HEADER IMMUNE SYSTEM 06-AUG-23 8TQ5 TITLE CRYSTAL STRUCTURE OF FAB DX17 IN COMPLEX WITH MHC-I (HLA-B*44:05) COMPND MOL_ID: 1; COMPND 2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN B ALPHA CHAIN (HLA- COMPND 3 B*44:05); COMPND 4 CHAIN: A; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: BETA-2-MICROGLOBULIN; COMPND 8 CHAIN: B; COMPND 9 FRAGMENT: UNP RESIDUES 21-119; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: MHC CLASS II ANTIGEN; COMPND 13 CHAIN: P; COMPND 14 FRAGMENT: HLA-DPA1*02:01 DERIVED PEPTIDE 77-85 (UNP RESIDUES 36-44); COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: FAB DX17 H-CHAIN; COMPND 18 CHAIN: H; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 5; COMPND 21 MOLECULE: FAB DX17 L-CHAIN; COMPND 22 CHAIN: L; COMPND 23 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: HLA-B; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21B; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 GENE: B2M, CDABP0092, HDCMA22P; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET3A; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 21 ORGANISM_COMMON: HUMAN; SOURCE 22 ORGANISM_TAXID: 9606; SOURCE 23 GENE: HLA-DPA1; SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 26 MOL_ID: 4; SOURCE 27 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 28 ORGANISM_COMMON: MOUSE; SOURCE 29 ORGANISM_TAXID: 10090; SOURCE 30 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 31 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 33 EXPRESSION_SYSTEM_CELL: EXPI293F; SOURCE 34 MOL_ID: 5; SOURCE 35 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 36 ORGANISM_COMMON: MOUSE; SOURCE 37 ORGANISM_TAXID: 10090; SOURCE 38 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 39 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 40 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 41 EXPRESSION_SYSTEM_CELL: EXPI293F; SOURCE 42 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 43 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1 KEYWDS HISTOCOMPATIBILITY COMPLEX CLASS I, MHC-I, IMMUNE RESPONSE, IMMUNE KEYWDS 2 SYSTEM FAB, ANTIBODY, ANTI-MHC ANTIBODY, CANCER TUMOR, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.JIANG,K.NATARAJAN,L.F.BOYD,D.H.MARGULIES REVDAT 1 05-FEB-25 8TQ5 0 JRNL AUTH J.JIANG,K.NATARAJAN,L.F.BOYD,D.H.MARGULIES JRNL TITL CRYSTAL STRUCTURE OF FAB DX17 IN COMPLEX WITH MHC-I JRNL TITL 2 (HLA-B*44:05) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.30 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) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.24 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 3 NUMBER OF REFLECTIONS : 46941 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.195 REMARK 3 R VALUE (WORKING SET) : 0.193 REMARK 3 FREE R VALUE : 0.234 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.260 REMARK 3 FREE R VALUE TEST SET COUNT : 2000 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 43.2400 - 5.5400 0.97 3404 151 0.1708 0.1900 REMARK 3 2 5.5400 - 4.4000 1.00 3324 148 0.1386 0.1562 REMARK 3 3 4.4000 - 3.8400 0.96 3171 141 0.1565 0.1873 REMARK 3 4 3.8400 - 3.4900 0.99 3260 146 0.1888 0.2643 REMARK 3 5 3.4900 - 3.2400 0.99 3259 144 0.2009 0.2649 REMARK 3 6 3.2400 - 3.0500 0.99 3219 144 0.2185 0.2757 REMARK 3 7 3.0500 - 2.9000 0.94 3084 137 0.2190 0.2472 REMARK 3 8 2.9000 - 2.7700 0.99 3209 143 0.2217 0.2669 REMARK 3 9 2.7700 - 2.6700 0.99 3195 142 0.2261 0.2858 REMARK 3 10 2.6700 - 2.5700 0.99 3221 143 0.2395 0.3080 REMARK 3 11 2.5700 - 2.4900 0.99 3189 142 0.2510 0.3152 REMARK 3 12 2.4900 - 2.4200 0.99 3171 141 0.2480 0.2702 REMARK 3 13 2.4200 - 2.3600 0.98 3182 142 0.2645 0.3203 REMARK 3 14 2.3600 - 2.3000 0.95 3053 136 0.2942 0.3410 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) : 0.277 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.962 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 39.68 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.64 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 : 0.003 6583 REMARK 3 ANGLE : 0.653 8973 REMARK 3 CHIRALITY : 0.049 977 REMARK 3 PLANARITY : 0.004 1164 REMARK 3 DIHEDRAL : 16.513 2366 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 23 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 56 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.2003 -2.2238 19.3605 REMARK 3 T TENSOR REMARK 3 T11: 0.7917 T22: 0.3583 REMARK 3 T33: 0.5092 T12: -0.0113 REMARK 3 T13: -0.0990 T23: -0.0298 REMARK 3 L TENSOR REMARK 3 L11: 3.1793 L22: 3.1463 REMARK 3 L33: 6.1310 L12: 0.2278 REMARK 3 L13: -1.9259 L23: -1.3758 REMARK 3 S TENSOR REMARK 3 S11: -0.1014 S12: -0.0902 S13: -0.5650 REMARK 3 S21: -0.3700 S22: -0.0932 S23: -0.1271 REMARK 3 S31: 1.3912 S32: 0.2636 S33: 0.2183 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 57 THROUGH 84 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.6298 -5.8792 8.0363 REMARK 3 T TENSOR REMARK 3 T11: 1.2959 T22: 0.5122 REMARK 3 T33: 0.6681 T12: -0.0604 REMARK 3 T13: -0.0334 T23: -0.1935 REMARK 3 L TENSOR REMARK 3 L11: 1.9283 L22: 2.9661 REMARK 3 L33: 5.4018 L12: 0.5999 REMARK 3 L13: -0.6956 L23: -3.2008 REMARK 3 S TENSOR REMARK 3 S11: -0.2749 S12: 0.3963 S13: -0.8466 REMARK 3 S21: -1.3300 S22: 0.2719 S23: -0.1329 REMARK 3 S31: 1.8864 S32: -0.2154 S33: 0.0521 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 85 THROUGH 174 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.3268 4.6646 9.7322 REMARK 3 T TENSOR REMARK 3 T11: 0.8170 T22: 0.5037 REMARK 3 T33: 0.5850 T12: -0.2010 REMARK 3 T13: -0.1882 T23: -0.0457 REMARK 3 L TENSOR REMARK 3 L11: 1.8361 L22: 1.2691 REMARK 3 L33: 3.3783 L12: 0.3753 REMARK 3 L13: 0.7739 L23: -0.8817 REMARK 3 S TENSOR REMARK 3 S11: 0.0081 S12: 0.1856 S13: -0.1970 REMARK 3 S21: -0.5276 S22: 0.2031 S23: 0.3340 REMARK 3 S31: 0.7444 S32: -0.7097 S33: -0.1291 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 175 THROUGH 197 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.1403 17.3019 42.0880 REMARK 3 T TENSOR REMARK 3 T11: 0.3325 T22: 0.5269 REMARK 3 T33: 0.2370 T12: -0.0527 REMARK 3 T13: 0.0420 T23: 0.0158 REMARK 3 L TENSOR REMARK 3 L11: 2.0394 L22: 6.8413 REMARK 3 L33: 2.3351 L12: -0.1272 REMARK 3 L13: 0.6633 L23: 2.1487 REMARK 3 S TENSOR REMARK 3 S11: -0.2967 S12: 0.3786 S13: 0.0196 REMARK 3 S21: -0.2209 S22: 0.7185 S23: 0.0129 REMARK 3 S31: 0.2158 S32: -0.0030 S33: -0.3666 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 198 THROUGH 267 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.3002 24.0491 38.8052 REMARK 3 T TENSOR REMARK 3 T11: 0.2051 T22: 0.3288 REMARK 3 T33: 0.2686 T12: -0.0372 REMARK 3 T13: 0.0253 T23: 0.0250 REMARK 3 L TENSOR REMARK 3 L11: 1.4231 L22: 7.5825 REMARK 3 L33: 4.3407 L12: -2.0438 REMARK 3 L13: -0.2781 L23: 2.9466 REMARK 3 S TENSOR REMARK 3 S11: 0.1775 S12: -0.1641 S13: 0.0025 REMARK 3 S21: -0.4719 S22: -0.0185 S23: 0.1794 REMARK 3 S31: -0.1442 S32: -0.3008 S33: -0.1803 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 11 ) REMARK 3 ORIGIN FOR THE GROUP (A): 31.4541 17.3609 21.2930 REMARK 3 T TENSOR REMARK 3 T11: 0.3930 T22: 0.2953 REMARK 3 T33: 0.3317 T12: 0.0358 REMARK 3 T13: 0.0047 T23: -0.0081 REMARK 3 L TENSOR REMARK 3 L11: 3.3700 L22: 3.2789 REMARK 3 L33: 6.0009 L12: -1.1842 REMARK 3 L13: 1.1320 L23: -3.3030 REMARK 3 S TENSOR REMARK 3 S11: 0.1741 S12: 0.2872 S13: -0.1965 REMARK 3 S21: -0.4625 S22: 0.0503 S23: -0.0258 REMARK 3 S31: 1.1346 S32: 0.4322 S33: -0.2386 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 12 THROUGH 19 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.5838 10.0524 44.8507 REMARK 3 T TENSOR REMARK 3 T11: 0.3923 T22: 0.6362 REMARK 3 T33: 0.4185 T12: 0.0644 REMARK 3 T13: -0.0544 T23: 0.0564 REMARK 3 L TENSOR REMARK 3 L11: 4.0969 L22: 7.7308 REMARK 3 L33: 5.8058 L12: 1.1925 REMARK 3 L13: -0.4682 L23: -1.4536 REMARK 3 S TENSOR REMARK 3 S11: 0.5411 S12: -0.8012 S13: -0.7011 REMARK 3 S21: 0.9380 S22: 0.4518 S23: -0.0027 REMARK 3 S31: 0.6097 S32: -0.2335 S33: -1.1890 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 20 THROUGH 41 ) REMARK 3 ORIGIN FOR THE GROUP (A): 35.5947 10.7340 25.3722 REMARK 3 T TENSOR REMARK 3 T11: 0.4586 T22: 0.3161 REMARK 3 T33: 0.3127 T12: 0.0921 REMARK 3 T13: -0.0241 T23: -0.0260 REMARK 3 L TENSOR REMARK 3 L11: 3.8874 L22: 1.8544 REMARK 3 L33: 5.4415 L12: -0.5071 REMARK 3 L13: 4.4954 L23: -1.3986 REMARK 3 S TENSOR REMARK 3 S11: 0.2263 S12: 0.4497 S13: -0.2185 REMARK 3 S21: -0.3186 S22: 0.0233 S23: -0.0603 REMARK 3 S31: 0.4518 S32: 0.6023 S33: -0.1031 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 42 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): 43.4137 5.5843 29.1897 REMARK 3 T TENSOR REMARK 3 T11: 0.6780 T22: 0.6084 REMARK 3 T33: 0.6432 T12: 0.2693 REMARK 3 T13: -0.0482 T23: -0.0959 REMARK 3 L TENSOR REMARK 3 L11: 8.0838 L22: 4.6000 REMARK 3 L33: 3.4546 L12: 5.8887 REMARK 3 L13: 3.3332 L23: 1.6340 REMARK 3 S TENSOR REMARK 3 S11: 0.2346 S12: -0.1074 S13: -1.6451 REMARK 3 S21: -0.4976 S22: -0.1513 S23: -0.5890 REMARK 3 S31: 0.5812 S32: 0.5158 S33: 0.0057 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 52 THROUGH 71 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.1280 8.1513 24.1249 REMARK 3 T TENSOR REMARK 3 T11: 0.5678 T22: 0.3135 REMARK 3 T33: 0.4690 T12: 0.0562 REMARK 3 T13: -0.0290 T23: -0.0209 REMARK 3 L TENSOR REMARK 3 L11: 5.1179 L22: 2.5351 REMARK 3 L33: 6.5753 L12: -0.9687 REMARK 3 L13: 4.7048 L23: -0.7766 REMARK 3 S TENSOR REMARK 3 S11: 0.2319 S12: -0.0687 S13: -0.5605 REMARK 3 S21: -0.4368 S22: 0.1627 S23: -0.0268 REMARK 3 S31: 0.8963 S32: 0.2005 S33: -0.3497 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 72 THROUGH 77 ) REMARK 3 ORIGIN FOR THE GROUP (A): 45.9324 14.9687 42.7939 REMARK 3 T TENSOR REMARK 3 T11: 0.4897 T22: 0.5114 REMARK 3 T33: 0.5883 T12: -0.0050 REMARK 3 T13: 0.0099 T23: -0.1618 REMARK 3 L TENSOR REMARK 3 L11: 6.3711 L22: 3.4725 REMARK 3 L33: 6.1081 L12: -3.5510 REMARK 3 L13: 4.0269 L23: -4.3572 REMARK 3 S TENSOR REMARK 3 S11: 0.1007 S12: -0.5403 S13: 0.3947 REMARK 3 S21: 0.2410 S22: -0.3216 S23: -0.2409 REMARK 3 S31: -0.9635 S32: 0.3480 S33: 0.2067 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 78 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): 41.1901 16.4305 20.8187 REMARK 3 T TENSOR REMARK 3 T11: 0.4499 T22: 0.6691 REMARK 3 T33: 0.3074 T12: 0.1421 REMARK 3 T13: 0.0652 T23: 0.0682 REMARK 3 L TENSOR REMARK 3 L11: 4.8081 L22: 0.3835 REMARK 3 L33: 4.1016 L12: -0.1496 REMARK 3 L13: 4.4819 L23: -0.1148 REMARK 3 S TENSOR REMARK 3 S11: 0.2697 S12: 0.8975 S13: 0.1484 REMARK 3 S21: -0.3984 S22: 0.1555 S23: -0.1921 REMARK 3 S31: 0.0757 S32: 1.2208 S33: -0.1624 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 91 THROUGH 99 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.1762 19.6740 34.5311 REMARK 3 T TENSOR REMARK 3 T11: 0.3034 T22: 0.3944 REMARK 3 T33: 0.4408 T12: 0.0246 REMARK 3 T13: 0.0238 T23: -0.0318 REMARK 3 L TENSOR REMARK 3 L11: 9.0206 L22: 8.5163 REMARK 3 L33: 6.2924 L12: 1.1318 REMARK 3 L13: -3.0758 L23: -0.6332 REMARK 3 S TENSOR REMARK 3 S11: 0.2753 S12: 0.1247 S13: 1.2763 REMARK 3 S21: 0.5031 S22: -0.4185 S23: 0.1150 REMARK 3 S31: -0.4934 S32: -0.3878 S33: 0.1886 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'P' AND (RESID 1 THROUGH 9 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.6321 -4.0018 8.0627 REMARK 3 T TENSOR REMARK 3 T11: 1.2830 T22: 0.8137 REMARK 3 T33: 0.6265 T12: -0.2642 REMARK 3 T13: -0.1773 T23: -0.1923 REMARK 3 L TENSOR REMARK 3 L11: 2.6072 L22: 2.2775 REMARK 3 L33: 6.7879 L12: 1.1325 REMARK 3 L13: -2.7389 L23: -3.8322 REMARK 3 S TENSOR REMARK 3 S11: -0.1120 S12: 1.1764 S13: -0.2846 REMARK 3 S21: 0.0109 S22: 0.3826 S23: -0.0038 REMARK 3 S31: 0.3895 S32: -0.2335 S33: -0.0919 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 82 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.3482 34.1876 19.8687 REMARK 3 T TENSOR REMARK 3 T11: 0.2256 T22: 0.2650 REMARK 3 T33: 0.2587 T12: -0.0407 REMARK 3 T13: -0.0902 T23: 0.0066 REMARK 3 L TENSOR REMARK 3 L11: 2.0761 L22: 3.4709 REMARK 3 L33: 4.5103 L12: 0.0018 REMARK 3 L13: -0.5755 L23: -0.9490 REMARK 3 S TENSOR REMARK 3 S11: -0.1831 S12: 0.0026 S13: 0.2998 REMARK 3 S21: -0.0857 S22: 0.1535 S23: 0.1527 REMARK 3 S31: 0.0900 S32: -0.0707 S33: -0.0041 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 83 THROUGH 116 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.0597 35.4240 13.3233 REMARK 3 T TENSOR REMARK 3 T11: 0.2567 T22: 0.2781 REMARK 3 T33: 0.2885 T12: -0.0394 REMARK 3 T13: -0.1075 T23: 0.0273 REMARK 3 L TENSOR REMARK 3 L11: 0.7360 L22: 3.1680 REMARK 3 L33: 3.5931 L12: -1.1970 REMARK 3 L13: -0.3443 L23: -1.1558 REMARK 3 S TENSOR REMARK 3 S11: -0.0816 S12: 0.0953 S13: 0.0205 REMARK 3 S21: -0.0907 S22: 0.0469 S23: 0.1178 REMARK 3 S31: -0.0117 S32: 0.0717 S33: 0.0119 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 117 THROUGH 141 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.5851 71.4924 4.5266 REMARK 3 T TENSOR REMARK 3 T11: 0.0990 T22: 0.3486 REMARK 3 T33: 0.3029 T12: 0.0182 REMARK 3 T13: 0.0347 T23: -0.0727 REMARK 3 L TENSOR REMARK 3 L11: 1.7239 L22: 2.9613 REMARK 3 L33: 3.4965 L12: 0.1024 REMARK 3 L13: 2.5404 L23: -0.2054 REMARK 3 S TENSOR REMARK 3 S11: 0.1768 S12: 0.3401 S13: -0.0088 REMARK 3 S21: 0.3836 S22: -0.2740 S23: -0.0023 REMARK 3 S31: -0.4629 S32: 1.0491 S33: 0.4112 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 142 THROUGH 164 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.2636 67.7496 5.0494 REMARK 3 T TENSOR REMARK 3 T11: 0.1906 T22: 0.3876 REMARK 3 T33: 0.3281 T12: 0.0010 REMARK 3 T13: 0.0440 T23: 0.0781 REMARK 3 L TENSOR REMARK 3 L11: 1.0697 L22: 1.4851 REMARK 3 L33: 4.4075 L12: -0.7143 REMARK 3 L13: 2.1438 L23: -1.8227 REMARK 3 S TENSOR REMARK 3 S11: -0.0375 S12: -0.0146 S13: -0.1913 REMARK 3 S21: 0.1298 S22: 0.3571 S23: 0.2343 REMARK 3 S31: 0.1900 S32: -0.8611 S33: -0.3118 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 165 THROUGH 209 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.1961 68.9638 2.1226 REMARK 3 T TENSOR REMARK 3 T11: 0.1080 T22: 0.3902 REMARK 3 T33: 0.2814 T12: -0.0135 REMARK 3 T13: 0.0022 T23: 0.0377 REMARK 3 L TENSOR REMARK 3 L11: 0.1155 L22: 4.7336 REMARK 3 L33: 4.5492 L12: -0.2379 REMARK 3 L13: -0.1285 L23: -2.6138 REMARK 3 S TENSOR REMARK 3 S11: 0.0568 S12: -0.1538 S13: 0.0903 REMARK 3 S21: 0.1877 S22: 0.0835 S23: 0.1279 REMARK 3 S31: -0.0176 S32: -0.4354 S33: -0.0993 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 210 THROUGH 221 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.9825 77.7122 6.4001 REMARK 3 T TENSOR REMARK 3 T11: 0.3338 T22: 0.5104 REMARK 3 T33: 0.5155 T12: 0.0574 REMARK 3 T13: 0.0677 T23: -0.0808 REMARK 3 L TENSOR REMARK 3 L11: 1.4613 L22: 3.6794 REMARK 3 L33: 3.1543 L12: 0.2923 REMARK 3 L13: -0.6156 L23: -3.3532 REMARK 3 S TENSOR REMARK 3 S11: -0.0167 S12: 0.1439 S13: 0.5161 REMARK 3 S21: 1.4095 S22: 0.5253 S23: -0.1750 REMARK 3 S31: -0.9652 S32: -0.1809 S33: -0.4791 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.3459 31.9540 -5.2422 REMARK 3 T TENSOR REMARK 3 T11: 0.5406 T22: 0.3608 REMARK 3 T33: 0.2816 T12: -0.0884 REMARK 3 T13: -0.1134 T23: -0.0317 REMARK 3 L TENSOR REMARK 3 L11: 2.0785 L22: 2.8870 REMARK 3 L33: 3.3778 L12: -0.6092 REMARK 3 L13: 0.2166 L23: -1.3318 REMARK 3 S TENSOR REMARK 3 S11: -0.0046 S12: 0.3329 S13: -0.0966 REMARK 3 S21: -0.6394 S22: -0.0369 S23: 0.2966 REMARK 3 S31: 0.6690 S32: -0.0505 S33: 0.0454 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 91 THROUGH 144 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.9466 57.2330 -3.0816 REMARK 3 T TENSOR REMARK 3 T11: 0.1558 T22: 0.4075 REMARK 3 T33: 0.3004 T12: -0.0105 REMARK 3 T13: -0.0410 T23: -0.0252 REMARK 3 L TENSOR REMARK 3 L11: 0.1444 L22: 0.8339 REMARK 3 L33: 1.0883 L12: -0.0868 REMARK 3 L13: 0.0155 L23: -0.8795 REMARK 3 S TENSOR REMARK 3 S11: 0.0891 S12: -0.0785 S13: 0.0480 REMARK 3 S21: -0.2383 S22: -0.0621 S23: 0.1081 REMARK 3 S31: 0.2480 S32: -0.0335 S33: -0.0262 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 145 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.7034 68.1381 -3.9266 REMARK 3 T TENSOR REMARK 3 T11: 0.0955 T22: 0.3629 REMARK 3 T33: 0.3513 T12: 0.0112 REMARK 3 T13: -0.0060 T23: 0.0160 REMARK 3 L TENSOR REMARK 3 L11: 1.3836 L22: 4.2821 REMARK 3 L33: 4.1765 L12: 1.0920 REMARK 3 L13: 1.7196 L23: 1.7887 REMARK 3 S TENSOR REMARK 3 S11: 0.0890 S12: -0.0546 S13: -0.0231 REMARK 3 S21: 0.0639 S22: 0.0058 S23: -0.3110 REMARK 3 S31: 0.0985 S32: 0.3259 S33: -0.0799 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 8TQ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-AUG-23. REMARK 100 THE DEPOSITION ID IS D_1000276346. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-JUL-21 REMARK 200 TEMPERATURE (KELVIN) : 273 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 : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 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 : 46944 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 43.240 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 200 DATA REDUNDANCY : 9.000 REMARK 200 R MERGE (I) : 0.08300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38 REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.50000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 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: PDB ENTRY 7TUE REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.14 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG20000, 0.1 M MES, PH 6.5, VAPOR REMARK 280 DIFFUSION, HANGING DROP, 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 38.55750 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.74500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.21350 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.74500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.55750 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.21350 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: PENTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 10100 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 36420 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, P, 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 LYS A 268 REMARK 465 PRO A 269 REMARK 465 LEU A 270 REMARK 465 THR A 271 REMARK 465 LEU A 272 REMARK 465 ARG A 273 REMARK 465 TRP A 274 REMARK 465 CYS L 214 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 45 CG CD CE NZ REMARK 470 LEU A 82 CG CD1 CD2 REMARK 470 LEU A 126 CG CD1 CD2 REMARK 470 ARG A 181 CG CD NE CZ NH1 NH2 REMARK 470 MET B 0 CG SD CE REMARK 470 GLU B 44 CG CD OE1 OE2 REMARK 470 LYS B 48 CG CD CE NZ REMARK 470 LYS B 58 CG CD CE NZ REMARK 470 ARG H 220 CG CD NE CZ NH1 NH2 REMARK 470 THR L 7 OG1 CG2 REMARK 470 LYS L 142 CG CD CE NZ REMARK 470 GLU L 213 CG CD OE1 OE2 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 THR L 7 O 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 ARG A 14 88.42 -151.86 REMARK 500 ASP A 29 -129.24 53.42 REMARK 500 TYR A 123 -61.67 -105.03 REMARK 500 SER A 131 -7.35 -153.89 REMARK 500 GLN A 224 43.69 -104.70 REMARK 500 ILE B 1 134.43 66.37 REMARK 500 PRO B 32 -168.02 -72.71 REMARK 500 TRP B 60 -5.43 75.47 REMARK 500 SER H 15 -19.43 -173.41 REMARK 500 ARG H 66 18.50 -141.63 REMARK 500 GLN H 86 -169.28 -120.54 REMARK 500 PRO H 154 -156.09 -83.14 REMARK 500 SER H 179 -84.22 54.67 REMARK 500 THR L 7 -84.07 -43.77 REMARK 500 SER L 30 -135.28 60.59 REMARK 500 ALA L 51 -38.99 69.70 REMARK 500 THR L 69 -39.82 -131.84 REMARK 500 PRO L 95 33.87 -95.49 REMARK 500 PRO L 141 -169.25 -76.05 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 8TQ4 RELATED DB: PDB REMARK 900 RELATED ID: 8TQ6 RELATED DB: PDB REMARK 900 RELATED ID: 8TQ7 RELATED DB: PDB REMARK 900 RELATED ID: 8TQ8 RELATED DB: PDB REMARK 900 RELATED ID: 8TQ9 RELATED DB: PDB REMARK 900 RELATED ID: 8TQA RELATED DB: PDB DBREF 8TQ5 A 2 274 UNP Q860B7 Q860B7_HUMAN 1 273 DBREF 8TQ5 B 1 99 UNP P61769 B2MG_HUMAN 21 119 DBREF 8TQ5 P 1 9 UNP Q9TQB0 Q9TQB0_HUMAN 36 44 DBREF 8TQ5 H 1 221 PDB 8TQ5 8TQ5 1 221 DBREF 8TQ5 L 1 214 PDB 8TQ5 8TQ5 1 214 SEQADV 8TQ5 GLY A 1 UNP Q860B7 EXPRESSION TAG SEQADV 8TQ5 MET B 0 UNP P61769 INITIATING METHIONINE SEQRES 1 A 274 GLY SER HIS SER MET ARG TYR PHE TYR THR ALA MET SER SEQRES 2 A 274 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE THR VAL GLY SEQRES 3 A 274 TYR VAL ASP ASP THR LEU PHE VAL ARG PHE ASP SER ASP SEQRES 4 A 274 ALA THR SER PRO ARG LYS GLU PRO ARG ALA PRO TRP ILE SEQRES 5 A 274 GLU GLN GLU GLY PRO GLU TYR TRP ASP ARG GLU THR GLN SEQRES 6 A 274 ILE SER LYS THR ASN THR GLN THR TYR ARG GLU ASN LEU SEQRES 7 A 274 ARG THR ALA LEU ARG TYR TYR ASN GLN SER GLU ALA GLY SEQRES 8 A 274 SER HIS ILE ILE GLN ARG MET TYR GLY CYS ASP VAL GLY SEQRES 9 A 274 PRO ASP GLY ARG LEU LEU ARG GLY TYR ASP GLN TYR ALA SEQRES 10 A 274 TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP LEU SEQRES 11 A 274 SER SER TRP THR ALA ALA ASP THR ALA ALA GLN ILE THR SEQRES 12 A 274 GLN ARG LYS TRP GLU ALA ALA ARG VAL ALA GLU GLN ASP SEQRES 13 A 274 ARG ALA TYR LEU GLU GLY LEU CYS VAL GLU SER LEU ARG SEQRES 14 A 274 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG ALA SEQRES 15 A 274 ASP PRO PRO LYS THR HIS VAL THR HIS HIS PRO ILE SER SEQRES 16 A 274 ASP HIS GLU VAL THR LEU ARG CYS TRP ALA LEU GLY PHE SEQRES 17 A 274 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY SEQRES 18 A 274 GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG SEQRES 19 A 274 PRO ALA GLY ASP ARG THR PHE GLN LYS TRP ALA ALA VAL SEQRES 20 A 274 VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS HIS SEQRES 21 A 274 VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG SEQRES 22 A 274 TRP SEQRES 1 B 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG SEQRES 2 B 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS SEQRES 3 B 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP SEQRES 4 B 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SEQRES 5 B 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU SEQRES 6 B 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU SEQRES 7 B 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO SEQRES 8 B 100 LYS ILE VAL LYS TRP ASP ARG ASP MET SEQRES 1 P 9 GLU GLU PHE GLY ARG ALA PHE SER PHE SEQRES 1 H 221 GLN VAL GLN LEU LYS GLN SER GLY PRO GLY LEU VAL GLN SEQRES 2 H 221 PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY SEQRES 3 H 221 PHE SER LEU THR SER TYR GLY LEU HIS TRP VAL ARG GLN SEQRES 4 H 221 SER PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE TRP SEQRES 5 H 221 SER GLY GLY SER THR ASP TYR ASN ALA ALA PHE ILE SER SEQRES 6 H 221 ARG LEU SER ILE ARG LYS ASP ASN SER LYS SER GLN VAL SEQRES 7 H 221 PHE PHE LYS MET ASN SER LEU GLN ALA ASN ASP THR ALA SEQRES 8 H 221 ILE TYR TYR CYS ALA ARG SER LEU THR THR ALA THR SER SEQRES 9 H 221 ALA TRP PHE PRO TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 H 221 VAL SER ALA ALA LYS THR THR PRO PRO SER VAL TYR PRO SEQRES 11 H 221 LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER MET VAL SEQRES 12 H 221 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO SEQRES 13 H 221 VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER GLY SEQRES 14 H 221 VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR SEQRES 15 H 221 THR LEU SER SER SER VAL THR VAL PRO SER SER THR TRP SEQRES 16 H 221 PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SEQRES 17 H 221 SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP SEQRES 1 L 214 SER ILE VAL MET THR GLN THR PRO LYS PHE LEU LEU VAL SEQRES 2 L 214 SER ALA GLY ASP ARG VAL THR ILE THR CYS LYS ALA SER SEQRES 3 L 214 GLN THR VAL SER ASN ASP VAL THR TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR TYR ALA SER SEQRES 5 L 214 ASN ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 L 214 GLY TYR GLY THR ASP PHE THR PHE THR ILE ASN THR VAL SEQRES 7 L 214 GLN ALA GLU ASP LEU ALA VAL TYR PHE CYS GLN GLN ASP SEQRES 8 L 214 TYR SER SER PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9 L 214 GLU LYS LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 L 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 L 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 L 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 L 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 L 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 L 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS HET NAG H 401 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 6 NAG C8 H15 N O6 FORMUL 7 HOH *197(H2 O) HELIX 1 AA1 ALA A 49 GLU A 53 5 5 HELIX 2 AA2 GLY A 56 TYR A 85 1 30 HELIX 3 AA3 ASP A 137 ALA A 150 1 14 HELIX 4 AA4 ARG A 151 GLY A 162 1 12 HELIX 5 AA5 GLY A 162 GLY A 175 1 14 HELIX 6 AA6 GLY A 175 GLN A 180 1 6 HELIX 7 AA7 GLU A 253 GLN A 255 5 3 HELIX 8 AA8 GLN H 86 THR H 90 5 5 HELIX 9 AA9 SER H 163 SER H 165 5 3 HELIX 10 AB1 PRO H 207 SER H 210 5 4 HELIX 11 AB2 GLN L 79 LEU L 83 5 5 HELIX 12 AB3 SER L 121 GLY L 128 1 8 HELIX 13 AB4 LYS L 183 ARG L 188 1 6 SHEET 1 AA1 8 GLU A 46 PRO A 47 0 SHEET 2 AA1 8 THR A 31 ASP A 37 -1 N ARG A 35 O GLU A 46 SHEET 3 AA1 8 ARG A 21 VAL A 28 -1 N GLY A 26 O PHE A 33 SHEET 4 AA1 8 HIS A 3 MET A 12 -1 N ARG A 6 O TYR A 27 SHEET 5 AA1 8 ILE A 94 VAL A 103 -1 O ILE A 95 N ALA A 11 SHEET 6 AA1 8 LEU A 109 TYR A 118 -1 O LEU A 110 N ASP A 102 SHEET 7 AA1 8 LYS A 121 LEU A 126 -1 O TYR A 123 N TYR A 116 SHEET 8 AA1 8 TRP A 133 ALA A 135 -1 O THR A 134 N ALA A 125 SHEET 1 AA2 4 LYS A 186 PRO A 193 0 SHEET 2 AA2 4 GLU A 198 PHE A 208 -1 O TRP A 204 N HIS A 188 SHEET 3 AA2 4 PHE A 241 PRO A 250 -1 O ALA A 245 N CYS A 203 SHEET 4 AA2 4 GLU A 229 LEU A 230 -1 N GLU A 229 O ALA A 246 SHEET 1 AA3 4 LYS A 186 PRO A 193 0 SHEET 2 AA3 4 GLU A 198 PHE A 208 -1 O TRP A 204 N HIS A 188 SHEET 3 AA3 4 PHE A 241 PRO A 250 -1 O ALA A 245 N CYS A 203 SHEET 4 AA3 4 ARG A 234 PRO A 235 -1 N ARG A 234 O GLN A 242 SHEET 1 AA4 3 GLU A 222 ASP A 223 0 SHEET 2 AA4 3 THR A 214 ARG A 219 -1 N ARG A 219 O GLU A 222 SHEET 3 AA4 3 TYR A 257 GLN A 262 -1 O HIS A 260 N THR A 216 SHEET 1 AA5 4 LYS B 6 SER B 11 0 SHEET 2 AA5 4 ASN B 21 PHE B 30 -1 O SER B 28 N LYS B 6 SHEET 3 AA5 4 PHE B 62 PHE B 70 -1 O THR B 68 N LEU B 23 SHEET 4 AA5 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67 SHEET 1 AA6 4 LYS B 6 SER B 11 0 SHEET 2 AA6 4 ASN B 21 PHE B 30 -1 O SER B 28 N LYS B 6 SHEET 3 AA6 4 PHE B 62 PHE B 70 -1 O THR B 68 N LEU B 23 SHEET 4 AA6 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63 SHEET 1 AA7 4 GLU B 44 ARG B 45 0 SHEET 2 AA7 4 ILE B 35 LYS B 41 -1 N LYS B 41 O GLU B 44 SHEET 3 AA7 4 TYR B 78 HIS B 84 -1 O ALA B 79 N LEU B 40 SHEET 4 AA7 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82 SHEET 1 AA8 4 GLN H 3 SER H 7 0 SHEET 2 AA8 4 LEU H 18 SER H 25 -1 O THR H 23 N LYS H 5 SHEET 3 AA8 4 GLN H 77 MET H 82 -1 O PHE H 80 N ILE H 20 SHEET 4 AA8 4 LEU H 67 ASP H 72 -1 N ARG H 70 O PHE H 79 SHEET 1 AA9 6 LEU H 11 VAL H 12 0 SHEET 2 AA9 6 THR H 114 VAL H 118 1 O THR H 117 N VAL H 12 SHEET 3 AA9 6 ALA H 91 ARG H 97 -1 N ALA H 91 O VAL H 116 SHEET 4 AA9 6 LEU H 34 SER H 40 -1 N VAL H 37 O TYR H 94 SHEET 5 AA9 6 GLY H 44 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA9 6 THR H 57 TYR H 59 -1 O ASP H 58 N VAL H 50 SHEET 1 AB1 4 LEU H 11 VAL H 12 0 SHEET 2 AB1 4 THR H 114 VAL H 118 1 O THR H 117 N VAL H 12 SHEET 3 AB1 4 ALA H 91 ARG H 97 -1 N ALA H 91 O VAL H 116 SHEET 4 AB1 4 TYR H 109 TRP H 110 -1 O TYR H 109 N ARG H 97 SHEET 1 AB2 4 SER H 127 LEU H 131 0 SHEET 2 AB2 4 MET H 142 TYR H 152 -1 O LYS H 150 N SER H 127 SHEET 3 AB2 4 LEU H 181 PRO H 191 -1 O TYR H 182 N TYR H 152 SHEET 4 AB2 4 VAL H 170 THR H 172 -1 N HIS H 171 O SER H 187 SHEET 1 AB3 4 SER H 127 LEU H 131 0 SHEET 2 AB3 4 MET H 142 TYR H 152 -1 O LYS H 150 N SER H 127 SHEET 3 AB3 4 LEU H 181 PRO H 191 -1 O TYR H 182 N TYR H 152 SHEET 4 AB3 4 VAL H 176 GLN H 178 -1 N GLN H 178 O LEU H 181 SHEET 1 AB4 3 THR H 158 TRP H 161 0 SHEET 2 AB4 3 THR H 201 HIS H 206 -1 O ASN H 203 N THR H 160 SHEET 3 AB4 3 THR H 211 LYS H 216 -1 O VAL H 213 N VAL H 204 SHEET 1 AB5 4 MET L 4 GLN L 6 0 SHEET 2 AB5 4 VAL L 19 ALA L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AB5 4 ASP L 70 ILE L 75 -1 O PHE L 73 N ILE L 21 SHEET 4 AB5 4 PHE L 62 TYR L 67 -1 N THR L 63 O THR L 74 SHEET 1 AB6 6 PHE L 10 VAL L 13 0 SHEET 2 AB6 6 THR L 102 LYS L 106 1 O GLU L 105 N VAL L 13 SHEET 3 AB6 6 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB6 6 VAL L 33 GLN L 38 -1 N GLN L 38 O VAL L 85 SHEET 5 AB6 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AB6 6 ASN L 53 ARG L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AB7 4 THR L 114 PHE L 118 0 SHEET 2 AB7 4 GLY L 129 PHE L 139 -1 O ASN L 137 N THR L 114 SHEET 3 AB7 4 TYR L 173 THR L 182 -1 O TYR L 173 N PHE L 139 SHEET 4 AB7 4 VAL L 159 TRP L 163 -1 N LEU L 160 O THR L 178 SHEET 1 AB8 4 SER L 153 ARG L 155 0 SHEET 2 AB8 4 ILE L 144 ILE L 150 -1 N ILE L 150 O SER L 153 SHEET 3 AB8 4 SER L 191 HIS L 198 -1 O THR L 197 N ASN L 145 SHEET 4 AB8 4 ILE L 205 ASN L 210 -1 O LYS L 207 N CYS L 194 SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.04 SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.03 SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.04 SSBOND 4 CYS H 22 CYS H 95 1555 1555 2.04 SSBOND 5 CYS H 147 CYS H 202 1555 1555 2.05 SSBOND 6 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 7 CYS L 134 CYS L 194 1555 1555 2.05 LINK ND2 ASN H 88 C1 NAG H 401 1555 1555 1.45 CISPEP 1 TYR A 209 PRO A 210 0 1.31 CISPEP 2 HIS B 31 PRO B 32 0 0.24 CISPEP 3 PHE H 153 PRO H 154 0 -1.32 CISPEP 4 TRP H 195 PRO H 196 0 6.25 CISPEP 5 SER L 94 PRO L 95 0 5.36 CISPEP 6 TYR L 140 PRO L 141 0 1.30 CRYST1 77.115 104.427 131.490 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 0.012968 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009576 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007605 0.00000