HEADER IMMUNE SYSTEM 15-NOV-24 9ECY TITLE CRYSTAL STRUCTURE OF THE SARS-COV-2 NTD-TARGETED NEUTRALIZING ANTIBODY TITLE 2 WRAIR-2039 COMPND MOL_ID: 1; COMPND 2 MOLECULE: WRAIR-2039 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: WRAIR-2039 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: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTIBODY, HUMAN ANTIBODY, NEUTRALIZING ANTIBODY, SARS-COV-2, IMMUNE KEYWDS 2 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR R.S.SANKHALA,J.L.JENSEN,M.G.JOYCE REVDAT 1 20-AUG-25 9ECY 0 JRNL AUTH R.S.SANKHALA,J.L.JENSEN,M.G.JOYCE JRNL TITL CRYSTAL STRUCTURE OF THE SARS-COV-2 NTD-TARGETED JRNL TITL 2 NEUTRALIZING ANTIBODY WRAIR-2039 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.54 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.21.1_5286: ???) 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) : 1.54 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.93 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.020 REMARK 3 COMPLETENESS FOR RANGE (%) : 89.8 REMARK 3 NUMBER OF REFLECTIONS : 60035 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.159 REMARK 3 R VALUE (WORKING SET) : 0.157 REMARK 3 FREE R VALUE : 0.194 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.250 REMARK 3 FREE R VALUE TEST SET COUNT : 3152 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 53.9300 - 4.3900 0.95 2840 138 0.1793 0.1820 REMARK 3 2 4.3900 - 3.4800 0.95 2687 146 0.1347 0.1792 REMARK 3 3 3.4800 - 3.0400 0.95 2717 108 0.1477 0.1895 REMARK 3 4 3.0400 - 2.7700 0.92 2543 143 0.1445 0.1761 REMARK 3 5 2.7700 - 2.5700 0.95 2621 174 0.1490 0.1737 REMARK 3 6 2.5700 - 2.4200 0.95 2615 155 0.1500 0.1924 REMARK 3 7 2.4200 - 2.2900 0.95 2614 152 0.1504 0.2022 REMARK 3 8 2.2900 - 2.1900 0.95 2645 131 0.1455 0.2115 REMARK 3 9 2.1900 - 2.1100 0.96 2605 158 0.1501 0.2151 REMARK 3 10 2.1100 - 2.0400 0.96 2630 153 0.1586 0.2060 REMARK 3 11 2.0400 - 1.9700 0.90 2456 144 0.1586 0.2113 REMARK 3 12 1.9700 - 1.9200 0.94 2574 153 0.1580 0.1962 REMARK 3 13 1.9200 - 1.8700 0.95 2576 165 0.1513 0.1767 REMARK 3 14 1.8700 - 1.8200 0.95 2574 146 0.1532 0.1968 REMARK 3 15 1.8200 - 1.7800 0.94 2573 144 0.1623 0.2056 REMARK 3 16 1.7800 - 1.7400 0.91 2481 133 0.1793 0.2363 REMARK 3 17 1.7400 - 1.7100 0.90 2482 113 0.1880 0.1940 REMARK 3 18 1.7100 - 1.6800 0.92 2456 154 0.2005 0.2420 REMARK 3 19 1.6700 - 1.6500 0.90 2459 138 0.2141 0.2844 REMARK 3 20 1.6500 - 1.6200 0.86 2361 125 0.2028 0.2103 REMARK 3 21 1.6200 - 1.5900 0.80 2171 116 0.2001 0.2343 REMARK 3 22 1.5900 - 1.5700 0.68 1811 93 0.2220 0.2686 REMARK 3 23 1.5700 - 1.5400 0.51 1392 70 0.2444 0.3206 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) : 0.170 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.560 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 20.37 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 : 0.021 3426 REMARK 3 ANGLE : 1.785 4669 REMARK 3 CHIRALITY : 0.099 533 REMARK 3 PLANARITY : 0.015 593 REMARK 3 DIHEDRAL : 16.619 1250 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 11 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.1653 39.9778 2.9409 REMARK 3 T TENSOR REMARK 3 T11: 0.2208 T22: 0.2213 REMARK 3 T33: 0.2113 T12: -0.0033 REMARK 3 T13: 0.0110 T23: 0.0244 REMARK 3 L TENSOR REMARK 3 L11: 1.9195 L22: 0.2401 REMARK 3 L33: 1.3728 L12: 0.5718 REMARK 3 L13: 0.2634 L23: 0.3845 REMARK 3 S TENSOR REMARK 3 S11: -0.0169 S12: 0.0650 S13: 0.0734 REMARK 3 S21: 0.0295 S22: -0.0292 S23: 0.1377 REMARK 3 S31: 0.1166 S32: -0.2092 S33: 0.0041 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 18 THROUGH 52 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.6231 43.0246 -7.1302 REMARK 3 T TENSOR REMARK 3 T11: 0.1866 T22: 0.2317 REMARK 3 T33: 0.2193 T12: -0.0027 REMARK 3 T13: -0.0063 T23: 0.0083 REMARK 3 L TENSOR REMARK 3 L11: 0.8567 L22: 0.9920 REMARK 3 L33: 1.0478 L12: -0.3431 REMARK 3 L13: 0.2413 L23: -0.2761 REMARK 3 S TENSOR REMARK 3 S11: -0.0548 S12: 0.1291 S13: -0.1249 REMARK 3 S21: -0.0899 S22: 0.0572 S23: 0.1857 REMARK 3 S31: -0.0322 S32: -0.1942 S33: -0.0009 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 52A THROUGH 72 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.1334 37.0186 -13.1665 REMARK 3 T TENSOR REMARK 3 T11: 0.3048 T22: 0.2486 REMARK 3 T33: 0.2710 T12: -0.0222 REMARK 3 T13: 0.0172 T23: -0.0180 REMARK 3 L TENSOR REMARK 3 L11: 1.7898 L22: 1.0772 REMARK 3 L33: 0.9842 L12: 0.1684 REMARK 3 L13: 0.0767 L23: 0.0858 REMARK 3 S TENSOR REMARK 3 S11: -0.2134 S12: 0.2662 S13: 0.0443 REMARK 3 S21: -0.5687 S22: 0.0501 S23: 0.1297 REMARK 3 S31: 0.2684 S32: -0.0631 S33: -0.0052 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 73 THROUGH 106 ) REMARK 3 ORIGIN FOR THE GROUP (A): 31.5474 42.5154 -5.6160 REMARK 3 T TENSOR REMARK 3 T11: 0.1752 T22: 0.2175 REMARK 3 T33: 0.2002 T12: -0.0075 REMARK 3 T13: 0.0077 T23: 0.0159 REMARK 3 L TENSOR REMARK 3 L11: 0.5867 L22: 1.1119 REMARK 3 L33: 1.4553 L12: -0.4592 REMARK 3 L13: 0.6930 L23: -0.0603 REMARK 3 S TENSOR REMARK 3 S11: 0.0202 S12: 0.0767 S13: -0.0793 REMARK 3 S21: -0.1121 S22: 0.0111 S23: 0.1774 REMARK 3 S31: 0.1285 S32: -0.1270 S33: 0.0003 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 107 THROUGH 157 ) REMARK 3 ORIGIN FOR THE GROUP (A): 31.7521 51.6917 21.4273 REMARK 3 T TENSOR REMARK 3 T11: 0.1442 T22: 0.1208 REMARK 3 T33: 0.1442 T12: -0.0081 REMARK 3 T13: 0.0008 T23: -0.0022 REMARK 3 L TENSOR REMARK 3 L11: 1.0691 L22: 0.6847 REMARK 3 L33: 0.7499 L12: -0.0768 REMARK 3 L13: 0.0098 L23: 0.1378 REMARK 3 S TENSOR REMARK 3 S11: -0.0036 S12: -0.1327 S13: 0.1975 REMARK 3 S21: 0.0622 S22: 0.0114 S23: -0.0772 REMARK 3 S31: -0.0712 S32: 0.0083 S33: -0.0285 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 158 THROUGH 190 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.7139 57.2140 21.3196 REMARK 3 T TENSOR REMARK 3 T11: 0.1740 T22: 0.1820 REMARK 3 T33: 0.1729 T12: 0.0054 REMARK 3 T13: 0.0045 T23: 0.0029 REMARK 3 L TENSOR REMARK 3 L11: 1.2530 L22: 1.6066 REMARK 3 L33: 0.6631 L12: 0.5025 REMARK 3 L13: -0.1067 L23: 0.2063 REMARK 3 S TENSOR REMARK 3 S11: -0.0570 S12: -0.1589 S13: 0.2609 REMARK 3 S21: 0.0095 S22: 0.0632 S23: -0.0174 REMARK 3 S31: -0.0675 S32: -0.0091 S33: -0.0051 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 191 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.0190 49.0672 25.1992 REMARK 3 T TENSOR REMARK 3 T11: 0.1870 T22: 0.1528 REMARK 3 T33: 0.1493 T12: -0.0150 REMARK 3 T13: 0.0086 T23: -0.0135 REMARK 3 L TENSOR REMARK 3 L11: 2.4717 L22: 2.3058 REMARK 3 L33: 1.8060 L12: -1.1722 REMARK 3 L13: -1.0680 L23: 1.0477 REMARK 3 S TENSOR REMARK 3 S11: -0.0486 S12: -0.1329 S13: 0.1088 REMARK 3 S21: 0.2822 S22: -0.0197 S23: 0.0852 REMARK 3 S31: 0.1340 S32: -0.1320 S33: 0.0319 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 39.4045 67.2847 -9.3686 REMARK 3 T TENSOR REMARK 3 T11: 0.1744 T22: 0.1863 REMARK 3 T33: 0.1864 T12: -0.0230 REMARK 3 T13: 0.0285 T23: 0.0043 REMARK 3 L TENSOR REMARK 3 L11: 1.2776 L22: 2.2755 REMARK 3 L33: 3.0418 L12: 0.2119 REMARK 3 L13: -0.6413 L23: 2.0947 REMARK 3 S TENSOR REMARK 3 S11: 0.0344 S12: -0.1223 S13: 0.1177 REMARK 3 S21: -0.1142 S22: 0.2077 S23: -0.1626 REMARK 3 S31: -0.1570 S32: 0.3885 S33: -0.0622 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 19 THROUGH 106A) REMARK 3 ORIGIN FOR THE GROUP (A): 32.9090 60.7051 -12.7080 REMARK 3 T TENSOR REMARK 3 T11: 0.1583 T22: 0.1806 REMARK 3 T33: 0.1431 T12: 0.0075 REMARK 3 T13: -0.0008 T23: 0.0139 REMARK 3 L TENSOR REMARK 3 L11: 1.8108 L22: 1.5787 REMARK 3 L33: 0.8870 L12: 0.0274 REMARK 3 L13: -0.3621 L23: 0.2679 REMARK 3 S TENSOR REMARK 3 S11: 0.0740 S12: 0.1099 S13: 0.0741 REMARK 3 S21: -0.0184 S22: -0.0450 S23: -0.0261 REMARK 3 S31: -0.0189 S32: -0.0797 S33: 0.0021 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 107 THROUGH 187 ) REMARK 3 ORIGIN FOR THE GROUP (A): 39.3492 62.9943 24.8459 REMARK 3 T TENSOR REMARK 3 T11: 0.1762 T22: 0.1564 REMARK 3 T33: 0.1859 T12: 0.0018 REMARK 3 T13: -0.0150 T23: -0.0084 REMARK 3 L TENSOR REMARK 3 L11: 0.8864 L22: 1.5513 REMARK 3 L33: 2.0706 L12: 0.3960 REMARK 3 L13: -0.3563 L23: 0.5566 REMARK 3 S TENSOR REMARK 3 S11: 0.0764 S12: 0.0452 S13: -0.0971 REMARK 3 S21: -0.0234 S22: 0.0536 S23: -0.1897 REMARK 3 S31: -0.0399 S32: -0.0096 S33: 0.0236 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 188 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): 39.4502 69.2244 31.7258 REMARK 3 T TENSOR REMARK 3 T11: 0.1666 T22: 0.1522 REMARK 3 T33: 0.1792 T12: -0.0021 REMARK 3 T13: -0.0093 T23: -0.0112 REMARK 3 L TENSOR REMARK 3 L11: 0.8023 L22: 2.7084 REMARK 3 L33: 4.0044 L12: -0.3724 REMARK 3 L13: 0.5851 L23: -1.5394 REMARK 3 S TENSOR REMARK 3 S11: 0.0528 S12: -0.1056 S13: 0.0042 REMARK 3 S21: 0.1093 S22: 0.1398 S23: -0.0217 REMARK 3 S31: -0.1385 S32: -0.1315 S33: 0.0008 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 9ECY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1000289349. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-MAR-21 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 : 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) : 0.979180 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 : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62489 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.530 REMARK 200 RESOLUTION RANGE LOW (A) : 102.480 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.56 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 (%): 49.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.12 M ALCOHOL MIXTURE (1,6 REMARK 280 -HEXANEDIOL; 1-BUTANOL; 1,2-PROPANEDIOL; 2-PROPANOL; 1,4- REMARK 280 BUTANEDIOL; 1,3-PROPANEDIOL), 0.1 M BUFFER SYSTEM 1 (IMIDAZOLE REMARK 280 AND MES MONOHYDRATE, PH 6.5), 30% PRECIPITANT MIX 1 (40% V/V PEG REMARK 280 500 MME; 20% V/V PEG 20000), VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 291K 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 31.71100 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.23750 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.53550 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.23750 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.71100 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.53550 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4990 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19540 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL 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 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 HZ2 LYS L 45 O HOH L 401 1.03 REMARK 500 NZ LYS L 45 O HOH L 401 1.17 REMARK 500 HZ3 LYS H 214 O HOH H 401 1.27 REMARK 500 HZ1 LYS L 45 O HOH L 401 1.29 REMARK 500 HZ3 LYS L 45 O HOH L 401 1.29 REMARK 500 HH22 ARG L 189 O HOH L 403 1.46 REMARK 500 NZ LYS H 214 O HOH H 401 1.73 REMARK 500 NZ LYS H 117 O HOH H 402 1.86 REMARK 500 O HOH H 518 O HOH H 543 1.90 REMARK 500 O HOH L 529 O HOH L 556 2.01 REMARK 500 O HOH H 544 O HOH H 576 2.01 REMARK 500 O HOH L 527 O HOH L 540 2.09 REMARK 500 O HOH H 565 O HOH H 580 2.15 REMARK 500 O HOH H 429 O HOH H 572 2.18 REMARK 500 O HOH H 542 O HOH L 533 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 CYS H 140 CB CYS H 140 SG -0.102 REMARK 500 SER H 188 CB SER H 188 OG 0.087 REMARK 500 VAL L 144 CB VAL L 144 CG2 -0.167 REMARK 500 SER L 175 CB SER L 175 OG -0.090 REMARK 500 GLU L 210 CD GLU L 210 OE1 0.104 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 GLY H 162 C - N - CA ANGL. DEV. = -12.7 DEGREES REMARK 500 LYS L 156 CD - CE - NZ ANGL. DEV. = 13.9 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 ALA H 100C 44.32 -152.39 REMARK 500 ASN L 27B -88.61 -130.03 REMARK 500 ASN L 51 -39.20 75.52 REMARK 500 SER L 90 -155.54 -145.66 REMARK 500 ASP L 151 -119.06 52.10 REMARK 500 ASN L 170 -6.94 79.44 REMARK 500 REMARK 500 REMARK: NULL DBREF 9ECY H 1 215 PDB 9ECY 9ECY 1 215 DBREF 9ECY L 1 212 PDB 9ECY 9ECY 1 212 SEQRES 1 H 222 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 222 PRO GLY ALA SER VAL LYS VAL SER CYS LYS VAL SER GLY SEQRES 3 H 222 TYR MET LEU ILE GLU LEU SER MET HIS TRP VAL ARG GLN SEQRES 4 H 222 ALA PRO GLY LYS GLY LEU GLU TRP MET GLY GLY PHE ASP SEQRES 5 H 222 PRO GLU ASP ALA GLU THR ILE TYR ALA GLN GLU PHE GLN SEQRES 6 H 222 GLY ARG VAL THR MET THR GLU ASP THR SER THR ASP THR SEQRES 7 H 222 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 222 ALA VAL TYR TYR CYS THR THR GLY PRO ALA VAL THR ASN SEQRES 9 H 222 ARG PRO ALA ASP TYR TRP GLY PRO GLY THR LEU VAL THR SEQRES 10 H 222 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 11 H 222 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 12 H 222 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 13 H 222 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 14 H 222 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 15 H 222 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 16 H 222 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 17 H 222 PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SEQRES 18 H 222 SER SEQRES 1 L 218 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 L 218 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY SER SER SEQRES 3 L 218 SER ASN ILE GLY ALA SER TYR ASP VAL HIS TRP TYR GLN SEQRES 4 L 218 GLN LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR ALA SEQRES 5 L 218 ASN SER ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 L 218 GLY SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7 L 218 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 L 218 SER TYR ASP SER SER LEU SER TYR SER VAL VAL PHE GLY SEQRES 9 L 218 GLY GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA SEQRES 10 L 218 ALA PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU SEQRES 11 L 218 LEU GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER SEQRES 12 L 218 ASP PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA SEQRES 13 L 218 ASP SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR SEQRES 14 L 218 PRO SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER SEQRES 15 L 218 TYR LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SEQRES 16 L 218 SER TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL SEQRES 17 L 218 GLU LYS THR VAL ALA PRO THR GLU CYS SER HET GOL H 301 14 HET PE5 L 301 65 HET GOL L 302 14 HET GOL L 303 14 HET GOL L 304 14 HETNAM GOL GLYCEROL HETNAM PE5 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL HETSYN PE5 2-(2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}- HETSYN 2 PE5 ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL; POLYETHYLENE HETSYN 3 PE5 GLYCOL PEG400 FORMUL 3 GOL 4(C3 H8 O3) FORMUL 4 PE5 C18 H38 O9 FORMUL 8 HOH *378(H2 O) HELIX 1 AA1 MET H 28 ILE H 30 5 3 HELIX 2 AA2 ARG H 83 THR H 87 5 5 HELIX 3 AA3 SER H 156 ALA H 158 5 3 HELIX 4 AA4 SER H 187 THR H 191 5 5 HELIX 5 AA5 LYS H 201 ASN H 204 5 4 HELIX 6 AA6 ASN L 27B SER L 30 5 5 HELIX 7 AA7 GLN L 79 GLU L 83 5 5 HELIX 8 AA8 SER L 121 ALA L 127 1 7 HELIX 9 AA9 THR L 181 SER L 187 1 7 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AA1 4 THR H 77 LEU H 82 -1 O ALA H 78 N CYS H 22 SHEET 4 AA1 4 VAL H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AA2 6 GLU H 10 LYS H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AA2 6 ALA H 88 PRO H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 LEU H 32 GLN H 39 -1 N SER H 33 O GLY H 95 SHEET 5 AA2 6 LEU H 45 ASP H 52 -1 O MET H 48 N TRP H 36 SHEET 6 AA2 6 GLU H 56 TYR H 59 -1 O GLU H 56 N ASP H 52 SHEET 1 AA3 4 GLU H 10 LYS H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AA3 4 ALA H 88 PRO H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 TYR H 102 TRP H 103 -1 O TYR H 102 N THR H 94 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 THR H 131 SER H 132 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA6 3 THR H 205 ARG H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 5 SER L 9 GLY L 13 0 SHEET 2 AA7 5 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11 SHEET 3 AA7 5 ALA L 84 TYR L 91 -1 N ALA L 84 O LEU L 104 SHEET 4 AA7 5 HIS L 34 GLN L 38 -1 N GLN L 38 O ASP L 85 SHEET 5 AA7 5 LYS L 45 ILE L 48 -1 O LEU L 47 N TRP L 35 SHEET 1 AA8 4 SER L 9 GLY L 13 0 SHEET 2 AA8 4 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11 SHEET 3 AA8 4 ALA L 84 TYR L 91 -1 N ALA L 84 O LEU L 104 SHEET 4 AA8 4 VAL L 96 PHE L 98 -1 O VAL L 97 N SER L 90 SHEET 1 AA9 3 VAL L 19 THR L 24 0 SHEET 2 AA9 3 SER L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 3 AA9 3 PHE L 62 SER L 67 -1 N SER L 67 O SER L 70 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 ALA L 130 PHE L 139 -1 O LEU L 135 N THR L 116 SHEET 3 AB1 4 TYR L 172 LEU L 180 -1 O SER L 176 N CYS L 134 SHEET 4 AB1 4 VAL L 159 THR L 161 -1 N GLU L 160 O TYR L 177 SHEET 1 AB2 4 SER L 114 PHE L 118 0 SHEET 2 AB2 4 ALA L 130 PHE L 139 -1 O LEU L 135 N THR L 116 SHEET 3 AB2 4 TYR L 172 LEU L 180 -1 O SER L 176 N CYS L 134 SHEET 4 AB2 4 SER L 165 LYS L 166 -1 N SER L 165 O ALA L 173 SHEET 1 AB3 4 SER L 153 VAL L 155 0 SHEET 2 AB3 4 THR L 145 ALA L 150 -1 N ALA L 150 O SER L 153 SHEET 3 AB3 4 TYR L 191 HIS L 197 -1 O GLN L 194 N ALA L 147 SHEET 4 AB3 4 SER L 200 VAL L 206 -1 O VAL L 202 N VAL L 195 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.11 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.05 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.17 SSBOND 4 CYS L 134 CYS L 193 1555 1555 2.07 CISPEP 1 PHE H 146 PRO H 147 0 -10.24 CISPEP 2 GLU H 148 PRO H 149 0 -2.39 CISPEP 3 GLU H 148 PRO H 149 0 -1.08 CISPEP 4 TYR L 140 PRO L 141 0 -0.74 CRYST1 63.422 69.071 102.475 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.015767 0.000000 0.000000 0.00000 SCALE2 0.000000 0.014478 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009758 0.00000