HEADER TRANSFERASE/IMMUNE SYSTEM 14-DEC-16 5U8R TITLE STRUCTURE OF THE ECTODOMAIN OF THE HUMAN TYPE 1 INSULIN-LIKE GROWTH TITLE 2 FACTOR RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: INSULIN-LIKE GROWTH FACTOR 1 RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: INSULIN-LIKE GROWTH FACTOR I RECEPTOR,IGF-I RECEPTOR; COMPND 5 EC: 2.7.10.1; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 OTHER_DETAILS: A17DELTA-BETA CONSTRUCT, SEE WHITTEN ET AL., J. MOL. COMPND 9 BIOL., V394, PP878-92 (2009).; COMPND 10 MOL_ID: 2; COMPND 11 MOLECULE: FV 24-60 HEAVY CHAIN; COMPND 12 CHAIN: H; COMPND 13 ENGINEERED: YES; COMPND 14 OTHER_DETAILS: HEAVY CHAIN VARIABLE DOMAIN (RESIDUES 1-118) OF MAB COMPND 15 24-60, INCLUDING ADDITIONAL GLY-THR AT THE N TERMINUS AND GLU-ASN- COMPND 16 LEU-TYR-PHE-GLN AT C TERMINUS.; COMPND 17 MOL_ID: 3; COMPND 18 MOLECULE: FV 24-60 LIGHT CHAIN; COMPND 19 CHAIN: L; COMPND 20 ENGINEERED: YES; COMPND 21 OTHER_DETAILS: LIGHT CHAIN VARIABLE DOMAIN (RESIDUES 1-107) OF MAB COMPND 22 24-60, INCLUDING ADDITIONAL GLY AT THE N TERMINUS. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: IGF1R; SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: LEC8; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: FIII; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: FIII-IGFR.ECD; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 13 ORGANISM_TAXID: 10090; SOURCE 14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PGPHFT; SOURCE 17 EXPRESSION_SYSTEM_PLASMID: PGPHFT-SUMO-SCFV; SOURCE 18 MOL_ID: 3; SOURCE 19 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 20 ORGANISM_TAXID: 10090; SOURCE 21 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 23 EXPRESSION_SYSTEM_VECTOR_TYPE: PGPHFT; SOURCE 24 EXPRESSION_SYSTEM_PLASMID: PGPHFT-SUMO-SCFV KEYWDS RECEPTOR, TYROSINE KINASE, TYPE 1 INSULIN-LIKE, GROWTH FACTOR KEYWDS 2 RECEPTOR, TRANSFERASE-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR M.LAWRENCE,Y.XU REVDAT 1 28-FEB-18 5U8R 0 JRNL AUTH Y.XU,G.K.-W.KONG,J.G.MENTING,M.B.MARGETTS,D.R.THOMAS, JRNL AUTH 2 L.M.JENKIN,B.R.FORBES,C.W.WARD,M.C.LAWRENCE JRNL TITL HOW LIGAND BINDS TO THE TYPE 1 INSULIN-LIKE GROWTH FACTOR JRNL TITL 2 RECEPTOR JRNL REF NAT COMMUN 2018 JRNL REFN ESSN 2041-1723 REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.11.1-2575_1692 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) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.36 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.337 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 45805 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.257 REMARK 3 R VALUE (WORKING SET) : 0.256 REMARK 3 FREE R VALUE : 0.285 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.729 REMARK 3 FREE R VALUE TEST SET COUNT : 2166 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 46.3648 - 7.3893 1.00 3109 170 0.2355 0.2230 REMARK 3 2 7.3893 - 5.8689 1.00 2992 147 0.2530 0.2719 REMARK 3 3 5.8689 - 5.1281 1.00 2957 158 0.2101 0.2830 REMARK 3 4 5.1281 - 4.6597 1.00 2944 139 0.1959 0.2346 REMARK 3 5 4.6597 - 4.3260 1.00 2919 132 0.1982 0.2349 REMARK 3 6 4.3260 - 4.0711 1.00 2934 141 0.2263 0.3246 REMARK 3 7 4.0711 - 3.8673 1.00 2901 148 0.2669 0.3165 REMARK 3 8 3.8673 - 3.6990 0.99 2900 118 0.2756 0.3215 REMARK 3 9 3.6990 - 3.5567 0.99 2872 142 0.3027 0.3308 REMARK 3 10 3.5567 - 3.4340 0.99 2847 150 0.3300 0.3298 REMARK 3 11 3.4340 - 3.3267 0.99 2867 154 0.3514 0.3583 REMARK 3 12 3.3267 - 3.2316 0.99 2848 140 0.3696 0.4138 REMARK 3 13 3.2316 - 3.1465 0.98 2818 143 0.4020 0.4102 REMARK 3 14 3.1465 - 3.0698 0.99 2849 146 0.4215 0.4794 REMARK 3 15 3.0698 - 3.0000 0.99 2882 138 0.4523 0.4781 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) : 0.559 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.330 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 92.43 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 133.9 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 : 0.002 8551 REMARK 3 ANGLE : 0.481 11618 REMARK 3 CHIRALITY : 0.043 1270 REMARK 3 PLANARITY : 0.003 1488 REMARK 3 DIHEDRAL : 11.428 5136 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 16 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 307 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.8498 -31.2037 40.4523 REMARK 3 T TENSOR REMARK 3 T11: 1.6018 T22: 0.8123 REMARK 3 T33: 0.7948 T12: 0.1922 REMARK 3 T13: -0.1048 T23: -0.2168 REMARK 3 L TENSOR REMARK 3 L11: 3.9148 L22: 1.3281 REMARK 3 L33: 4.2235 L12: -0.6597 REMARK 3 L13: -1.1666 L23: 1.3300 REMARK 3 S TENSOR REMARK 3 S11: -0.1462 S12: -1.0352 S13: 0.2821 REMARK 3 S21: 0.8903 S22: 0.2446 S23: -0.3546 REMARK 3 S31: 0.0924 S32: 0.2082 S33: -0.1451 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 308 THROUGH 456 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.9679 -12.2245 -8.6280 REMARK 3 T TENSOR REMARK 3 T11: 1.2704 T22: 0.7101 REMARK 3 T33: 0.9653 T12: -0.2707 REMARK 3 T13: 0.1188 T23: -0.0475 REMARK 3 L TENSOR REMARK 3 L11: 5.6527 L22: 4.1106 REMARK 3 L33: 6.1747 L12: -1.0385 REMARK 3 L13: 0.6307 L23: -1.9017 REMARK 3 S TENSOR REMARK 3 S11: 0.0318 S12: 0.5522 S13: 0.2207 REMARK 3 S21: -0.0687 S22: -0.2574 S23: -1.1271 REMARK 3 S31: -0.1218 S32: -0.1949 S33: 0.2619 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 457 THROUGH 600 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.4678 18.5765 0.9479 REMARK 3 T TENSOR REMARK 3 T11: 1.5021 T22: 0.9010 REMARK 3 T33: 0.5314 T12: -0.2590 REMARK 3 T13: -0.0534 T23: 0.1640 REMARK 3 L TENSOR REMARK 3 L11: 2.2608 L22: 2.0823 REMARK 3 L33: 2.1555 L12: -0.7425 REMARK 3 L13: 0.9173 L23: 0.4693 REMARK 3 S TENSOR REMARK 3 S11: -0.1991 S12: 0.3844 S13: -0.3010 REMARK 3 S21: -0.1635 S22: 0.0829 S23: 0.0162 REMARK 3 S31: 0.9617 S32: 0.5772 S33: 0.0960 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 601 THROUGH 897 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.7039 25.8452 59.5740 REMARK 3 T TENSOR REMARK 3 T11: 2.0039 T22: 1.6366 REMARK 3 T33: 0.5787 T12: 0.3225 REMARK 3 T13: -0.1260 T23: 0.0191 REMARK 3 L TENSOR REMARK 3 L11: 0.1452 L22: -0.3811 REMARK 3 L33: 7.3412 L12: 1.1892 REMARK 3 L13: 1.4433 L23: 1.2612 REMARK 3 S TENSOR REMARK 3 S11: 0.2753 S12: 0.0681 S13: 0.0969 REMARK 3 S21: 0.0049 S22: -0.0384 S23: 0.1815 REMARK 3 S31: 0.8107 S32: 0.9984 S33: -0.1697 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 0 THROUGH 21 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.5979 -59.4394 12.7971 REMARK 3 T TENSOR REMARK 3 T11: 0.8898 T22: 0.6892 REMARK 3 T33: 0.6264 T12: 0.1537 REMARK 3 T13: 0.1311 T23: -0.0032 REMARK 3 L TENSOR REMARK 3 L11: 3.7008 L22: 6.2014 REMARK 3 L33: 2.7639 L12: -0.1126 REMARK 3 L13: 2.8811 L23: 0.9407 REMARK 3 S TENSOR REMARK 3 S11: 0.9459 S12: -0.2755 S13: -2.4235 REMARK 3 S21: 1.1390 S22: 0.3378 S23: 0.7664 REMARK 3 S31: 1.1802 S32: 0.2143 S33: -1.2627 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 22 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.1219 -51.4332 18.3956 REMARK 3 T TENSOR REMARK 3 T11: 0.5434 T22: 0.2913 REMARK 3 T33: 0.2901 T12: 0.3246 REMARK 3 T13: 0.0904 T23: -0.1381 REMARK 3 L TENSOR REMARK 3 L11: 6.5620 L22: 7.7140 REMARK 3 L33: 6.4723 L12: 1.3373 REMARK 3 L13: -1.9966 L23: 1.8958 REMARK 3 S TENSOR REMARK 3 S11: 0.0235 S12: -1.6625 S13: -0.6017 REMARK 3 S21: 1.8504 S22: -0.2229 S23: -0.6709 REMARK 3 S31: 0.6425 S32: 1.0642 S33: -0.1290 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 40 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.9617 -49.6987 3.2352 REMARK 3 T TENSOR REMARK 3 T11: 0.3943 T22: 0.8482 REMARK 3 T33: 0.4404 T12: -0.0607 REMARK 3 T13: -0.0656 T23: 0.0115 REMARK 3 L TENSOR REMARK 3 L11: 8.9817 L22: 1.9822 REMARK 3 L33: 6.3421 L12: -2.9871 REMARK 3 L13: -5.4553 L23: -3.9816 REMARK 3 S TENSOR REMARK 3 S11: -0.2668 S12: 2.2220 S13: -1.7006 REMARK 3 S21: -2.8627 S22: -1.4496 S23: 0.7015 REMARK 3 S31: 0.8506 S32: -0.9071 S33: 0.8972 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 52 THROUGH 64 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.4428 -41.2990 13.3421 REMARK 3 T TENSOR REMARK 3 T11: 0.7023 T22: 0.6783 REMARK 3 T33: 0.8255 T12: 0.1739 REMARK 3 T13: -0.0154 T23: 0.1803 REMARK 3 L TENSOR REMARK 3 L11: 6.0326 L22: 9.6575 REMARK 3 L33: 6.5839 L12: 0.3681 REMARK 3 L13: 2.0449 L23: 4.7864 REMARK 3 S TENSOR REMARK 3 S11: -0.7986 S12: 0.8679 S13: 1.2963 REMARK 3 S21: -1.0198 S22: -1.1552 S23: 1.5313 REMARK 3 S31: -0.8214 S32: -0.6788 S33: 1.2974 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 65 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.7837 -49.4997 16.6244 REMARK 3 T TENSOR REMARK 3 T11: 0.9705 T22: 0.6643 REMARK 3 T33: 0.6994 T12: 0.2676 REMARK 3 T13: 0.2279 T23: -0.1635 REMARK 3 L TENSOR REMARK 3 L11: 3.3680 L22: 4.8761 REMARK 3 L33: 6.8430 L12: 0.4015 REMARK 3 L13: 3.5628 L23: -1.2817 REMARK 3 S TENSOR REMARK 3 S11: -0.0142 S12: -0.0143 S13: 0.2755 REMARK 3 S21: 0.4410 S22: -1.1317 S23: 0.4781 REMARK 3 S31: 0.0076 S32: -1.6412 S33: 0.7688 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 84 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.5832 -53.1231 0.4100 REMARK 3 T TENSOR REMARK 3 T11: 1.4155 T22: 0.8142 REMARK 3 T33: 0.9810 T12: 0.3540 REMARK 3 T13: -0.4127 T23: 0.2104 REMARK 3 L TENSOR REMARK 3 L11: 3.0477 L22: 2.6301 REMARK 3 L33: 2.9726 L12: 1.7145 REMARK 3 L13: 2.9375 L23: 1.1648 REMARK 3 S TENSOR REMARK 3 S11: 0.8385 S12: 0.7407 S13: 1.1255 REMARK 3 S21: -2.6684 S22: -1.4048 S23: -1.0674 REMARK 3 S31: 0.3765 S32: 0.1169 S33: 0.3563 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 92 THROUGH 117 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.3611 -53.9364 10.8287 REMARK 3 T TENSOR REMARK 3 T11: 0.7406 T22: 0.4172 REMARK 3 T33: 0.4374 T12: 0.1424 REMARK 3 T13: 0.0598 T23: 0.0786 REMARK 3 L TENSOR REMARK 3 L11: 9.2875 L22: 4.3552 REMARK 3 L33: 6.6692 L12: 2.0755 REMARK 3 L13: 3.4091 L23: 0.8969 REMARK 3 S TENSOR REMARK 3 S11: 0.1968 S12: -0.8260 S13: -0.4634 REMARK 3 S21: 0.6543 S22: 0.0840 S23: 0.3430 REMARK 3 S31: -0.3611 S32: 0.1112 S33: -0.1375 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 0 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.3945 -48.3014 -3.7629 REMARK 3 T TENSOR REMARK 3 T11: 1.1708 T22: 1.0895 REMARK 3 T33: 0.5786 T12: -0.0537 REMARK 3 T13: 0.1722 T23: 0.0658 REMARK 3 L TENSOR REMARK 3 L11: 3.9715 L22: 9.4573 REMARK 3 L33: 7.2952 L12: -4.2730 REMARK 3 L13: -0.5900 L23: 4.5743 REMARK 3 S TENSOR REMARK 3 S11: 0.4584 S12: 0.5321 S13: 0.5249 REMARK 3 S21: -2.2378 S22: 0.1404 S23: -1.1700 REMARK 3 S31: -0.6421 S32: 0.3290 S33: -0.5665 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 33 THROUGH 52 ) REMARK 3 ORIGIN FOR THE GROUP (A): 33.8847 -53.7933 6.8661 REMARK 3 T TENSOR REMARK 3 T11: 0.5662 T22: 0.4193 REMARK 3 T33: 0.4429 T12: 0.1601 REMARK 3 T13: 0.1016 T23: 0.0106 REMARK 3 L TENSOR REMARK 3 L11: 3.2898 L22: 6.0760 REMARK 3 L33: 7.6373 L12: 4.2406 REMARK 3 L13: -1.0582 L23: -0.4993 REMARK 3 S TENSOR REMARK 3 S11: -0.5805 S12: 0.5964 S13: -0.7863 REMARK 3 S21: -0.3797 S22: 0.3322 S23: -0.4251 REMARK 3 S31: 0.5081 S32: -0.0018 S33: 0.2066 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 53 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 42.5536 -49.9458 4.7979 REMARK 3 T TENSOR REMARK 3 T11: 0.9306 T22: 1.0906 REMARK 3 T33: 0.6836 T12: 0.0392 REMARK 3 T13: 0.1122 T23: -0.1843 REMARK 3 L TENSOR REMARK 3 L11: 4.2052 L22: 7.6780 REMARK 3 L33: 9.2006 L12: 0.3700 REMARK 3 L13: -0.6213 L23: -5.4663 REMARK 3 S TENSOR REMARK 3 S11: 0.2519 S12: -0.0889 S13: 0.1573 REMARK 3 S21: 0.6066 S22: 0.0732 S23: -0.9899 REMARK 3 S31: -0.8485 S32: 0.3139 S33: -0.3672 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 76 THROUGH 84 ) REMARK 3 ORIGIN FOR THE GROUP (A): 42.5215 -63.6404 1.4306 REMARK 3 T TENSOR REMARK 3 T11: 1.5301 T22: 1.3637 REMARK 3 T33: 0.7692 T12: 0.3301 REMARK 3 T13: -0.0515 T23: -0.3140 REMARK 3 L TENSOR REMARK 3 L11: 2.5701 L22: 4.5822 REMARK 3 L33: 3.0870 L12: 1.1308 REMARK 3 L13: 0.5409 L23: -3.2122 REMARK 3 S TENSOR REMARK 3 S11: 1.1875 S12: -1.7811 S13: 0.5794 REMARK 3 S21: 1.6885 S22: -0.0593 S23: -0.9383 REMARK 3 S31: 2.1506 S32: 1.3599 S33: -1.2511 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 85 THROUGH 107 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.6949 -50.2075 0.4629 REMARK 3 T TENSOR REMARK 3 T11: 1.1839 T22: 0.5879 REMARK 3 T33: 0.2062 T12: 0.3160 REMARK 3 T13: -0.1258 T23: 0.1703 REMARK 3 L TENSOR REMARK 3 L11: 6.4150 L22: 5.5650 REMARK 3 L33: 1.9933 L12: -2.9196 REMARK 3 L13: -0.4874 L23: 3.1157 REMARK 3 S TENSOR REMARK 3 S11: 0.5301 S12: 1.5396 S13: 0.3899 REMARK 3 S21: -2.4934 S22: -0.1030 S23: 0.3398 REMARK 3 S31: 0.7123 S32: 0.7362 S33: -0.2112 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 5U8R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-16. REMARK 100 THE DEPOSITION ID IS D_1000225479. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-OCT-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON REMARK 200 BEAMLINE : MX2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45844 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 8.900 REMARK 200 R MERGE (I) : 0.25000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.13 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5 REMARK 200 DATA REDUNDANCY IN SHELL : 7.20 REMARK 200 R MERGE FOR SHELL (I) : 3.47000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.600 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: DOMAINS FROM 1IGR, 4ZXB, 3UMT REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 72.40 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.46 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M AMMONIUM SULFATE, 0.1 M REMARK 280 IMIDAZOLE-MALATE PH 7.0, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 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 47.51500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 100.86500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 47.51500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 100.86500 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 300 REMARK: ASSEMBLY DETERMINED BY NON-DENATURING GEL 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 APPLY THE FOLLOWING TO CHAINS: A, H, L REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLU A 38 REMARK 465 ASP A 39 REMARK 465 TYR A 40 REMARK 465 THR A 155 REMARK 465 MET A 156 REMARK 465 GLU A 157 REMARK 465 GLU A 158 REMARK 465 LYS A 159 REMARK 465 PRO A 160 REMARK 465 MET A 161 REMARK 465 ASP A 509 REMARK 465 GLY A 510 REMARK 465 GLN A 511 REMARK 465 ASP A 512 REMARK 465 ALA A 513 REMARK 465 CYS A 514 REMARK 465 GLY A 515 REMARK 465 SER A 516 REMARK 465 TYR A 643 REMARK 465 ALA A 644 REMARK 465 ASP A 645 REMARK 465 GLY A 646 REMARK 465 THR A 647 REMARK 465 ILE A 648 REMARK 465 ASP A 649 REMARK 465 ILE A 650 REMARK 465 GLU A 651 REMARK 465 GLU A 652 REMARK 465 VAL A 653 REMARK 465 THR A 654 REMARK 465 GLU A 655 REMARK 465 ASN A 656 REMARK 465 PRO A 657 REMARK 465 LYS A 658 REMARK 465 THR A 659 REMARK 465 GLU A 660 REMARK 465 VAL A 661 REMARK 465 CYS A 662 REMARK 465 GLY A 663 REMARK 465 GLY A 664 REMARK 465 GLU A 665 REMARK 465 LYS A 666 REMARK 465 GLY A 667 REMARK 465 PRO A 668 REMARK 465 CYS A 669 REMARK 465 CYS A 670 REMARK 465 ALA A 671 REMARK 465 CYS A 672 REMARK 465 PRO A 673 REMARK 465 LYS A 674 REMARK 465 THR A 675 REMARK 465 GLU A 676 REMARK 465 ALA A 677 REMARK 465 GLU A 678 REMARK 465 LYS A 679 REMARK 465 GLN A 680 REMARK 465 ALA A 681 REMARK 465 PRO A 725 REMARK 465 GLU A 726 REMARK 465 ARG A 727 REMARK 465 LYS A 728 REMARK 465 ARG A 729 REMARK 465 ARG A 730 REMARK 465 ASP A 731 REMARK 465 VAL A 732 REMARK 465 MET A 733 REMARK 465 GLN A 734 REMARK 465 VAL A 735 REMARK 465 ALA A 736 REMARK 465 ASN A 737 REMARK 465 ALA A 738 REMARK 465 GLY A 739 REMARK 465 ASN A 740 REMARK 465 ASN A 741 REMARK 465 GLU A 742 REMARK 465 THR A 743 REMARK 465 THR A 898 REMARK 465 GLY A 899 REMARK 465 TYR A 900 REMARK 465 GLU A 901 REMARK 465 ASN A 902 REMARK 465 PHE A 903 REMARK 465 ILE A 904 REMARK 465 HIS A 905 REMARK 465 GLY H -1 REMARK 465 SER H 118 REMARK 465 GLU H 119 REMARK 465 ASN H 120 REMARK 465 LEU H 121 REMARK 465 TYR H 122 REMARK 465 PHE H 123 REMARK 465 GLN H 124 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 O LYS A 503 OH TYR A 573 2.13 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 ASN A 11 -81.43 55.93 REMARK 500 THR A 49 -35.20 -133.30 REMARK 500 GLU A 53 -148.10 60.25 REMARK 500 ASN A 94 -3.67 67.02 REMARK 500 GLU A 147 71.89 -112.23 REMARK 500 CYS A 148 -83.94 -138.83 REMARK 500 ASN A 168 -119.23 56.99 REMARK 500 ASP A 213 74.90 57.28 REMARK 500 HIS A 223 -81.81 -102.21 REMARK 500 GLU A 242 -120.26 57.30 REMARK 500 TRP A 244 -21.58 -161.24 REMARK 500 ASN A 333 78.69 -151.42 REMARK 500 ASN A 338 -69.36 -95.44 REMARK 500 ASN A 374 -10.01 66.79 REMARK 500 LEU A 379 -98.10 -88.89 REMARK 500 ASN A 387 70.37 57.79 REMARK 500 ASN A 451 8.47 46.97 REMARK 500 CYS A 458 -87.94 -75.88 REMARK 500 SER A 471 -159.99 -122.35 REMARK 500 ASN A 473 -10.29 -152.03 REMARK 500 ASN A 504 95.41 -61.39 REMARK 500 HIS A 539 -90.11 -78.00 REMARK 500 TRP A 544 72.57 52.51 REMARK 500 ASN A 561 -121.65 65.39 REMARK 500 ASP A 562 -68.75 53.93 REMARK 500 ASP A 586 76.10 56.86 REMARK 500 SER A 612 -74.24 59.54 REMARK 500 TYR A 626 -133.16 58.40 REMARK 500 LEU A 627 -54.61 58.16 REMARK 500 ASN A 754 -70.20 -139.24 REMARK 500 ASN A 762 81.50 57.66 REMARK 500 GLU A 815 -154.02 61.52 REMARK 500 ASN A 816 61.01 -103.16 REMARK 500 ARG A 865 80.88 52.59 REMARK 500 LYS H 43 -17.24 69.85 REMARK 500 SER H 44 -135.68 59.84 REMARK 500 ARG H 85 57.74 39.36 REMARK 500 SER H 98 -157.35 -159.79 REMARK 500 SER L 30 -88.20 59.28 REMARK 500 ALA L 51 -38.19 67.10 REMARK 500 SER L 52 -54.06 -131.37 REMARK 500 SER L 77 93.91 60.68 REMARK 500 SER L 91 19.68 -154.00 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue MLT A 1002 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue MLT A 1003 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue IMD H 201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1004 REMARK 800 bound to ASN A 21 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A REMARK 800 1005 through NAG A 1006 bound to ASN A 105 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1007 REMARK 800 bound to ASN A 504 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A REMARK 800 1008 through NAG A 1009 bound to ASN A 577 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1010 REMARK 800 bound to ASN A 610 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1011 REMARK 800 bound to ASN A 883 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5U8Q RELATED DB: PDB REMARK 900 THE SAME ASSEMBLY COMPLEXED WITH IGF-I DBREF 5U8R A 1 905 UNP P08069 IGF1R_HUMAN 31 935 DBREF 5U8R H -1 124 PDB 5U8R 5U8R -1 124 DBREF 5U8R L 0 107 PDB 5U8R 5U8R 0 107 SEQADV 5U8R A UNP P08069 THR 748 DELETION SEQADV 5U8R A UNP P08069 THR 749 DELETION SEQADV 5U8R A UNP P08069 MET 750 DELETION SEQADV 5U8R A UNP P08069 SER 751 DELETION SEQADV 5U8R A UNP P08069 SER 752 DELETION SEQADV 5U8R A UNP P08069 ARG 753 DELETION SEQADV 5U8R A UNP P08069 SER 754 DELETION SEQADV 5U8R A UNP P08069 ARG 755 DELETION SEQADV 5U8R A UNP P08069 ASN 756 DELETION SEQADV 5U8R A UNP P08069 THR 757 DELETION SEQADV 5U8R A UNP P08069 THR 758 DELETION SEQADV 5U8R A UNP P08069 ALA 759 DELETION SEQADV 5U8R A UNP P08069 ALA 760 DELETION SEQADV 5U8R A UNP P08069 ASP 761 DELETION SEQADV 5U8R A UNP P08069 THR 762 DELETION SEQADV 5U8R A UNP P08069 TYR 763 DELETION SEQADV 5U8R A UNP P08069 ASN 764 DELETION SEQADV 5U8R A UNP P08069 ILE 765 DELETION SEQADV 5U8R A UNP P08069 THR 766 DELETION SEQADV 5U8R A UNP P08069 ASP 767 DELETION SEQADV 5U8R ALA A 738 UNP P08069 PRO 768 CONFLICT SEQADV 5U8R GLY A 739 UNP P08069 GLU 769 CONFLICT SEQADV 5U8R ASN A 740 UNP P08069 GLU 770 CONFLICT SEQADV 5U8R ASN A 741 UNP P08069 LEU 771 CONFLICT SEQRES 1 A 885 GLU ILE CYS GLY PRO GLY ILE ASP ILE ARG ASN ASP TYR SEQRES 2 A 885 GLN GLN LEU LYS ARG LEU GLU ASN CYS THR VAL ILE GLU SEQRES 3 A 885 GLY TYR LEU HIS ILE LEU LEU ILE SER LYS ALA GLU ASP SEQRES 4 A 885 TYR ARG SER TYR ARG PHE PRO LYS LEU THR VAL ILE THR SEQRES 5 A 885 GLU TYR LEU LEU LEU PHE ARG VAL ALA GLY LEU GLU SER SEQRES 6 A 885 LEU GLY ASP LEU PHE PRO ASN LEU THR VAL ILE ARG GLY SEQRES 7 A 885 TRP LYS LEU PHE TYR ASN TYR ALA LEU VAL ILE PHE GLU SEQRES 8 A 885 MET THR ASN LEU LYS ASP ILE GLY LEU TYR ASN LEU ARG SEQRES 9 A 885 ASN ILE THR ARG GLY ALA ILE ARG ILE GLU LYS ASN ALA SEQRES 10 A 885 ASP LEU CYS TYR LEU SER THR VAL ASP TRP SER LEU ILE SEQRES 11 A 885 LEU ASP ALA VAL SER ASN ASN TYR ILE VAL GLY ASN LYS SEQRES 12 A 885 PRO PRO LYS GLU CYS GLY ASP LEU CYS PRO GLY THR MET SEQRES 13 A 885 GLU GLU LYS PRO MET CYS GLU LYS THR THR ILE ASN ASN SEQRES 14 A 885 GLU TYR ASN TYR ARG CYS TRP THR THR ASN ARG CYS GLN SEQRES 15 A 885 LYS MET CYS PRO SER THR CYS GLY LYS ARG ALA CYS THR SEQRES 16 A 885 GLU ASN ASN GLU CYS CYS HIS PRO GLU CYS LEU GLY SER SEQRES 17 A 885 CYS SER ALA PRO ASP ASN ASP THR ALA CYS VAL ALA CYS SEQRES 18 A 885 ARG HIS TYR TYR TYR ALA GLY VAL CYS VAL PRO ALA CYS SEQRES 19 A 885 PRO PRO ASN THR TYR ARG PHE GLU GLY TRP ARG CYS VAL SEQRES 20 A 885 ASP ARG ASP PHE CYS ALA ASN ILE LEU SER ALA GLU SER SEQRES 21 A 885 SER ASP SER GLU GLY PHE VAL ILE HIS ASP GLY GLU CYS SEQRES 22 A 885 MET GLN GLU CYS PRO SER GLY PHE ILE ARG ASN GLY SER SEQRES 23 A 885 GLN SER MET TYR CYS ILE PRO CYS GLU GLY PRO CYS PRO SEQRES 24 A 885 LYS VAL CYS GLU GLU GLU LYS LYS THR LYS THR ILE ASP SEQRES 25 A 885 SER VAL THR SER ALA GLN MET LEU GLN GLY CYS THR ILE SEQRES 26 A 885 PHE LYS GLY ASN LEU LEU ILE ASN ILE ARG ARG GLY ASN SEQRES 27 A 885 ASN ILE ALA SER GLU LEU GLU ASN PHE MET GLY LEU ILE SEQRES 28 A 885 GLU VAL VAL THR GLY TYR VAL LYS ILE ARG HIS SER HIS SEQRES 29 A 885 ALA LEU VAL SER LEU SER PHE LEU LYS ASN LEU ARG LEU SEQRES 30 A 885 ILE LEU GLY GLU GLU GLN LEU GLU GLY ASN TYR SER PHE SEQRES 31 A 885 TYR VAL LEU ASP ASN GLN ASN LEU GLN GLN LEU TRP ASP SEQRES 32 A 885 TRP ASP HIS ARG ASN LEU THR ILE LYS ALA GLY LYS MET SEQRES 33 A 885 TYR PHE ALA PHE ASN PRO LYS LEU CYS VAL SER GLU ILE SEQRES 34 A 885 TYR ARG MET GLU GLU VAL THR GLY THR LYS GLY ARG GLN SEQRES 35 A 885 SER LYS GLY ASP ILE ASN THR ARG ASN ASN GLY GLU ARG SEQRES 36 A 885 ALA SER CYS GLU SER ASP VAL LEU HIS PHE THR SER THR SEQRES 37 A 885 THR THR SER LYS ASN ARG ILE ILE ILE THR TRP HIS ARG SEQRES 38 A 885 TYR ARG PRO PRO ASP TYR ARG ASP LEU ILE SER PHE THR SEQRES 39 A 885 VAL TYR TYR LYS GLU ALA PRO PHE LYS ASN VAL THR GLU SEQRES 40 A 885 TYR ASP GLY GLN ASP ALA CYS GLY SER ASN SER TRP ASN SEQRES 41 A 885 MET VAL ASP VAL ASP LEU PRO PRO ASN LYS ASP VAL GLU SEQRES 42 A 885 PRO GLY ILE LEU LEU HIS GLY LEU LYS PRO TRP THR GLN SEQRES 43 A 885 TYR ALA VAL TYR VAL LYS ALA VAL THR LEU THR MET VAL SEQRES 44 A 885 GLU ASN ASP HIS ILE ARG GLY ALA LYS SER GLU ILE LEU SEQRES 45 A 885 TYR ILE ARG THR ASN ALA SER VAL PRO SER ILE PRO LEU SEQRES 46 A 885 ASP VAL LEU SER ALA SER ASN SER SER SER GLN LEU ILE SEQRES 47 A 885 VAL LYS TRP ASN PRO PRO SER LEU PRO ASN GLY ASN LEU SEQRES 48 A 885 SER TYR TYR ILE VAL ARG TRP GLN ARG GLN PRO GLN ASP SEQRES 49 A 885 GLY TYR LEU TYR ARG HIS ASN TYR CYS SER LYS ASP LYS SEQRES 50 A 885 ILE PRO ILE ARG LYS TYR ALA ASP GLY THR ILE ASP ILE SEQRES 51 A 885 GLU GLU VAL THR GLU ASN PRO LYS THR GLU VAL CYS GLY SEQRES 52 A 885 GLY GLU LYS GLY PRO CYS CYS ALA CYS PRO LYS THR GLU SEQRES 53 A 885 ALA GLU LYS GLN ALA GLU LYS GLU GLU ALA GLU TYR ARG SEQRES 54 A 885 LYS VAL PHE GLU ASN PHE LEU HIS ASN SER ILE PHE VAL SEQRES 55 A 885 PRO ARG PRO GLU ARG LYS ARG ARG ASP VAL MET GLN VAL SEQRES 56 A 885 ALA ASN ALA GLY ASN ASN GLU THR GLU TYR PRO PHE PHE SEQRES 57 A 885 GLU SER ARG VAL ASP ASN LYS GLU ARG THR VAL ILE SER SEQRES 58 A 885 ASN LEU ARG PRO PHE THR LEU TYR ARG ILE ASP ILE HIS SEQRES 59 A 885 SER CYS ASN HIS GLU ALA GLU LYS LEU GLY CYS SER ALA SEQRES 60 A 885 SER ASN PHE VAL PHE ALA ARG THR MET PRO ALA GLU GLY SEQRES 61 A 885 ALA ASP ASP ILE PRO GLY PRO VAL THR TRP GLU PRO ARG SEQRES 62 A 885 PRO GLU ASN SER ILE PHE LEU LYS TRP PRO GLU PRO GLU SEQRES 63 A 885 ASN PRO ASN GLY LEU ILE LEU MET TYR GLU ILE LYS TYR SEQRES 64 A 885 GLY SER GLN VAL GLU ASP GLN ARG GLU CYS VAL SER ARG SEQRES 65 A 885 GLN GLU TYR ARG LYS TYR GLY GLY ALA LYS LEU ASN ARG SEQRES 66 A 885 LEU ASN PRO GLY ASN TYR THR ALA ARG ILE GLN ALA THR SEQRES 67 A 885 SER LEU SER GLY ASN GLY SER TRP THR ASP PRO VAL PHE SEQRES 68 A 885 PHE TYR VAL GLN ALA LYS THR GLY TYR GLU ASN PHE ILE SEQRES 69 A 885 HIS SEQRES 1 H 126 GLY THR GLN VAL GLN LEU GLN GLN SER GLY PRO ASP VAL SEQRES 2 H 126 VAL ARG PRO GLY VAL SER VAL LYS ILE SER CYS LYS GLY SEQRES 3 H 126 SER GLY TYR THR PHE THR ASP TYR ALA ILE HIS TRP VAL SEQRES 4 H 126 LYS GLN SER HIS ALA LYS SER LEU GLU TRP ILE GLY VAL SEQRES 5 H 126 ILE SER THR TYR ASN GLY ASN THR LYS TYR ASN GLN LYS SEQRES 6 H 126 PHE LYS GLY LYS ALA ALA ILE THR VAL ASP LYS SER SER SEQRES 7 H 126 SER THR ALA TYR LEU GLU LEU ALA ARG LEU THR SER GLU SEQRES 8 H 126 ASP SER ALA ILE TYR TYR CYS ALA SER TYR GLY ASP LEU SEQRES 9 H 126 TYR VAL MET ASP TYR TRP GLY GLN GLY THR SER VAL THR SEQRES 10 H 126 VAL SER SER GLU ASN LEU TYR PHE GLN SEQRES 1 L 108 GLY ASP ILE VAL LEU THR GLN SER PRO ALA THR LEU SER SEQRES 2 L 108 VAL THR PRO GLY ASP SER VAL SER LEU SER CYS ARG ALA SEQRES 3 L 108 SER GLN THR ILE SER ASN ASN LEU HIS TRP TYR GLN GLN SEQRES 4 L 108 LYS SER HIS GLU SER PRO ARG LEU LEU ILE LYS TYR ALA SEQRES 5 L 108 SER GLN SER ILE SER GLY ILE PRO SER ARG PHE SER GLY SEQRES 6 L 108 SER GLY SER GLY THR ASP PHE THR LEU SER ILE ASN SER SEQRES 7 L 108 VAL GLU THR GLU ASP PHE GLY MET TYR PHE CYS GLN GLN SEQRES 8 L 108 SER ASN SER TRP PRO ARG THR PHE GLY ALA GLY THR LYS SEQRES 9 L 108 LEU GLU LEU LYS HET SO4 A1001 5 HET MLT A1002 9 HET MLT A1003 9 HET NAG A1004 14 HET NAG A1005 14 HET NAG A1006 14 HET NAG A1007 14 HET NAG A1008 14 HET NAG A1009 14 HET NAG A1010 14 HET NAG A1011 14 HET IMD H 201 5 HETNAM SO4 SULFATE ION HETNAM MLT D-MALATE HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM IMD IMIDAZOLE HETSYN MLT (2R)-2-HYDROXYBUTANEDIOIC ACID; 2-HYDROXY-SUCCINIC ACID FORMUL 4 SO4 O4 S 2- FORMUL 5 MLT 2(C4 H6 O5) FORMUL 7 NAG 8(C8 H15 N O6) FORMUL 13 IMD C3 H5 N2 1+ HELIX 1 AA1 ASP A 12 GLU A 20 5 9 HELIX 2 AA2 SER A 65 LEU A 69 5 5 HELIX 3 AA3 PRO A 144 CYS A 148 5 5 HELIX 4 AA4 PRO A 186 GLY A 190 5 5 HELIX 5 AA5 ARG A 249 ALA A 253 1 5 HELIX 6 AA6 VAL A 314 MET A 319 1 6 HELIX 7 AA7 ASN A 339 GLY A 349 1 11 HELIX 8 AA8 CYS A 425 GLY A 437 1 13 HELIX 9 AA9 GLU A 684 LEU A 696 1 13 HELIX 10 AB1 GLU A 779 GLY A 784 1 6 HELIX 11 AB2 ARG A 852 GLY A 859 1 8 HELIX 12 AB3 THR H 28 TYR H 32 5 5 HELIX 13 AB4 LYS L 49 GLN L 53 5 5 SHEET 1 AA1 5 ILE A 2 CYS A 3 0 SHEET 2 AA1 5 VAL A 24 ILE A 25 1 O VAL A 24 N CYS A 3 SHEET 3 AA1 5 VAL A 50 ILE A 51 1 O VAL A 50 N ILE A 25 SHEET 4 AA1 5 VAL A 75 ILE A 76 1 O VAL A 75 N ILE A 51 SHEET 5 AA1 5 ASN A 105 ILE A 106 1 O ASN A 105 N ILE A 76 SHEET 1 AA2 6 ILE A 7 ARG A 10 0 SHEET 2 AA2 6 LEU A 29 LEU A 32 1 O HIS A 30 N ILE A 9 SHEET 3 AA2 6 LEU A 55 PHE A 58 1 O LEU A 56 N LEU A 29 SHEET 4 AA2 6 TYR A 85 PHE A 90 1 O VAL A 88 N LEU A 57 SHEET 5 AA2 6 ALA A 110 ASN A 116 1 O ALA A 110 N ALA A 86 SHEET 6 AA2 6 TYR A 138 ASN A 142 1 O TYR A 138 N ILE A 111 SHEET 1 AA3 2 LYS A 164 ILE A 167 0 SHEET 2 AA3 2 GLU A 170 TYR A 173 -1 O GLU A 170 N ILE A 167 SHEET 1 AA4 2 ALA A 193 CYS A 194 0 SHEET 2 AA4 2 CYS A 200 CYS A 201 -1 O CYS A 201 N ALA A 193 SHEET 1 AA5 2 CYS A 205 CYS A 209 0 SHEET 2 AA5 2 CYS A 218 CYS A 221 -1 O ALA A 220 N LEU A 206 SHEET 1 AA6 2 TYR A 224 TYR A 226 0 SHEET 2 AA6 2 VAL A 229 VAL A 231 -1 O VAL A 229 N TYR A 226 SHEET 1 AA7 4 ARG A 245 ASP A 248 0 SHEET 2 AA7 4 THR A 238 PHE A 241 -1 N TYR A 239 O VAL A 247 SHEET 3 AA7 4 GLU A 272 MET A 274 1 O CYS A 273 N ARG A 240 SHEET 4 AA7 4 VAL A 267 HIS A 269 -1 N HIS A 269 O GLU A 272 SHEET 1 AA8 2 PHE A 281 ARG A 283 0 SHEET 2 AA8 2 CYS A 291 PRO A 293 -1 O ILE A 292 N ILE A 282 SHEET 1 AA9 4 VAL A 301 ILE A 311 0 SHEET 2 AA9 4 ILE A 325 ILE A 332 1 O LEU A 331 N ILE A 311 SHEET 3 AA9 4 VAL A 353 VAL A 354 1 O VAL A 353 N PHE A 326 SHEET 4 AA9 4 LEU A 377 ILE A 378 1 O LEU A 377 N VAL A 354 SHEET 1 AB1 5 VAL A 301 ILE A 311 0 SHEET 2 AB1 5 ILE A 325 ILE A 332 1 O LEU A 331 N ILE A 311 SHEET 3 AB1 5 VAL A 358 ARG A 361 1 O LYS A 359 N ILE A 332 SHEET 4 AB1 5 TYR A 388 LEU A 393 1 O LEU A 393 N ILE A 360 SHEET 5 AB1 5 LYS A 415 ALA A 419 1 O LYS A 415 N SER A 389 SHEET 1 AB2 2 ASP A 461 LEU A 463 0 SHEET 2 AB2 2 ALA A 567 SER A 569 1 O LYS A 568 N LEU A 463 SHEET 1 AB3 3 PHE A 465 THR A 470 0 SHEET 2 AB3 3 ILE A 475 TRP A 479 -1 O THR A 478 N THR A 466 SHEET 3 AB3 3 GLY A 535 LEU A 538 -1 O LEU A 538 N ILE A 475 SHEET 1 AB4 4 ASN A 520 VAL A 522 0 SHEET 2 AB4 4 LEU A 490 GLU A 499 -1 N VAL A 495 O VAL A 522 SHEET 3 AB4 4 GLN A 546 LEU A 556 -1 O VAL A 554 N SER A 492 SHEET 4 AB4 4 LEU A 572 ARG A 575 -1 O ILE A 574 N TYR A 547 SHEET 1 AB5 3 LEU A 585 ALA A 590 0 SHEET 2 AB5 3 GLN A 596 ASN A 602 -1 O LYS A 600 N LEU A 588 SHEET 3 AB5 3 ARG A 757 SER A 761 -1 O ILE A 760 N LEU A 597 SHEET 1 AB6 4 PHE A 747 VAL A 752 0 SHEET 2 AB6 4 TYR A 614 ARG A 620 -1 N TYR A 614 O VAL A 752 SHEET 3 AB6 4 LEU A 768 SER A 775 -1 O ASP A 772 N ARG A 617 SHEET 4 AB6 4 VAL A 791 ARG A 794 -1 O VAL A 791 N ILE A 771 SHEET 1 AB7 3 THR A 809 ARG A 813 0 SHEET 2 AB7 3 SER A 817 LYS A 821 -1 O LYS A 821 N THR A 809 SHEET 3 AB7 3 GLY A 860 LEU A 863 -1 O LEU A 863 N ILE A 818 SHEET 1 AB8 4 GLN A 846 SER A 851 0 SHEET 2 AB8 4 ILE A 832 GLY A 840 -1 N TYR A 835 O VAL A 850 SHEET 3 AB8 4 GLY A 869 SER A 879 -1 O ARG A 874 N LYS A 838 SHEET 4 AB8 4 VAL A 890 VAL A 894 -1 O PHE A 892 N TYR A 871 SHEET 1 AB9 4 GLN H 3 GLN H 6 0 SHEET 2 AB9 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AB9 4 THR H 78 LEU H 83 -1 O LEU H 83 N VAL H 18 SHEET 4 AB9 4 ALA H 68 ASP H 73 -1 N ALA H 69 O GLU H 82 SHEET 1 AC1 6 ASP H 10 VAL H 12 0 SHEET 2 AC1 6 THR H 112 VAL H 116 1 O SER H 113 N ASP H 10 SHEET 3 AC1 6 ALA H 92 SER H 98 -1 N ALA H 92 O VAL H 114 SHEET 4 AC1 6 ILE H 34 GLN H 39 -1 N HIS H 35 O ALA H 97 SHEET 5 AC1 6 LEU H 45 ILE H 51 -1 O GLU H 46 N LYS H 38 SHEET 6 AC1 6 THR H 58 TYR H 60 -1 O LYS H 59 N VAL H 50 SHEET 1 AC2 4 ASP H 10 VAL H 12 0 SHEET 2 AC2 4 THR H 112 VAL H 116 1 O SER H 113 N ASP H 10 SHEET 3 AC2 4 ALA H 92 SER H 98 -1 N ALA H 92 O VAL H 114 SHEET 4 AC2 4 TYR H 107 TRP H 108 -1 O TYR H 107 N SER H 98 SHEET 1 AC3 4 LEU L 4 SER L 7 0 SHEET 2 AC3 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AC3 4 ASP L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AC3 4 PHE L 62 GLY L 66 -1 N SER L 63 O SER L 74 SHEET 1 AC4 5 THR L 10 VAL L 13 0 SHEET 2 AC4 5 THR L 102 LEU L 106 1 O GLU L 105 N VAL L 13 SHEET 3 AC4 5 MET L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AC4 5 LEU L 33 GLN L 38 -1 N HIS L 34 O GLN L 89 SHEET 5 AC4 5 ARG L 45 ILE L 48 -1 O ARG L 45 N GLN L 37 SSBOND 1 CYS A 3 CYS A 22 1555 1555 2.03 SSBOND 2 CYS A 120 CYS A 148 1555 1555 2.03 SSBOND 3 CYS A 152 CYS A 175 1555 1555 2.03 SSBOND 4 CYS A 162 CYS A 181 1555 1555 2.03 SSBOND 5 CYS A 185 CYS A 194 1555 1555 2.03 SSBOND 6 CYS A 189 CYS A 200 1555 1555 2.04 SSBOND 7 CYS A 201 CYS A 209 1555 1555 2.02 SSBOND 8 CYS A 205 CYS A 218 1555 1555 2.03 SSBOND 9 CYS A 221 CYS A 230 1555 1555 2.03 SSBOND 10 CYS A 234 CYS A 246 1555 1555 2.03 SSBOND 11 CYS A 252 CYS A 273 1555 1555 2.03 SSBOND 12 CYS A 277 CYS A 291 1555 1555 2.03 SSBOND 13 CYS A 294 CYS A 298 1555 1555 2.03 SSBOND 14 CYS A 302 CYS A 323 1555 1555 2.03 SSBOND 15 CYS A 425 CYS A 458 1555 1555 2.03 SSBOND 16 CYS A 633 CYS A 849 1555 1555 2.03 SSBOND 17 CYS A 776 CYS A 785 1555 1555 2.03 SSBOND 18 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 19 CYS L 23 CYS L 88 1555 1555 2.03 LINK ND2 ASN A 21 C1 NAG A1004 1555 1555 1.44 LINK ND2 ASN A 105 C1 NAG A1005 1555 1555 1.45 LINK ND2 ASN A 504 C1 NAG A1007 1555 1555 1.44 LINK ND2 ASN A 577 C1 NAG A1008 1555 1555 1.44 LINK ND2 ASN A 610 C1 NAG A1010 1555 1555 1.44 LINK ND2 ASN A 883 C1 NAG A1011 1555 1555 1.44 LINK O4 NAG A1005 C1 NAG A1006 1555 1555 1.44 LINK O4 NAG A1008 C1 NAG A1009 1555 1555 1.45 CISPEP 1 GLY A 4 PRO A 5 0 0.79 CISPEP 2 SER L 7 PRO L 8 0 -0.80 CISPEP 3 TRP L 94 PRO L 95 0 -2.05 SITE 1 AC1 3 LYS A 80 LEU A 81 ARG A 108 SITE 1 AC2 3 ARG A 245 ASP A 248 ASP H 31 SITE 1 AC3 2 HIS A 30 TYR A 54 SITE 1 AC4 4 SER H 40 HIS H 41 SER H 44 MET L 85 SITE 1 AC5 2 GLU A 20 ASN A 21 SITE 1 AC6 7 ASN A 105 LEU A 129 ILE A 130 LEU A 131 SITE 2 AC6 7 ASP A 132 ARG A 222 HIS A 223 SITE 1 AC7 1 ASN A 504 SITE 1 AC8 4 ASN A 577 LYS A 782 LYS L 103 GLU L 105 SITE 1 AC9 1 ASN A 610 SITE 1 AD1 4 GLN A 876 ASN A 883 GLY A 884 SER A 885 CRYST1 95.030 201.730 117.750 90.00 90.00 90.00 P 21 21 2 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 0.010523 0.000000 0.000000 0.00000 SCALE2 0.000000 0.004957 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008493 0.00000