS DBREF 9PYF A 1 218 PDB 9PYF 9PYF 1 218 DBREF 9PYF F -7 244 UNP P00749 UROK_HUMAN 156 425 DBREF 9PYF I 1 218 PDB 9PYF 9PYF 1 218 DBREF 9PYF D 2 215 PDB 9PYF 9PYF 2 215 DBREF 9PYF H 2 215 PDB 9PYF 9PYF 2 215 SEQADV 9PYF MET F -21 UNP P00749 INITIATING METHIONINE SEQADV 9PYF ARG F -20 UNP P00749 EXPRESSION TAG SEQADV 9PYF GLY F -19 UNP P00749 EXPRESSION TAG SEQADV 9PYF SER F -18 UNP P00749 EXPRESSION TAG SEQADV 9PYF HIS F -17 UNP P00749 EXPRESSION TAG SEQADV 9PYF HIS F -16 UNP P00749 EXPRESSION TAG SEQADV 9PYF HIS F -15 UNP P00749 EXPRESSION TAG SEQADV 9PYF HIS F -14 UNP P00749 EXPRESSION TAG SEQADV 9PYF HIS F -13 UNP P00749 EXPRESSION TAG SEQADV 9PYF HIS F -12 UNP P00749 EXPRESSION TAG SEQADV 9PYF GLY F -11 UNP P00749 EXPRESSION TAG SEQADV 9PYF SER F -10 UNP P00749 EXPRESSION TAG SEQADV 9PYF ALA F -9 UNP P00749 EXPRESSION TAG SEQADV 9PYF CYS F -8 UNP P00749 EXPRESSION TAG SEQADV 9PYF ALA F 122 UNP P00749 CYS 299 ENGINEERED MUTATION SEQADV 9PYF GLN F 145 UNP P00749 ASN 322 CONFLICT SEQRES 1 A 216 GLU ILE VAL LEU THR GLN SER PRO LEU SER LEU PRO VAL SEQRES 2 A 216 THR PRO GLY GLU PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 A 216 GLN LEU MET ASN ARG ASN GLY ASN ASN PHE LEU ASP TRP SEQRES 4 A 216 TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU ILE SEQRES 5 A 216 TYR LEU GLY SER ASN ARG ALA PRO GLY VAL PRO ASP ARG SEQRES 6 A 216 PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU LYS SEQRES 7 A 216 ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR TYR SEQRES 8 A 216 CYS MET ALA ARG VAL GLU ALA PRO TYR SER PHE GLY GLN SEQRES 9 A 216 GLY THR LYS LEU GLU ILE ARG THR VAL VAL ALA PRO SER SEQRES 10 A 216 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 A 216 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 A 216 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 A 216 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 A 216 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 A 216 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 A 216 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 A 216 THR LYS SER PHE ASN ARG GLY GLU SEQRES 1 F 284 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA SEQRES 2 F 284 CYS LYS PRO SER SER PRO PRO GLU GLU LEU LYS PHE GLN SEQRES 3 F 284 CYS GLY GLN LYS THR LEU ARG PRO ARG PHE LYS ILE ILE SEQRES 4 F 284 GLY GLY GLU PHE THR THR ILE GLU ASN GLN PRO TRP PHE SEQRES 5 F 284 ALA ALA ILE TYR ARG ARG HIS ARG GLY GLY SER VAL THR SEQRES 6 F 284 TYR VAL CYS GLY GLY SER LEU ILE SER PRO CYS TRP VAL SEQRES 7 F 284 ILE SER ALA THR HIS CYS PHE ILE ASP TYR PRO LYS LYS SEQRES 8 F 284 GLU ASP TYR ILE VAL TYR LEU GLY ARG SER ARG LEU ASN SEQRES 9 F 284 SER ASN THR GLN GLY GLU MET LYS PHE GLU VAL GLU ASN SEQRES 10 F 284 LEU ILE LEU HIS LYS ASP TYR SER ALA ASP THR LEU ALA SEQRES 11 F 284 HIS HIS ASN ASP ILE ALA LEU LEU LYS ILE ARG SER LYS SEQRES 12 F 284 GLU GLY ARG CYS ALA GLN PRO SER ARG THR ILE GLN THR SEQRES 13 F 284 ILE ALA LEU PRO SER MET TYR ASN ASP PRO GLN PHE GLY SEQRES 14 F 284 THR SER CYS GLU ILE THR GLY PHE GLY LYS GLU GLN SER SEQRES 15 F 284 THR ASP TYR LEU TYR PRO GLU GLN LEU LYS MET THR VAL SEQRES 16 F 284 VAL LYS LEU ILE SER HIS ARG GLU CYS GLN GLN PRO HIS SEQRES 17 F 284 TYR TYR GLY SER GLU VAL THR THR LYS MET LEU CYS ALA SEQRES 18 F 284 ALA ASP PRO GLN TRP LYS THR ASP SER CYS GLN GLY ASP SEQRES 19 F 284 SER GLY GLY PRO LEU VAL CYS SER LEU GLN GLY ARG MET SEQRES 20 F 284 THR LEU THR GLY ILE VAL SER TRP GLY ARG GLY CYS ALA SEQRES 21 F 284 LEU LYS ASP LYS PRO GLY VAL TYR THR ARG VAL SER HIS SEQRES 22 F 284 PHE LEU PRO TRP ILE ARG SER HIS THR LYS GLU SEQRES 1 I 216 GLU ILE VAL LEU THR GLN SER PRO LEU SER LEU PRO VAL SEQRES 2 I 216 THR PRO GLY GLU PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 I 216 GLN LEU MET ASN ARG ASN GLY ASN ASN PHE LEU ASP TRP SEQRES 4 I 216 TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU ILE SEQRES 5 I 216 TYR LEU GLY SER ASN ARG ALA PRO GLY VAL PRO ASP ARG SEQRES 6 I 216 PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU LYS SEQRES 7 I 216 ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR TYR SEQRES 8 I 216 CYS MET ALA ARG VAL GLU ALA PRO TYR SER PHE GLY GLN SEQRES 9 I 216 GLY THR LYS LEU GLU ILE ARG THR VAL VAL ALA PRO SER SEQRES 10 I 216 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 I 216 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 I 216 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 I 216 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 I 216 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 I 216 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 I 216 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 I 216 THR LYS SER PHE ASN ARG GLY GLU SEQRES 1 D 213 GLN LEU THR GLN SER GLY GLY GLY LEU VAL LYS PRO GLY SEQRES 2 D 213 ARG SER LEU ARG LEU SER CYS THR ALA SER GLY PHE THR SEQRES 3 D 213 PHE GLY ASP TYR ALA MET SER TRP VAL ARG GLN ALA PRO SEQRES 4 D 213 GLY LYS GLY LEU GLU TRP VAL GLY PHE VAL ARG SER GLU SEQRES 5 D 213 SER ALA GLY ALA THR THR GLU TYR ALA ALA SER VAL LYS SEQRES 6 D 213 GLY ARG PHE THR ILE SER ARG ASP ASP SER LYS SER ILE SEQRES 7 D 213 ALA TYR LEU GLN MET ASN ALA LEU LYS THR GLU ASP THR SEQRES 8 D 213 ALA VAL TYR TYR CYS ILE ARG GLY ALA ASN TRP ASN TRP SEQRES 9 D 213 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR SEQRES 10 D 213 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 11 D 213 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 12 D 213 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 13 D 213 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 14 D 213 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 15 D 213 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 16 D 213 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 17 D 213 LYS LYS VAL GLU PRO SEQRES 1 H 213 GLN LEU THR GLN SER GLY GLY GLY LEU VAL LYS PRO GLY SEQRES 2 H 213 ARG SER LEU ARG LEU SER CYS THR ALA SER GLY PHE THR SEQRES 3 H 213 PHE GLY ASP TYR ALA MET SER TRP VAL ARG GLN ALA PRO SEQRES 4 H 213 GLY LYS GLY LEU GLU TRP VAL GLY PHE VAL ARG SER GLU SEQRES 5 H 213 SER ALA GLY ALA THR THR GLU TYR ALA ALA SER VAL LYS SEQRES 6 H 213 GLY ARG PHE THR ILE SER ARG ASP ASP SER LYS SER ILE SEQRES 7 H 213 ALA TYR LEU GLN MET ASN ALA LEU LYS THR GLU ASP THR SEQRES 8 H 213 ALA VAL TYR TYR CYS ILE ARG GLY ALA ASN TRP ASN TRP SEQRES 9 H 213 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR SEQRES 10 H 213 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 11 H 213 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 12 H 213 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 13 H 213 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 14 H 213 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 15 H 213 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 16 H 213 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 17 H 213 LYS LYS VAL GLU PRO FORMUL 6 HOH *44(H2 O) HELIX 1 AA1 GLU A 84 VAL A 88 5 5 HELIX 2 AA2 SER A 126 GLY A 133 1 8 HELIX 3 AA3 LYS A 188 HIS A 194 1 7 HELIX 4 AA4 THR F 23 GLN F 27 5 5 HELIX 5 AA5 THR F 56 ASP F 60A 1 6 HELIX 6 AA6 SER F 164 GLN F 169 1 6 HELIX 7 AA7 TYR F 172 VAL F 176 5 5 HELIX 8 AA8 PHE F 234 GLU F 244 1 11 HELIX 9 AA9 GLU I 84 VAL I 88 5 5 HELIX 10 AB1 SER I 187 GLU I 192 5 6 HELIX 11 AB2 THR D 27 TYR D 31 5 5 HELIX 12 AB3 LYS D 88 THR D 92 5 5 HELIX 13 AB4 SER D 189 LEU D 191 5 3 HELIX 14 AB5 LYS D 203 ASN D 206 5 4 HELIX 15 AB6 ALA H 63 LYS H 66 5 4 SHEET 1 AA1 4 THR A 5 SER A 7 0 SHEET 2 AA1 4 ALA A 19 ARG A 24 -1 O ARG A 24 N THR A 5 SHEET 3 AA1 4 ASP A 75 ILE A 80 -1 O PHE A 76 N CYS A 23 SHEET 4 AA1 4 PHE A 67 SER A 72 -1 N SER A 70 O THR A 77 SHEET 1 AA2 6 SER A 10 PRO A 12 0 SHEET 2 AA2 6 THR A 107 GLU A 110 1 O LYS A 108 N LEU A 11 SHEET 3 AA2 6 GLY A 89 ALA A 95 -1 N GLY A 89 O LEU A 109 SHEET 4 AA2 6 LEU A 38 GLN A 43 -1 N TYR A 41 O TYR A 92 SHEET 5 AA2 6 GLN A 50 TYR A 54 -1 O LEU A 52 N TRP A 40 SHEET 6 AA2 6 ASN A 58 ARG A 59 -1 O ASN A 58 N TYR A 54 SHEET 1 AA3 4 SER A 10 PRO A 12 0 SHEET 2 AA3 4 THR A 107 GLU A 110 1 O LYS A 108 N LEU A 11 SHEET 3 AA3 4 GLY A 89 ALA A 95 -1 N GLY A 89 O LEU A 109 SHEET 4 AA3 4 SER A 102 PHE A 103 -1 O SER A 102 N ALA A 95 SHEET 1 AA4 4 SER A 119 PHE A 123 0 SHEET 2 AA4 4 THR A 134 PHE A 144 -1 O VAL A 138 N PHE A 123 SHEET 3 AA4 4 TYR A 178 SER A 187 -1 O TYR A 178 N PHE A 144 SHEET 4 AA4 4 SER A 164 VAL A 168 -1 N SER A 167 O SER A 181 SHEET 1 AA5 3 LYS A 150 VAL A 155 0 SHEET 2 AA5 3 VAL A 196 THR A 202 -1 O GLU A 200 N GLN A 152 SHEET 3 AA5 3 VAL A 210 ASN A 215 -1 O PHE A 214 N TYR A 197 SHEET 1 AA6 8 GLU F 20 PHE F 21 0 SHEET 2 AA6 8 LYS F 156 ILE F 163 -1 O MET F 157 N GLU F 20 SHEET 3 AA6 8 MET F 180 ALA F 184 -1 O CYS F 182 N ILE F 163 SHEET 4 AA6 8 GLY F 226 ARG F 230 -1 O TYR F 228 N LEU F 181 SHEET 5 AA6 8 MET F 207 TRP F 215 -1 N ILE F 212 O THR F 229 SHEET 6 AA6 8 PRO F 198 SER F 202 -1 N LEU F 199 O GLY F 211 SHEET 7 AA6 8 SER F 135 GLY F 140 -1 N GLU F 137 O VAL F 200 SHEET 8 AA6 8 LYS F 156 ILE F 163 -1 O THR F 158 N ILE F 138 SHEET 1 AA7 7 PHE F 30 ARG F 37A 0 SHEET 2 AA7 7 SER F 37D SER F 48 -1 O GLY F 44 N ALA F 31 SHEET 3 AA7 7 TRP F 51 SER F 54 -1 O TRP F 51 N SER F 48 SHEET 4 AA7 7 ALA F 104 ARG F 109 -1 O ALA F 104 N SER F 54 SHEET 5 AA7 7 MET F 81 LEU F 90 -1 N ASN F 87 O LYS F 107 SHEET 6 AA7 7 TYR F 64 LEU F 68 -1 N VAL F 66 O PHE F 83 SHEET 7 AA7 7 PHE F 30 ARG F 37A-1 N TYR F 34 O ILE F 65 SHEET 1 AA8 4 LEU I 4 SER I 7 0 SHEET 2 AA8 4 ALA I 19 SER I 25 -1 O SER I 22 N SER I 7 SHEET 3 AA8 4 PHE I 76 ILE I 80 -1 O ILE I 80 N ALA I 19 SHEET 4 AA8 4 PHE I 67 GLY I 71 -1 N SER I 70 O THR I 77 SHEET 1 AA9 2 SER I 10 LEU I 11 0 SHEET 2 AA9 2 LYS I 108 LEU I 109 1 O LYS I 108 N LEU I 11 SHEET 1 AB1 4 ASN I 58 ARG I 59 0 SHEET 2 AB1 4 GLN I 50 TYR I 54 -1 N TYR I 54 O ASN I 58 SHEET 3 AB1 4 LEU I 38 LEU I 42 -1 N TRP I 40 O ILE I 53 SHEET 4 AB1 4 TYR I 92 ALA I 95 -1 O TYR I 92 N TYR I 41 SHEET 1 AB2 3 SER I 136 CYS I 139 0 SHEET 2 AB2 3 SER I 179 THR I 185 -1 O LEU I 184 N VAL I 137 SHEET 3 AB2 3 SER I 167 THR I 169 -1 N THR I 169 O SER I 179 SHEET 1 AB3 2 TRP I 153 VAL I 155 0 SHEET 2 AB3 2 TYR I 197 CYS I 199 -1 O ALA I 198 N LYS I 154 SHEET 1 AB4 4 LEU D 3 GLN D 5 0 SHEET 2 AB4 4 LEU D 17 ALA D 23 -1 O THR D 22 N THR D 4 SHEET 3 AB4 4 ILE D 79 MET D 84 -1 O LEU D 82 N LEU D 19 SHEET 4 AB4 4 THR D 70 ASP D 74 -1 N SER D 72 O TYR D 81 SHEET 1 AB5 6 LEU D 10 VAL D 11 0 SHEET 2 AB5 6 THR D 109 VAL D 113 1 O THR D 112 N VAL D 11 SHEET 3 AB5 6 ALA D 93 CYS D 97 -1 N ALA D 93 O VAL D 111 SHEET 4 AB5 6 MET D 33 ARG D 37 -1 N VAL D 36 O TYR D 96 SHEET 5 AB5 6 GLU D 45 VAL D 50 -1 O GLU D 45 N ARG D 37 SHEET 6 AB5 6 THR D 59 TYR D 61 -1 O GLU D 60 N PHE D 49 SHEET 1 AB6 4 SER D 122 LEU D 126 0 SHEET 2 AB6 4 THR D 137 TYR D 147 -1 O LEU D 143 N PHE D 124 SHEET 3 AB6 4 TYR D 178 PRO D 187 -1 O LEU D 180 N VAL D 144 SHEET 4 AB6 4 VAL D 165 THR D 167 -1 N HIS D 166 O VAL D 183 SHEET 1 AB7 4 SER D 122 LEU D 126 0 SHEET 2 AB7 4 THR D 137 TYR D 147 -1 O LEU D 143 N PHE D 124 SHEET 3 AB7 4 TYR D 178 PRO D 187 -1 O LEU D 180 N VAL D 144 SHEET 4 AB7 4 VAL D 171 LEU D 172 -1 N VAL D 171 O SER D 179 SHEET 1 AB8 3 THR D 153 TRP D 156 0 SHEET 2 AB8 3 ILE D 197 HIS D 202 -1 O ASN D 199 N SER D 155 SHEET 3 AB8 3 THR D 207 LYS D 212 -1 O VAL D 209 N VAL D 200 SHEET 1 AB9 4 LEU H 3 GLY H 7 0 SHEET 2 AB9 4 LEU H 17 ALA H 23 -1 O SER H 20 N SER H 6 SHEET 3 AB9 4 ILE H 79 MET H 84 -1 O LEU H 82 N LEU H 19 SHEET 4 AB9 4 SER H 72 ASP H 74 -1 N SER H 72 O TYR H 81 SHEET 1 AC1 2 LEU H 10 VAL H 11 0 SHEET 2 AC1 2 THR H 112 VAL H 113 1 O THR H 112 N VAL H 11 SHEET 1 AC2 5 THR H 59 TYR H 61 0 SHEET 2 AC2 5 GLU H 45 VAL H 50 -1 N PHE H 49 O GLU H 60 SHEET 3 AC2 5 MET H 33 ARG H 37 -1 N ARG H 37 O GLU H 45 SHEET 4 AC2 5 VAL H 94 CYS H 97 -1 O TYR H 96 N VAL H 36 SHEET 5 AC2 5 THR H 109 LEU H 110 -1 O THR H 109 N TYR H 95 SHEET 1 AC3 2 ALA H 138 LEU H 143 0 SHEET 2 AC3 2 SER H 181 VAL H 186 -1 O VAL H 184 N LEU H 140 SHEET 1 AC4 2 VAL H 171 LEU H 172 0 SHEET 2 AC4 2 TYR H 178 SER H 179 -1 O SER H 179 N VAL H 171 SSBOND 1 CYS A 23 CYS A 93 1555 1555 2.03 SSBOND 2 CYS A 139 CYS A 199 1555 1555 2.03 SSBOND 3 CYS F 42 CYS F 58 1555 1555 2.04 SSBOND 4 CYS F 50 CYS F 111 1555 1555 2.04 SSBOND 5 CYS F 136 CYS F 201 1555 1555 2.04 SSBOND 6 CYS F 168 CYS F 182 1555 1555 2.07 SSBOND 7 CYS F 191 CYS F 220 1555 1555 2.07 SSBOND 8 CYS I 23 CYS I 93 1555 1555 2.05 SSBOND 9 CYS D 21 CYS D 97 1555 1555 2.04 SSBOND 10 CYS D 142 CYS D 198 1555 1555 2.02 SSBOND 11 CYS H 21 CYS H 97 1555 1555 2.04 CISPEP 1 SER A 7 PRO A 8 0 5.62 CISPEP 2 TYR A 145 PRO A 146 0 1.75 CISPEP 3 SER I 7 PRO I 8 0 -4.80 CISPEP 4 TYR I 145 PRO I 146 0 1.51 CISPEP 5 SER D 134 GLY D 135 0 0.11 CISPEP 6 PHE D 148 PRO D 149 0 -6.39 CISPEP 7 GLU D 150 PRO D 151 0 -5.56 CRYST1 86.745 86.745 172.420 90.00 90.00 90.00 P 43 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 0.011528 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011528 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005800 0.00000