HEADER IMMUNE SYSTEM 28-SEP-20 7AJ6 TITLE LN02 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: LN02; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: LN02 HEAVY CHAIN; COMPND 7 CHAIN: H; 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 HIV, FAB, BROADLY NEUTRALIZING ANTIBODY, BNAB, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR C.CAILLAT,G.FENWICK,G.PANTALEO,W.WEISSENHORN REVDAT 1 06-OCT-21 7AJ6 0 JRNL AUTH C.CAILLAT,G.FENWICK,G.PANTALEO,W.WEISSENHORN JRNL TITL LN02 FAB JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.17.1_3660 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.52 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 3 NUMBER OF REFLECTIONS : 37730 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.178 REMARK 3 R VALUE (WORKING SET) : 0.177 REMARK 3 FREE R VALUE : 0.214 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910 REMARK 3 FREE R VALUE TEST SET COUNT : 1852 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 48.5200 - 4.4700 0.99 2873 132 0.1551 0.1846 REMARK 3 2 4.4700 - 3.5500 1.00 2804 143 0.1437 0.1772 REMARK 3 3 3.5500 - 3.1000 0.99 2787 159 0.1707 0.2021 REMARK 3 4 3.1000 - 2.8100 0.99 2755 139 0.1809 0.2153 REMARK 3 5 2.8100 - 2.6100 0.99 2779 163 0.1927 0.2415 REMARK 3 6 2.6100 - 2.4600 0.99 2757 135 0.1913 0.2188 REMARK 3 7 2.4600 - 2.3400 0.99 2772 138 0.1938 0.2331 REMARK 3 8 2.3400 - 2.2300 0.99 2729 154 0.1971 0.2548 REMARK 3 9 2.2300 - 2.1500 0.98 2731 143 0.2043 0.2689 REMARK 3 10 2.1500 - 2.0700 0.98 2712 155 0.2145 0.2685 REMARK 3 11 2.0700 - 2.0100 0.98 2727 123 0.2286 0.2847 REMARK 3 12 2.0100 - 1.9500 0.98 2704 150 0.2560 0.2825 REMARK 3 13 1.9500 - 1.9000 0.98 2748 118 0.2843 0.3139 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) : 0.225 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.735 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 32.86 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.22 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.009 3329 REMARK 3 ANGLE : 1.107 4548 REMARK 3 CHIRALITY : 0.072 515 REMARK 3 PLANARITY : 0.008 576 REMARK 3 DIHEDRAL : 15.767 460 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 19 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 158 THROUGH 177 ) REMARK 3 ORIGIN FOR THE GROUP (A): -29.5614 7.7836 41.6322 REMARK 3 T TENSOR REMARK 3 T11: 0.2241 T22: 0.1983 REMARK 3 T33: 0.2273 T12: 0.0106 REMARK 3 T13: 0.0262 T23: -0.0372 REMARK 3 L TENSOR REMARK 3 L11: 1.4704 L22: 1.7790 REMARK 3 L33: 1.4667 L12: 1.0356 REMARK 3 L13: 0.8422 L23: -0.5080 REMARK 3 S TENSOR REMARK 3 S11: 0.0124 S12: 0.1263 S13: -0.2035 REMARK 3 S21: -0.0467 S22: -0.0854 S23: 0.2023 REMARK 3 S31: 0.2507 S32: -0.0550 S33: 0.0000 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 178 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.7510 10.1121 41.7940 REMARK 3 T TENSOR REMARK 3 T11: 0.2184 T22: 0.3463 REMARK 3 T33: 0.3741 T12: 0.0342 REMARK 3 T13: 0.0190 T23: -0.0214 REMARK 3 L TENSOR REMARK 3 L11: 2.0947 L22: 2.5458 REMARK 3 L33: 3.4570 L12: 1.1980 REMARK 3 L13: 0.1455 L23: 0.7531 REMARK 3 S TENSOR REMARK 3 S11: 0.0070 S12: 0.2754 S13: 0.0250 REMARK 3 S21: 0.1641 S22: 0.1001 S23: -0.7037 REMARK 3 S31: 0.1224 S32: 0.6452 S33: 0.0183 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 3 THROUGH 38 ) REMARK 3 ORIGIN FOR THE GROUP (A): -48.9017 -3.4039 16.2063 REMARK 3 T TENSOR REMARK 3 T11: 0.3710 T22: 0.4364 REMARK 3 T33: 0.3513 T12: -0.0999 REMARK 3 T13: -0.0416 T23: -0.0142 REMARK 3 L TENSOR REMARK 3 L11: 1.9100 L22: 1.8788 REMARK 3 L33: 2.6300 L12: 1.1130 REMARK 3 L13: -0.2300 L23: 0.3940 REMARK 3 S TENSOR REMARK 3 S11: 0.1741 S12: 0.0716 S13: -0.1468 REMARK 3 S21: 0.0313 S22: -0.0711 S23: 0.3202 REMARK 3 S31: 0.3338 S32: -0.4967 S33: 0.0000 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 39 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): -40.1130 -4.3937 12.5625 REMARK 3 T TENSOR REMARK 3 T11: 0.4786 T22: 0.3532 REMARK 3 T33: 0.3028 T12: -0.0234 REMARK 3 T13: -0.0385 T23: -0.0300 REMARK 3 L TENSOR REMARK 3 L11: 0.7216 L22: 3.2555 REMARK 3 L33: 2.7040 L12: -0.1943 REMARK 3 L13: -1.2595 L23: 0.0993 REMARK 3 S TENSOR REMARK 3 S11: 0.1106 S12: 0.2767 S13: -0.3489 REMARK 3 S21: -0.1627 S22: 0.0360 S23: -0.2353 REMARK 3 S31: 0.5232 S32: 0.2250 S33: 0.0000 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 76 THROUGH 101 ) REMARK 3 ORIGIN FOR THE GROUP (A): -45.6377 2.0497 15.6829 REMARK 3 T TENSOR REMARK 3 T11: 0.3112 T22: 0.3642 REMARK 3 T33: 0.2061 T12: -0.0721 REMARK 3 T13: -0.0161 T23: -0.0156 REMARK 3 L TENSOR REMARK 3 L11: 1.2019 L22: 1.8307 REMARK 3 L33: 2.7088 L12: 1.3240 REMARK 3 L13: 0.0118 L23: 0.3302 REMARK 3 S TENSOR REMARK 3 S11: 0.0608 S12: 0.1151 S13: -0.0720 REMARK 3 S21: 0.2212 S22: 0.0260 S23: 0.0831 REMARK 3 S31: 0.2331 S32: -0.1607 S33: 0.0000 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 102 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -38.6638 -12.6027 33.0087 REMARK 3 T TENSOR REMARK 3 T11: 0.4927 T22: 0.2484 REMARK 3 T33: 0.3780 T12: -0.0657 REMARK 3 T13: -0.1142 T23: 0.0116 REMARK 3 L TENSOR REMARK 3 L11: 0.0645 L22: 0.0526 REMARK 3 L33: 0.2839 L12: -0.2023 REMARK 3 L13: 0.2566 L23: -0.1533 REMARK 3 S TENSOR REMARK 3 S11: 0.3641 S12: -0.1382 S13: -0.5320 REMARK 3 S21: -0.4840 S22: 0.3402 S23: 0.0233 REMARK 3 S31: 0.6839 S32: -0.3277 S33: -0.0410 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 114 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.1283 8.3749 55.2859 REMARK 3 T TENSOR REMARK 3 T11: 0.2955 T22: 0.2261 REMARK 3 T33: 0.2609 T12: -0.0297 REMARK 3 T13: -0.0094 T23: -0.0102 REMARK 3 L TENSOR REMARK 3 L11: 1.7140 L22: 0.7546 REMARK 3 L33: 1.1551 L12: 0.3765 REMARK 3 L13: -0.0922 L23: -0.5967 REMARK 3 S TENSOR REMARK 3 S11: 0.0056 S12: -0.0035 S13: 0.1217 REMARK 3 S21: 0.0959 S22: -0.0345 S23: -0.0476 REMARK 3 S31: -0.2970 S32: 0.0954 S33: 0.0000 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 130 THROUGH 150 ) REMARK 3 ORIGIN FOR THE GROUP (A): -33.1248 -3.0864 49.3592 REMARK 3 T TENSOR REMARK 3 T11: 0.1728 T22: 0.2066 REMARK 3 T33: 0.2811 T12: -0.0079 REMARK 3 T13: 0.0185 T23: 0.0107 REMARK 3 L TENSOR REMARK 3 L11: 1.6470 L22: 2.0485 REMARK 3 L33: 0.8939 L12: 0.2153 REMARK 3 L13: 0.8279 L23: -0.8650 REMARK 3 S TENSOR REMARK 3 S11: 0.1232 S12: -0.0467 S13: -0.2198 REMARK 3 S21: 0.0711 S22: -0.0468 S23: 0.1983 REMARK 3 S31: -0.0561 S32: -0.0443 S33: 0.0000 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 151 THROUGH 173 ) REMARK 3 ORIGIN FOR THE GROUP (A): -35.7276 -1.2323 47.4041 REMARK 3 T TENSOR REMARK 3 T11: 0.2133 T22: 0.2627 REMARK 3 T33: 0.3241 T12: -0.0030 REMARK 3 T13: 0.0352 T23: -0.0044 REMARK 3 L TENSOR REMARK 3 L11: 1.5661 L22: 2.9301 REMARK 3 L33: 0.6997 L12: -0.2043 REMARK 3 L13: 0.0614 L23: 0.1652 REMARK 3 S TENSOR REMARK 3 S11: 0.0868 S12: -0.0303 S13: -0.1662 REMARK 3 S21: -0.0681 S22: -0.0974 S23: 0.1707 REMARK 3 S31: -0.1886 S32: -0.1924 S33: 0.0000 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 174 THROUGH 187 ) REMARK 3 ORIGIN FOR THE GROUP (A): -29.4259 7.5184 59.7751 REMARK 3 T TENSOR REMARK 3 T11: 0.3742 T22: 0.2477 REMARK 3 T33: 0.2616 T12: -0.0270 REMARK 3 T13: 0.0109 T23: -0.0147 REMARK 3 L TENSOR REMARK 3 L11: 1.6398 L22: 1.5256 REMARK 3 L33: 0.5165 L12: -0.4310 REMARK 3 L13: -0.1361 L23: -0.7986 REMARK 3 S TENSOR REMARK 3 S11: -0.0687 S12: -0.3774 S13: 0.2003 REMARK 3 S21: 0.4290 S22: -0.1951 S23: -0.0844 REMARK 3 S31: -0.2977 S32: -0.4235 S33: 0.0000 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 188 THROUGH 208 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.3218 -5.7300 57.4914 REMARK 3 T TENSOR REMARK 3 T11: 0.2559 T22: 0.2581 REMARK 3 T33: 0.3265 T12: -0.0378 REMARK 3 T13: 0.0309 T23: -0.0015 REMARK 3 L TENSOR REMARK 3 L11: 0.7289 L22: 2.2952 REMARK 3 L33: 0.8163 L12: -0.4295 REMARK 3 L13: -0.1426 L23: -1.0958 REMARK 3 S TENSOR REMARK 3 S11: 0.0440 S12: -0.0777 S13: -0.2716 REMARK 3 S21: 0.4041 S22: -0.0143 S23: -0.1756 REMARK 3 S31: 0.0355 S32: -0.1557 S33: 0.0000 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 2 THROUGH 23 ) REMARK 3 ORIGIN FOR THE GROUP (A): -35.7786 22.0828 26.2857 REMARK 3 T TENSOR REMARK 3 T11: 0.2551 T22: 0.3317 REMARK 3 T33: 0.2799 T12: -0.0067 REMARK 3 T13: -0.0184 T23: 0.0025 REMARK 3 L TENSOR REMARK 3 L11: 1.6978 L22: 1.9376 REMARK 3 L33: 1.8783 L12: 1.0739 REMARK 3 L13: 0.6761 L23: -1.0634 REMARK 3 S TENSOR REMARK 3 S11: 0.0970 S12: 0.1188 S13: 0.0855 REMARK 3 S21: -0.1791 S22: 0.0028 S23: 0.0073 REMARK 3 S31: -0.5470 S32: 0.2818 S33: 0.0000 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 24 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): -37.6634 14.3302 16.3649 REMARK 3 T TENSOR REMARK 3 T11: 0.2798 T22: 0.3253 REMARK 3 T33: 0.2351 T12: -0.0110 REMARK 3 T13: -0.0078 T23: -0.0089 REMARK 3 L TENSOR REMARK 3 L11: 0.7799 L22: 3.2833 REMARK 3 L33: 3.3477 L12: 0.0630 REMARK 3 L13: 1.5450 L23: 0.5114 REMARK 3 S TENSOR REMARK 3 S11: -0.0900 S12: 0.1212 S13: -0.0883 REMARK 3 S21: -0.2565 S22: 0.0635 S23: -0.1275 REMARK 3 S31: 0.2167 S32: 0.1412 S33: 0.0000 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 52 THROUGH 87 ) REMARK 3 ORIGIN FOR THE GROUP (A): -41.1588 23.3360 16.6833 REMARK 3 T TENSOR REMARK 3 T11: 0.3890 T22: 0.3537 REMARK 3 T33: 0.3446 T12: 0.0099 REMARK 3 T13: -0.0235 T23: 0.0422 REMARK 3 L TENSOR REMARK 3 L11: 0.3559 L22: 2.2033 REMARK 3 L33: 2.8394 L12: -0.1943 REMARK 3 L13: 0.9714 L23: 0.6353 REMARK 3 S TENSOR REMARK 3 S11: 0.0045 S12: 0.1307 S13: 0.2760 REMARK 3 S21: -0.4214 S22: 0.1482 S23: 0.1259 REMARK 3 S31: -0.5514 S32: -0.1616 S33: 0.0000 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 88 THROUGH 99 ) REMARK 3 ORIGIN FOR THE GROUP (A): -38.0341 11.9918 12.7217 REMARK 3 T TENSOR REMARK 3 T11: 0.3248 T22: 0.3694 REMARK 3 T33: 0.2612 T12: -0.0122 REMARK 3 T13: 0.0245 T23: -0.0019 REMARK 3 L TENSOR REMARK 3 L11: 1.3289 L22: 0.0818 REMARK 3 L33: 0.5853 L12: -0.2760 REMARK 3 L13: 0.2581 L23: -0.1596 REMARK 3 S TENSOR REMARK 3 S11: 0.1085 S12: 0.3114 S13: -0.0068 REMARK 3 S21: -0.1728 S22: 0.1094 S23: -0.1732 REMARK 3 S31: -0.4204 S32: 0.5077 S33: 0.0032 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 100 THROUGH 103 ) REMARK 3 ORIGIN FOR THE GROUP (A): -40.6476 8.1130 7.3915 REMARK 3 T TENSOR REMARK 3 T11: 0.4084 T22: 0.4203 REMARK 3 T33: 0.2331 T12: -0.0253 REMARK 3 T13: -0.0174 T23: -0.0182 REMARK 3 L TENSOR REMARK 3 L11: 0.6737 L22: 1.2897 REMARK 3 L33: 0.7004 L12: 0.2567 REMARK 3 L13: -0.5724 L23: -0.8149 REMARK 3 S TENSOR REMARK 3 S11: -0.0228 S12: 0.7270 S13: -0.3758 REMARK 3 S21: -0.3519 S22: 0.1745 S23: 0.0791 REMARK 3 S31: 0.2539 S32: 0.6332 S33: 0.0000 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 104 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): -36.3454 19.4890 35.9679 REMARK 3 T TENSOR REMARK 3 T11: 0.2316 T22: 0.2592 REMARK 3 T33: 0.3310 T12: 0.0143 REMARK 3 T13: -0.0357 T23: -0.0427 REMARK 3 L TENSOR REMARK 3 L11: 1.7354 L22: 0.6309 REMARK 3 L33: 1.1111 L12: 0.4562 REMARK 3 L13: 0.8649 L23: -0.6336 REMARK 3 S TENSOR REMARK 3 S11: 0.0241 S12: -0.0703 S13: 0.5259 REMARK 3 S21: 0.1774 S22: -0.0696 S23: -0.1203 REMARK 3 S31: -0.1583 S32: -0.2634 S33: 0.0000 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 120 THROUGH 134 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.3047 1.7314 49.1533 REMARK 3 T TENSOR REMARK 3 T11: 0.4812 T22: 0.3231 REMARK 3 T33: 0.6785 T12: 0.0983 REMARK 3 T13: -0.0371 T23: -0.0357 REMARK 3 L TENSOR REMARK 3 L11: 1.4098 L22: 1.0906 REMARK 3 L33: 1.7423 L12: 1.2475 REMARK 3 L13: 0.0438 L23: -0.2824 REMARK 3 S TENSOR REMARK 3 S11: 0.0399 S12: 0.1060 S13: -1.2189 REMARK 3 S21: 0.4284 S22: -0.0601 S23: 0.2891 REMARK 3 S31: 0.6146 S32: 0.4441 S33: 0.0072 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 135 THROUGH 157 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.1952 10.7112 41.2193 REMARK 3 T TENSOR REMARK 3 T11: 0.2397 T22: 0.2308 REMARK 3 T33: 0.3033 T12: 0.0159 REMARK 3 T13: 0.0292 T23: -0.0163 REMARK 3 L TENSOR REMARK 3 L11: 0.7944 L22: 0.9828 REMARK 3 L33: 1.8830 L12: 0.4522 REMARK 3 L13: 0.5162 L23: 0.3149 REMARK 3 S TENSOR REMARK 3 S11: -0.0300 S12: -0.0016 S13: -0.2039 REMARK 3 S21: -0.0196 S22: 0.0418 S23: 0.0313 REMARK 3 S31: 0.2761 S32: 0.2175 S33: 0.0000 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 7AJ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-SEP-20. REMARK 100 THE DEPOSITION ID IS D_1292109638. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-JUL-19 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 : SOLEIL REMARK 200 BEAMLINE : PROXIMA 2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.980107 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37744 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 48.520 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 200 DATA REDUNDANCY : 7.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.3800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97 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: PHENIX REMARK 200 STARTING MODEL: 2J6E, 4YKA, 4NPY, 6AZZ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.73 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7 30%(V/V) JEFFAMINE M REMARK 280 -600 REAGENT PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 38.00950 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.22400 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 38.00950 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.22400 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 APPLY THE FOLLOWING TO CHAINS: L, 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 LYS H 214 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 NE2 GLN H 171 O HOH H 301 2.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP L 51 -50.14 74.45 REMARK 500 ASP L 52 13.16 -149.74 REMARK 500 SER L 69 33.12 -94.59 REMARK 500 ALA L 84 169.70 177.93 REMARK 500 ASN L 128 33.40 73.44 REMARK 500 ASP L 151 -115.51 54.05 REMARK 500 THR H 15 -3.25 76.91 REMARK 500 SER H 100 -138.82 -119.12 REMARK 500 SER H 100 -138.82 -129.63 REMARK 500 REMARK 500 REMARK: NULL DBREF 7AJ6 L 3 208 PDB 7AJ6 7AJ6 3 208 DBREF 7AJ6 H 2 214 PDB 7AJ6 7AJ6 2 214 SEQRES 1 L 209 TYR VAL LEU GLY GLN SER SER SER MET SER VAL ALA PRO SEQRES 2 L 209 GLY GLN THR ALA LYS ILE SER CYS TRP GLY TYR TYR MET SEQRES 3 L 209 GLY THR LYS PRO VAL ASN TRP TYR GLN LEU LYS PRO GLY SEQRES 4 L 209 ARG ALA PRO SER LEU ILE ILE SER TYR ASP ASP GLU ARG SEQRES 5 L 209 ALA SER GLY THR PRO ALA ARG PHE SER GLY SER HIS SER SEQRES 6 L 209 GLY SER THR ALA THR LEU THR ILE SER ASN VAL VAL PRO SEQRES 7 L 209 ALA ASP GLU ALA ASP TYR PHE CYS GLN VAL TRP ASP SER SEQRES 8 L 209 LYS TYR GLU GLU ILE TYR PHE GLY GLY GLY THR ALA LEU SEQRES 9 L 209 THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR SEQRES 10 L 209 LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS SEQRES 11 L 209 ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY SEQRES 12 L 209 ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL SEQRES 13 L 209 LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SER SEQRES 14 L 209 ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU THR SEQRES 15 L 209 PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS GLN SEQRES 16 L 209 VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA SEQRES 17 L 209 PRO SEQRES 1 H 223 ALA PRO LEU PRO GLU SER GLY PRO GLY VAL VAL ARG PRO SEQRES 2 H 223 THR GLY THR LEU SER LEU THR CYS THR ALA ALA TYR GLY SEQRES 3 H 223 SER ILE SER ARG HIS PHE TRP GLY TRP VAL ARG GLN SER SEQRES 4 H 223 PRO GLN GLY THR LEU GLU TRP ILE ALA HIS MET HIS HIS SEQRES 5 H 223 LEU GLY VAL LYS TYR VAL ASN PRO SER LEU LYS ASN ARG SEQRES 6 H 223 VAL SER ILE SER MET ASP THR SER LYS ASN GLN MET SER SEQRES 7 H 223 LEU THR LEU LYS THR VAL THR ALA THR ASP ALA ALA LYS SEQRES 8 H 223 TYR HIS CYS VAL ARG MET GLY ALA ARG MET SER ASP ILE SEQRES 9 H 223 ALA PHE PHE SER PHE GLY ASP TRP GLY PRO GLY SER LEU SEQRES 10 H 223 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 H 223 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 H 223 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 H 223 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 H 223 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 H 223 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 H 223 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 H 223 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 18 H 223 PRO LYS FORMUL 3 HOH *243(H2 O) HELIX 1 AA1 VAL L 79 GLU L 83 5 5 HELIX 2 AA2 SER L 121 ALA L 127 1 7 HELIX 3 AA3 THR L 181 HIS L 188 1 8 HELIX 4 AA4 PRO H 61 LYS H 64 5 4 HELIX 5 AA5 THR H 83 ALA H 87 5 5 HELIX 6 AA6 SER H 156 ALA H 158 5 3 HELIX 7 AA7 SER H 187 GLN H 192 1 6 HELIX 8 AA8 LYS H 201 ASN H 204 5 4 SHEET 1 AA1 6 MET L 11 VAL L 13 0 SHEET 2 AA1 6 THR L 102 VAL L 106 1 O ALA L 103 N MET L 11 SHEET 3 AA1 6 ALA L 84 ASP L 92 -1 N ALA L 84 O LEU L 104 SHEET 4 AA1 6 ASN L 34 LEU L 38 -1 N TYR L 36 O PHE L 87 SHEET 5 AA1 6 SER L 45 SER L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AA1 6 GLU L 53 ARG L 54 -1 O GLU L 53 N SER L 49 SHEET 1 AA2 8 MET L 11 VAL L 13 0 SHEET 2 AA2 8 THR L 102 VAL L 106 1 O ALA L 103 N MET L 11 SHEET 3 AA2 8 ALA L 84 ASP L 92 -1 N ALA L 84 O LEU L 104 SHEET 4 AA2 8 GLU L 95B GLY L 99 -1 O GLY L 99 N CYS L 88 SHEET 5 AA2 8 VAL L 4 GLN L 7 1 N LEU L 5 O PHE L 98 SHEET 6 AA2 8 ALA L 19 TRP L 24 -1 O TRP L 24 N GLY L 6 SHEET 7 AA2 8 THR L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 8 AA2 8 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA3 4 SER L 114 PHE L 118 0 SHEET 2 AA3 4 ALA L 130 PHE L 139 -1 O LEU L 135 N THR L 116 SHEET 3 AA3 4 TYR L 172 LEU L 180 -1 O LEU L 180 N ALA L 130 SHEET 4 AA3 4 VAL L 159 THR L 161 -1 N GLU L 160 O TYR L 177 SHEET 1 AA4 4 SER L 114 PHE L 118 0 SHEET 2 AA4 4 ALA L 130 PHE L 139 -1 O LEU L 135 N THR L 116 SHEET 3 AA4 4 TYR L 172 LEU L 180 -1 O LEU L 180 N ALA L 130 SHEET 4 AA4 4 SER L 165 LYS L 166 -1 N SER L 165 O ALA L 173 SHEET 1 AA5 4 SER L 153 PRO L 154 0 SHEET 2 AA5 4 THR L 145 ALA L 150 -1 N ALA L 150 O SER L 153 SHEET 3 AA5 4 TYR L 191 HIS L 197 -1 O GLN L 194 N ALA L 147 SHEET 4 AA5 4 SER L 200 VAL L 206 -1 O VAL L 202 N VAL L 195 SHEET 1 AA6 6 VAL H 11 VAL H 12 0 SHEET 2 AA6 6 SER H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA6 6 ALA H 88 MET H 99 -1 N TYR H 90 O SER H 107 SHEET 4 AA6 6 TRP H 34 GLN H 39 -1 N VAL H 37 O HIS H 91 SHEET 5 AA6 6 LEU H 45 MET H 51 -1 O ALA H 49 N TRP H 36 SHEET 6 AA6 6 LYS H 57 VAL H 59 -1 O TYR H 58 N HIS H 50 SHEET 1 AA7 4 VAL H 11 VAL H 12 0 SHEET 2 AA7 4 SER H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA7 4 ALA H 88 MET H 99 -1 N TYR H 90 O SER H 107 SHEET 4 AA7 4 ALA H 100C TRP H 103 -1 O PHE H 100D N ARG H 98 SHEET 1 AA8 3 LEU H 18 THR H 23 0 SHEET 2 AA8 3 GLN H 77 LEU H 82 -1 O MET H 78 N CYS H 22 SHEET 3 AA8 3 VAL H 67 ASP H 72 -1 N ASP H 72 O GLN H 77 SHEET 1 AA9 4 SER H 120 SER H 127 0 SHEET 2 AA9 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AA9 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA9 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AB1 4 SER H 120 SER H 127 0 SHEET 2 AB1 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AB1 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AB1 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AB2 3 THR H 151 TRP H 154 0 SHEET 2 AB2 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AB2 3 THR H 205 ARG H 210 -1 O VAL H 207 N VAL H 198 SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.07 SSBOND 2 CYS L 134 CYS L 193 1555 1555 2.05 SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.00 SSBOND 4 CYS H 140 CYS H 196 1555 1555 2.02 CISPEP 1 TYR L 140 PRO L 141 0 3.12 CISPEP 2 PHE H 146 PRO H 147 0 -8.60 CISPEP 3 GLU H 148 PRO H 149 0 -3.34 CRYST1 76.019 66.448 97.559 90.00 95.92 90.00 C 1 2 1 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 0.013155 0.000000 0.001365 0.00000 SCALE2 0.000000 0.015049 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010305 0.00000