HEADER IMMUNE SYSTEM 29-MAY-24 9FIK TITLE STRUCTURE OF THE FAB FRAGMENT OF THE ANTIBODY NTF30037 IN COMPLEX WITH TITLE 2 NTF3 COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEUROTROPHIN-3; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: NT-3,HDNF,NERVE GROWTH FACTOR 2,NGF-2,NEUROTROPHIC FACTOR; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NTF30037 HEAVY CHAIN; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: NTF30037 LIGHT CHAIN; COMPND 12 CHAIN: C; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: NTF3; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM_CELL_LINE: HEK293 KEYWDS NTF3, PHAGE DISPLAY, X RAY CRYSTALLOGRAPHY, ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR P.GALLEGO,A.AAGAARD,T.SJOGREN,S.CHIN,F.NEAL REVDAT 1 02-APR-25 9FIK 0 JRNL AUTH S.CHIN,P.GALLEGO,A.AAGAARD,T.SJOGREN,F.NEAL JRNL TITL IDENTIFICATION OF UNIQUE BINDING MODE ANTI-NTF3 ANTIBODIES JRNL TITL 2 FROM A NOVEL LONG VH CDR3 PHAGE DISPLAY LIBRARY JRNL REF SLAS DISCOV 2025 JRNL REFN ESSN 2472-5560 REMARK 2 REMARK 2 RESOLUTION. 1.86 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.68 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 77.6 REMARK 3 NUMBER OF REFLECTIONS : 51851 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.186 REMARK 3 R VALUE (WORKING SET) : 0.186 REMARK 3 FREE R VALUE : 0.186 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL 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 58.6800 - 5.7800 0.99 2377 2377 0.1743 0.1743 REMARK 3 2 5.7700 - 4.5800 1.00 2281 2281 0.1297 0.1297 REMARK 3 3 4.5800 - 4.0000 0.99 2251 2251 0.1203 0.1203 REMARK 3 4 4.0000 - 3.6400 1.00 2249 2249 0.1386 0.1386 REMARK 3 5 3.6400 - 3.3800 0.99 2214 2214 0.1511 0.1511 REMARK 3 6 3.3800 - 3.1800 0.99 2232 2232 0.1698 0.1698 REMARK 3 7 3.1800 - 3.0200 0.99 2217 2217 0.1814 0.1814 REMARK 3 8 3.0200 - 2.8900 0.99 2223 2223 0.1930 0.1930 REMARK 3 9 2.8900 - 2.7800 0.99 2201 2201 0.1957 0.1957 REMARK 3 10 2.7800 - 2.6800 0.99 2161 2161 0.2229 0.2229 REMARK 3 11 2.6800 - 2.6000 0.99 2216 2216 0.2158 0.2158 REMARK 3 12 2.6000 - 2.5200 0.99 2217 2217 0.2105 0.2105 REMARK 3 13 2.5200 - 2.4600 0.98 2175 2175 0.2174 0.2174 REMARK 3 14 2.4600 - 2.4000 0.98 2163 2163 0.2258 0.2258 REMARK 3 15 2.4000 - 2.3400 0.99 2212 2212 0.2342 0.2342 REMARK 3 16 2.3400 - 2.2900 0.98 2155 0 0.2348 0.2348 REMARK 3 17 2.2900 - 2.2500 0.99 2186 0 0.2365 0.2365 REMARK 3 18 2.2500 - 2.2000 0.98 2181 0 0.2405 0.2405 REMARK 3 19 2.2000 - 2.1600 0.98 2166 0 0.2472 0.2472 REMARK 3 20 2.1600 - 2.1300 0.97 2139 0 0.2471 0.2471 REMARK 3 21 2.1300 - 2.0900 0.90 1976 1976 0.2512 0.2512 REMARK 3 22 2.0900 - 2.0600 0.77 1701 1701 0.2580 0.2580 REMARK 3 23 2.0600 - 2.0300 0.65 1419 1419 0.2688 0.2688 REMARK 3 24 2.0300 - 2.0000 0.46 1016 1016 0.2625 0.2625 REMARK 3 25 2.0000 - 1.9800 0.30 654 654 0.2750 0.2750 REMARK 3 26 1.9800 - 1.9500 0.00 404 404 0.3127 0.3127 REMARK 3 27 1.9500 - 1.9300 0.00 254 254 0.2952 0.2952 REMARK 3 28 1.9300 - 1.9000 0.00 143 143 0.3072 0.3072 REMARK 3 29 1.9000 - 1.8800 0.00 53 53 0.2989 0.2989 REMARK 3 30 1.8800 - 1.8600 0.00 15 15 0.3160 0.3160 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) : 0.155 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.088 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 21.18 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.93 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 : 0.008 4333 REMARK 3 ANGLE : 0.997 5904 REMARK 3 CHIRALITY : 0.066 659 REMARK 3 PLANARITY : 0.008 754 REMARK 3 DIHEDRAL : 6.967 618 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 26 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 11 THROUGH 36 ) REMARK 3 ORIGIN FOR THE GROUP (A): -41.3791 -50.6014 -7.8694 REMARK 3 T TENSOR REMARK 3 T11: 0.2132 T22: 0.0828 REMARK 3 T33: 0.2287 T12: 0.0105 REMARK 3 T13: -0.0327 T23: 0.0194 REMARK 3 L TENSOR REMARK 3 L11: 1.1272 L22: 4.2673 REMARK 3 L33: 1.6204 L12: 0.4757 REMARK 3 L13: -0.2145 L23: 0.6144 REMARK 3 S TENSOR REMARK 3 S11: -0.0663 S12: 0.2766 S13: -0.0794 REMARK 3 S21: -0.3893 S22: 0.1737 S23: 0.2365 REMARK 3 S31: -0.0071 S32: -0.1104 S33: -0.0333 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 37 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.4681 -56.1687 -7.0031 REMARK 3 T TENSOR REMARK 3 T11: 0.3957 T22: 0.0964 REMARK 3 T33: 0.9999 T12: 0.0966 REMARK 3 T13: 0.0437 T23: -0.1761 REMARK 3 L TENSOR REMARK 3 L11: 0.1645 L22: 2.4165 REMARK 3 L33: 0.7675 L12: -0.6095 REMARK 3 L13: -0.1061 L23: 0.0550 REMARK 3 S TENSOR REMARK 3 S11: 0.1920 S12: 0.0697 S13: -0.5345 REMARK 3 S21: -0.0456 S22: 0.1145 S23: -1.2718 REMARK 3 S31: 0.6560 S32: 0.5129 S33: -0.2993 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 52 THROUGH 62 ) REMARK 3 ORIGIN FOR THE GROUP (A): -49.2902 -55.3009 -9.7057 REMARK 3 T TENSOR REMARK 3 T11: 0.2677 T22: 0.1944 REMARK 3 T33: 0.4177 T12: -0.0252 REMARK 3 T13: -0.0796 T23: 0.0295 REMARK 3 L TENSOR REMARK 3 L11: 5.7313 L22: 3.6759 REMARK 3 L33: 2.7435 L12: -0.8672 REMARK 3 L13: -0.4415 L23: -0.1638 REMARK 3 S TENSOR REMARK 3 S11: 0.1056 S12: 0.4964 S13: -0.0035 REMARK 3 S21: -0.5111 S22: 0.0576 S23: 0.8249 REMARK 3 S31: 0.1168 S32: -0.5096 S33: -0.0063 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 63 THROUGH 115 ) REMARK 3 ORIGIN FOR THE GROUP (A): -48.5848 -47.8628 -4.0128 REMARK 3 T TENSOR REMARK 3 T11: 0.2398 T22: 0.0130 REMARK 3 T33: 0.3637 T12: 0.0049 REMARK 3 T13: -0.0066 T23: 0.0076 REMARK 3 L TENSOR REMARK 3 L11: 0.4503 L22: 2.9280 REMARK 3 L33: 1.9326 L12: -0.5321 REMARK 3 L13: -0.7738 L23: -0.1301 REMARK 3 S TENSOR REMARK 3 S11: 0.3211 S12: 0.2527 S13: -0.2282 REMARK 3 S21: -0.0720 S22: 0.0492 S23: 0.4322 REMARK 3 S31: -0.1506 S32: -0.4206 S33: 0.2410 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID -1 THROUGH 15 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.2920 -20.1116 32.3434 REMARK 3 T TENSOR REMARK 3 T11: 0.2467 T22: 0.6509 REMARK 3 T33: 0.2534 T12: -0.0465 REMARK 3 T13: 0.0440 T23: -0.1923 REMARK 3 L TENSOR REMARK 3 L11: 2.9653 L22: 0.4963 REMARK 3 L33: 3.7546 L12: -0.4069 REMARK 3 L13: 2.3370 L23: -0.1466 REMARK 3 S TENSOR REMARK 3 S11: -0.0576 S12: -0.9460 S13: 0.4682 REMARK 3 S21: 0.3390 S22: -0.0558 S23: -0.1851 REMARK 3 S31: -0.4355 S32: 0.1784 S33: 0.4166 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 16 THROUGH 60 ) REMARK 3 ORIGIN FOR THE GROUP (A): -35.1123 -25.1308 23.8610 REMARK 3 T TENSOR REMARK 3 T11: 0.1927 T22: 0.3718 REMARK 3 T33: 0.1797 T12: -0.0572 REMARK 3 T13: 0.0351 T23: -0.0401 REMARK 3 L TENSOR REMARK 3 L11: 3.0789 L22: 0.4998 REMARK 3 L33: 2.3666 L12: -0.1567 REMARK 3 L13: 1.3883 L23: -0.0425 REMARK 3 S TENSOR REMARK 3 S11: 0.1634 S12: -0.8590 S13: 0.2359 REMARK 3 S21: 0.1096 S22: -0.1062 S23: 0.1175 REMARK 3 S31: -0.0829 S32: -0.3088 S33: 0.0334 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 61 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): -37.1524 -25.1485 30.6702 REMARK 3 T TENSOR REMARK 3 T11: 0.2412 T22: 0.6931 REMARK 3 T33: 0.2749 T12: -0.0781 REMARK 3 T13: 0.0647 T23: -0.0640 REMARK 3 L TENSOR REMARK 3 L11: 3.1898 L22: 1.1412 REMARK 3 L33: 2.6122 L12: -0.3065 REMARK 3 L13: 1.1108 L23: -0.0784 REMARK 3 S TENSOR REMARK 3 S11: 0.1464 S12: -1.3403 S13: 0.1569 REMARK 3 S21: 0.1272 S22: -0.0250 S23: 0.1084 REMARK 3 S31: -0.1239 S32: -0.3649 S33: 0.0649 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 84 THROUGH 100 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.4197 -28.3291 30.0126 REMARK 3 T TENSOR REMARK 3 T11: 0.2471 T22: 0.5404 REMARK 3 T33: 0.1620 T12: -0.0619 REMARK 3 T13: 0.0136 T23: 0.0136 REMARK 3 L TENSOR REMARK 3 L11: 1.6666 L22: 0.0979 REMARK 3 L33: 2.4291 L12: 0.1869 REMARK 3 L13: 0.8778 L23: -0.0927 REMARK 3 S TENSOR REMARK 3 S11: 0.2494 S12: -1.0007 S13: -0.1596 REMARK 3 S21: 0.1643 S22: 0.0079 S23: 0.0996 REMARK 3 S31: 0.1625 S32: -0.0655 S33: -0.1978 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 101 THROUGH 136 ) REMARK 3 ORIGIN FOR THE GROUP (A): -29.7742 -27.2514 21.3221 REMARK 3 T TENSOR REMARK 3 T11: 0.1746 T22: 0.3083 REMARK 3 T33: 0.1288 T12: -0.0313 REMARK 3 T13: 0.0322 T23: -0.0375 REMARK 3 L TENSOR REMARK 3 L11: 2.2375 L22: 0.5531 REMARK 3 L33: 2.1536 L12: 0.1980 REMARK 3 L13: 1.2875 L23: 0.4294 REMARK 3 S TENSOR REMARK 3 S11: 0.0678 S12: -0.7097 S13: 0.0253 REMARK 3 S21: 0.0613 S22: -0.0613 S23: 0.0647 REMARK 3 S31: -0.0483 S32: -0.1199 S33: -0.1257 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 137 THROUGH 160 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.8109 -22.1061 40.2300 REMARK 3 T TENSOR REMARK 3 T11: 0.3267 T22: 1.2094 REMARK 3 T33: 0.2870 T12: -0.0838 REMARK 3 T13: -0.0481 T23: 0.0265 REMARK 3 L TENSOR REMARK 3 L11: 0.4619 L22: 2.3011 REMARK 3 L33: 1.8442 L12: -0.4892 REMARK 3 L13: 0.8171 L23: -0.0240 REMARK 3 S TENSOR REMARK 3 S11: -0.1575 S12: 0.1498 S13: 0.0234 REMARK 3 S21: -0.2381 S22: 0.1163 S23: -0.4078 REMARK 3 S31: -0.1814 S32: 1.1090 S33: 0.1843 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 161 THROUGH 174 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.2387 -17.3469 41.6206 REMARK 3 T TENSOR REMARK 3 T11: 0.4801 T22: 1.0656 REMARK 3 T33: 0.2622 T12: -0.0222 REMARK 3 T13: -0.1111 T23: -0.0488 REMARK 3 L TENSOR REMARK 3 L11: 2.4602 L22: 0.9177 REMARK 3 L33: 3.1891 L12: -0.2273 REMARK 3 L13: -0.0710 L23: -0.6423 REMARK 3 S TENSOR REMARK 3 S11: -0.1478 S12: -0.3450 S13: 0.3007 REMARK 3 S21: 0.0026 S22: -0.0320 S23: -0.0343 REMARK 3 S31: -0.8176 S32: 0.3272 S33: 0.3090 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 175 THROUGH 205 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.0280 -20.2585 36.2594 REMARK 3 T TENSOR REMARK 3 T11: 0.3891 T22: 0.8986 REMARK 3 T33: 0.2253 T12: -0.0941 REMARK 3 T13: -0.0697 T23: 0.0062 REMARK 3 L TENSOR REMARK 3 L11: 3.3308 L22: 1.2495 REMARK 3 L33: 2.7482 L12: -0.6004 REMARK 3 L13: 1.7222 L23: 0.3197 REMARK 3 S TENSOR REMARK 3 S11: 0.1223 S12: -0.2409 S13: 0.2902 REMARK 3 S21: 0.0911 S22: -0.3183 S23: -0.2487 REMARK 3 S31: -0.7067 S32: 0.4245 S33: 0.1254 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 206 THROUGH 217 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.5289 -12.9442 44.1963 REMARK 3 T TENSOR REMARK 3 T11: 0.7652 T22: 1.0624 REMARK 3 T33: 0.4051 T12: -0.2633 REMARK 3 T13: -0.1239 T23: -0.0101 REMARK 3 L TENSOR REMARK 3 L11: 7.4196 L22: 1.3093 REMARK 3 L33: 2.5312 L12: 0.9260 REMARK 3 L13: 2.0698 L23: -0.0081 REMARK 3 S TENSOR REMARK 3 S11: -0.2827 S12: -0.3906 S13: 0.7955 REMARK 3 S21: 0.2330 S22: 0.0667 S23: -0.3412 REMARK 3 S31: -0.8961 S32: 0.8643 S33: 0.3888 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 218 THROUGH 232 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.0777 -17.2910 48.0628 REMARK 3 T TENSOR REMARK 3 T11: 0.5158 T22: 1.3173 REMARK 3 T33: 0.3889 T12: 0.0133 REMARK 3 T13: -0.0653 T23: -0.0786 REMARK 3 L TENSOR REMARK 3 L11: 5.3559 L22: 1.7605 REMARK 3 L33: 0.9095 L12: -2.7865 REMARK 3 L13: 1.9380 L23: -1.2642 REMARK 3 S TENSOR REMARK 3 S11: 0.0977 S12: -0.0037 S13: 0.3958 REMARK 3 S21: 0.0275 S22: 0.0501 S23: -0.2747 REMARK 3 S31: -0.4353 S32: 0.4910 S33: 0.4104 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 3 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.1987 -34.0399 8.6292 REMARK 3 T TENSOR REMARK 3 T11: 0.2065 T22: 0.0881 REMARK 3 T33: 0.2079 T12: -0.0065 REMARK 3 T13: 0.0011 T23: 0.0363 REMARK 3 L TENSOR REMARK 3 L11: 2.5425 L22: 1.3564 REMARK 3 L33: 1.3057 L12: 0.7137 REMARK 3 L13: 0.2870 L23: 0.2106 REMARK 3 S TENSOR REMARK 3 S11: -0.0869 S12: -0.2175 S13: -0.4781 REMARK 3 S21: 0.0391 S22: 0.0857 S23: -0.1068 REMARK 3 S31: 0.2401 S32: -0.0534 S33: 0.0447 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 26 THROUGH 49 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.5286 -29.3951 11.9221 REMARK 3 T TENSOR REMARK 3 T11: 0.1615 T22: 0.0919 REMARK 3 T33: 0.1356 T12: -0.0320 REMARK 3 T13: 0.0133 T23: -0.0033 REMARK 3 L TENSOR REMARK 3 L11: 3.1360 L22: 0.3425 REMARK 3 L33: 1.8035 L12: 0.1997 REMARK 3 L13: 0.3360 L23: 0.2597 REMARK 3 S TENSOR REMARK 3 S11: 0.0780 S12: -0.4929 S13: 0.1558 REMARK 3 S21: 0.0737 S22: -0.1482 S23: 0.1507 REMARK 3 S31: 0.0210 S32: -0.0462 S33: 0.0293 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 50 THROUGH 70 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.1602 -26.4045 2.0325 REMARK 3 T TENSOR REMARK 3 T11: 0.2149 T22: 0.0791 REMARK 3 T33: 0.2368 T12: -0.0220 REMARK 3 T13: 0.0198 T23: -0.0066 REMARK 3 L TENSOR REMARK 3 L11: 2.7066 L22: 0.9875 REMARK 3 L33: 2.0681 L12: 0.6545 REMARK 3 L13: 0.4322 L23: 0.4592 REMARK 3 S TENSOR REMARK 3 S11: -0.0153 S12: 0.3294 S13: 0.1616 REMARK 3 S21: -0.2676 S22: -0.0081 S23: -0.0737 REMARK 3 S31: -0.1939 S32: 0.0335 S33: 0.1694 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 71 THROUGH 84 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.7359 -26.0526 4.5616 REMARK 3 T TENSOR REMARK 3 T11: 0.1778 T22: 0.0721 REMARK 3 T33: 0.1758 T12: -0.0257 REMARK 3 T13: 0.0061 T23: -0.0149 REMARK 3 L TENSOR REMARK 3 L11: 2.3307 L22: 0.1171 REMARK 3 L33: 1.9005 L12: -0.1024 REMARK 3 L13: 0.5257 L23: 0.3297 REMARK 3 S TENSOR REMARK 3 S11: -0.0184 S12: -0.0730 S13: 0.0824 REMARK 3 S21: 0.0820 S22: -0.0638 S23: 0.0314 REMARK 3 S31: -0.1299 S32: 0.0329 S33: 0.1091 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 85 THROUGH 104 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.3163 -35.1480 15.6561 REMARK 3 T TENSOR REMARK 3 T11: 0.2073 T22: 0.1418 REMARK 3 T33: 0.1906 T12: -0.0675 REMARK 3 T13: 0.0178 T23: 0.0071 REMARK 3 L TENSOR REMARK 3 L11: 3.3687 L22: 1.0425 REMARK 3 L33: 1.2717 L12: 0.6656 REMARK 3 L13: 0.6600 L23: 0.7816 REMARK 3 S TENSOR REMARK 3 S11: 0.0037 S12: -0.5648 S13: -0.3681 REMARK 3 S21: 0.0880 S22: -0.1449 S23: 0.0304 REMARK 3 S31: 0.2996 S32: -0.0745 S33: 0.0649 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 105 THROUGH 117 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.2154 -25.9888 12.8919 REMARK 3 T TENSOR REMARK 3 T11: 0.1731 T22: 0.1555 REMARK 3 T33: 0.1480 T12: -0.0075 REMARK 3 T13: 0.0111 T23: 0.0280 REMARK 3 L TENSOR REMARK 3 L11: 3.2865 L22: 0.5074 REMARK 3 L33: 1.7576 L12: 0.3023 REMARK 3 L13: 0.8257 L23: 0.5019 REMARK 3 S TENSOR REMARK 3 S11: 0.0441 S12: -0.5414 S13: 0.1314 REMARK 3 S21: 0.0274 S22: -0.1018 S23: -0.0110 REMARK 3 S31: 0.1253 S32: 0.3244 S33: 0.0071 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 118 THROUGH 154 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.6295 -30.6856 35.0289 REMARK 3 T TENSOR REMARK 3 T11: 0.3315 T22: 0.8402 REMARK 3 T33: 0.1896 T12: 0.1163 REMARK 3 T13: -0.0371 T23: 0.1067 REMARK 3 L TENSOR REMARK 3 L11: 0.4121 L22: 0.0426 REMARK 3 L33: 2.5118 L12: -0.1569 REMARK 3 L13: 1.0312 L23: -0.3522 REMARK 3 S TENSOR REMARK 3 S11: -0.0607 S12: -0.7704 S13: -0.0722 REMARK 3 S21: 0.1105 S22: 0.0108 S23: -0.1398 REMARK 3 S31: 0.5282 S32: 0.5742 S33: -0.1927 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 155 THROUGH 165 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.2306 -41.6740 33.8533 REMARK 3 T TENSOR REMARK 3 T11: 0.7935 T22: 0.8528 REMARK 3 T33: 0.4285 T12: 0.1330 REMARK 3 T13: -0.0183 T23: 0.2198 REMARK 3 L TENSOR REMARK 3 L11: 1.5890 L22: 0.9650 REMARK 3 L33: 0.1416 L12: -0.5370 REMARK 3 L13: 0.4735 L23: -0.1456 REMARK 3 S TENSOR REMARK 3 S11: -0.0033 S12: -1.0579 S13: -0.9879 REMARK 3 S21: 0.2590 S22: 0.0475 S23: 0.0375 REMARK 3 S31: 0.8285 S32: 0.4296 S33: -0.1471 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 166 THROUGH 177 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.1778 -21.2972 22.5929 REMARK 3 T TENSOR REMARK 3 T11: 0.2120 T22: 0.3590 REMARK 3 T33: 0.2146 T12: -0.0139 REMARK 3 T13: -0.0180 T23: -0.0360 REMARK 3 L TENSOR REMARK 3 L11: 4.6846 L22: 2.9868 REMARK 3 L33: 3.9967 L12: 0.3493 REMARK 3 L13: -0.0496 L23: -0.1014 REMARK 3 S TENSOR REMARK 3 S11: 0.1705 S12: -0.5416 S13: 0.4309 REMARK 3 S21: 0.0845 S22: -0.0533 S23: 0.1266 REMARK 3 S31: -0.3545 S32: 0.0949 S33: -0.0148 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 178 THROUGH 191 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.2249 -37.1882 41.3645 REMARK 3 T TENSOR REMARK 3 T11: 0.6537 T22: 1.0523 REMARK 3 T33: 0.3177 T12: 0.2577 REMARK 3 T13: -0.0031 T23: 0.2812 REMARK 3 L TENSOR REMARK 3 L11: 1.0306 L22: 0.1553 REMARK 3 L33: 1.3391 L12: -0.1411 REMARK 3 L13: 1.0492 L23: -0.1342 REMARK 3 S TENSOR REMARK 3 S11: -0.0913 S12: -0.8057 S13: -0.4742 REMARK 3 S21: 0.3266 S22: -0.0884 S23: -0.3085 REMARK 3 S31: 0.8403 S32: 0.5103 S33: -0.1973 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 192 THROUGH 201 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.2070 -37.8678 30.9115 REMARK 3 T TENSOR REMARK 3 T11: 0.5872 T22: 0.9020 REMARK 3 T33: 0.3222 T12: 0.3438 REMARK 3 T13: -0.0009 T23: 0.1771 REMARK 3 L TENSOR REMARK 3 L11: 2.5963 L22: 1.9500 REMARK 3 L33: 7.6762 L12: -0.6896 REMARK 3 L13: 4.1049 L23: -2.5377 REMARK 3 S TENSOR REMARK 3 S11: 0.0407 S12: -0.7638 S13: -0.6304 REMARK 3 S21: 0.3538 S22: 0.1233 S23: -0.1670 REMARK 3 S31: 0.7465 S32: 0.7856 S33: -0.1999 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 202 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.4495 -34.2862 27.0371 REMARK 3 T TENSOR REMARK 3 T11: 0.4144 T22: 0.9072 REMARK 3 T33: 0.2506 T12: 0.2450 REMARK 3 T13: -0.0227 T23: 0.0829 REMARK 3 L TENSOR REMARK 3 L11: 1.6284 L22: 0.1916 REMARK 3 L33: 7.1978 L12: 0.2131 REMARK 3 L13: 3.3877 L23: 0.2860 REMARK 3 S TENSOR REMARK 3 S11: 0.1075 S12: -0.6564 S13: -0.2153 REMARK 3 S21: 0.1483 S22: 0.0795 S23: -0.2464 REMARK 3 S31: 0.4434 S32: 0.5943 S33: -0.1388 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 9FIK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1292138788. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-JAN-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID30B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.8856 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : STARANISO REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51862 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.859 REMARK 200 RESOLUTION RANGE LOW (A) : 58.680 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.2 REMARK 200 DATA REDUNDANCY : 13.40 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03 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: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.50 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 15 % W/V POLYETHYLENE GLYCOL 8,000, REMARK 280 0.2 M SODIUM ACETATE, 0.1 M MES PH 6.5, VAPOR DIFFUSION, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 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 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 104.10850 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 104.10850 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 34.87300 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.27450 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.87300 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.27450 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 104.10850 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.87300 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 54.27450 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 104.10850 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.87300 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 54.27450 REMARK 290 SMTRY3 8 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6250 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 26530 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 TYR A 1 REMARK 465 ALA A 2 REMARK 465 GLU A 3 REMARK 465 HIS A 4 REMARK 465 LYS A 5 REMARK 465 SER A 6 REMARK 465 HIS A 7 REMARK 465 ARG A 8 REMARK 465 GLY A 9 REMARK 465 GLU A 10 REMARK 465 ILE A 116 REMARK 465 GLY A 117 REMARK 465 ARG A 118 REMARK 465 THR A 119 REMARK 465 GLU A 120 REMARK 465 SER B 145 REMARK 465 LYS B 146 REMARK 465 SER B 147 REMARK 465 THR B 148 REMARK 465 CYS B 233 REMARK 465 ASP B 234 REMARK 465 LYS B 235 REMARK 465 THR C 213 REMARK 465 GLU C 214 REMARK 465 CYS C 215 REMARK 465 SER C 216 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 C 18 O HOH C 401 2.05 REMARK 500 OD1 ASP C 93 O HOH C 402 2.14 REMARK 500 O HOH A 339 O HOH A 385 2.17 REMARK 500 O HOH C 479 O HOH C 611 2.19 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 O HOH A 336 O HOH A 336 4545 1.83 REMARK 500 O HOH A 310 O HOH A 310 4545 1.90 REMARK 500 O HOH A 381 O HOH A 381 4545 1.94 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 A 71 95.95 -69.76 REMARK 500 LYS B 41 -169.81 -117.79 REMARK 500 TYR B 115 63.74 69.61 REMARK 500 ASP B 161 60.49 60.31 REMARK 500 SER C 27 -131.78 53.16 REMARK 500 ASP C 52 -43.86 72.64 REMARK 500 SER C 53 7.49 -150.58 REMARK 500 ASP C 155 -100.60 49.64 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH C 632 DISTANCE = 5.82 ANGSTROMS REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 PEG C 303 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 NA C 304 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU C 202 OE1 REMARK 620 2 HOH C 426 O 116.6 REMARK 620 3 HOH C 600 O 83.4 132.7 REMARK 620 4 HOH C 617 O 105.8 114.9 97.6 REMARK 620 N 1 2 3 DBREF 9FIK A 1 119 UNP P20783 NTF3_HUMAN 139 257 DBREF 9FIK B -1 235 PDB 9FIK 9FIK -1 235 DBREF 9FIK C 3 216 PDB 9FIK 9FIK 3 216 SEQADV 9FIK GLU A 120 UNP P20783 EXPRESSION TAG SEQRES 1 A 120 TYR ALA GLU HIS LYS SER HIS ARG GLY GLU TYR SER VAL SEQRES 2 A 120 CYS ASP SER GLU SER LEU TRP VAL THR ASP LYS SER SER SEQRES 3 A 120 ALA ILE ASP ILE ARG GLY HIS GLN VAL THR VAL LEU GLY SEQRES 4 A 120 GLU ILE LYS THR GLY ASN SER PRO VAL LYS GLN TYR PHE SEQRES 5 A 120 TYR GLU THR ARG CYS LYS GLU ALA ARG PRO VAL LYS ASN SEQRES 6 A 120 GLY CYS ARG GLY ILE ASP ASP LYS HIS TRP ASN SER GLN SEQRES 7 A 120 CYS LYS THR SER GLN THR TYR VAL ARG ALA LEU THR SER SEQRES 8 A 120 GLU ASN ASN LYS LEU VAL GLY TRP ARG TRP ILE ARG ILE SEQRES 9 A 120 ASP THR SER CYS VAL CYS ALA LEU SER ARG LYS ILE GLY SEQRES 10 A 120 ARG THR GLU SEQRES 1 B 237 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 B 237 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 237 PHE THR PHE SER ASN ALA TRP MET ASN TRP VAL ARG GLN SEQRES 4 B 237 ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY ARG ILE LYS SEQRES 5 B 237 SER LYS THR ASP GLY GLY THR THR ASP TYR ALA ALA PRO SEQRES 6 B 237 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP SER LYS SEQRES 7 B 237 ASN THR LEU TYR LEU GLN MET ASN SER LEU LYS THR GLU SEQRES 8 B 237 ASP THR ALA VAL TYR TYR CYS THR THR SER GLY GLY LEU SEQRES 9 B 237 LEU TYR GLY SER PRO SER PHE GLY ASP TYR TYR GLY TYR SEQRES 10 B 237 TRP MET ASP TYR TRP GLY GLN GLY THR THR VAL THR VAL SEQRES 11 B 237 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 12 B 237 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 13 B 237 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 14 B 237 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 15 B 237 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 16 B 237 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 17 B 237 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 18 B 237 SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER SEQRES 19 B 237 CYS ASP LYS SEQRES 1 C 214 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER VAL ALA SEQRES 2 C 214 PRO GLY GLN THR ALA ARG ILE THR CYS GLY GLY SER SER SEQRES 3 C 214 VAL GLY ARG LYS SER VAL HIS TRP TYR GLN GLN SER PRO SEQRES 4 C 214 GLY GLN ALA PRO VAL LEU VAL VAL TYR ASP ASP SER ASP SEQRES 5 C 214 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER ASN SEQRES 6 C 214 SER GLY ASP THR ALA THR LEU THR ILE SER ARG VAL GLU SEQRES 7 C 214 VAL GLY ASP GLU ALA ASP TYR TYR CYS GLN VAL TRP ASP SEQRES 8 C 214 ILE ASP SER ASP HIS VAL VAL PHE GLY GLY GLY THR LYS SEQRES 9 C 214 VAL THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL SEQRES 10 C 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN SEQRES 11 C 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO SEQRES 12 C 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO SEQRES 13 C 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SEQRES 14 C 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU SEQRES 15 C 214 THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS SEQRES 16 C 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL SEQRES 17 C 214 ALA PRO THR GLU CYS SER HET GOL A 201 6 HET GOL A 202 6 HET GOL A 203 6 HET GOL B 301 6 HET PEG C 301 7 HET GOL C 302 6 HET PEG C 303 6 HET NA C 304 1 HETNAM GOL GLYCEROL HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM NA SODIUM ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 4 GOL 5(C3 H8 O3) FORMUL 8 PEG 2(C4 H10 O3) FORMUL 11 NA NA 1+ FORMUL 12 HOH *477(H2 O) HELIX 1 AA1 THR B 26 ALA B 30 5 5 HELIX 2 AA2 ALA B 62 LYS B 65 5 4 HELIX 3 AA3 LYS B 87 THR B 91 5 5 HELIX 4 AA4 SER B 173 ALA B 175 5 3 HELIX 5 AA5 SER B 204 LEU B 206 5 3 HELIX 6 AA6 GLU C 80 GLU C 84 5 5 HELIX 7 AA7 SER C 125 GLN C 130 1 6 HELIX 8 AA8 THR C 185 HIS C 192 1 8 SHEET 1 AA1 2 SER A 16 VAL A 21 0 SHEET 2 AA1 2 PHE A 52 CYS A 57 -1 O PHE A 52 N VAL A 21 SHEET 1 AA2 4 SER A 26 ILE A 28 0 SHEET 2 AA2 4 GLN A 34 VAL A 37 -1 O VAL A 35 N ALA A 27 SHEET 3 AA2 4 TRP A 75 GLU A 92 -1 O SER A 91 N THR A 36 SHEET 4 AA2 4 LYS A 95 ARG A 114 -1 O SER A 113 N ASN A 76 SHEET 1 AA3 2 GLU A 40 ILE A 41 0 SHEET 2 AA3 2 VAL A 48 LYS A 49 -1 O VAL A 48 N ILE A 41 SHEET 1 AA4 4 GLN B 1 SER B 5 0 SHEET 2 AA4 4 LEU B 16 SER B 23 -1 O SER B 23 N GLN B 1 SHEET 3 AA4 4 THR B 78 MET B 83 -1 O MET B 83 N LEU B 16 SHEET 4 AA4 4 PHE B 68 ASP B 73 -1 N SER B 71 O TYR B 80 SHEET 1 AA5 6 LEU B 9 VAL B 10 0 SHEET 2 AA5 6 THR B 124 VAL B 128 1 O THR B 127 N VAL B 10 SHEET 3 AA5 6 ALA B 92 GLY B 100 -1 N TYR B 94 O THR B 124 SHEET 4 AA5 6 TRP B 31 GLN B 37 -1 N VAL B 35 O TYR B 95 SHEET 5 AA5 6 LEU B 43 ILE B 49 -1 O GLU B 44 N ARG B 36 SHEET 6 AA5 6 THR B 58 TYR B 60 -1 O ASP B 59 N ARG B 48 SHEET 1 AA6 4 LEU B 9 VAL B 10 0 SHEET 2 AA6 4 THR B 124 VAL B 128 1 O THR B 127 N VAL B 10 SHEET 3 AA6 4 ALA B 92 GLY B 100 -1 N TYR B 94 O THR B 124 SHEET 4 AA6 4 TRP B 116 TRP B 120 -1 O TRP B 116 N GLY B 100 SHEET 1 AA7 4 SER B 137 LEU B 141 0 SHEET 2 AA7 4 THR B 152 TYR B 162 -1 O GLY B 156 N LEU B 141 SHEET 3 AA7 4 TYR B 193 PRO B 202 -1 O LEU B 195 N VAL B 159 SHEET 4 AA7 4 VAL B 180 THR B 182 -1 N HIS B 181 O VAL B 198 SHEET 1 AA8 4 SER B 137 LEU B 141 0 SHEET 2 AA8 4 THR B 152 TYR B 162 -1 O GLY B 156 N LEU B 141 SHEET 3 AA8 4 TYR B 193 PRO B 202 -1 O LEU B 195 N VAL B 159 SHEET 4 AA8 4 VAL B 186 LEU B 187 -1 N VAL B 186 O SER B 194 SHEET 1 AA9 3 THR B 168 TRP B 171 0 SHEET 2 AA9 3 TYR B 211 HIS B 217 -1 O ASN B 216 N THR B 168 SHEET 3 AA9 3 THR B 222 VAL B 228 -1 O VAL B 224 N VAL B 215 SHEET 1 AB1 4 LEU C 6 THR C 7 0 SHEET 2 AB1 4 ALA C 20 GLY C 26 -1 O GLY C 25 N THR C 7 SHEET 3 AB1 4 THR C 71 ILE C 76 -1 O ALA C 72 N CYS C 24 SHEET 4 AB1 4 PHE C 63 ASN C 67 -1 N SER C 64 O THR C 75 SHEET 1 AB2 5 SER C 11 VAL C 14 0 SHEET 2 AB2 5 THR C 105 VAL C 109 1 O THR C 108 N VAL C 12 SHEET 3 AB2 5 ALA C 85 ASP C 93 -1 N ALA C 85 O VAL C 107 SHEET 4 AB2 5 HIS C 35 GLN C 39 -1 N GLN C 39 O ASP C 86 SHEET 5 AB2 5 VAL C 46 VAL C 49 -1 O VAL C 49 N TRP C 36 SHEET 1 AB3 4 SER C 11 VAL C 14 0 SHEET 2 AB3 4 THR C 105 VAL C 109 1 O THR C 108 N VAL C 12 SHEET 3 AB3 4 ALA C 85 ASP C 93 -1 N ALA C 85 O VAL C 107 SHEET 4 AB3 4 HIS C 98 PHE C 101 -1 O HIS C 98 N ASP C 93 SHEET 1 AB4 4 SER C 118 PHE C 122 0 SHEET 2 AB4 4 ALA C 134 PHE C 143 -1 O LEU C 139 N THR C 120 SHEET 3 AB4 4 TYR C 176 LEU C 184 -1 O ALA C 178 N ILE C 140 SHEET 4 AB4 4 VAL C 163 THR C 165 -1 N GLU C 164 O TYR C 181 SHEET 1 AB5 4 SER C 118 PHE C 122 0 SHEET 2 AB5 4 ALA C 134 PHE C 143 -1 O LEU C 139 N THR C 120 SHEET 3 AB5 4 TYR C 176 LEU C 184 -1 O ALA C 178 N ILE C 140 SHEET 4 AB5 4 SER C 169 LYS C 170 -1 N SER C 169 O ALA C 177 SHEET 1 AB6 4 SER C 157 VAL C 159 0 SHEET 2 AB6 4 THR C 149 ALA C 154 -1 N ALA C 154 O SER C 157 SHEET 3 AB6 4 TYR C 195 HIS C 201 -1 O THR C 200 N THR C 149 SHEET 4 AB6 4 SER C 204 VAL C 210 -1 O VAL C 206 N VAL C 199 SSBOND 1 CYS A 14 CYS A 79 1555 1555 2.06 SSBOND 2 CYS A 57 CYS A 108 1555 1555 2.05 SSBOND 3 CYS A 67 CYS A 110 1555 1555 2.05 SSBOND 4 CYS B 20 CYS B 96 1555 1555 2.07 SSBOND 5 CYS B 157 CYS B 213 1555 1555 2.06 SSBOND 6 CYS C 24 CYS C 89 1555 1555 2.07 SSBOND 7 CYS C 138 CYS C 197 1555 1555 2.06 LINK OE1 GLU C 202 NA NA C 304 1555 1555 2.55 LINK NA NA C 304 O HOH C 426 1555 1555 2.81 LINK NA NA C 304 O HOH C 600 1555 1555 3.15 LINK NA NA C 304 O HOH C 617 1555 1555 2.78 CISPEP 1 PHE B 163 PRO B 164 0 -8.79 CISPEP 2 GLU B 165 PRO B 166 0 -2.57 CISPEP 3 TYR C 144 PRO C 145 0 1.12 CRYST1 69.746 108.549 208.217 90.00 90.00 90.00 C 2 2 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.014338 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009212 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004803 0.00000