HEADER IMMUNE SYSTEM 14-JUN-24 9C9K TITLE ANTI-OSPA FAB 319-33 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 319-33 MONOCLONAL FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 319-33 MONOCLONAL FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS HUMAN ANTI-OSPA ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.J.RUDOLPH,N.MANTIS REVDAT 1 27-AUG-25 9C9K 0 JRNL AUTH M.J.RUDOLPH,N.MANTIS JRNL TITL ANTI-OSPA FAB 319-33 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.60 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) : 1.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.17 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 66895 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.173 REMARK 3 R VALUE (WORKING SET) : 0.172 REMARK 3 FREE R VALUE : 0.200 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920 REMARK 3 FREE R VALUE TEST SET COUNT : 3294 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 45.1720 - 4.6154 0.99 2857 159 0.1833 0.1970 REMARK 3 2 4.6154 - 3.6639 1.00 2722 160 0.1361 0.1545 REMARK 3 3 3.6639 - 3.2009 1.00 2694 147 0.1598 0.1951 REMARK 3 4 3.2009 - 2.9083 1.00 2719 117 0.1706 0.2068 REMARK 3 5 2.9083 - 2.6999 1.00 2679 135 0.1722 0.1959 REMARK 3 6 2.6999 - 2.5407 0.99 2656 129 0.1685 0.2162 REMARK 3 7 2.5407 - 2.4135 1.00 2647 144 0.1658 0.2055 REMARK 3 8 2.4135 - 2.3084 1.00 2642 148 0.1625 0.2013 REMARK 3 9 2.3084 - 2.2195 1.00 2655 141 0.1581 0.1827 REMARK 3 10 2.2195 - 2.1429 1.00 2613 148 0.1611 0.2074 REMARK 3 11 2.1429 - 2.0759 1.00 2640 145 0.1601 0.1868 REMARK 3 12 2.0759 - 2.0166 1.00 2634 125 0.1602 0.1968 REMARK 3 13 2.0166 - 1.9635 1.00 2646 138 0.1672 0.1675 REMARK 3 14 1.9635 - 1.9156 1.00 2618 135 0.1712 0.2310 REMARK 3 15 1.9156 - 1.8721 1.00 2628 130 0.1889 0.2340 REMARK 3 16 1.8721 - 1.8322 0.99 2624 129 0.2021 0.2344 REMARK 3 17 1.8322 - 1.7956 1.00 2654 117 0.2081 0.2302 REMARK 3 18 1.7956 - 1.7617 1.00 2595 134 0.2094 0.2653 REMARK 3 19 1.7617 - 1.7302 1.00 2627 138 0.2088 0.2204 REMARK 3 20 1.7302 - 1.7009 1.00 2621 142 0.2203 0.2782 REMARK 3 21 1.7009 - 1.6735 1.00 2613 132 0.2445 0.2741 REMARK 3 22 1.6735 - 1.6477 1.00 2607 144 0.2509 0.2637 REMARK 3 23 1.6477 - 1.6235 1.00 2589 135 0.2569 0.2412 REMARK 3 24 1.6235 - 1.6010 0.99 2621 122 0.2677 0.3031 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) : 0.160 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.000 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.009 3407 REMARK 3 ANGLE : 1.074 4636 REMARK 3 CHIRALITY : 0.065 510 REMARK 3 PLANARITY : 0.007 595 REMARK 3 DIHEDRAL : 11.010 2022 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 13 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 2 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.2866 16.4522 21.7069 REMARK 3 T TENSOR REMARK 3 T11: 0.1898 T22: 0.1681 REMARK 3 T33: 0.3596 T12: -0.0264 REMARK 3 T13: 0.0162 T23: 0.1076 REMARK 3 L TENSOR REMARK 3 L11: 4.1962 L22: 5.8695 REMARK 3 L33: 6.8723 L12: -1.9531 REMARK 3 L13: -2.7100 L23: 5.1285 REMARK 3 S TENSOR REMARK 3 S11: -0.1549 S12: -0.1579 S13: -0.7534 REMARK 3 S21: 0.1800 S22: -0.1617 S23: 0.1555 REMARK 3 S31: 0.2541 S32: -0.2275 S33: 0.3057 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 26 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.4627 28.8240 23.9347 REMARK 3 T TENSOR REMARK 3 T11: 0.1498 T22: 0.1554 REMARK 3 T33: 0.1499 T12: -0.0120 REMARK 3 T13: -0.0092 T23: 0.0394 REMARK 3 L TENSOR REMARK 3 L11: 5.8384 L22: 3.5115 REMARK 3 L33: 0.9757 L12: 0.3620 REMARK 3 L13: 0.0908 L23: -0.2116 REMARK 3 S TENSOR REMARK 3 S11: 0.1119 S12: -0.2770 S13: -0.2124 REMARK 3 S21: 0.4250 S22: -0.0094 S23: 0.2441 REMARK 3 S31: -0.0034 S32: -0.1344 S33: -0.0079 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 40 THROUGH 68 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.3530 28.0127 13.5277 REMARK 3 T TENSOR REMARK 3 T11: 0.1578 T22: 0.1388 REMARK 3 T33: 0.1544 T12: -0.0014 REMARK 3 T13: -0.0398 T23: -0.0019 REMARK 3 L TENSOR REMARK 3 L11: 6.1274 L22: 3.7558 REMARK 3 L33: 2.3247 L12: 0.5044 REMARK 3 L13: -1.4115 L23: -0.0315 REMARK 3 S TENSOR REMARK 3 S11: 0.0959 S12: 0.2222 S13: -0.3901 REMARK 3 S21: -0.2574 S22: -0.0440 S23: 0.1509 REMARK 3 S31: 0.1067 S32: -0.1670 S33: -0.0237 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 69 THROUGH 109 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.4114 24.2127 20.1180 REMARK 3 T TENSOR REMARK 3 T11: 0.1350 T22: 0.1498 REMARK 3 T33: 0.1919 T12: -0.0171 REMARK 3 T13: -0.0136 T23: 0.0481 REMARK 3 L TENSOR REMARK 3 L11: 3.4447 L22: 2.7638 REMARK 3 L33: 0.5928 L12: -0.5486 REMARK 3 L13: -0.4918 L23: 0.6298 REMARK 3 S TENSOR REMARK 3 S11: -0.0250 S12: -0.0915 S13: -0.4781 REMARK 3 S21: 0.1181 S22: -0.0180 S23: 0.2061 REMARK 3 S31: 0.1079 S32: -0.0580 S33: 0.0517 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 110 THROUGH 191 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.1192 13.4380 17.5870 REMARK 3 T TENSOR REMARK 3 T11: 0.1977 T22: 0.1811 REMARK 3 T33: 0.1819 T12: 0.0092 REMARK 3 T13: 0.0077 T23: 0.0213 REMARK 3 L TENSOR REMARK 3 L11: 4.6527 L22: 1.1030 REMARK 3 L33: 0.4711 L12: -0.4961 REMARK 3 L13: 0.0071 L23: 0.0587 REMARK 3 S TENSOR REMARK 3 S11: -0.0649 S12: -0.1032 S13: -0.2826 REMARK 3 S21: 0.0650 S22: 0.0316 S23: 0.1749 REMARK 3 S31: 0.0939 S32: 0.0775 S33: 0.0118 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 192 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.2330 7.1250 24.0246 REMARK 3 T TENSOR REMARK 3 T11: 0.3762 T22: 0.3239 REMARK 3 T33: 0.2679 T12: 0.0216 REMARK 3 T13: 0.0156 T23: 0.1025 REMARK 3 L TENSOR REMARK 3 L11: 3.6897 L22: 4.9238 REMARK 3 L33: 3.0820 L12: 3.9958 REMARK 3 L13: 2.1027 L23: 1.2057 REMARK 3 S TENSOR REMARK 3 S11: 0.3147 S12: -1.1600 S13: -0.7559 REMARK 3 S21: 0.3643 S22: -0.1984 S23: -0.1510 REMARK 3 S31: 0.5375 S32: -0.0937 S33: -0.0735 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.9022 43.7801 15.6085 REMARK 3 T TENSOR REMARK 3 T11: 0.1889 T22: 0.1644 REMARK 3 T33: 0.1552 T12: -0.0177 REMARK 3 T13: 0.0149 T23: 0.0029 REMARK 3 L TENSOR REMARK 3 L11: 7.3606 L22: 0.2577 REMARK 3 L33: 3.7823 L12: 0.2176 REMARK 3 L13: 4.1485 L23: 0.6135 REMARK 3 S TENSOR REMARK 3 S11: 0.1689 S12: 0.4335 S13: -0.1969 REMARK 3 S21: -0.0583 S22: 0.0688 S23: -0.1091 REMARK 3 S31: 0.0660 S32: 0.2531 S33: -0.1984 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 19 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.3158 44.5100 16.2643 REMARK 3 T TENSOR REMARK 3 T11: 0.1268 T22: 0.0811 REMARK 3 T33: 0.1169 T12: 0.0001 REMARK 3 T13: -0.0100 T23: -0.0379 REMARK 3 L TENSOR REMARK 3 L11: 6.9938 L22: 1.5056 REMARK 3 L33: 4.0478 L12: -1.5352 REMARK 3 L13: 3.5750 L23: -1.1622 REMARK 3 S TENSOR REMARK 3 S11: -0.0534 S12: -0.0218 S13: 0.2737 REMARK 3 S21: -0.1659 S22: -0.0245 S23: 0.1388 REMARK 3 S31: -0.0502 S32: 0.0165 S33: 0.1052 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 40 THROUGH 76 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.3181 43.5669 24.6175 REMARK 3 T TENSOR REMARK 3 T11: 0.1606 T22: 0.2014 REMARK 3 T33: 0.1316 T12: -0.0018 REMARK 3 T13: -0.0111 T23: -0.0022 REMARK 3 L TENSOR REMARK 3 L11: 3.0070 L22: 1.8748 REMARK 3 L33: 1.8552 L12: 0.6690 REMARK 3 L13: 0.4141 L23: 0.7762 REMARK 3 S TENSOR REMARK 3 S11: 0.0404 S12: -0.2565 S13: 0.0386 REMARK 3 S21: 0.1553 S22: -0.1277 S23: -0.0213 REMARK 3 S31: -0.0780 S32: -0.0016 S33: 0.0466 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 77 THROUGH 103 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.5344 39.6407 19.6432 REMARK 3 T TENSOR REMARK 3 T11: 0.1576 T22: 0.1485 REMARK 3 T33: 0.1142 T12: 0.0016 REMARK 3 T13: -0.0081 T23: 0.0041 REMARK 3 L TENSOR REMARK 3 L11: 3.4016 L22: 1.5628 REMARK 3 L33: 1.2726 L12: 1.3513 REMARK 3 L13: 1.5720 L23: 0.6513 REMARK 3 S TENSOR REMARK 3 S11: 0.0890 S12: -0.0386 S13: -0.0398 REMARK 3 S21: 0.0819 S22: -0.0122 S23: -0.0701 REMARK 3 S31: 0.0292 S32: 0.0183 S33: -0.0907 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 104 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.1859 38.1417 17.7688 REMARK 3 T TENSOR REMARK 3 T11: 0.1399 T22: 0.1805 REMARK 3 T33: 0.2476 T12: -0.0018 REMARK 3 T13: -0.0162 T23: -0.0325 REMARK 3 L TENSOR REMARK 3 L11: 4.4740 L22: 3.4727 REMARK 3 L33: 4.8863 L12: -3.9421 REMARK 3 L13: -4.6767 L23: 4.1187 REMARK 3 S TENSOR REMARK 3 S11: -0.0743 S12: -0.4286 S13: 0.8484 REMARK 3 S21: 0.0063 S22: 0.3987 S23: -0.4338 REMARK 3 S31: -0.1888 S32: 0.3142 S33: -0.2441 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 115 THROUGH 164 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.1598 19.0749 6.4798 REMARK 3 T TENSOR REMARK 3 T11: 0.1511 T22: 0.1985 REMARK 3 T33: 0.1501 T12: 0.0263 REMARK 3 T13: -0.0129 T23: -0.0118 REMARK 3 L TENSOR REMARK 3 L11: 1.4927 L22: 5.6406 REMARK 3 L33: 3.0924 L12: -0.8547 REMARK 3 L13: -0.6813 L23: 2.8560 REMARK 3 S TENSOR REMARK 3 S11: 0.0498 S12: 0.0605 S13: 0.0113 REMARK 3 S21: -0.1055 S22: -0.1465 S23: 0.1069 REMARK 3 S31: 0.0977 S32: -0.0142 S33: 0.0862 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 165 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.8611 20.8812 6.5495 REMARK 3 T TENSOR REMARK 3 T11: 0.1568 T22: 0.2252 REMARK 3 T33: 0.1240 T12: 0.0468 REMARK 3 T13: -0.0535 T23: 0.0129 REMARK 3 L TENSOR REMARK 3 L11: 1.4633 L22: 6.8424 REMARK 3 L33: 3.6796 L12: -1.1562 REMARK 3 L13: -1.2374 L23: 4.1904 REMARK 3 S TENSOR REMARK 3 S11: -0.0615 S12: -0.0549 S13: 0.0750 REMARK 3 S21: -0.1604 S22: 0.1110 S23: -0.1432 REMARK 3 S31: 0.0507 S32: 0.1803 S33: -0.0547 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 9C9K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1000285049. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-JUL-20 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 24-ID-E REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66957 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 9.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6 REMARK 200 DATA REDUNDANCY IN SHELL : 10.40 REMARK 200 R MERGE FOR SHELL (I) : 1.65600 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 (%): 53.25 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM ZINC ACETATE, 100 MM IMIDAZOLE REMARK 280 PH 8.0, 2.5 M NACL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 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+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.69450 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 60.87350 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 60.87350 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 16.84725 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 60.87350 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 60.87350 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 50.54175 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 60.87350 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 60.87350 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 16.84725 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 60.87350 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 60.87350 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 50.54175 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 33.69450 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L 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 GLU H 1 REMARK 465 SER H 130 REMARK 465 SER H 131 REMARK 465 LYS H 132 REMARK 465 SER H 133 REMARK 465 THR H 134 REMARK 465 SER H 135 REMARK 465 LYS H 217 REMARK 465 SER H 218 REMARK 465 CYS H 219 REMARK 465 ASP H 220 REMARK 465 LYS H 221 REMARK 465 THR H 222 REMARK 465 HIS H 223 REMARK 465 CYS L 215 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 OD2 ASP H 147 O HOH H 401 1.79 REMARK 500 OE2 GLU L 144 O HOH L 401 1.84 REMARK 500 O HOH L 408 O HOH L 464 1.89 REMARK 500 O GLU L 1 O HOH L 402 2.06 REMARK 500 OD1 ASP L 71 O HOH L 403 2.07 REMARK 500 O HOH L 438 O HOH L 598 2.08 REMARK 500 OD1 ASP L 71 O HOH L 404 2.09 REMARK 500 OD2 ASP L 71 O HOH L 405 2.09 REMARK 500 O HOH L 550 O HOH L 597 2.10 REMARK 500 O HOH H 544 O HOH H 556 2.10 REMARK 500 O HOH L 410 O HOH L 541 2.11 REMARK 500 O HOH H 484 O HOH L 422 2.12 REMARK 500 O HOH H 401 O HOH H 508 2.13 REMARK 500 O HOH L 510 O HOH L 531 2.16 REMARK 500 NH2 ARG H 38 CL CL H 319 2.17 REMARK 500 O HOH H 484 O HOH L 585 2.18 REMARK 500 OE1 GLU L 1 O HOH L 402 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 OE1 GLU L 196 O HOH L 401 7555 1.92 REMARK 500 O HOH L 485 O HOH L 598 3555 1.99 REMARK 500 CL CL L 328 O HOH L 579 7555 2.09 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 CYS H 22 89.86 -153.73 REMARK 500 ASP H 147 55.98 70.94 REMARK 500 PRO L 8 -179.27 -69.94 REMARK 500 ALA L 52 -31.27 65.74 REMARK 500 ASN L 139 71.04 54.52 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN H 302 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU H 46 OE2 REMARK 620 2 ASP L 186 OD1 157.5 REMARK 620 3 HOH L 559 O 121.3 80.4 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN H 301 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP H 55 OD2 REMARK 620 2 ASP H 57 OD2 111.5 REMARK 620 3 IMD H 326 N1 114.9 105.9 REMARK 620 4 HOH H 543 O 102.3 113.1 109.4 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN H 304 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP H 90 OD1 REMARK 620 2 HOH H 502 O 104.5 REMARK 620 3 HOH H 540 O 106.0 117.7 REMARK 620 4 HOH H 551 O 125.8 74.7 122.6 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN H 306 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 LYS H 146 NZ REMARK 620 2 ASP H 147 OD2 110.0 REMARK 620 3 HOH H 401 O 151.1 41.6 REMARK 620 4 HOH H 495 O 120.1 85.1 70.9 REMARK 620 5 HOH L 567 O 109.4 125.3 90.7 105.9 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN H 308 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU H 151 OE1 REMARK 620 2 HOH H 546 O 115.4 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN L 306 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS H 167 NE2 REMARK 620 2 HOH H 437 O 98.2 REMARK 620 3 ASN L 138 OD1 101.5 88.7 REMARK 620 4 ASN L 139 OD1 93.7 166.4 82.3 REMARK 620 5 HOH L 524 O 92.3 95.8 164.8 90.4 REMARK 620 6 HOH L 555 O 153.9 81.2 104.6 91.1 62.0 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN H 307 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP H 211 OD1 REMARK 620 2 ASP H 211 OD2 56.3 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN H 303 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH H 411 O REMARK 620 2 IMD L 334 N3 116.5 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN H 305 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH H 472 O REMARK 620 2 GLU L 17 OE1 90.6 REMARK 620 3 GLU L 17 OE2 91.7 1.3 REMARK 620 4 HOH L 556 O 104.9 164.4 163.3 REMARK 620 5 HOH L 581 O 120.6 64.5 64.3 105.4 REMARK 620 6 HOH L 596 O 57.0 137.6 138.9 54.9 106.6 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN L 302 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 IMD H 327 N1 REMARK 620 2 GLU L 80 OE1 139.2 REMARK 620 3 IMD L 335 N1 137.7 3.0 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN L 313 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH H 505 O REMARK 620 2 HOH L 522 O 110.0 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN L 311 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH H 548 O REMARK 620 2 ASP L 171 OD2 115.1 REMARK 620 3 HOH L 564 O 103.8 111.2 REMARK 620 4 HOH L 573 O 110.2 98.1 119.0 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN L 312 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU L 1 OE2 REMARK 620 2 GLU L 188 OE1 104.5 REMARK 620 3 GLU L 188 OE2 102.2 2.4 REMARK 620 4 HOH L 539 O 109.2 125.9 126.5 REMARK 620 5 HOH L 579 O 116.5 86.3 88.1 113.4 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN L 308 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU L 144 OE2 REMARK 620 2 GLU L 196 OE2 152.7 REMARK 620 3 HOH L 401 O 158.1 8.1 REMARK 620 4 HOH L 505 O 167.9 17.1 14.9 REMARK 620 5 HOH L 571 O 159.0 16.2 8.3 18.8 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN L 305 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU L 162 OE1 REMARK 620 2 IMD L 332 N1 114.4 REMARK 620 3 HOH L 575 O 111.6 112.1 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN L 303 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU L 166 OE1 REMARK 620 2 GLU L 166 OE2 55.2 REMARK 620 3 IMD L 336 N1 91.1 133.8 REMARK 620 4 HOH L 572 O 97.7 104.9 110.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN L 304 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP L 168 OD1 REMARK 620 2 LYS L 170 NZ 161.9 REMARK 620 3 HOH L 409 O 104.5 64.8 REMARK 620 4 HOH L 424 O 105.1 72.2 122.6 REMARK 620 5 HOH L 570 O 94.9 101.8 103.9 121.1 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN L 301 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS L 190 NE2 REMARK 620 2 IMD L 333 N1 120.7 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN L 307 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU L 214 OE2 REMARK 620 2 HOH L 566 O 85.4 REMARK 620 3 HOH L 580 O 85.8 0.5 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN L 310 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH L 558 O REMARK 620 2 HOH L 601 O 107.3 REMARK 620 N 1 DBREF 9C9K H 1 223 PDB 9C9K 9C9K 1 223 DBREF 9C9K L 1 215 PDB 9C9K 9C9K 1 215 SEQRES 1 H 223 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 223 PRO GLY GLU SER LEU LYS ILE SER CYS LYS VAL SER GLY SEQRES 3 H 223 TYR SER PHE SER THR TYR TRP ILE GLY TRP VAL ARG GLN SEQRES 4 H 223 MET PRO GLY LYS GLY LEU GLU TRP MET GLY ILE ILE TYR SEQRES 5 H 223 PRO GLY ASP SER ASP THR ARG TYR SER PRO SER PHE GLN SEQRES 6 H 223 GLY GLN VAL THR ILE SER ALA ASP LYS SER ILE SER THR SEQRES 7 H 223 ALA TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR SEQRES 8 H 223 ALA MET TYR TYR CYS ALA ARG SER ARG TRP TYR PHE ASP SEQRES 9 H 223 LEU TRP GLY ARG GLY THR LEU VAL THR VAL SER SER ALA SEQRES 10 H 223 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 11 H 223 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 12 H 223 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 13 H 223 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 14 H 223 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 15 H 223 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 16 H 223 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 17 H 223 LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS ASP LYS SEQRES 18 H 223 THR HIS SEQRES 1 L 215 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 L 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 215 GLN SER VAL SER SER SER TYR LEU ALA TRP TYR GLN GLN SEQRES 4 L 215 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 L 215 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 L 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 L 215 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8 L 215 TYR ASP SER SER PRO LEU THR PHE GLY GLY GLY THR LYS SEQRES 9 L 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS HET ZN H 301 1 HET ZN H 302 1 HET ZN H 303 1 HET ZN H 304 1 HET ZN H 305 1 HET ZN H 306 1 HET ZN H 307 1 HET ZN H 308 1 HET CL H 309 1 HET CL H 310 1 HET CL H 311 1 HET CL H 312 1 HET CL H 313 1 HET CL H 314 1 HET CL H 315 1 HET CL H 316 1 HET CL H 317 1 HET CL H 318 1 HET CL H 319 1 HET CL H 320 1 HET CL H 321 1 HET CL H 322 1 HET CL H 323 1 HET CL H 324 1 HET CL H 325 1 HET IMD H 326 5 HET IMD H 327 5 HET ZN L 301 1 HET ZN L 302 1 HET ZN L 303 1 HET ZN L 304 1 HET ZN L 305 1 HET ZN L 306 1 HET ZN L 307 1 HET ZN L 308 1 HET ZN L 309 1 HET ZN L 310 1 HET ZN L 311 1 HET ZN L 312 1 HET ZN L 313 1 HET CL L 314 1 HET CL L 315 1 HET CL L 316 1 HET CL L 317 1 HET CL L 318 1 HET CL L 319 1 HET CL L 320 1 HET CL L 321 1 HET CL L 322 1 HET CL L 323 1 HET CL L 324 1 HET CL L 325 1 HET CL L 326 1 HET CL L 327 1 HET CL L 328 1 HET CL L 329 1 HET CL L 330 1 HET CL L 331 1 HET IMD L 332 5 HET IMD L 333 5 HET IMD L 334 5 HET IMD L 335 5 HET IMD L 336 5 HET EDO L 337 4 HETNAM ZN ZINC ION HETNAM CL CHLORIDE ION HETNAM IMD IMIDAZOLE HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 3 ZN 21(ZN 2+) FORMUL 11 CL 35(CL 1-) FORMUL 28 IMD 7(C3 H5 N2 1+) FORMUL 66 EDO C2 H6 O2 FORMUL 67 HOH *382(H2 O) HELIX 1 AA1 SER H 28 TYR H 32 5 5 HELIX 2 AA2 LYS H 74 ILE H 76 5 3 HELIX 3 AA3 LYS H 87 THR H 91 5 5 HELIX 4 AA4 SER H 159 ALA H 161 5 3 HELIX 5 AA5 SER H 190 LEU H 192 5 3 HELIX 6 AA6 LYS H 204 ASN H 207 5 4 HELIX 7 AA7 SER L 30 SER L 32 5 3 HELIX 8 AA8 GLU L 80 PHE L 84 5 5 HELIX 9 AA9 SER L 122 SER L 128 1 7 HELIX 10 AB1 LYS L 184 GLU L 188 1 5 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AA1 4 THR H 78 TRP H 83 -1 O ALA H 79 N CYS H 22 SHEET 4 AA1 4 VAL H 68 ASP H 73 -1 N ASP H 73 O THR H 78 SHEET 1 AA2 6 GLU H 10 LYS H 12 0 SHEET 2 AA2 6 THR H 110 VAL H 114 1 O LEU H 111 N GLU H 10 SHEET 3 AA2 6 ALA H 92 SER H 99 -1 N ALA H 92 O VAL H 112 SHEET 4 AA2 6 TRP H 33 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA2 6 GLU H 46 ILE H 51 -1 O ILE H 51 N ILE H 34 SHEET 6 AA2 6 THR H 58 TYR H 60 -1 O ARG H 59 N ILE H 50 SHEET 1 AA3 4 GLU H 10 LYS H 12 0 SHEET 2 AA3 4 THR H 110 VAL H 114 1 O LEU H 111 N GLU H 10 SHEET 3 AA3 4 ALA H 92 SER H 99 -1 N ALA H 92 O VAL H 112 SHEET 4 AA3 4 PHE H 103 TRP H 106 -1 O LEU H 105 N ARG H 98 SHEET 1 AA4 4 SER H 123 LEU H 127 0 SHEET 2 AA4 4 THR H 138 TYR H 148 -1 O LEU H 144 N PHE H 125 SHEET 3 AA4 4 TYR H 179 PRO H 188 -1 O LEU H 181 N VAL H 145 SHEET 4 AA4 4 VAL H 166 THR H 168 -1 N HIS H 167 O VAL H 184 SHEET 1 AA5 4 SER H 123 LEU H 127 0 SHEET 2 AA5 4 THR H 138 TYR H 148 -1 O LEU H 144 N PHE H 125 SHEET 3 AA5 4 TYR H 179 PRO H 188 -1 O LEU H 181 N VAL H 145 SHEET 4 AA5 4 VAL H 172 LEU H 173 -1 N VAL H 172 O SER H 180 SHEET 1 AA6 3 THR H 154 TRP H 157 0 SHEET 2 AA6 3 ILE H 198 HIS H 203 -1 O ASN H 200 N SER H 156 SHEET 3 AA6 3 THR H 208 ARG H 213 -1 O VAL H 210 N VAL H 201 SHEET 1 AA7 3 LEU L 4 SER L 7 0 SHEET 2 AA7 3 ALA L 19 VAL L 29 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 3 PHE L 63 ILE L 76 -1 O LEU L 74 N LEU L 21 SHEET 1 AA8 6 THR L 10 LEU L 13 0 SHEET 2 AA8 6 THR L 103 ILE L 107 1 O GLU L 106 N LEU L 11 SHEET 3 AA8 6 VAL L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA8 6 LEU L 34 GLN L 39 -1 N ALA L 35 O GLN L 90 SHEET 5 AA8 6 ARG L 46 TYR L 50 -1 O LEU L 48 N TRP L 36 SHEET 6 AA8 6 SER L 54 ARG L 55 -1 O SER L 54 N TYR L 50 SHEET 1 AA9 4 SER L 115 PHE L 119 0 SHEET 2 AA9 4 THR L 130 PHE L 140 -1 O ASN L 138 N SER L 115 SHEET 3 AA9 4 TYR L 174 SER L 183 -1 O LEU L 182 N ALA L 131 SHEET 4 AA9 4 SER L 160 VAL L 164 -1 N SER L 163 O SER L 177 SHEET 1 AB1 4 ALA L 154 GLN L 156 0 SHEET 2 AB1 4 LYS L 146 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 AB1 4 VAL L 192 THR L 198 -1 O GLU L 196 N GLN L 148 SHEET 4 AB1 4 VAL L 206 ASN L 211 -1 O VAL L 206 N VAL L 197 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.07 SSBOND 2 CYS H 143 CYS H 199 1555 1555 2.04 SSBOND 3 CYS L 23 CYS L 89 1555 1555 2.05 SSBOND 4 CYS L 135 CYS L 195 1555 1555 2.01 LINK OE2 GLU H 46 ZN ZN H 302 1555 1555 1.95 LINK OD2 ASP H 55 ZN ZN H 301 1555 1555 1.97 LINK OD2 ASP H 57 ZN ZN H 301 1555 1555 2.02 LINK OD1 ASP H 90 ZN ZN H 304 1555 1555 1.99 LINK NZ LYS H 146 ZN ZN H 306 1555 1555 2.46 LINK OD2 ASP H 147 ZN ZN H 306 1555 1555 2.05 LINK OE1 GLU H 151 ZN ZN H 308 1555 1555 1.92 LINK NE2 HIS H 167 ZN ZN L 306 1555 1555 2.11 LINK OD1 ASP H 211 ZN ZN H 307 1555 1555 2.54 LINK OD2 ASP H 211 ZN ZN H 307 1555 1555 2.03 LINK ZN ZN H 301 N1 IMD H 326 1555 1555 1.99 LINK ZN ZN H 301 O HOH H 543 1555 1555 2.27 LINK ZN ZN H 302 OD1 ASP L 186 7555 1555 1.96 LINK ZN ZN H 302 O HOH L 559 1555 7555 2.23 LINK ZN ZN H 303 O HOH H 411 1555 1555 2.25 LINK ZN ZN H 303 N3 IMD L 334 1555 6555 1.96 LINK ZN ZN H 304 O HOH H 502 1555 1555 1.73 LINK ZN ZN H 304 O HOH H 540 1555 1555 2.20 LINK ZN ZN H 304 O HOH H 551 1555 1555 2.14 LINK ZN ZN H 305 O HOH H 472 1555 1555 2.49 LINK ZN ZN H 305 OE1 GLU L 17 3555 1555 2.44 LINK ZN ZN H 305 OE2 GLU L 17 3555 1555 2.24 LINK ZN ZN H 305 O HOH L 556 1555 4454 2.48 LINK ZN ZN H 305 O HOH L 581 1555 4454 2.57 LINK ZN ZN H 305 O HOH L 596 1555 4454 2.48 LINK ZN ZN H 306 O HOH H 401 1555 1555 2.69 LINK ZN ZN H 306 O HOH H 495 1555 1555 2.26 LINK ZN ZN H 306 O HOH L 567 1555 1555 2.38 LINK ZN ZN H 308 O HOH H 546 1555 1555 2.03 LINK N1 IMD H 327 ZN ZN L 302 1555 4454 1.93 LINK O HOH H 437 ZN ZN L 306 1555 1555 2.03 LINK O HOH H 505 ZN ZN L 313 7556 1555 2.37 LINK O HOH H 548 ZN ZN L 311 6555 1555 2.28 LINK OE2 GLU L 1 ZN ZN L 312 1555 1555 2.03 LINK OE1 GLU L 80 ZN ZN L 302 1555 1555 1.91 LINK OD1 ASN L 138 ZN ZN L 306 1555 1555 1.99 LINK OD1 ASN L 139 ZN ZN L 306 1555 1555 2.06 LINK OE2 GLU L 144 ZN ZN L 308 1555 7555 2.02 LINK OE1 GLU L 162 ZN ZN L 305 1555 1555 2.05 LINK OE1 GLU L 166 ZN ZN L 303 1555 1555 2.46 LINK OE2 GLU L 166 ZN ZN L 303 1555 1555 2.25 LINK OD1 ASP L 168 ZN ZN L 304 1555 1555 2.11 LINK NZ LYS L 170 ZN ZN L 304 1555 1555 2.14 LINK OD2 ASP L 171 ZN ZN L 311 1555 1555 2.13 LINK OE1 GLU L 188 ZN ZN L 312 1555 7555 2.11 LINK OE2 GLU L 188 ZN ZN L 312 1555 7555 2.66 LINK NE2 HIS L 190 ZN ZN L 301 1555 1555 2.07 LINK OE2 GLU L 196 ZN ZN L 308 1555 1555 2.03 LINK OE2 GLU L 214 ZN ZN L 307 1555 7555 1.99 LINK ZN ZN L 301 N1 IMD L 333 1555 1555 2.03 LINK ZN ZN L 302 N1 IMD L 335 1555 1555 2.01 LINK ZN ZN L 303 N1 IMD L 336 1555 1555 1.98 LINK ZN ZN L 303 O HOH L 572 1555 1555 2.15 LINK ZN ZN L 304 O HOH L 409 1555 1555 2.25 LINK ZN ZN L 304 O HOH L 424 1555 1555 2.29 LINK ZN ZN L 304 O HOH L 570 1555 1555 2.47 LINK ZN ZN L 305 N1 IMD L 332 1555 1555 2.07 LINK ZN ZN L 305 O HOH L 575 1555 7555 2.24 LINK ZN ZN L 306 O HOH L 524 1555 1555 2.19 LINK ZN ZN L 306 O HOH L 555 1555 1555 2.51 LINK ZN ZN L 307 O HOH L 566 1555 7555 2.42 LINK ZN ZN L 307 O HOH L 580 1555 7555 2.28 LINK ZN ZN L 308 O HOH L 401 1555 7555 2.63 LINK ZN ZN L 308 O HOH L 505 1555 1555 2.28 LINK ZN ZN L 308 O HOH L 571 1555 7555 2.47 LINK ZN ZN L 309 O HOH L 607 1555 1555 1.98 LINK ZN ZN L 310 O HOH L 558 1555 1555 2.59 LINK ZN ZN L 310 O HOH L 601 1555 1555 2.12 LINK ZN ZN L 311 O HOH L 564 1555 1555 2.11 LINK ZN ZN L 311 O HOH L 573 1555 1555 2.38 LINK ZN ZN L 312 O HOH L 539 1555 7555 1.99 LINK ZN ZN L 312 O HOH L 579 1555 7555 2.28 LINK ZN ZN L 313 O HOH L 522 1555 1555 2.31 CISPEP 1 ARG H 100 TRP H 101 0 16.84 CISPEP 2 PHE H 149 PRO H 150 0 -7.08 CISPEP 3 GLU H 151 PRO H 152 0 2.11 CISPEP 4 SER L 7 PRO L 8 0 -13.81 CISPEP 5 SER L 95 PRO L 96 0 0.96 CISPEP 6 TYR L 141 PRO L 142 0 1.92 CRYST1 121.747 121.747 67.389 90.00 90.00 90.00 P 41 21 2 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 0.008214 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008214 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014839 0.00000